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Database: PDB
Entry: 4KKE
LinkDB: 4KKE
Original site: 4KKE 
HEADER    TRANSFERASE                             06-MAY-13   4KKE              
TITLE     THE CRYSTAL STRUCTURE OF AMP-BOUND JNK3                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 10;                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: MAP KINASE 10, MAPK 10, MAP KINASE P49 3F12, STRESS-        
COMPND   5 ACTIVATED PROTEIN KINASE 1B, SAPK1B, STRESS-ACTIVATED PROTEIN KINASE 
COMPND   6 JNK3, C-JUN N-TERMINAL KINASE 3;                                     
COMPND   7 EC: 2.7.11.24;                                                       
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MAPK10, JNK3, JNK3A, PRKM10, SAPK1B;                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    KINASE DOMAIN, KINASE, C-JUN, TRANSFERASE                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.G.HAN,M.B.SHIM,H.C.AHN                                              
REVDAT   1   21-MAY-14 4KKE    0                                                
JRNL        AUTH   B.G.HAN,M.B.SHIM,H.C.AHN                                     
JRNL        TITL   THE CRYSTAL STRUCTURE OF AMP-BOUND JNK3                      
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.85                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 19776                          
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) : 0.233                           
REMARK   3   R VALUE            (WORKING SET) : 0.230                           
REMARK   3   FREE R VALUE                     : 0.291                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1070                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1372                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.42                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4270                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 85                           
REMARK   3   BIN FREE R VALUE                    : 0.4490                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2877                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 23                                      
REMARK   3   SOLVENT ATOMS            : 94                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 43.23                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.58000                                              
REMARK   3    B22 (A**2) : -1.82000                                             
REMARK   3    B33 (A**2) : -2.76000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.00000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.320         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.254         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.218         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.972         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.939                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.894                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2968 ; 0.007 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2863 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4022 ; 1.157 ; 1.979       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6599 ; 0.742 ; 3.002       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   352 ; 6.383 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   138 ;36.481 ;24.348       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   537 ;15.572 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    17 ;14.198 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   444 ; 0.086 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3284 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   666 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4KKE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAY-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB079448.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-JUN-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.25                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PAL/PLS                            
REMARK 200  BEAMLINE                       : 5C (4A)                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97951                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19776                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.850                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.06                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 16% PEG MME 550, 10% ETHYLENE GLYCOL,    
REMARK 280  0.1 M HEPES, 10 MM TCEP, PH 7.25, VAPOR DIFFUSION, HANGING DROP,    
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       25.98950            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       53.81550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.65550            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       53.81550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.98950            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.65550            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    38                                                      
REMARK 465     GLY A    39                                                      
REMARK 465     SER A    40                                                      
REMARK 465     LYS A    41                                                      
REMARK 465     SER A    42                                                      
REMARK 465     LYS A    43                                                      
REMARK 465     VAL A    44                                                      
REMARK 465     GLY A   215                                                      
REMARK 465     THR A   216                                                      
REMARK 465     SER A   401                                                      
REMARK 465     GLU A   402                                                      
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  55       48.46    -92.33                                   
REMARK 500    ASN A  66       61.36     61.74                                   
REMARK 500    GLN A 140      -52.22   -127.72                                   
REMARK 500    ASP A 162      172.72    -59.97                                   
REMARK 500    ARG A 188       -1.84     73.66                                   
REMARK 500    ASP A 189       34.49   -140.58                                   
REMARK 500    PHE A 263       69.13   -119.57                                   
REMARK 500    ALA A 320       44.00   -154.01                                   
REMARK 500    ILE A 375       78.02     53.69                                   
REMARK 500    ASP A 377      -72.78    -77.50                                   
REMARK 500    LYS A 378       -4.38     74.38                                   
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 AMP A 501                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4KKG   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4KKH   RELATED DB: PDB                                   
DBREF  4KKE A   40   402  UNP    P53779   MK10_HUMAN      40    402             
SEQADV 4KKE MET A   38  UNP  P53779              EXPRESSION TAG                 
SEQADV 4KKE GLY A   39  UNP  P53779              EXPRESSION TAG                 
SEQRES   1 A  365  MET GLY SER LYS SER LYS VAL ASP ASN GLN PHE TYR SER          
SEQRES   2 A  365  VAL GLU VAL GLY ASP SER THR PHE THR VAL LEU LYS ARG          
SEQRES   3 A  365  TYR GLN ASN LEU LYS PRO ILE GLY SER GLY ALA GLN GLY          
SEQRES   4 A  365  ILE VAL CYS ALA ALA TYR ASP ALA VAL LEU ASP ARG ASN          
SEQRES   5 A  365  VAL ALA ILE LYS LYS LEU SER ARG PRO PHE GLN ASN GLN          
SEQRES   6 A  365  THR HIS ALA LYS ARG ALA TYR ARG GLU LEU VAL LEU MET          
SEQRES   7 A  365  LYS CYS VAL ASN HIS LYS ASN ILE ILE SER LEU LEU ASN          
SEQRES   8 A  365  VAL PHE THR PRO GLN LYS THR LEU GLU GLU PHE GLN ASP          
SEQRES   9 A  365  VAL TYR LEU VAL MET GLU LEU MET ASP ALA ASN LEU CYS          
SEQRES  10 A  365  GLN VAL ILE GLN MET GLU LEU ASP HIS GLU ARG MET SER          
SEQRES  11 A  365  TYR LEU LEU TYR GLN MET LEU CYS GLY ILE LYS HIS LEU          
SEQRES  12 A  365  HIS SER ALA GLY ILE ILE HIS ARG ASP LEU LYS PRO SER          
SEQRES  13 A  365  ASN ILE VAL VAL LYS SER ASP CYS THR LEU LYS ILE LEU          
SEQRES  14 A  365  ASP PHE GLY LEU ALA ARG THR ALA GLY THR SER PHE MET          
SEQRES  15 A  365  MET THR PRO TYR VAL VAL THR ARG TYR TYR ARG ALA PRO          
SEQRES  16 A  365  GLU VAL ILE LEU GLY MET GLY TYR LYS GLU ASN VAL ASP          
SEQRES  17 A  365  ILE TRP SER VAL GLY CYS ILE MET GLY GLU MET VAL ARG          
SEQRES  18 A  365  HIS LYS ILE LEU PHE PRO GLY ARG ASP TYR ILE ASP GLN          
SEQRES  19 A  365  TRP ASN LYS VAL ILE GLU GLN LEU GLY THR PRO CYS PRO          
SEQRES  20 A  365  GLU PHE MET LYS LYS LEU GLN PRO THR VAL ARG ASN TYR          
SEQRES  21 A  365  VAL GLU ASN ARG PRO LYS TYR ALA GLY LEU THR PHE PRO          
SEQRES  22 A  365  LYS LEU PHE PRO ASP SER LEU PHE PRO ALA ASP SER GLU          
SEQRES  23 A  365  HIS ASN LYS LEU LYS ALA SER GLN ALA ARG ASP LEU LEU          
SEQRES  24 A  365  SER LYS MET LEU VAL ILE ASP PRO ALA LYS ARG ILE SER          
SEQRES  25 A  365  VAL ASP ASP ALA LEU GLN HIS PRO TYR ILE ASN VAL TRP          
SEQRES  26 A  365  TYR ASP PRO ALA GLU VAL GLU ALA PRO PRO PRO GLN ILE          
SEQRES  27 A  365  TYR ASP LYS GLN LEU ASP GLU ARG GLU HIS THR ILE GLU          
SEQRES  28 A  365  GLU TRP LYS GLU LEU ILE TYR LYS GLU VAL MET ASN SER          
SEQRES  29 A  365  GLU                                                          
HET    AMP  A 501      23                                                       
HETNAM     AMP ADENOSINE MONOPHOSPHATE                                          
FORMUL   2  AMP    C10 H14 N5 O7 P                                              
FORMUL   3  HOH   *94(H2 O)                                                     
HELIX    1   1 PRO A   98  GLN A  100  5                                   3    
HELIX    2   2 ASN A  101  VAL A  118  1                                  18    
HELIX    3   3 LEU A  153  GLN A  158  1                                   6    
HELIX    4   4 ASP A  162  ALA A  183  1                                  22    
HELIX    5   5 LYS A  191  SER A  193  5                                   3    
HELIX    6   6 ALA A  231  LEU A  236  1                                   6    
HELIX    7   7 ASN A  243  HIS A  259  1                                  17    
HELIX    8   8 ASP A  267  GLY A  280  1                                  14    
HELIX    9   9 CYS A  283  LYS A  288  1                                   6    
HELIX   10  10 GLN A  291  ASN A  300  1                                  10    
HELIX   11  11 THR A  308  PHE A  313  1                                   6    
HELIX   12  12 PRO A  314  PHE A  318  5                                   5    
HELIX   13  13 SER A  322  LEU A  340  1                                  19    
HELIX   14  14 SER A  349  GLN A  355  1                                   7    
HELIX   15  15 ILE A  359  TYR A  363  5                                   5    
HELIX   16  16 THR A  386  ASN A  400  1                                  15    
SHEET    1   A 2 PHE A  48  GLU A  52  0                                        
SHEET    2   A 2 THR A  57  LEU A  61 -1  O  PHE A  58   N  VAL A  51           
SHEET    1   B 5 TYR A  64  GLY A  73  0                                        
SHEET    2   B 5 GLY A  76  ASP A  83 -1  O  TYR A  82   N  GLN A  65           
SHEET    3   B 5 ARG A  88  SER A  96 -1  O  VAL A  90   N  ALA A  81           
SHEET    4   B 5 ASP A 141  GLU A 147 -1  O  MET A 146   N  ALA A  91           
SHEET    5   B 5 LEU A 126  PHE A 130 -1  N  LEU A 127   O  VAL A 145           
SHEET    1   C 3 ALA A 151  ASN A 152  0                                        
SHEET    2   C 3 ILE A 195  VAL A 197 -1  O  VAL A 197   N  ALA A 151           
SHEET    3   C 3 LEU A 203  ILE A 205 -1  O  LYS A 204   N  VAL A 196           
SITE     1 AC1 19 ILE A  70  GLY A  71  SER A  72  GLY A  73                    
SITE     2 AC1 19 VAL A  78  ALA A  91  LYS A  93  GLU A 147                    
SITE     3 AC1 19 MET A 149  ASN A 152  SER A 193  ASN A 194                    
SITE     4 AC1 19 LEU A 206  HOH A 607  HOH A 610  HOH A 639                    
SITE     5 AC1 19 HOH A 645  HOH A 646  HOH A 655                               
CRYST1   51.979   71.311  107.631  90.00  90.00  90.00 P 21 21 21    4          
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      0.019239  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014023  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009291        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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