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Database: PDB
Entry: 4J6S
LinkDB: 4J6S
Original site: 4J6S 
HEADER    HYDROLASE                               11-FEB-13   4J6S              
TITLE     14-3-3GAMMA COMPLEXED WITH THE N-TERMINAL SEQUENCE OF TYROSINE        
TITLE    2 HYDROXYLASE (RESIDUES 1-43)                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 14-3-3 PROTEIN GAMMA;                                      
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: PROTEIN KINASE C INHIBITOR PROTEIN 1, KCIP-1, 14-3-3 PROTEIN
COMPND   5 GAMMA, N-TERMINALLY PROCESSED;                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: N-TERMINAL MOTIF OF TYROSINE HYDROXYLASE;                  
COMPND   9 CHAIN: E, F, G, H;                                                   
COMPND  10 SYNONYM: TYROSINE 3-HYDROXYLASE, TH;                                 
COMPND  11 EC: 1.14.16.2;                                                       
COMPND  12 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: YWHAG;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
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    14-3-3 PROTEINS, PEPTIDE BINDING, DOPAMINE SYNTHESIS, SIGNAL          
KEYWDS   2 TRANSDUCTION, REGULATORY PROTEINS, TYROSINE HYDROXYLASE,             
KEYWDS   3 PHOSPHORYLATION, HYDROLASE                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.MILENI,A.MARTINEZ,R.C.STEVENS                                       
REVDAT   4   08-JAN-14 4J6S    1       JRNL                                     
REVDAT   3   20-NOV-13 4J6S    1       JRNL                                     
REVDAT   2   30-OCT-13 4J6S    1       JRNL                                     
REVDAT   1   02-OCT-13 4J6S    0                                                
JRNL        AUTH   A.A.SKJEVIK,M.MILENI,A.BAUMANN,O.HALSKAU,K.TEIGEN,           
JRNL        AUTH 2 R.C.STEVENS,A.MARTINEZ                                       
JRNL        TITL   THE N-TERMINAL SEQUENCE OF TYROSINE HYDROXYLASE IS A         
JRNL        TITL 2 CONFORMATIONALLY VERSATILE MOTIF THAT BINDS 14-3-3 PROTEINS  
JRNL        TITL 3 AND MEMBRANES.                                               
JRNL        REF    J.MOL.BIOL.                   V. 426   150 2014              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   24055376                                                     
JRNL        DOI    10.1016/J.JMB.2013.09.012                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.08 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.08                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.90                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 87.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 20915                          
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) : 0.212                           
REMARK   3   R VALUE            (WORKING SET) : 0.210                           
REMARK   3   FREE R VALUE                     : 0.254                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1100                            
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) : 3.08                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.16                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1565                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 89.86                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2810                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 83                           
REMARK   3   BIN FREE R VALUE                    : 0.3640                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7970                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 68.71                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.07000                                              
REMARK   3    B22 (A**2) : -0.51000                                             
REMARK   3    B33 (A**2) : 0.44000                                              
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.514         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.930                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.899                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8078 ; 0.009 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  7674 ; 0.000 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 10901 ; 1.192 ; 1.971       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 17671 ; 3.587 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   982 ; 5.092 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   413 ;34.465 ;24.915       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1513 ;19.284 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    59 ;14.852 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1220 ; 0.062 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9121 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1778 ; 0.005 ; 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 4J6S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-FEB-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB077667.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-OCT-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.1                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0331                             
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS PACKAGE                        
REMARK 200  DATA SCALING SOFTWARE          : XDS PACKAGE                        
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 111792                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.080                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 87.1                               
REMARK 200  DATA REDUNDANCY                : 5.100                              
REMARK 200  R MERGE                    (I) : 0.11100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.08                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.16                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.49200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.290                              
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 1A4O                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.53                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 2000 MME,        0.1M            
REMARK 280  POTASSIUM THIOCYANATE, PH 7.1, VAPOR DIFFUSION, TEMPERATURE 283.0K  
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       42.09500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       68.45000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       57.56000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       68.45000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       42.09500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       57.56000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1140 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13440 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1080 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, F                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1230 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13510 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, G                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1170 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13710 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, H                                  
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    -7                                                      
REMARK 465     SER A    -6                                                      
REMARK 465     ARG A    -5                                                      
REMARK 465     ARG A    -4                                                      
REMARK 465     ALA A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     VAL A    -1                                                      
REMARK 465     GLN A   237                                                      
REMARK 465     GLN A   238                                                      
REMARK 465     ASP A   239                                                      
REMARK 465     ASP A   240                                                      
REMARK 465     ASP A   241                                                      
REMARK 465     GLY A   242                                                      
REMARK 465     GLY A   243                                                      
REMARK 465     GLU A   244                                                      
REMARK 465     GLY A   245                                                      
REMARK 465     ASN A   246                                                      
REMARK 465     ASN A   247                                                      
REMARK 465     MET B    -7                                                      
REMARK 465     SER B    -6                                                      
REMARK 465     ARG B    -5                                                      
REMARK 465     ARG B    -4                                                      
REMARK 465     ASP B   240                                                      
REMARK 465     ASP B   241                                                      
REMARK 465     GLY B   242                                                      
REMARK 465     GLY B   243                                                      
REMARK 465     GLU B   244                                                      
REMARK 465     GLY B   245                                                      
REMARK 465     ASN B   246                                                      
REMARK 465     ASN B   247                                                      
REMARK 465     MET C    -7                                                      
REMARK 465     SER C    -6                                                      
REMARK 465     ARG C    -5                                                      
REMARK 465     ARG C    -4                                                      
REMARK 465     ALA C    -3                                                      
REMARK 465     SER C    -2                                                      
REMARK 465     VAL C    -1                                                      
REMARK 465     ASP C   236                                                      
REMARK 465     GLN C   237                                                      
REMARK 465     GLN C   238                                                      
REMARK 465     ASP C   239                                                      
REMARK 465     ASP C   240                                                      
REMARK 465     ASP C   241                                                      
REMARK 465     GLY C   242                                                      
REMARK 465     GLY C   243                                                      
REMARK 465     GLU C   244                                                      
REMARK 465     GLY C   245                                                      
REMARK 465     ASN C   246                                                      
REMARK 465     ASN C   247                                                      
REMARK 465     MET D    -7                                                      
REMARK 465     SER D    -6                                                      
REMARK 465     ARG D    -5                                                      
REMARK 465     ARG D    -4                                                      
REMARK 465     GLN D   237                                                      
REMARK 465     GLN D   238                                                      
REMARK 465     ASP D   239                                                      
REMARK 465     ASP D   240                                                      
REMARK 465     ASP D   241                                                      
REMARK 465     GLY D   242                                                      
REMARK 465     GLY D   243                                                      
REMARK 465     GLU D   244                                                      
REMARK 465     GLY D   245                                                      
REMARK 465     ASN D   246                                                      
REMARK 465     ASN D   247                                                      
REMARK 465     MET E   487                                                      
REMARK 465     PRO E   488                                                      
REMARK 465     THR E   489                                                      
REMARK 465     PRO E   490                                                      
REMARK 465     ASP E   491                                                      
REMARK 465     ALA E   492                                                      
REMARK 465     THR E   493                                                      
REMARK 465     THR E   494                                                      
REMARK 465     PRO E   495                                                      
REMARK 465     GLN E   496                                                      
REMARK 465     ALA E   497                                                      
REMARK 465     LYS E   498                                                      
REMARK 465     GLY E   499                                                      
REMARK 465     PHE E   500                                                      
REMARK 465     ARG E   501                                                      
REMARK 465     ALA E   509                                                      
REMARK 465     LYS E   510                                                      
REMARK 465     GLN E   511                                                      
REMARK 465     ALA E   512                                                      
REMARK 465     GLU E   513                                                      
REMARK 465     ALA E   514                                                      
REMARK 465     ILE E   515                                                      
REMARK 465     MET E   516                                                      
REMARK 465     SER E   517                                                      
REMARK 465     PRO E   518                                                      
REMARK 465     ARG E   519                                                      
REMARK 465     PHE E   520                                                      
REMARK 465     ILE E   521                                                      
REMARK 465     GLY E   522                                                      
REMARK 465     ARG E   523                                                      
REMARK 465     ARG E   524                                                      
REMARK 465     GLN E   525                                                      
REMARK 465     SER E   526                                                      
REMARK 465     LEU E   527                                                      
REMARK 465     ILE E   528                                                      
REMARK 465     GLU E   529                                                      
REMARK 465     MET F   487                                                      
REMARK 465     PRO F   488                                                      
REMARK 465     THR F   489                                                      
REMARK 465     PRO F   490                                                      
REMARK 465     ASP F   491                                                      
REMARK 465     ALA F   492                                                      
REMARK 465     THR F   493                                                      
REMARK 465     THR F   494                                                      
REMARK 465     PRO F   495                                                      
REMARK 465     GLN F   496                                                      
REMARK 465     ALA F   497                                                      
REMARK 465     LYS F   498                                                      
REMARK 465     GLY F   499                                                      
REMARK 465     PHE F   500                                                      
REMARK 465     LYS F   510                                                      
REMARK 465     GLN F   511                                                      
REMARK 465     ALA F   512                                                      
REMARK 465     GLU F   513                                                      
REMARK 465     ALA F   514                                                      
REMARK 465     ILE F   515                                                      
REMARK 465     MET F   516                                                      
REMARK 465     SER F   517                                                      
REMARK 465     PRO F   518                                                      
REMARK 465     ARG F   519                                                      
REMARK 465     PHE F   520                                                      
REMARK 465     ILE F   521                                                      
REMARK 465     GLY F   522                                                      
REMARK 465     ARG F   523                                                      
REMARK 465     ARG F   524                                                      
REMARK 465     GLN F   525                                                      
REMARK 465     SER F   526                                                      
REMARK 465     LEU F   527                                                      
REMARK 465     ILE F   528                                                      
REMARK 465     GLU F   529                                                      
REMARK 465     MET G   487                                                      
REMARK 465     PRO G   488                                                      
REMARK 465     THR G   489                                                      
REMARK 465     PRO G   490                                                      
REMARK 465     ASP G   491                                                      
REMARK 465     ALA G   492                                                      
REMARK 465     THR G   493                                                      
REMARK 465     THR G   494                                                      
REMARK 465     PRO G   495                                                      
REMARK 465     GLN G   496                                                      
REMARK 465     ALA G   497                                                      
REMARK 465     LYS G   498                                                      
REMARK 465     GLY G   499                                                      
REMARK 465     PHE G   500                                                      
REMARK 465     LYS G   510                                                      
REMARK 465     GLN G   511                                                      
REMARK 465     ALA G   512                                                      
REMARK 465     GLU G   513                                                      
REMARK 465     ALA G   514                                                      
REMARK 465     ILE G   515                                                      
REMARK 465     MET G   516                                                      
REMARK 465     SER G   517                                                      
REMARK 465     PRO G   518                                                      
REMARK 465     ARG G   519                                                      
REMARK 465     PHE G   520                                                      
REMARK 465     ILE G   521                                                      
REMARK 465     GLY G   522                                                      
REMARK 465     ARG G   523                                                      
REMARK 465     ARG G   524                                                      
REMARK 465     GLN G   525                                                      
REMARK 465     SER G   526                                                      
REMARK 465     LEU G   527                                                      
REMARK 465     ILE G   528                                                      
REMARK 465     GLU G   529                                                      
REMARK 465     MET H   487                                                      
REMARK 465     PRO H   488                                                      
REMARK 465     THR H   489                                                      
REMARK 465     PRO H   490                                                      
REMARK 465     ASP H   491                                                      
REMARK 465     ALA H   492                                                      
REMARK 465     THR H   493                                                      
REMARK 465     THR H   494                                                      
REMARK 465     PRO H   495                                                      
REMARK 465     GLN H   496                                                      
REMARK 465     ALA H   497                                                      
REMARK 465     LYS H   498                                                      
REMARK 465     GLY H   499                                                      
REMARK 465     PHE H   500                                                      
REMARK 465     LYS H   510                                                      
REMARK 465     GLN H   511                                                      
REMARK 465     ALA H   512                                                      
REMARK 465     GLU H   513                                                      
REMARK 465     ALA H   514                                                      
REMARK 465     ILE H   515                                                      
REMARK 465     MET H   516                                                      
REMARK 465     SER H   517                                                      
REMARK 465     PRO H   518                                                      
REMARK 465     ARG H   519                                                      
REMARK 465     PHE H   520                                                      
REMARK 465     ILE H   521                                                      
REMARK 465     GLY H   522                                                      
REMARK 465     ARG H   523                                                      
REMARK 465     ARG H   524                                                      
REMARK 465     GLN H   525                                                      
REMARK 465     SER H   526                                                      
REMARK 465     LEU H   527                                                      
REMARK 465     ILE H   528                                                      
REMARK 465     GLU H   529                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A  19       75.55   -113.98                                   
REMARK 500    TYR A 107      -61.73   -128.41                                   
REMARK 500    THR A 210       55.29   -111.44                                   
REMARK 500    THR A 234       55.98    -99.84                                   
REMARK 500    SER A 235       63.36   -150.01                                   
REMARK 500    SER B  -2       77.06   -176.30                                   
REMARK 500    VAL B  -1       27.78     39.98                                   
REMARK 500    ARG B  19       77.93   -111.33                                   
REMARK 500    TYR B 107      -63.80   -129.70                                   
REMARK 500    THR B 210       56.24   -111.72                                   
REMARK 500    ASP B 236       51.81   -151.43                                   
REMARK 500    GLN B 238      103.75    -43.87                                   
REMARK 500    ARG C  19       77.61   -112.80                                   
REMARK 500    TYR C 107      -61.21   -127.81                                   
REMARK 500    THR C 210       56.93   -111.02                                   
REMARK 500    THR C 234       46.82   -102.91                                   
REMARK 500    VAL D   2       18.07   -149.31                                   
REMARK 500    ARG D  19       78.23   -109.77                                   
REMARK 500    TYR D 107      -62.80   -129.67                                   
REMARK 500    THR D 210       55.69   -112.13                                   
REMARK 500    SEP E 505     -159.31   -111.99                                   
REMARK 500    LEU E 507       79.92   -116.62                                   
REMARK 500    ASP F 508      -86.11   -153.55                                   
REMARK 500    GLU G 506      139.58    -37.78                                   
REMARK 500    ARG H 502      157.57    170.62                                   
REMARK 500    LEU H 507     -163.68   -102.83                                   
REMARK 500    ASP H 508      -73.31   -128.58                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE CRYSTALLIZED SEQUENCE CORRESPONDING TO TYROSINE 3-MONOOXYGENASE  
REMARK 999 REPRESENTS THE SPLICING-ISOFORM TH1. THIS FORM IS THE MOST ABUNDANT  
REMARK 999 IN BRAIN AND IS THE ONE USED FOR THE CURRENT WORK. THE CLOSEST       
REMARK 999 DATABASE REFERENCE ACCESSION CODE IS THE UNPROT ENTRY P07101-3       
DBREF  4J6S A   -7   247  UNP    P61981   1433G_HUMAN      1    247             
DBREF  4J6S B   -7   247  UNP    P61981   1433G_HUMAN      1    247             
DBREF  4J6S C   -7   247  UNP    P61981   1433G_HUMAN      1    247             
DBREF  4J6S D   -7   247  UNP    P61981   1433G_HUMAN      1    247             
DBREF  4J6S E  487   529  PDB    4J6S     4J6S           487    529             
DBREF  4J6S F  487   529  PDB    4J6S     4J6S           487    529             
DBREF  4J6S G  487   529  PDB    4J6S     4J6S           487    529             
DBREF  4J6S H  487   529  PDB    4J6S     4J6S           487    529             
SEQADV 4J6S SER A   -6  UNP  P61981              EXPRESSION TAG                 
SEQADV 4J6S ARG A   -5  UNP  P61981              EXPRESSION TAG                 
SEQADV 4J6S ARG A   -4  UNP  P61981              EXPRESSION TAG                 
SEQADV 4J6S ALA A   -3  UNP  P61981              EXPRESSION TAG                 
SEQADV 4J6S SER A   -2  UNP  P61981              EXPRESSION TAG                 
SEQADV 4J6S VAL A   -1  UNP  P61981              EXPRESSION TAG                 
SEQADV 4J6S GLY A    0  UNP  P61981              EXPRESSION TAG                 
SEQADV 4J6S LEU A    1  UNP  P61981              EXPRESSION TAG                 
SEQADV 4J6S SER B   -6  UNP  P61981              EXPRESSION TAG                 
SEQADV 4J6S ARG B   -5  UNP  P61981              EXPRESSION TAG                 
SEQADV 4J6S ARG B   -4  UNP  P61981              EXPRESSION TAG                 
SEQADV 4J6S ALA B   -3  UNP  P61981              EXPRESSION TAG                 
SEQADV 4J6S SER B   -2  UNP  P61981              EXPRESSION TAG                 
SEQADV 4J6S VAL B   -1  UNP  P61981              EXPRESSION TAG                 
SEQADV 4J6S GLY B    0  UNP  P61981              EXPRESSION TAG                 
SEQADV 4J6S LEU B    1  UNP  P61981              EXPRESSION TAG                 
SEQADV 4J6S SER C   -6  UNP  P61981              EXPRESSION TAG                 
SEQADV 4J6S ARG C   -5  UNP  P61981              EXPRESSION TAG                 
SEQADV 4J6S ARG C   -4  UNP  P61981              EXPRESSION TAG                 
SEQADV 4J6S ALA C   -3  UNP  P61981              EXPRESSION TAG                 
SEQADV 4J6S SER C   -2  UNP  P61981              EXPRESSION TAG                 
SEQADV 4J6S VAL C   -1  UNP  P61981              EXPRESSION TAG                 
SEQADV 4J6S GLY C    0  UNP  P61981              EXPRESSION TAG                 
SEQADV 4J6S LEU C    1  UNP  P61981              EXPRESSION TAG                 
SEQADV 4J6S SER D   -6  UNP  P61981              EXPRESSION TAG                 
SEQADV 4J6S ARG D   -5  UNP  P61981              EXPRESSION TAG                 
SEQADV 4J6S ARG D   -4  UNP  P61981              EXPRESSION TAG                 
SEQADV 4J6S ALA D   -3  UNP  P61981              EXPRESSION TAG                 
SEQADV 4J6S SER D   -2  UNP  P61981              EXPRESSION TAG                 
SEQADV 4J6S VAL D   -1  UNP  P61981              EXPRESSION TAG                 
SEQADV 4J6S GLY D    0  UNP  P61981              EXPRESSION TAG                 
SEQADV 4J6S LEU D    1  UNP  P61981              EXPRESSION TAG                 
SEQRES   1 A  255  MET SER ARG ARG ALA SER VAL GLY LEU VAL ASP ARG GLU          
SEQRES   2 A  255  GLN LEU VAL GLN LYS ALA ARG LEU ALA GLU GLN ALA GLU          
SEQRES   3 A  255  ARG TYR ASP ASP MET ALA ALA ALA MET LYS ASN VAL THR          
SEQRES   4 A  255  GLU LEU ASN GLU PRO LEU SER ASN GLU GLU ARG ASN LEU          
SEQRES   5 A  255  LEU SER VAL ALA TYR LYS ASN VAL VAL GLY ALA ARG ARG          
SEQRES   6 A  255  SER SER TRP ARG VAL ILE SER SER ILE GLU GLN LYS THR          
SEQRES   7 A  255  SER ALA ASP GLY ASN GLU LYS LYS ILE GLU MET VAL ARG          
SEQRES   8 A  255  ALA TYR ARG GLU LYS ILE GLU LYS GLU LEU GLU ALA VAL          
SEQRES   9 A  255  CYS GLN ASP VAL LEU SER LEU LEU ASP ASN TYR LEU ILE          
SEQRES  10 A  255  LYS ASN CYS SER GLU THR GLN TYR GLU SER LYS VAL PHE          
SEQRES  11 A  255  TYR LEU LYS MET LYS GLY ASP TYR TYR ARG TYR LEU ALA          
SEQRES  12 A  255  GLU VAL ALA THR GLY GLU LYS ARG ALA THR VAL VAL GLU          
SEQRES  13 A  255  SER SER GLU LYS ALA TYR SER GLU ALA HIS GLU ILE SER          
SEQRES  14 A  255  LYS GLU HIS MET GLN PRO THR HIS PRO ILE ARG LEU GLY          
SEQRES  15 A  255  LEU ALA LEU ASN TYR SER VAL PHE TYR TYR GLU ILE GLN          
SEQRES  16 A  255  ASN ALA PRO GLU GLN ALA CYS HIS LEU ALA LYS THR ALA          
SEQRES  17 A  255  PHE ASP ASP ALA ILE ALA GLU LEU ASP THR LEU ASN GLU          
SEQRES  18 A  255  ASP SER TYR LYS ASP SER THR LEU ILE MET GLN LEU LEU          
SEQRES  19 A  255  ARG ASP ASN LEU THR LEU TRP THR SER ASP GLN GLN ASP          
SEQRES  20 A  255  ASP ASP GLY GLY GLU GLY ASN ASN                              
SEQRES   1 B  255  MET SER ARG ARG ALA SER VAL GLY LEU VAL ASP ARG GLU          
SEQRES   2 B  255  GLN LEU VAL GLN LYS ALA ARG LEU ALA GLU GLN ALA GLU          
SEQRES   3 B  255  ARG TYR ASP ASP MET ALA ALA ALA MET LYS ASN VAL THR          
SEQRES   4 B  255  GLU LEU ASN GLU PRO LEU SER ASN GLU GLU ARG ASN LEU          
SEQRES   5 B  255  LEU SER VAL ALA TYR LYS ASN VAL VAL GLY ALA ARG ARG          
SEQRES   6 B  255  SER SER TRP ARG VAL ILE SER SER ILE GLU GLN LYS THR          
SEQRES   7 B  255  SER ALA ASP GLY ASN GLU LYS LYS ILE GLU MET VAL ARG          
SEQRES   8 B  255  ALA TYR ARG GLU LYS ILE GLU LYS GLU LEU GLU ALA VAL          
SEQRES   9 B  255  CYS GLN ASP VAL LEU SER LEU LEU ASP ASN TYR LEU ILE          
SEQRES  10 B  255  LYS ASN CYS SER GLU THR GLN TYR GLU SER LYS VAL PHE          
SEQRES  11 B  255  TYR LEU LYS MET LYS GLY ASP TYR TYR ARG TYR LEU ALA          
SEQRES  12 B  255  GLU VAL ALA THR GLY GLU LYS ARG ALA THR VAL VAL GLU          
SEQRES  13 B  255  SER SER GLU LYS ALA TYR SER GLU ALA HIS GLU ILE SER          
SEQRES  14 B  255  LYS GLU HIS MET GLN PRO THR HIS PRO ILE ARG LEU GLY          
SEQRES  15 B  255  LEU ALA LEU ASN TYR SER VAL PHE TYR TYR GLU ILE GLN          
SEQRES  16 B  255  ASN ALA PRO GLU GLN ALA CYS HIS LEU ALA LYS THR ALA          
SEQRES  17 B  255  PHE ASP ASP ALA ILE ALA GLU LEU ASP THR LEU ASN GLU          
SEQRES  18 B  255  ASP SER TYR LYS ASP SER THR LEU ILE MET GLN LEU LEU          
SEQRES  19 B  255  ARG ASP ASN LEU THR LEU TRP THR SER ASP GLN GLN ASP          
SEQRES  20 B  255  ASP ASP GLY GLY GLU GLY ASN ASN                              
SEQRES   1 C  255  MET SER ARG ARG ALA SER VAL GLY LEU VAL ASP ARG GLU          
SEQRES   2 C  255  GLN LEU VAL GLN LYS ALA ARG LEU ALA GLU GLN ALA GLU          
SEQRES   3 C  255  ARG TYR ASP ASP MET ALA ALA ALA MET LYS ASN VAL THR          
SEQRES   4 C  255  GLU LEU ASN GLU PRO LEU SER ASN GLU GLU ARG ASN LEU          
SEQRES   5 C  255  LEU SER VAL ALA TYR LYS ASN VAL VAL GLY ALA ARG ARG          
SEQRES   6 C  255  SER SER TRP ARG VAL ILE SER SER ILE GLU GLN LYS THR          
SEQRES   7 C  255  SER ALA ASP GLY ASN GLU LYS LYS ILE GLU MET VAL ARG          
SEQRES   8 C  255  ALA TYR ARG GLU LYS ILE GLU LYS GLU LEU GLU ALA VAL          
SEQRES   9 C  255  CYS GLN ASP VAL LEU SER LEU LEU ASP ASN TYR LEU ILE          
SEQRES  10 C  255  LYS ASN CYS SER GLU THR GLN TYR GLU SER LYS VAL PHE          
SEQRES  11 C  255  TYR LEU LYS MET LYS GLY ASP TYR TYR ARG TYR LEU ALA          
SEQRES  12 C  255  GLU VAL ALA THR GLY GLU LYS ARG ALA THR VAL VAL GLU          
SEQRES  13 C  255  SER SER GLU LYS ALA TYR SER GLU ALA HIS GLU ILE SER          
SEQRES  14 C  255  LYS GLU HIS MET GLN PRO THR HIS PRO ILE ARG LEU GLY          
SEQRES  15 C  255  LEU ALA LEU ASN TYR SER VAL PHE TYR TYR GLU ILE GLN          
SEQRES  16 C  255  ASN ALA PRO GLU GLN ALA CYS HIS LEU ALA LYS THR ALA          
SEQRES  17 C  255  PHE ASP ASP ALA ILE ALA GLU LEU ASP THR LEU ASN GLU          
SEQRES  18 C  255  ASP SER TYR LYS ASP SER THR LEU ILE MET GLN LEU LEU          
SEQRES  19 C  255  ARG ASP ASN LEU THR LEU TRP THR SER ASP GLN GLN ASP          
SEQRES  20 C  255  ASP ASP GLY GLY GLU GLY ASN ASN                              
SEQRES   1 D  255  MET SER ARG ARG ALA SER VAL GLY LEU VAL ASP ARG GLU          
SEQRES   2 D  255  GLN LEU VAL GLN LYS ALA ARG LEU ALA GLU GLN ALA GLU          
SEQRES   3 D  255  ARG TYR ASP ASP MET ALA ALA ALA MET LYS ASN VAL THR          
SEQRES   4 D  255  GLU LEU ASN GLU PRO LEU SER ASN GLU GLU ARG ASN LEU          
SEQRES   5 D  255  LEU SER VAL ALA TYR LYS ASN VAL VAL GLY ALA ARG ARG          
SEQRES   6 D  255  SER SER TRP ARG VAL ILE SER SER ILE GLU GLN LYS THR          
SEQRES   7 D  255  SER ALA ASP GLY ASN GLU LYS LYS ILE GLU MET VAL ARG          
SEQRES   8 D  255  ALA TYR ARG GLU LYS ILE GLU LYS GLU LEU GLU ALA VAL          
SEQRES   9 D  255  CYS GLN ASP VAL LEU SER LEU LEU ASP ASN TYR LEU ILE          
SEQRES  10 D  255  LYS ASN CYS SER GLU THR GLN TYR GLU SER LYS VAL PHE          
SEQRES  11 D  255  TYR LEU LYS MET LYS GLY ASP TYR TYR ARG TYR LEU ALA          
SEQRES  12 D  255  GLU VAL ALA THR GLY GLU LYS ARG ALA THR VAL VAL GLU          
SEQRES  13 D  255  SER SER GLU LYS ALA TYR SER GLU ALA HIS GLU ILE SER          
SEQRES  14 D  255  LYS GLU HIS MET GLN PRO THR HIS PRO ILE ARG LEU GLY          
SEQRES  15 D  255  LEU ALA LEU ASN TYR SER VAL PHE TYR TYR GLU ILE GLN          
SEQRES  16 D  255  ASN ALA PRO GLU GLN ALA CYS HIS LEU ALA LYS THR ALA          
SEQRES  17 D  255  PHE ASP ASP ALA ILE ALA GLU LEU ASP THR LEU ASN GLU          
SEQRES  18 D  255  ASP SER TYR LYS ASP SER THR LEU ILE MET GLN LEU LEU          
SEQRES  19 D  255  ARG ASP ASN LEU THR LEU TRP THR SER ASP GLN GLN ASP          
SEQRES  20 D  255  ASP ASP GLY GLY GLU GLY ASN ASN                              
SEQRES   1 E   43  MET PRO THR PRO ASP ALA THR THR PRO GLN ALA LYS GLY          
SEQRES   2 E   43  PHE ARG ARG ALA VAL SEP GLU LEU ASP ALA LYS GLN ALA          
SEQRES   3 E   43  GLU ALA ILE MET SER PRO ARG PHE ILE GLY ARG ARG GLN          
SEQRES   4 E   43  SER LEU ILE GLU                                              
SEQRES   1 F   43  MET PRO THR PRO ASP ALA THR THR PRO GLN ALA LYS GLY          
SEQRES   2 F   43  PHE ARG ARG ALA VAL SEP GLU LEU ASP ALA LYS GLN ALA          
SEQRES   3 F   43  GLU ALA ILE MET SER PRO ARG PHE ILE GLY ARG ARG GLN          
SEQRES   4 F   43  SER LEU ILE GLU                                              
SEQRES   1 G   43  MET PRO THR PRO ASP ALA THR THR PRO GLN ALA LYS GLY          
SEQRES   2 G   43  PHE ARG ARG ALA VAL SEP GLU LEU ASP ALA LYS GLN ALA          
SEQRES   3 G   43  GLU ALA ILE MET SER PRO ARG PHE ILE GLY ARG ARG GLN          
SEQRES   4 G   43  SER LEU ILE GLU                                              
SEQRES   1 H   43  MET PRO THR PRO ASP ALA THR THR PRO GLN ALA LYS GLY          
SEQRES   2 H   43  PHE ARG ARG ALA VAL SEP GLU LEU ASP ALA LYS GLN ALA          
SEQRES   3 H   43  GLU ALA ILE MET SER PRO ARG PHE ILE GLY ARG ARG GLN          
SEQRES   4 H   43  SER LEU ILE GLU                                              
MODRES 4J6S SEP E  505  SER  PHOSPHOSERINE                                      
MODRES 4J6S SEP F  505  SER  PHOSPHOSERINE                                      
MODRES 4J6S SEP G  505  SER  PHOSPHOSERINE                                      
MODRES 4J6S SEP H  505  SER  PHOSPHOSERINE                                      
HET    SEP  E 505      10                                                       
HET    SEP  F 505      10                                                       
HET    SEP  G 505      10                                                       
HET    SEP  H 505      10                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETSYN     SEP PHOSPHONOSERINE                                                  
FORMUL   5  SEP    4(C3 H8 N O6 P)                                              
HELIX    1   1 ASP A    3  ALA A   17  1                                  15    
HELIX    2   2 ARG A   19  LEU A   33  1                                  15    
HELIX    3   3 SER A   38  GLY A   74  1                                  37    
HELIX    4   4 ASN A   75  TYR A  107  1                                  33    
HELIX    5   5 GLN A  116  ALA A  138  1                                  23    
HELIX    6   6 GLY A  140  MET A  165  1                                  26    
HELIX    7   7 HIS A  169  ILE A  186  1                                  18    
HELIX    8   8 ALA A  189  GLU A  207  1                                  19    
HELIX    9   9 LEU A  208  LEU A  211  5                                   4    
HELIX   10  10 ASN A  212  THR A  234  1                                  23    
HELIX   11  11 ASP B    3  ALA B   17  1                                  15    
HELIX   12  12 ARG B   19  LEU B   33  1                                  15    
HELIX   13  13 SER B   38  GLY B   74  1                                  37    
HELIX   14  14 ASN B   75  TYR B  107  1                                  33    
HELIX   15  15 GLN B  116  ALA B  138  1                                  23    
HELIX   16  16 THR B  139  MET B  165  1                                  27    
HELIX   17  17 HIS B  169  ILE B  186  1                                  18    
HELIX   18  18 ALA B  189  GLU B  207  1                                  19    
HELIX   19  19 LEU B  208  LEU B  211  5                                   4    
HELIX   20  20 ASN B  212  THR B  234  1                                  23    
HELIX   21  21 ASP C    3  ALA C   17  1                                  15    
HELIX   22  22 ARG C   19  LEU C   33  1                                  15    
HELIX   23  23 SER C   38  ASP C   73  1                                  36    
HELIX   24  24 ASN C   75  TYR C  107  1                                  33    
HELIX   25  25 GLN C  116  GLU C  136  1                                  21    
HELIX   26  26 THR C  139  MET C  165  1                                  27    
HELIX   27  27 HIS C  169  ILE C  186  1                                  18    
HELIX   28  28 ALA C  189  GLU C  207  1                                  19    
HELIX   29  29 LEU C  208  LEU C  211  5                                   4    
HELIX   30  30 ASN C  212  THR C  234  1                                  23    
HELIX   31  31 ASP D    3  ALA D   17  1                                  15    
HELIX   32  32 ARG D   19  LEU D   33  1                                  15    
HELIX   33  33 SER D   38  GLY D   74  1                                  37    
HELIX   34  34 ASN D   75  TYR D  107  1                                  33    
HELIX   35  35 GLN D  116  GLU D  136  1                                  21    
HELIX   36  36 THR D  139  MET D  165  1                                  27    
HELIX   37  37 HIS D  169  ILE D  186  1                                  18    
HELIX   38  38 ALA D  189  GLU D  207  1                                  19    
HELIX   39  39 LEU D  208  LEU D  211  5                                   4    
HELIX   40  40 ASN D  212  THR D  234  1                                  23    
LINK         C   VAL E 504                 N   SEP E 505     1555   1555  1.34  
LINK         C   SEP E 505                 N   GLU E 506     1555   1555  1.33  
LINK         C   VAL F 504                 N   SEP F 505     1555   1555  1.33  
LINK         C   SEP F 505                 N   GLU F 506     1555   1555  1.33  
LINK         C   VAL G 504                 N   SEP G 505     1555   1555  1.34  
LINK         C   SEP G 505                 N   GLU G 506     1555   1555  1.33  
LINK         C   VAL H 504                 N   SEP H 505     1555   1555  1.32  
LINK         C   SEP H 505                 N   GLU H 506     1555   1555  1.33  
CRYST1   84.190  115.120  136.900  90.00  90.00  90.00 P 21 21 21   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      0.011878  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008687  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007305        0.00000                         
MTRIX1   1  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2   1  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3   1  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1   2  0.969915 -0.173886  0.170376        2.45011    1                    
MTRIX2   2 -0.169959 -0.984738 -0.037484       -5.52172    1                    
MTRIX3   2  0.174294  0.007400 -0.984666      -28.90455    1                    
MTRIX1   3 -0.991492 -0.038446 -0.124363      -47.99815    1                    
MTRIX2   3 -0.113003 -0.219996  0.968933        5.62040    1                    
MTRIX3   3 -0.064611  0.974743  0.213780       -8.37577    1                    
MTRIX1   4 -0.966844  0.142667 -0.211800      -46.93277    1                    
MTRIX2   4  0.238886  0.212140 -0.947592       -3.89462    1                    
MTRIX3   4 -0.090259 -0.966769 -0.239187      -28.48492    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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