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Database: PDB
Entry: 4UX9
LinkDB: 4UX9
Original site: 4UX9 
HEADER    TRANSFERASE                             20-AUG-14   4UX9              
TITLE     CRYSTAL STRUCTURE OF JNK1 BOUND TO A MKK7 DOCKING MOTIF               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 8;                        
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: MAP KINASE 8, MAPK 8, JNK-46, STRESS-ACTIVATED PROTEIN      
COMPND   5 KINASE 1C, SAPK1C, STRESS-ACTIVATED PROTEIN KINASE JNK1, C-JUN N-    
COMPND   6 TERMI NAL KINASE 1, JNK1;                                            
COMPND   7 EC: 2.7.11.24;                                                       
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: DUAL SPECIFICITY MITOGEN-ACTIVATED PROTEIN KINASE KINASE 7;
COMPND  11 CHAIN: F, G, H, I;                                                   
COMPND  12 FRAGMENT: RESIDUES 37-48;                                            
COMPND  13 SYNONYM: MAP KINASE KINASE 7, MAPKK 7, JNK-ACTIVATING KINASE 2,      
COMPND  14 MAPK/ERK KINASE 7, MEK 7, STRESS-ACTIVATED PROTEIN KINASE KINASE 4,  
COMPND  15 SAPK KINASE 4, SAPKK-4, SAPKK4, C-JUN N-TERMINAL KINASE KINASE 2, JNK
COMPND  16 KINASE 2, JNKK 2, MKK7;                                              
COMPND  17 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606                                                 
KEYWDS    TRANSFERASE, JNK1, INTRINSICALLY DISORDERED DOMAINS, MKK7             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.KRAGELJ,A.PALENCIA,M.H.NANAO,D.MAURIN,G.BOUVIGNIES,M.BLACKLEDGE,    
AUTHOR   2 M.RINGKJOBING-JENSEN                                                 
REVDAT   3   27-SEP-17 4UX9    1       REMARK                                   
REVDAT   2   06-APR-16 4UX9    1       JRNL                                     
REVDAT   1   25-MAR-15 4UX9    0                                                
JRNL        AUTH   J.KRAGELJ,A.PALENCIA,M.H.NANAO,D.MAURIN,G.BOUVIGNIES,        
JRNL        AUTH 2 M.BLACKLEDGE,M.R.JENSEN                                      
JRNL        TITL   STRUCTURE AND DYNAMICS OF THE MKK7-JNK SIGNALING COMPLEX.    
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 112  3409 2015              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   25737554                                                     
JRNL        DOI    10.1073/PNAS.1419528112                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.34 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.0                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.34                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.21                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 75430                          
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)  : 0.202                          
REMARK   3   R VALUE            (WORKING SET)  : 0.200                          
REMARK   3   FREE R VALUE                      : 0.241                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.280                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 3985                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.34                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.40                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 98.41                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 5036                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2739                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 5036                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2739                   
REMARK   3   BIN FREE R VALUE                        : 0.0000                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 0.00                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 0                        
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11211                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 204                                     
REMARK   3   SOLVENT ATOMS            : 276                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 66.09                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 66.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.07090                                             
REMARK   3    B22 (A**2) : 4.15420                                              
REMARK   3    B33 (A**2) : -2.08340                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 3.48200                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.329               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.285               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.216               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.299               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.222               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.947                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.931                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 11660  ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 15802  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 5421   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 279    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1660   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 11660  ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 1490   ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 13046  ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.09                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.19                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 3.28                     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4UX9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-AUG-14.                  
REMARK 100 THE DEPOSITION ID IS D_1290061579.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-MAR-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97625                            
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : TOROIDAL MIRROR                    
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 75436                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.340                              
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     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.05000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.6600                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.34                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.73000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.660                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2XRW                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.91                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM HEPES 150 MM NACL 2 MM MGSO4 1     
REMARK 280  MM TCEP 2.6 M NH4SO4                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       54.33300            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       90.07950            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       54.33300            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       90.07950            
REMARK 290   SMTRY3   4  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: OCTAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 17060 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 60290 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -285.1 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, F, G, H, I                
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     SER A     2                                                      
REMARK 465     ARG A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     LYS A     5                                                      
REMARK 465     ARG A     6                                                      
REMARK 465     ASP A     7                                                      
REMARK 465     GLN A    37                                                      
REMARK 465     ARG A    59                                                      
REMARK 465     SER A   179                                                      
REMARK 465     PHE A   180                                                      
REMARK 465     MET A   181                                                      
REMARK 465     MET A   182                                                      
REMARK 465     THR A   183                                                      
REMARK 465     ASP A   339                                                      
REMARK 465     LYS A   340                                                      
REMARK 465     GLN A   341                                                      
REMARK 465     LEU A   342                                                      
REMARK 465     ASP A   343                                                      
REMARK 465     GLU A   344                                                      
REMARK 465     GLU A   364                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     SER B     4                                                      
REMARK 465     LYS B     5                                                      
REMARK 465     ARG B     6                                                      
REMARK 465     ASP B     7                                                      
REMARK 465     GLY B    35                                                      
REMARK 465     ALA B    36                                                      
REMARK 465     GLN B    37                                                      
REMARK 465     GLY B    38                                                      
REMARK 465     THR B   178                                                      
REMARK 465     SER B   179                                                      
REMARK 465     PHE B   180                                                      
REMARK 465     MET B   181                                                      
REMARK 465     MET B   182                                                      
REMARK 465     THR B   183                                                      
REMARK 465     GLU B   285                                                      
REMARK 465     HIS B   286                                                      
REMARK 465     ASN B   287                                                      
REMARK 465     LYS B   288                                                      
REMARK 465     ASP B   339                                                      
REMARK 465     LYS B   340                                                      
REMARK 465     GLN B   341                                                      
REMARK 465     LEU B   342                                                      
REMARK 465     ASP B   343                                                      
REMARK 465     GLU B   344                                                      
REMARK 465     ARG B   345                                                      
REMARK 465     GLU B   346                                                      
REMARK 465     HIS B   347                                                      
REMARK 465     THR B   348                                                      
REMARK 465     ILE B   349                                                      
REMARK 465     GLU B   350                                                      
REMARK 465     GLU B   351                                                      
REMARK 465     TRP B   352                                                      
REMARK 465     LEU B   363                                                      
REMARK 465     GLU B   364                                                      
REMARK 465     MET C     1                                                      
REMARK 465     SER C     2                                                      
REMARK 465     ARG C     3                                                      
REMARK 465     SER C     4                                                      
REMARK 465     LYS C     5                                                      
REMARK 465     ARG C     6                                                      
REMARK 465     ASP C     7                                                      
REMARK 465     ALA C    36                                                      
REMARK 465     THR C   178                                                      
REMARK 465     SER C   179                                                      
REMARK 465     PHE C   180                                                      
REMARK 465     MET C   181                                                      
REMARK 465     MET C   182                                                      
REMARK 465     THR C   183                                                      
REMARK 465     PRO C   184                                                      
REMARK 465     ALA C   282                                                      
REMARK 465     ASP C   283                                                      
REMARK 465     SER C   284                                                      
REMARK 465     GLU C   285                                                      
REMARK 465     HIS C   286                                                      
REMARK 465     ASN C   287                                                      
REMARK 465     LYS C   288                                                      
REMARK 465     ASP C   339                                                      
REMARK 465     LYS C   340                                                      
REMARK 465     GLN C   341                                                      
REMARK 465     LEU C   342                                                      
REMARK 465     ASP C   343                                                      
REMARK 465     GLU C   344                                                      
REMARK 465     ARG C   345                                                      
REMARK 465     GLU C   346                                                      
REMARK 465     GLU C   364                                                      
REMARK 465     MET D     1                                                      
REMARK 465     SER D     2                                                      
REMARK 465     ARG D     3                                                      
REMARK 465     SER D     4                                                      
REMARK 465     LYS D     5                                                      
REMARK 465     ARG D     6                                                      
REMARK 465     ASP D     7                                                      
REMARK 465     ASN D     8                                                      
REMARK 465     GLY D    33                                                      
REMARK 465     SER D    34                                                      
REMARK 465     GLY D    35                                                      
REMARK 465     ALA D    36                                                      
REMARK 465     GLN D    37                                                      
REMARK 465     GLY D    38                                                      
REMARK 465     SER D   284                                                      
REMARK 465     GLU D   285                                                      
REMARK 465     HIS D   286                                                      
REMARK 465     LYS D   340                                                      
REMARK 465     GLN D   341                                                      
REMARK 465     LEU D   342                                                      
REMARK 465     GLN F    37                                                      
REMARK 465     ARG F    38                                                      
REMARK 465     GLN G    37                                                      
REMARK 465     ARG G    38                                                      
REMARK 465     PRO G    39                                                      
REMARK 465     ARG G    40                                                      
REMARK 465     THR I    42                                                      
REMARK 465     LEU I    43                                                      
REMARK 465     ALA I    48                                                      
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     GLN C  37    CG   CD   OE1  NE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    TYR B 185   CA    TYR B 185   C      -0.188                       
REMARK 500    TYR B 185   C     TYR B 185   O       0.115                       
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    ASP A  17      -40.30   -133.43                                   
REMARK 500    PHE A 101      122.63    -34.68                                   
REMARK 500    GLN A 102      -65.68   -140.48                                   
REMARK 500    ARG A 150      -28.18     73.76                                   
REMARK 500    LEU A 168      -65.56   -106.90                                   
REMARK 500    ASN B  28       45.26     72.81                                   
REMARK 500    ARG B  59       62.30     36.24                                   
REMARK 500    PHE B 101      126.29    -36.66                                   
REMARK 500    GLN B 102      -49.35   -142.31                                   
REMARK 500    ARG B 150      -24.85     79.08                                   
REMARK 500    LEU B 168      -79.97    -95.23                                   
REMARK 500    LYS B 203     -159.41   -112.79                                   
REMARK 500    ASN B 205        9.80    -65.67                                   
REMARK 500    GLN C 102      -54.94   -133.05                                   
REMARK 500    ARG C 150      -16.82     71.23                                   
REMARK 500    GLU C 331       55.86   -102.61                                   
REMARK 500    ARG D  59       73.51     40.38                                   
REMARK 500    ASN D  81       86.73   -158.16                                   
REMARK 500    GLU D 100       70.07   -107.20                                   
REMARK 500    GLN D 102       -9.59   -147.96                                   
REMARK 500    ARG D 150      -12.64     70.57                                   
REMARK 500    LEU D 168      -55.98   -120.60                                   
REMARK 500    ASN D 205        6.77    -65.93                                   
REMARK 500    TYR D 325      127.69    -39.39                                   
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 ANP A 1000                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP B 1000                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP C 1000                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP D 1000                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 1364                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1363                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1364                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1364                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 H 1049                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1365                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 1365                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1365                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 1365                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 1366                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 1367                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 1366                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1366                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 1367                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1366                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1367                
DBREF  4UX9 A    1   364  UNP    P45983   MK08_HUMAN       1    364             
DBREF  4UX9 B    1   364  UNP    P45983   MK08_HUMAN       1    364             
DBREF  4UX9 C    1   364  UNP    P45983   MK08_HUMAN       1    364             
DBREF  4UX9 D    1   364  UNP    P45983   MK08_HUMAN       1    364             
DBREF  4UX9 F   37    48  UNP    O14733   MP2K7_HUMAN     37     48             
DBREF  4UX9 G   37    48  UNP    O14733   MP2K7_HUMAN     37     48             
DBREF  4UX9 H   37    48  UNP    O14733   MP2K7_HUMAN     37     48             
DBREF  4UX9 I   37    48  UNP    O14733   MP2K7_HUMAN     37     48             
SEQRES   1 A  364  MET SER ARG SER LYS ARG ASP ASN ASN PHE TYR SER VAL          
SEQRES   2 A  364  GLU ILE GLY ASP SER THR PHE THR VAL LEU LYS ARG TYR          
SEQRES   3 A  364  GLN ASN LEU LYS PRO ILE GLY SER GLY ALA GLN GLY ILE          
SEQRES   4 A  364  VAL CYS ALA ALA TYR ASP ALA ILE LEU GLU ARG ASN VAL          
SEQRES   5 A  364  ALA ILE LYS LYS LEU SER ARG PRO PHE GLN ASN GLN THR          
SEQRES   6 A  364  HIS ALA LYS ARG ALA TYR ARG GLU LEU VAL LEU MET LYS          
SEQRES   7 A  364  CYS VAL ASN HIS LYS ASN ILE ILE GLY LEU LEU ASN VAL          
SEQRES   8 A  364  PHE THR PRO GLN LYS SER LEU GLU GLU PHE GLN ASP VAL          
SEQRES   9 A  364  TYR ILE VAL MET GLU LEU MET ASP ALA ASN LEU CYS GLN          
SEQRES  10 A  364  VAL ILE GLN MET GLU LEU ASP HIS GLU ARG MET SER TYR          
SEQRES  11 A  364  LEU LEU TYR GLN MET LEU CYS GLY ILE LYS HIS LEU HIS          
SEQRES  12 A  364  SER ALA GLY ILE ILE HIS ARG ASP LEU LYS PRO SER ASN          
SEQRES  13 A  364  ILE VAL VAL LYS SER ASP CYS THR LEU LYS ILE LEU ASP          
SEQRES  14 A  364  PHE GLY LEU ALA ARG THR ALA GLY THR SER PHE MET MET          
SEQRES  15 A  364  THR PRO TYR VAL VAL THR ARG TYR TYR ARG ALA PRO GLU          
SEQRES  16 A  364  VAL ILE LEU GLY MET GLY TYR LYS GLU ASN VAL ASP LEU          
SEQRES  17 A  364  TRP SER VAL GLY CYS ILE MET GLY GLU MET VAL CYS HIS          
SEQRES  18 A  364  LYS ILE LEU PHE PRO GLY ARG ASP TYR ILE ASP GLN TRP          
SEQRES  19 A  364  ASN LYS VAL ILE GLU GLN LEU GLY THR PRO CYS PRO GLU          
SEQRES  20 A  364  PHE MET LYS LYS LEU GLN PRO THR VAL ARG THR TYR VAL          
SEQRES  21 A  364  GLU ASN ARG PRO LYS TYR ALA GLY TYR SER PHE GLU LYS          
SEQRES  22 A  364  LEU PHE PRO ASP VAL LEU PHE PRO ALA ASP SER GLU HIS          
SEQRES  23 A  364  ASN LYS LEU LYS ALA SER GLN ALA ARG ASP LEU LEU SER          
SEQRES  24 A  364  LYS MET LEU VAL ILE ASP ALA SER LYS ARG ILE SER VAL          
SEQRES  25 A  364  ASP GLU ALA LEU GLN HIS PRO TYR ILE ASN VAL TRP TYR          
SEQRES  26 A  364  ASP PRO SER GLU ALA GLU ALA PRO PRO PRO LYS ILE PRO          
SEQRES  27 A  364  ASP LYS GLN LEU ASP GLU ARG GLU HIS THR ILE GLU GLU          
SEQRES  28 A  364  TRP LYS GLU LEU ILE TYR LYS GLU VAL MET ASP LEU GLU          
SEQRES   1 B  364  MET SER ARG SER LYS ARG ASP ASN ASN PHE TYR SER VAL          
SEQRES   2 B  364  GLU ILE GLY ASP SER THR PHE THR VAL LEU LYS ARG TYR          
SEQRES   3 B  364  GLN ASN LEU LYS PRO ILE GLY SER GLY ALA GLN GLY ILE          
SEQRES   4 B  364  VAL CYS ALA ALA TYR ASP ALA ILE LEU GLU ARG ASN VAL          
SEQRES   5 B  364  ALA ILE LYS LYS LEU SER ARG PRO PHE GLN ASN GLN THR          
SEQRES   6 B  364  HIS ALA LYS ARG ALA TYR ARG GLU LEU VAL LEU MET LYS          
SEQRES   7 B  364  CYS VAL ASN HIS LYS ASN ILE ILE GLY LEU LEU ASN VAL          
SEQRES   8 B  364  PHE THR PRO GLN LYS SER LEU GLU GLU PHE GLN ASP VAL          
SEQRES   9 B  364  TYR ILE VAL MET GLU LEU MET ASP ALA ASN LEU CYS GLN          
SEQRES  10 B  364  VAL ILE GLN MET GLU LEU ASP HIS GLU ARG MET SER TYR          
SEQRES  11 B  364  LEU LEU TYR GLN MET LEU CYS GLY ILE LYS HIS LEU HIS          
SEQRES  12 B  364  SER ALA GLY ILE ILE HIS ARG ASP LEU LYS PRO SER ASN          
SEQRES  13 B  364  ILE VAL VAL LYS SER ASP CYS THR LEU LYS ILE LEU ASP          
SEQRES  14 B  364  PHE GLY LEU ALA ARG THR ALA GLY THR SER PHE MET MET          
SEQRES  15 B  364  THR PRO TYR VAL VAL THR ARG TYR TYR ARG ALA PRO GLU          
SEQRES  16 B  364  VAL ILE LEU GLY MET GLY TYR LYS GLU ASN VAL ASP LEU          
SEQRES  17 B  364  TRP SER VAL GLY CYS ILE MET GLY GLU MET VAL CYS HIS          
SEQRES  18 B  364  LYS ILE LEU PHE PRO GLY ARG ASP TYR ILE ASP GLN TRP          
SEQRES  19 B  364  ASN LYS VAL ILE GLU GLN LEU GLY THR PRO CYS PRO GLU          
SEQRES  20 B  364  PHE MET LYS LYS LEU GLN PRO THR VAL ARG THR TYR VAL          
SEQRES  21 B  364  GLU ASN ARG PRO LYS TYR ALA GLY TYR SER PHE GLU LYS          
SEQRES  22 B  364  LEU PHE PRO ASP VAL LEU PHE PRO ALA ASP SER GLU HIS          
SEQRES  23 B  364  ASN LYS LEU LYS ALA SER GLN ALA ARG ASP LEU LEU SER          
SEQRES  24 B  364  LYS MET LEU VAL ILE ASP ALA SER LYS ARG ILE SER VAL          
SEQRES  25 B  364  ASP GLU ALA LEU GLN HIS PRO TYR ILE ASN VAL TRP TYR          
SEQRES  26 B  364  ASP PRO SER GLU ALA GLU ALA PRO PRO PRO LYS ILE PRO          
SEQRES  27 B  364  ASP LYS GLN LEU ASP GLU ARG GLU HIS THR ILE GLU GLU          
SEQRES  28 B  364  TRP LYS GLU LEU ILE TYR LYS GLU VAL MET ASP LEU GLU          
SEQRES   1 C  364  MET SER ARG SER LYS ARG ASP ASN ASN PHE TYR SER VAL          
SEQRES   2 C  364  GLU ILE GLY ASP SER THR PHE THR VAL LEU LYS ARG TYR          
SEQRES   3 C  364  GLN ASN LEU LYS PRO ILE GLY SER GLY ALA GLN GLY ILE          
SEQRES   4 C  364  VAL CYS ALA ALA TYR ASP ALA ILE LEU GLU ARG ASN VAL          
SEQRES   5 C  364  ALA ILE LYS LYS LEU SER ARG PRO PHE GLN ASN GLN THR          
SEQRES   6 C  364  HIS ALA LYS ARG ALA TYR ARG GLU LEU VAL LEU MET LYS          
SEQRES   7 C  364  CYS VAL ASN HIS LYS ASN ILE ILE GLY LEU LEU ASN VAL          
SEQRES   8 C  364  PHE THR PRO GLN LYS SER LEU GLU GLU PHE GLN ASP VAL          
SEQRES   9 C  364  TYR ILE VAL MET GLU LEU MET ASP ALA ASN LEU CYS GLN          
SEQRES  10 C  364  VAL ILE GLN MET GLU LEU ASP HIS GLU ARG MET SER TYR          
SEQRES  11 C  364  LEU LEU TYR GLN MET LEU CYS GLY ILE LYS HIS LEU HIS          
SEQRES  12 C  364  SER ALA GLY ILE ILE HIS ARG ASP LEU LYS PRO SER ASN          
SEQRES  13 C  364  ILE VAL VAL LYS SER ASP CYS THR LEU LYS ILE LEU ASP          
SEQRES  14 C  364  PHE GLY LEU ALA ARG THR ALA GLY THR SER PHE MET MET          
SEQRES  15 C  364  THR PRO TYR VAL VAL THR ARG TYR TYR ARG ALA PRO GLU          
SEQRES  16 C  364  VAL ILE LEU GLY MET GLY TYR LYS GLU ASN VAL ASP LEU          
SEQRES  17 C  364  TRP SER VAL GLY CYS ILE MET GLY GLU MET VAL CYS HIS          
SEQRES  18 C  364  LYS ILE LEU PHE PRO GLY ARG ASP TYR ILE ASP GLN TRP          
SEQRES  19 C  364  ASN LYS VAL ILE GLU GLN LEU GLY THR PRO CYS PRO GLU          
SEQRES  20 C  364  PHE MET LYS LYS LEU GLN PRO THR VAL ARG THR TYR VAL          
SEQRES  21 C  364  GLU ASN ARG PRO LYS TYR ALA GLY TYR SER PHE GLU LYS          
SEQRES  22 C  364  LEU PHE PRO ASP VAL LEU PHE PRO ALA ASP SER GLU HIS          
SEQRES  23 C  364  ASN LYS LEU LYS ALA SER GLN ALA ARG ASP LEU LEU SER          
SEQRES  24 C  364  LYS MET LEU VAL ILE ASP ALA SER LYS ARG ILE SER VAL          
SEQRES  25 C  364  ASP GLU ALA LEU GLN HIS PRO TYR ILE ASN VAL TRP TYR          
SEQRES  26 C  364  ASP PRO SER GLU ALA GLU ALA PRO PRO PRO LYS ILE PRO          
SEQRES  27 C  364  ASP LYS GLN LEU ASP GLU ARG GLU HIS THR ILE GLU GLU          
SEQRES  28 C  364  TRP LYS GLU LEU ILE TYR LYS GLU VAL MET ASP LEU GLU          
SEQRES   1 D  364  MET SER ARG SER LYS ARG ASP ASN ASN PHE TYR SER VAL          
SEQRES   2 D  364  GLU ILE GLY ASP SER THR PHE THR VAL LEU LYS ARG TYR          
SEQRES   3 D  364  GLN ASN LEU LYS PRO ILE GLY SER GLY ALA GLN GLY ILE          
SEQRES   4 D  364  VAL CYS ALA ALA TYR ASP ALA ILE LEU GLU ARG ASN VAL          
SEQRES   5 D  364  ALA ILE LYS LYS LEU SER ARG PRO PHE GLN ASN GLN THR          
SEQRES   6 D  364  HIS ALA LYS ARG ALA TYR ARG GLU LEU VAL LEU MET LYS          
SEQRES   7 D  364  CYS VAL ASN HIS LYS ASN ILE ILE GLY LEU LEU ASN VAL          
SEQRES   8 D  364  PHE THR PRO GLN LYS SER LEU GLU GLU PHE GLN ASP VAL          
SEQRES   9 D  364  TYR ILE VAL MET GLU LEU MET ASP ALA ASN LEU CYS GLN          
SEQRES  10 D  364  VAL ILE GLN MET GLU LEU ASP HIS GLU ARG MET SER TYR          
SEQRES  11 D  364  LEU LEU TYR GLN MET LEU CYS GLY ILE LYS HIS LEU HIS          
SEQRES  12 D  364  SER ALA GLY ILE ILE HIS ARG ASP LEU LYS PRO SER ASN          
SEQRES  13 D  364  ILE VAL VAL LYS SER ASP CYS THR LEU LYS ILE LEU ASP          
SEQRES  14 D  364  PHE GLY LEU ALA ARG THR ALA GLY THR SER PHE MET MET          
SEQRES  15 D  364  THR PRO TYR VAL VAL THR ARG TYR TYR ARG ALA PRO GLU          
SEQRES  16 D  364  VAL ILE LEU GLY MET GLY TYR LYS GLU ASN VAL ASP LEU          
SEQRES  17 D  364  TRP SER VAL GLY CYS ILE MET GLY GLU MET VAL CYS HIS          
SEQRES  18 D  364  LYS ILE LEU PHE PRO GLY ARG ASP TYR ILE ASP GLN TRP          
SEQRES  19 D  364  ASN LYS VAL ILE GLU GLN LEU GLY THR PRO CYS PRO GLU          
SEQRES  20 D  364  PHE MET LYS LYS LEU GLN PRO THR VAL ARG THR TYR VAL          
SEQRES  21 D  364  GLU ASN ARG PRO LYS TYR ALA GLY TYR SER PHE GLU LYS          
SEQRES  22 D  364  LEU PHE PRO ASP VAL LEU PHE PRO ALA ASP SER GLU HIS          
SEQRES  23 D  364  ASN LYS LEU LYS ALA SER GLN ALA ARG ASP LEU LEU SER          
SEQRES  24 D  364  LYS MET LEU VAL ILE ASP ALA SER LYS ARG ILE SER VAL          
SEQRES  25 D  364  ASP GLU ALA LEU GLN HIS PRO TYR ILE ASN VAL TRP TYR          
SEQRES  26 D  364  ASP PRO SER GLU ALA GLU ALA PRO PRO PRO LYS ILE PRO          
SEQRES  27 D  364  ASP LYS GLN LEU ASP GLU ARG GLU HIS THR ILE GLU GLU          
SEQRES  28 D  364  TRP LYS GLU LEU ILE TYR LYS GLU VAL MET ASP LEU GLU          
SEQRES   1 F   12  GLN ARG PRO ARG PRO THR LEU GLN LEU PRO LEU ALA              
SEQRES   1 G   12  GLN ARG PRO ARG PRO THR LEU GLN LEU PRO LEU ALA              
SEQRES   1 H   12  GLN ARG PRO ARG PRO THR LEU GLN LEU PRO LEU ALA              
SEQRES   1 I   12  GLN ARG PRO ARG PRO THR LEU GLN LEU PRO LEU ALA              
HET    ANP  A1000      31                                                       
HET    SO4  A1364       5                                                       
HET    SO4  A1365       5                                                       
HET    SO4  A1366       5                                                       
HET    SO4  A1367       5                                                       
HET    ANP  B1000      31                                                       
HET    SO4  B1363       5                                                       
HET    SO4  B1364       5                                                       
HET    SO4  B1365       5                                                       
HET    SO4  B1366       5                                                       
HET    ANP  C1000      31                                                       
HET    SO4  C1364       5                                                       
HET    SO4  C1365       5                                                       
HET    SO4  C1366       5                                                       
HET    SO4  C1367       5                                                       
HET    ANP  D1000      31                                                       
HET    SO4  D1365       5                                                       
HET    SO4  D1366       5                                                       
HET    SO4  D1367       5                                                       
HET    SO4  H1049       5                                                       
HETNAM     ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER                      
HETNAM     SO4 SULFATE ION                                                      
FORMUL   9  ANP    4(C10 H17 N6 O12 P3)                                         
FORMUL  10  SO4    16(O4 S 2-)                                                  
FORMUL  29  HOH   *276(H2 O)                                                    
HELIX    1   1 ASN A   63  VAL A   80  1                                  18    
HELIX    2   2 LEU A  115  GLN A  120  1                                   6    
HELIX    3   3 ASP A  124  ALA A  145  1                                  22    
HELIX    4   4 LYS A  153  SER A  155  5                                   3    
HELIX    5   5 THR A  188  ARG A  192  5                                   5    
HELIX    6   6 ALA A  193  LEU A  198  1                                   6    
HELIX    7   7 ASN A  205  HIS A  221  1                                  17    
HELIX    8   8 ILE A  231  GLY A  242  1                                  12    
HELIX    9   9 CYS A  245  LYS A  250  1                                   6    
HELIX   10  10 GLN A  253  ASN A  262  1                                  10    
HELIX   11  11 SER A  270  PHE A  275  1                                   6    
HELIX   12  12 PRO A  276  PHE A  280  5                                   5    
HELIX   13  13 LYS A  290  LEU A  302  1                                  13    
HELIX   14  14 SER A  311  HIS A  318  1                                   8    
HELIX   15  15 ILE A  321  TYR A  325  5                                   5    
HELIX   16  16 ASP A  326  GLU A  331  1                                   6    
HELIX   17  17 THR A  348  LEU A  363  1                                  16    
HELIX   18  18 PRO B   60  GLN B   62  5                                   3    
HELIX   19  19 ASN B   63  VAL B   80  1                                  18    
HELIX   20  20 LEU B  115  GLN B  120  1                                   6    
HELIX   21  21 ASP B  124  SER B  144  1                                  21    
HELIX   22  22 LYS B  153  SER B  155  5                                   3    
HELIX   23  23 THR B  188  ARG B  192  5                                   5    
HELIX   24  24 ALA B  193  LEU B  198  1                                   6    
HELIX   25  25 ASN B  205  HIS B  221  1                                  17    
HELIX   26  26 ILE B  231  GLY B  242  1                                  12    
HELIX   27  27 CYS B  245  LYS B  251  1                                   7    
HELIX   28  28 GLN B  253  ASN B  262  1                                  10    
HELIX   29  29 SER B  270  PHE B  275  1                                   6    
HELIX   30  30 PRO B  276  PHE B  280  5                                   5    
HELIX   31  31 LYS B  290  LEU B  302  1                                  13    
HELIX   32  32 ASP B  305  ARG B  309  5                                   5    
HELIX   33  33 SER B  311  GLN B  317  1                                   7    
HELIX   34  34 ILE B  321  TYR B  325  5                                   5    
HELIX   35  35 ASP B  326  GLU B  331  1                                   6    
HELIX   36  36 LYS B  353  ASP B  362  1                                  10    
HELIX   37  37 ASN C   63  VAL C   80  1                                  18    
HELIX   38  38 LEU C  115  GLN C  120  1                                   6    
HELIX   39  39 ASP C  124  ALA C  145  1                                  22    
HELIX   40  40 LYS C  153  SER C  155  5                                   3    
HELIX   41  41 THR C  188  ARG C  192  5                                   5    
HELIX   42  42 ALA C  193  LEU C  198  1                                   6    
HELIX   43  43 ASN C  205  HIS C  221  1                                  17    
HELIX   44  44 ILE C  231  GLY C  242  1                                  12    
HELIX   45  45 CYS C  245  LYS C  250  1                                   6    
HELIX   46  46 GLN C  253  ARG C  263  1                                  11    
HELIX   47  47 SER C  270  PHE C  275  1                                   6    
HELIX   48  48 PRO C  276  PHE C  280  5                                   5    
HELIX   49  49 LYS C  290  LEU C  302  1                                  13    
HELIX   50  50 ASP C  305  ARG C  309  5                                   5    
HELIX   51  51 SER C  311  GLN C  317  1                                   7    
HELIX   52  52 ILE C  321  TYR C  325  5                                   5    
HELIX   53  53 ASP C  326  GLU C  331  1                                   6    
HELIX   54  54 THR C  348  LEU C  363  1                                  16    
HELIX   55  55 ASN D   63  VAL D   80  1                                  18    
HELIX   56  56 LEU D  115  GLN D  120  1                                   6    
HELIX   57  57 ASP D  124  SER D  144  1                                  21    
HELIX   58  58 LYS D  153  SER D  155  5                                   3    
HELIX   59  59 ALA D  193  LEU D  198  1                                   6    
HELIX   60  60 ASN D  205  HIS D  221  1                                  17    
HELIX   61  61 ILE D  231  GLY D  242  1                                  12    
HELIX   62  62 CYS D  245  LYS D  250  1                                   6    
HELIX   63  63 GLN D  253  ARG D  263  1                                  11    
HELIX   64  64 SER D  270  PHE D  275  1                                   6    
HELIX   65  65 PRO D  276  PHE D  280  5                                   5    
HELIX   66  66 LYS D  290  LEU D  302  1                                  13    
HELIX   67  67 ASP D  305  ARG D  309  5                                   5    
HELIX   68  68 SER D  311  HIS D  318  1                                   8    
HELIX   69  69 ILE D  321  TYR D  325  5                                   5    
HELIX   70  70 ASP D  326  GLU D  331  1                                   6    
HELIX   71  71 THR D  348  GLU D  364  1                                  17    
SHEET    1  AA 2 PHE A  10  ILE A  15  0                                        
SHEET    2  AA 2 SER A  18  LEU A  23 -1  O  SER A  18   N  ILE A  15           
SHEET    1  AB 5 TYR A  26  GLY A  33  0                                        
SHEET    2  AB 5 ILE A  39  ASP A  45 -1  O  VAL A  40   N  ILE A  32           
SHEET    3  AB 5 ARG A  50  LEU A  57 -1  O  ARG A  50   N  ASP A  45           
SHEET    4  AB 5 VAL A 104  GLU A 109 -1  O  VAL A 104   N  LEU A  57           
SHEET    5  AB 5 LEU A  88  PHE A  92 -1  N  LEU A  89   O  VAL A 107           
SHEET    1  AC 3 ALA A 113  ASN A 114  0                                        
SHEET    2  AC 3 ILE A 157  VAL A 159 -1  O  VAL A 159   N  ALA A 113           
SHEET    3  AC 3 LEU A 165  ILE A 167 -1  O  LYS A 166   N  VAL A 158           
SHEET    1  BA 2 PHE B  10  ILE B  15  0                                        
SHEET    2  BA 2 SER B  18  LEU B  23 -1  O  SER B  18   N  ILE B  15           
SHEET    1  BB 5 TYR B  26  GLY B  33  0                                        
SHEET    2  BB 5 VAL B  40  ASP B  45 -1  O  VAL B  40   N  ILE B  32           
SHEET    3  BB 5 ARG B  50  SER B  58 -1  O  ARG B  50   N  ASP B  45           
SHEET    4  BB 5 ASP B 103  GLU B 109 -1  O  VAL B 104   N  LEU B  57           
SHEET    5  BB 5 LEU B  88  PHE B  92 -1  N  LEU B  89   O  VAL B 107           
SHEET    1  BC 3 ALA B 113  ASN B 114  0                                        
SHEET    2  BC 3 ILE B 157  LYS B 160 -1  O  VAL B 159   N  ALA B 113           
SHEET    3  BC 3 THR B 164  ILE B 167 -1  O  THR B 164   N  LYS B 160           
SHEET    1  CA 2 PHE C  10  ILE C  15  0                                        
SHEET    2  CA 2 SER C  18  LEU C  23 -1  O  SER C  18   N  ILE C  15           
SHEET    1  CB 5 TYR C  26  SER C  34  0                                        
SHEET    2  CB 5 ILE C  39  ASP C  45 -1  O  VAL C  40   N  ILE C  32           
SHEET    3  CB 5 ARG C  50  SER C  58 -1  O  ARG C  50   N  ASP C  45           
SHEET    4  CB 5 ASP C 103  GLU C 109 -1  O  VAL C 104   N  LEU C  57           
SHEET    5  CB 5 LEU C  88  PHE C  92 -1  N  LEU C  89   O  VAL C 107           
SHEET    1  CC 3 ALA C 113  ASN C 114  0                                        
SHEET    2  CC 3 ILE C 157  VAL C 159 -1  O  VAL C 159   N  ALA C 113           
SHEET    3  CC 3 LEU C 165  ILE C 167 -1  O  LYS C 166   N  VAL C 158           
SHEET    1  DA 2 PHE D  10  ILE D  15  0                                        
SHEET    2  DA 2 SER D  18  LEU D  23 -1  O  SER D  18   N  ILE D  15           
SHEET    1  DB 5 TYR D  26  PRO D  31  0                                        
SHEET    2  DB 5 VAL D  40  ASP D  45 -1  O  ALA D  42   N  LYS D  30           
SHEET    3  DB 5 ARG D  50  LYS D  56 -1  O  ARG D  50   N  ASP D  45           
SHEET    4  DB 5 TYR D 105  GLU D 109 -1  O  ILE D 106   N  LYS D  55           
SHEET    5  DB 5 LEU D  88  PHE D  92 -1  N  LEU D  89   O  VAL D 107           
SHEET    1  DC 3 ALA D 113  ASN D 114  0                                        
SHEET    2  DC 3 ILE D 157  VAL D 159 -1  O  VAL D 159   N  ALA D 113           
SHEET    3  DC 3 LEU D 165  ILE D 167 -1  O  LYS D 166   N  VAL D 158           
SITE     1 AC1 17 ILE A  32  GLY A  33  SER A  34  GLY A  35                    
SITE     2 AC1 17 ALA A  36  GLY A  38  VAL A  40  ALA A  53                    
SITE     3 AC1 17 LYS A  55  ILE A  86  MET A 108  GLU A 109                    
SITE     4 AC1 17 MET A 111  ASN A 114  SER A 155  ASN A 156                    
SITE     5 AC1 17 LEU A 168                                                     
SITE     1 AC2 16 ILE B  32  GLY B  33  SER B  34  VAL B  40                    
SITE     2 AC2 16 ALA B  53  LYS B  55  MET B 108  GLU B 109                    
SITE     3 AC2 16 MET B 111  ASN B 114  ASP B 151  LYS B 153                    
SITE     4 AC2 16 SER B 155  ASN B 156  LEU B 168  ASP B 169                    
SITE     1 AC3 18 ILE C  32  GLY C  33  SER C  34  GLY C  35                    
SITE     2 AC3 18 GLN C  37  GLY C  38  VAL C  40  ALA C  53                    
SITE     3 AC3 18 LYS C  55  ILE C  86  GLU C 109  MET C 111                    
SITE     4 AC3 18 ASN C 114  SER C 155  ASN C 156  LEU C 168                    
SITE     5 AC3 18 ASP C 169  HOH C2060                                          
SITE     1 AC4 12 ILE D  32  VAL D  40  ALA D  53  MET D 108                    
SITE     2 AC4 12 GLU D 109  MET D 111  ASN D 114  LYS D 153                    
SITE     3 AC4 12 SER D 155  ASN D 156  LEU D 168  HOH D2069                    
SITE     1 AC5  3 SO4 A1366  ARG C 263  ARG D 263                               
SITE     1 AC6  3 ARG B  72  ARG B 150  ARG B 174                               
SITE     1 AC7  4 LYS A  68  ARG A  72  ARG A 150  ARG A 174                    
SITE     1 AC8  2 ARG B  25  LEU B  48                                          
SITE     1 AC9  3 LYS A  30  ARG H  38  ARG H  40                               
SITE     1 BC1  5 ARG A 189  ARG A 192  TYR A 230  HOH A2039                    
SITE     2 BC1  5 THR B 255                                                     
SITE     1 BC2  4 ARG D 174  GLY D 177  THR D 178  SER D 179                    
SITE     1 BC3  2 LYS B 250  ARG B 257                                          
SITE     1 BC4  3 LYS C 153  SER C 155  HOH C2013                               
SITE     1 BC5  6 ARG C 189  ARG C 192  TYR C 230  HOH C2016                    
SITE     2 BC5  6 HOH C2030  THR D 255                                          
SITE     1 BC6  3 ARG C  72  ARG C 150  ARG C 174                               
SITE     1 BC7  6 THR D  65  LYS D  68  ARG D  69  ARG D  72                    
SITE     2 BC7  6 ARG D 150  ARG D 174                                          
SITE     1 BC8  5 THR A 255  HOH A2050  ARG B 189  ARG B 192                    
SITE     2 BC8  5 TYR B 230                                                     
SITE     1 BC9  2 ARG D  25  LEU D  48                                          
SITE     1 CC1  3 ARG A 263  ARG B 263  SO4 C1364                               
SITE     1 CC2  5 GLU A 239  ALA A 267  GLY A 268  TYR A 269                    
SITE     2 CC2  5 ARG D 228                                                     
CRYST1  108.666  180.159  101.144  90.00 110.30  90.00 C 1 2 1      16          
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      0.009203  0.000000  0.003404        0.00000                         
SCALE2      0.000000  0.005551  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010542        0.00000                         
MTRIX1   1  0.775900 -0.111300  0.620900      -53.07000    1                    
MTRIX2   1  0.114700 -0.992800 -0.034660      129.00000    1                    
MTRIX3   1  0.620300 -0.044320  0.783100      175.50000    1                    
MTRIX1   2 -0.775200  0.055400 -0.629300      187.70000    1                    
MTRIX2   2  0.078610 -0.980000 -0.183100      133.40000    1                    
MTRIX3   2 -0.626800 -0.191400  0.755300       81.10000    1                    
MTRIX1   3 -0.999900 -0.000405 -0.016850      130.80000    1                    
MTRIX2   3  0.005495  0.952900  0.303200      -33.88000    1                    
MTRIX3   3  0.015930  0.303300 -0.952800      216.00000    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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