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Database: PDB
Entry: 5UUT
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Original site: 5UUT 
HEADER    TRANSFERASE                             17-FEB-17   5UUT              
TITLE     N-MYRISTOYLTRANSFERASE 1 (NMT) BOUND TO MYRISTOYL-COA                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLYCYLPEPTIDE N-TETRADECANOYLTRANSFERASE 1;                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 29-416;                                       
COMPND   5 SYNONYM: MYRISTOYL-COA:PROTEIN N-MYRISTOYLTRANSFERASE 1,TYPE I N-    
COMPND   6 MYRISTOYLTRANSFERASE,PEPTIDE N-MYRISTOYLTRANSFERASE 1;               
COMPND   7 EC: 2.3.1.97;                                                        
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: NMT1, NMT;                                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    MYRISTOYLATION, MYRISTOYL-COA, CANCER, CO/POST-TRANSLATIONAL          
KEYWDS   2 MODIFICATION, TRANSFERASE                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    O.GOODWIN,S.PEGAN                                                     
REVDAT   2   30-JAN-19 5UUT    1       JRNL                                     
REVDAT   1   17-JAN-18 5UUT    0                                                
JRNL        AUTH   S.KIM,O.A.ALSAIDAN,O.GOODWIN,Q.LI,E.SULEJMANI,Z.HAN,A.BAI,   
JRNL        AUTH 2 T.ALBERS,Z.BEHARRY,Y.G.ZHENG,J.S.NORRIS,Z.M.SZULC,           
JRNL        AUTH 3 A.BIELAWSKA,I.LEBEDYEVA,S.D.PEGAN,H.CAI                      
JRNL        TITL   BLOCKING MYRISTOYLATION OF SRC INHIBITS ITS KINASE ACTIVITY  
JRNL        TITL 2 AND SUPPRESSES PROSTATE CANCER PROGRESSION.                  
JRNL        REF    CANCER RES.                   V.  77  6950 2017              
JRNL        REFN                   ESSN 1538-7445                               
JRNL        PMID   29038344                                                     
JRNL        DOI    10.1158/0008-5472.CAN-17-0981                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10.1_2155: ???)                            
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.45                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 39222                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.173                           
REMARK   3   R VALUE            (WORKING SET) : 0.171                           
REMARK   3   FREE R VALUE                     : 0.221                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.940                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1937                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 38.4600 -  5.4220    0.99     2876   162  0.1699 0.1883        
REMARK   3     2  5.4220 -  4.3055    1.00     2767   138  0.1323 0.1801        
REMARK   3     3  4.3055 -  3.7618    1.00     2722   139  0.1409 0.1753        
REMARK   3     4  3.7618 -  3.4181    1.00     2710   139  0.1620 0.1960        
REMARK   3     5  3.4181 -  3.1732    1.00     2689   145  0.1774 0.2422        
REMARK   3     6  3.1732 -  2.9862    1.00     2699   141  0.1912 0.2636        
REMARK   3     7  2.9862 -  2.8367    1.00     2677   137  0.2023 0.2798        
REMARK   3     8  2.8367 -  2.7132    1.00     2663   130  0.2114 0.2545        
REMARK   3     9  2.7132 -  2.6088    1.00     2702   137  0.2075 0.2760        
REMARK   3    10  2.6088 -  2.5188    1.00     2629   152  0.1938 0.2640        
REMARK   3    11  2.5188 -  2.4401    1.00     2651   136  0.1981 0.2825        
REMARK   3    12  2.4401 -  2.3703    1.00     2678   137  0.1942 0.2649        
REMARK   3    13  2.3703 -  2.3079    0.99     2643   136  0.2010 0.3296        
REMARK   3    14  2.3079 -  2.2516    0.83     2179   108  0.2033 0.2621        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.240            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.310           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008           6560                                  
REMARK   3   ANGLE     :  1.010           8932                                  
REMARK   3   CHIRALITY :  0.060            963                                  
REMARK   3   PLANARITY :  0.008           1123                                  
REMARK   3   DIHEDRAL  : 16.268           3922                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5UUT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000226499.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-JUN-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX300-HS                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39222                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.250                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 4.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.0900                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.41                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 22.5% PEG 4000, 5 MM NICL2, 100 MM       
REMARK 280  SODIUM CITRATE PH 4.5, AND 2.5% GLYCEROL, VAPOR DIFFUSION,          
REMARK 280  HANGING DROP, TEMPERATURE 293K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       39.38900            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       88.79100            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.38900            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       88.79100            
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                                                    
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: B                                     
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     GLY A   106                                                      
REMARK 465     PRO A   107                                                      
REMARK 465     HIS A   108                                                      
REMARK 465     MET A   109                                                      
REMARK 465     GLU A   110                                                      
REMARK 465     GLU A   111                                                      
REMARK 465     ALA A   112                                                      
REMARK 465     SER A   113                                                      
REMARK 465     LYS A   114                                                      
REMARK 465     ARG A   316                                                      
REMARK 465     ASN A   317                                                      
REMARK 465     MET A   408                                                      
REMARK 465     ASN A   409                                                      
REMARK 465     HIS A   410                                                      
REMARK 465     PRO A   411                                                      
REMARK 465     THR A   412                                                      
REMARK 465     HIS A   413                                                      
REMARK 465     LYS A   414                                                      
REMARK 465     GLY B   106                                                      
REMARK 465     PRO B   107                                                      
REMARK 465     HIS B   108                                                      
REMARK 465     MET B   109                                                      
REMARK 465     GLU B   110                                                      
REMARK 465     GLU B   111                                                      
REMARK 465     ALA B   112                                                      
REMARK 465     SER B   113                                                      
REMARK 465     LYS B   114                                                      
REMARK 465     ARG B   316                                                      
REMARK 465     ASN B   317                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE1  GLU A   489     O    HOH A   601              1.97            
REMARK 500   O    HOH B   616     O    HOH B   741              2.00            
REMARK 500   O    HOH B   642     O    HOH B   744              2.01            
REMARK 500   O    HOH A   641     O    HOH A   657              2.02            
REMARK 500   NE2  HIS A   135     O    HOH A   602              2.02            
REMARK 500   O    HOH A   638     O    HOH A   674              2.06            
REMARK 500   OD1  ASP B   141     O    HOH B   601              2.08            
REMARK 500   O    HOH A   658     O    HOH A   770              2.10            
REMARK 500   OE2  GLU B   244     O    HOH B   602              2.11            
REMARK 500   OE2  GLU A   489     O    HOH A   603              2.11            
REMARK 500   O    GLU A   139     O    HOH A   604              2.15            
REMARK 500   O    HOH B   716     O    HOH B   724              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A 308   CD    GLU A 308   OE1    -0.080                       
REMARK 500    GLU A 308   CD    GLU A 308   OE2    -0.074                       
REMARK 500    ARG B 295   NE    ARG B 295   CZ     -0.090                       
REMARK 500    ARG B 295   CZ    ARG B 295   NH1    -0.087                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A 185   CB  -  CG  -  OD2 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 116       77.56     58.67                                   
REMARK 500    TYR A 236     -119.43     52.33                                   
REMARK 500    ASN A 302       79.03   -114.20                                   
REMARK 500    ILE A 381      -65.06   -129.43                                   
REMARK 500    PHE A 422      -86.52   -113.01                                   
REMARK 500    THR A 427      -56.85   -121.62                                   
REMARK 500    MET A 456     -131.21     44.26                                   
REMARK 500    LYS A 466       32.04     70.75                                   
REMARK 500    TYR B 236     -117.61     52.34                                   
REMARK 500    ASN B 302       74.18   -113.30                                   
REMARK 500    ILE B 381      -67.27   -132.31                                   
REMARK 500    THR B 412      -64.80    -97.07                                   
REMARK 500    PHE B 422      -83.31   -112.27                                   
REMARK 500    THR B 427      -59.21   -123.43                                   
REMARK 500    GLN B 428      -61.18    -99.59                                   
REMARK 500    MET B 456     -136.03     48.95                                   
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 MYA A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CIT A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MYA B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CIT B 502                 
DBREF  5UUT A  109   496  UNP    P30419   NMT1_HUMAN      29    416             
DBREF  5UUT B  109   496  UNP    P30419   NMT1_HUMAN      29    416             
SEQADV 5UUT GLY A  106  UNP  P30419              EXPRESSION TAG                 
SEQADV 5UUT PRO A  107  UNP  P30419              EXPRESSION TAG                 
SEQADV 5UUT HIS A  108  UNP  P30419              EXPRESSION TAG                 
SEQADV 5UUT GLY B  106  UNP  P30419              EXPRESSION TAG                 
SEQADV 5UUT PRO B  107  UNP  P30419              EXPRESSION TAG                 
SEQADV 5UUT HIS B  108  UNP  P30419              EXPRESSION TAG                 
SEQRES   1 A  391  GLY PRO HIS MET GLU GLU ALA SER LYS ARG SER TYR GLN          
SEQRES   2 A  391  PHE TRP ASP THR GLN PRO VAL PRO LYS LEU GLY GLU VAL          
SEQRES   3 A  391  VAL ASN THR HIS GLY PRO VAL GLU PRO ASP LYS ASP ASN          
SEQRES   4 A  391  ILE ARG GLN GLU PRO TYR THR LEU PRO GLN GLY PHE THR          
SEQRES   5 A  391  TRP ASP ALA LEU ASP LEU GLY ASP ARG GLY VAL LEU LYS          
SEQRES   6 A  391  GLU LEU TYR THR LEU LEU ASN GLU ASN TYR VAL GLU ASP          
SEQRES   7 A  391  ASP ASP ASN MET PHE ARG PHE ASP TYR SER PRO GLU PHE          
SEQRES   8 A  391  LEU LEU TRP ALA LEU ARG PRO PRO GLY TRP LEU PRO GLN          
SEQRES   9 A  391  TRP HIS CYS GLY VAL ARG VAL VAL SER SER ARG LYS LEU          
SEQRES  10 A  391  VAL GLY PHE ILE SER ALA ILE PRO ALA ASN ILE HIS ILE          
SEQRES  11 A  391  TYR ASP THR GLU LYS LYS MET VAL GLU ILE ASN PHE LEU          
SEQRES  12 A  391  CYS VAL HIS LYS LYS LEU ARG SER LYS ARG VAL ALA PRO          
SEQRES  13 A  391  VAL LEU ILE ARG GLU ILE THR ARG ARG VAL HIS LEU GLU          
SEQRES  14 A  391  GLY ILE PHE GLN ALA VAL TYR THR ALA GLY VAL VAL LEU          
SEQRES  15 A  391  PRO LYS PRO VAL GLY THR CYS ARG TYR TRP HIS ARG SER          
SEQRES  16 A  391  LEU ASN PRO ARG LYS LEU ILE GLU VAL LYS PHE SER HIS          
SEQRES  17 A  391  LEU SER ARG ASN MET THR MET GLN ARG THR MET LYS LEU          
SEQRES  18 A  391  TYR ARG LEU PRO GLU THR PRO LYS THR ALA GLY LEU ARG          
SEQRES  19 A  391  PRO MET GLU THR LYS ASP ILE PRO VAL VAL HIS GLN LEU          
SEQRES  20 A  391  LEU THR ARG TYR LEU LYS GLN PHE HIS LEU THR PRO VAL          
SEQRES  21 A  391  MET SER GLN GLU GLU VAL GLU HIS TRP PHE TYR PRO GLN          
SEQRES  22 A  391  GLU ASN ILE ILE ASP THR PHE VAL VAL GLU ASN ALA ASN          
SEQRES  23 A  391  GLY GLU VAL THR ASP PHE LEU SER PHE TYR THR LEU PRO          
SEQRES  24 A  391  SER THR ILE MET ASN HIS PRO THR HIS LYS SER LEU LYS          
SEQRES  25 A  391  ALA ALA TYR SER PHE TYR ASN VAL HIS THR GLN THR PRO          
SEQRES  26 A  391  LEU LEU ASP LEU MET SER ASP ALA LEU VAL LEU ALA LYS          
SEQRES  27 A  391  MET LYS GLY PHE ASP VAL PHE ASN ALA LEU ASP LEU MET          
SEQRES  28 A  391  GLU ASN LYS THR PHE LEU GLU LYS LEU LYS PHE GLY ILE          
SEQRES  29 A  391  GLY ASP GLY ASN LEU GLN TYR TYR LEU TYR ASN TRP LYS          
SEQRES  30 A  391  CYS PRO SER MET GLY ALA GLU LYS VAL GLY LEU VAL LEU          
SEQRES  31 A  391  GLN                                                          
SEQRES   1 B  391  GLY PRO HIS MET GLU GLU ALA SER LYS ARG SER TYR GLN          
SEQRES   2 B  391  PHE TRP ASP THR GLN PRO VAL PRO LYS LEU GLY GLU VAL          
SEQRES   3 B  391  VAL ASN THR HIS GLY PRO VAL GLU PRO ASP LYS ASP ASN          
SEQRES   4 B  391  ILE ARG GLN GLU PRO TYR THR LEU PRO GLN GLY PHE THR          
SEQRES   5 B  391  TRP ASP ALA LEU ASP LEU GLY ASP ARG GLY VAL LEU LYS          
SEQRES   6 B  391  GLU LEU TYR THR LEU LEU ASN GLU ASN TYR VAL GLU ASP          
SEQRES   7 B  391  ASP ASP ASN MET PHE ARG PHE ASP TYR SER PRO GLU PHE          
SEQRES   8 B  391  LEU LEU TRP ALA LEU ARG PRO PRO GLY TRP LEU PRO GLN          
SEQRES   9 B  391  TRP HIS CYS GLY VAL ARG VAL VAL SER SER ARG LYS LEU          
SEQRES  10 B  391  VAL GLY PHE ILE SER ALA ILE PRO ALA ASN ILE HIS ILE          
SEQRES  11 B  391  TYR ASP THR GLU LYS LYS MET VAL GLU ILE ASN PHE LEU          
SEQRES  12 B  391  CYS VAL HIS LYS LYS LEU ARG SER LYS ARG VAL ALA PRO          
SEQRES  13 B  391  VAL LEU ILE ARG GLU ILE THR ARG ARG VAL HIS LEU GLU          
SEQRES  14 B  391  GLY ILE PHE GLN ALA VAL TYR THR ALA GLY VAL VAL LEU          
SEQRES  15 B  391  PRO LYS PRO VAL GLY THR CYS ARG TYR TRP HIS ARG SER          
SEQRES  16 B  391  LEU ASN PRO ARG LYS LEU ILE GLU VAL LYS PHE SER HIS          
SEQRES  17 B  391  LEU SER ARG ASN MET THR MET GLN ARG THR MET LYS LEU          
SEQRES  18 B  391  TYR ARG LEU PRO GLU THR PRO LYS THR ALA GLY LEU ARG          
SEQRES  19 B  391  PRO MET GLU THR LYS ASP ILE PRO VAL VAL HIS GLN LEU          
SEQRES  20 B  391  LEU THR ARG TYR LEU LYS GLN PHE HIS LEU THR PRO VAL          
SEQRES  21 B  391  MET SER GLN GLU GLU VAL GLU HIS TRP PHE TYR PRO GLN          
SEQRES  22 B  391  GLU ASN ILE ILE ASP THR PHE VAL VAL GLU ASN ALA ASN          
SEQRES  23 B  391  GLY GLU VAL THR ASP PHE LEU SER PHE TYR THR LEU PRO          
SEQRES  24 B  391  SER THR ILE MET ASN HIS PRO THR HIS LYS SER LEU LYS          
SEQRES  25 B  391  ALA ALA TYR SER PHE TYR ASN VAL HIS THR GLN THR PRO          
SEQRES  26 B  391  LEU LEU ASP LEU MET SER ASP ALA LEU VAL LEU ALA LYS          
SEQRES  27 B  391  MET LYS GLY PHE ASP VAL PHE ASN ALA LEU ASP LEU MET          
SEQRES  28 B  391  GLU ASN LYS THR PHE LEU GLU LYS LEU LYS PHE GLY ILE          
SEQRES  29 B  391  GLY ASP GLY ASN LEU GLN TYR TYR LEU TYR ASN TRP LYS          
SEQRES  30 B  391  CYS PRO SER MET GLY ALA GLU LYS VAL GLY LEU VAL LEU          
SEQRES  31 B  391  GLN                                                          
HET    MYA  A 501      63                                                       
HET    CIT  A 502      13                                                       
HET    MYA  B 501      63                                                       
HET    CIT  B 502      13                                                       
HETNAM     MYA TETRADECANOYL-COA                                                
HETNAM     CIT CITRIC ACID                                                      
HETSYN     MYA MYRISTOYL-COA                                                    
FORMUL   3  MYA    2(C35 H62 N7 O17 P3 S)                                       
FORMUL   4  CIT    2(C6 H8 O7)                                                  
FORMUL   7  HOH   *340(H2 O)                                                    
HELIX    1 AA1 PHE A  119  GLN A  123  5                                   5    
HELIX    2 AA2 ASP A  165  TYR A  180  1                                  16    
HELIX    3 AA3 SER A  193  ARG A  202  1                                  10    
HELIX    4 AA4 LEU A  207  GLN A  209  5                                   3    
HELIX    5 AA5 LYS A  252  ARG A  255  5                                   4    
HELIX    6 AA6 VAL A  259  LEU A  273  1                                  15    
HELIX    7 AA7 ASN A  302  VAL A  309  1                                   8    
HELIX    8 AA8 THR A  319  ARG A  328  1                                  10    
HELIX    9 AA9 GLU A  342  LYS A  344  5                                   3    
HELIX   10 AB1 ASP A  345  LEU A  357  1                                  13    
HELIX   11 AB2 LYS A  358  PHE A  360  5                                   3    
HELIX   12 AB3 SER A  367  TYR A  376  1                                  10    
HELIX   13 AB4 PRO A  430  LYS A  445  1                                  16    
HELIX   14 AB5 GLU A  457  PHE A  461  5                                   5    
HELIX   15 AB6 GLY A  487  VAL A  491  5                                   5    
HELIX   16 AB7 PHE B  119  GLN B  123  5                                   5    
HELIX   17 AB8 ASP B  165  TYR B  180  1                                  16    
HELIX   18 AB9 SER B  193  ARG B  202  1                                  10    
HELIX   19 AC1 LEU B  207  GLN B  209  5                                   3    
HELIX   20 AC2 LYS B  252  ARG B  255  5                                   4    
HELIX   21 AC3 ARG B  258  LEU B  273  1                                  16    
HELIX   22 AC4 ASN B  302  VAL B  309  1                                   8    
HELIX   23 AC5 THR B  319  TYR B  327  1                                   9    
HELIX   24 AC6 GLU B  342  LYS B  344  5                                   3    
HELIX   25 AC7 ASP B  345  LYS B  358  1                                  14    
HELIX   26 AC8 SER B  367  TYR B  376  1                                  10    
HELIX   27 AC9 PRO B  430  LYS B  445  1                                  16    
HELIX   28 AD1 GLU B  457  GLU B  463  1                                   7    
HELIX   29 AD2 GLY B  487  VAL B  491  5                                   5    
SHEET    1 AA112 PHE A 156  ALA A 160  0                                        
SHEET    2 AA112 HIS A 211  VAL A 216 -1  O  ARG A 215   N  THR A 157           
SHEET    3 AA112 LEU A 222  ILE A 235 -1  O  ILE A 226   N  CYS A 212           
SHEET    4 AA112 THR A 238  VAL A 250 -1  O  MET A 242   N  ALA A 231           
SHEET    5 AA112 ALA A 279  ALA A 283  1  O  VAL A 280   N  VAL A 243           
SHEET    6 AA112 GLY A 468  TYR A 479 -1  O  GLN A 475   N  ALA A 283           
SHEET    7 AA112 GLY A 292  SER A 300 -1  N  TYR A 296   O  GLY A 470           
SHEET    8 AA112 VAL A 449  LEU A 453 -1  O  PHE A 450   N  ARG A 299           
SHEET    9 AA112 ALA A 418  SER A 421  1  N  SER A 421   O  ASN A 451           
SHEET   10 AA112 VAL A 394  THR A 402 -1  N  TYR A 401   O  TYR A 420           
SHEET   11 AA112 ILE A 382  GLU A 388 -1  N  VAL A 387   O  ASP A 396           
SHEET   12 AA112 LEU A 338  PRO A 340 -1  N  ARG A 339   O  VAL A 386           
SHEET    1 AA2 4 PHE A 156  ALA A 160  0                                        
SHEET    2 AA2 4 HIS A 211  VAL A 216 -1  O  ARG A 215   N  THR A 157           
SHEET    3 AA2 4 LEU A 222  ILE A 235 -1  O  ILE A 226   N  CYS A 212           
SHEET    4 AA2 4 LEU A 362  VAL A 365 -1  O  THR A 363   N  HIS A 234           
SHEET    1 AA3 2 ARG A 189  PHE A 190  0                                        
SHEET    2 AA3 2 SER A 405  THR A 406 -1  O  THR A 406   N  ARG A 189           
SHEET    1 AA412 PHE B 156  ALA B 160  0                                        
SHEET    2 AA412 HIS B 211  VAL B 216 -1  O  ARG B 215   N  THR B 157           
SHEET    3 AA412 LEU B 222  ILE B 235 -1  O  GLY B 224   N  VAL B 214           
SHEET    4 AA412 THR B 238  VAL B 250 -1  O  MET B 242   N  ALA B 231           
SHEET    5 AA412 ALA B 279  ALA B 283  1  O  VAL B 280   N  VAL B 243           
SHEET    6 AA412 GLY B 468  TYR B 479 -1  O  TYR B 479   N  ALA B 279           
SHEET    7 AA412 GLY B 292  SER B 300 -1  N  CYS B 294   O  LEU B 474           
SHEET    8 AA412 VAL B 449  LEU B 453 -1  O  ALA B 452   N  TRP B 297           
SHEET    9 AA412 ALA B 418  SER B 421  1  N  ALA B 419   O  ASN B 451           
SHEET   10 AA412 VAL B 394  THR B 402 -1  N  TYR B 401   O  TYR B 420           
SHEET   11 AA412 ILE B 382  GLU B 388 -1  N  PHE B 385   O  LEU B 398           
SHEET   12 AA412 LEU B 338  PRO B 340 -1  N  ARG B 339   O  VAL B 386           
SHEET    1 AA5 4 PHE B 156  ALA B 160  0                                        
SHEET    2 AA5 4 HIS B 211  VAL B 216 -1  O  ARG B 215   N  THR B 157           
SHEET    3 AA5 4 LEU B 222  ILE B 235 -1  O  GLY B 224   N  VAL B 214           
SHEET    4 AA5 4 LEU B 362  VAL B 365 -1  O  THR B 363   N  HIS B 234           
SHEET    1 AA6 3 PHE B 188  PHE B 190  0                                        
SHEET    2 AA6 3 SER B 405  ILE B 407 -1  O  THR B 406   N  ARG B 189           
SHEET    3 AA6 3 SER B 415  LEU B 416 -1  O  LEU B 416   N  SER B 405           
CISPEP   1 PRO A  288    LYS A  289          0       -19.08                     
CISPEP   2 PRO A  288    LYS A  289          0       -19.30                     
CISPEP   3 PRO B  288    LYS B  289          0       -19.85                     
SITE     1 AC1 34 TYR A 117  GLN A 118  PHE A 119  TRP A 120                    
SITE     2 AC1 34 ASN A 179  TYR A 180  VAL A 181  ILE A 245                    
SITE     3 AC1 34 ASN A 246  PHE A 247  LEU A 248  CYS A 249                    
SITE     4 AC1 34 VAL A 250  ARG A 255  SER A 256  LYS A 257                    
SITE     5 AC1 34 ARG A 258  VAL A 259  ALA A 260  PRO A 261                    
SITE     6 AC1 34 THR A 268  VAL A 271  ILE A 276  PHE A 277                    
SITE     7 AC1 34 ALA A 279  TYR A 281  THR A 282  LEU A 287                    
SITE     8 AC1 34 TYR A 479  HOH A 686  HOH A 688  HOH A 705                    
SITE     9 AC1 34 HOH A 712  HOH A 725                                          
SITE     1 AC2 11 THR A 122  GLN A 123  GLU A 139  LYS A 142                    
SITE     2 AC2 11 ARG A 265  ASN A 389  ALA A 390  HOH A 647                    
SITE     3 AC2 11 HOH A 653  HOH A 669  HOH A 736                               
SITE     1 AC3 36 TYR B 117  GLN B 118  PHE B 119  TRP B 120                    
SITE     2 AC3 36 ASN B 179  TYR B 180  VAL B 181  ILE B 245                    
SITE     3 AC3 36 ASN B 246  PHE B 247  LEU B 248  CYS B 249                    
SITE     4 AC3 36 VAL B 250  ARG B 255  SER B 256  LYS B 257                    
SITE     5 AC3 36 ARG B 258  VAL B 259  ALA B 260  PRO B 261                    
SITE     6 AC3 36 ILE B 264  THR B 268  VAL B 271  HIS B 272                    
SITE     7 AC3 36 ILE B 276  PHE B 277  ALA B 279  TYR B 281                    
SITE     8 AC3 36 THR B 282  LEU B 287  TYR B 479  HOH B 646                    
SITE     9 AC3 36 HOH B 651  HOH B 700  HOH B 717  HOH B 719                    
SITE     1 AC4 10 THR B 122  GLN B 123  GLU B 139  LYS B 142                    
SITE     2 AC4 10 ARG B 265  ASN B 389  ALA B 390  HOH B 612                    
SITE     3 AC4 10 HOH B 683  HOH B 698                                          
CRYST1   78.778  177.582   58.566  90.00  90.00  90.00 P 21 21 2     8          
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      0.012694  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005631  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017075        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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