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Database: PDB
Entry: 3IU1
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Original site: 3IU1 
HEADER    TRANSFERASE                             29-AUG-09   3IU1              
TITLE     CRYSTAL STRUCTURE OF HUMAN TYPE-I N-MYRISTOYLTRANSFERASE WITH BOUND   
TITLE    2 MYRISTOYL-COA                                                        
CAVEAT     3IU1    THERE ARE CHIRALITY ERRORS AT C10 ATOM OF MYA A 1001 AND MYA 
CAVEAT   2 3IU1     B 2001.                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLYCYLPEPTIDE N-TETRADECANOYLTRANSFERASE 1;                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: PEPTIDE N-MYRISTOYLTRANSFERASE 1, MYRISTOYL-COA:PROTEIN N-  
COMPND   5 MYRISTOYLTRANSFERASE 1, NMT 1, TYPE I N-MYRISTOYLTRANSFERASE;        
COMPND   6 EC: 2.3.1.97;                                                        
COMPND   7 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: NMT, NMT1;                                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TRANSFERASE, N-MYRISTOYLTRANSFERASE, NMT1, ACYLTRANSFERASE,           
KEYWDS   2 PHOSPHOPROTEIN, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, 
KEYWDS   3 SGC                                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.QIU,A.HUTCHINSON,A.WERNIMONT,Y.-H.LIN,A.KANIA,M.RAVICHANDRAN,       
AUTHOR   2 I.KOZIERADZKI,D.COSSAR,M.SCHAPIRA,C.H.ARROWSMITH,C.BOUNTRA,          
AUTHOR   3 J.WEIGELT,A.M.EDWARDS,P.G.WYATT,M.A.J.FERGUSON,J.A.FREARSON,         
AUTHOR   4 S.Y.BRAND,D.A.ROBINSON,A.BOCHKAREV,R.HUI,STRUCTURAL GENOMICS         
AUTHOR   5 CONSORTIUM (SGC)                                                     
REVDAT   2   16-NOV-11 3IU1    1       REMARK                                   
REVDAT   1   15-SEP-09 3IU1    0                                                
JRNL        AUTH   W.QIU,A.HUTCHINSON,A.WERNIMONT,Y.-H.LIN,A.KANIA,             
JRNL        AUTH 2 M.RAVICHANDRAN,I.KOZIERADZKI,D.COSSAR,M.SCHAPIRA,            
JRNL        AUTH 3 C.H.ARROWSMITH,C.BOUNTRA,J.WEIGELT,A.M.EDWARDS,P.G.WYATT,    
JRNL        AUTH 4 M.A.J.FERGUSON,J.A.FREARSON,S.Y.BRAND,D.A.ROBINSON,          
JRNL        AUTH 5 A.BOCHKAREV,R.HUI                                            
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN TYPE-I N-MYRISTOYLTRANSFERASE     
JRNL        TITL 2 WITH BOUND MYRISTOYL-COA                                     
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.42 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0072                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.42                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.78                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 139000                         
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) : 0.199                           
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 7316                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.42                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.46                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6575                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3280                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 346                          
REMARK   3   BIN FREE R VALUE                    : 0.3470                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6242                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 126                                     
REMARK   3   SOLVENT ATOMS            : 1233                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.96                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.01000                                             
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.01000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.077         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.076         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.052         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.329         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.942                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6753 ; 0.006 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9228 ; 1.116 ; 1.979       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   816 ; 5.458 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   320 ;36.331 ;23.875       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1164 ;12.051 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    40 ;13.268 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1004 ; 0.087 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5138 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3911 ; 0.433 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6420 ; 0.822 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2842 ; 1.131 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2778 ; 1.874 ; 4.500       
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   : 1.40                                          
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 3IU1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-SEP-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB054863.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-AUG-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.7                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 146323                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.420                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 200.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.7                               
REMARK 200  DATA REDUNDANCY                : 5.600                              
REMARK 200  R MERGE                    (I) : 0.06500                            
REMARK 200  R SYM                      (I) : 0.04500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.0300                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.42                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.51                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 77.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.46400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.010                              
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 3H5Z                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.07                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 19% PEG3350, 0.2M DI-AMMONIUM HYDROGEN   
REMARK 280  CITRATE, PH 5.7, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21                        
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,Y+1/2,-Z+1/2                                         
REMARK 290       4555   -X,-Y+1/2,Z+1/2                                         
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        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.03000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       89.32500            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       39.03000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       89.32500            
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   114                                                      
REMARK 465     SER A   315                                                      
REMARK 465     ARG A   316                                                      
REMARK 465     GLY B   114                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A 166    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG B 115    CD   NE   CZ   NH1  NH2                             
REMARK 470     ASP B 184    CG   OD1  OD2                                       
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 202       52.02   -117.78                                   
REMARK 500    TYR A 236     -125.69     48.82                                   
REMARK 500    ILE A 381      -61.93   -131.30                                   
REMARK 500    THR A 412      -60.10   -109.16                                   
REMARK 500    PHE A 422     -101.48   -110.46                                   
REMARK 500    MET A 456     -132.22     47.01                                   
REMARK 500    TYR B 180     -157.69    -87.54                                   
REMARK 500    ARG B 202       52.69   -119.75                                   
REMARK 500    TYR B 236     -128.81     49.01                                   
REMARK 500    ILE B 381      -61.09   -133.73                                   
REMARK 500    ASN B 409      -20.14     79.49                                   
REMARK 500    PHE B 422     -101.02   -112.46                                   
REMARK 500    MET B 456     -132.73     45.67                                   
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 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MYA B 2001                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1RXT   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN WITH SHORTER TRUNCATION                                 
REMARK 900 RELATED ID: 3IU2   RELATED DB: PDB                                   
DBREF  3IU1 A  115   496  UNP    P30419   NMT1_HUMAN     115    496             
DBREF  3IU1 B  115   496  UNP    P30419   NMT1_HUMAN     115    496             
SEQADV 3IU1 GLY A  114  UNP  P30419              EXPRESSION TAG                 
SEQADV 3IU1 GLY B  114  UNP  P30419              EXPRESSION TAG                 
SEQRES   1 A  383  GLY ARG SER TYR GLN PHE TRP ASP THR GLN PRO VAL PRO          
SEQRES   2 A  383  LYS LEU GLY GLU VAL VAL ASN THR HIS GLY PRO VAL GLU          
SEQRES   3 A  383  PRO ASP LYS ASP ASN ILE ARG GLN GLU PRO TYR THR LEU          
SEQRES   4 A  383  PRO GLN GLY PHE THR TRP ASP ALA LEU ASP LEU GLY ASP          
SEQRES   5 A  383  ARG GLY VAL LEU LYS GLU LEU TYR THR LEU LEU ASN GLU          
SEQRES   6 A  383  ASN TYR VAL GLU ASP ASP ASP ASN MET PHE ARG PHE ASP          
SEQRES   7 A  383  TYR SER PRO GLU PHE LEU LEU TRP ALA LEU ARG PRO PRO          
SEQRES   8 A  383  GLY TRP LEU PRO GLN TRP HIS CYS GLY VAL ARG VAL VAL          
SEQRES   9 A  383  SER SER ARG LYS LEU VAL GLY PHE ILE SER ALA ILE PRO          
SEQRES  10 A  383  ALA ASN ILE HIS ILE TYR ASP THR GLU LYS LYS MET VAL          
SEQRES  11 A  383  GLU ILE ASN PHE LEU CYS VAL HIS LYS LYS LEU ARG SER          
SEQRES  12 A  383  LYS ARG VAL ALA PRO VAL LEU ILE ARG GLU ILE THR ARG          
SEQRES  13 A  383  ARG VAL HIS LEU GLU GLY ILE PHE GLN ALA VAL TYR THR          
SEQRES  14 A  383  ALA GLY VAL VAL LEU PRO LYS PRO VAL GLY THR CYS ARG          
SEQRES  15 A  383  TYR TRP HIS ARG SER LEU ASN PRO ARG LYS LEU ILE GLU          
SEQRES  16 A  383  VAL LYS PHE SER HIS LEU SER ARG ASN MET THR MET GLN          
SEQRES  17 A  383  ARG THR MET LYS LEU TYR ARG LEU PRO GLU THR PRO LYS          
SEQRES  18 A  383  THR ALA GLY LEU ARG PRO MET GLU THR LYS ASP ILE PRO          
SEQRES  19 A  383  VAL VAL HIS GLN LEU LEU THR ARG TYR LEU LYS GLN PHE          
SEQRES  20 A  383  HIS LEU THR PRO VAL MET SER GLN GLU GLU VAL GLU HIS          
SEQRES  21 A  383  TRP PHE TYR PRO GLN GLU ASN ILE ILE ASP THR PHE VAL          
SEQRES  22 A  383  VAL GLU ASN ALA ASN GLY GLU VAL THR ASP PHE LEU SER          
SEQRES  23 A  383  PHE TYR THR LEU PRO SER THR ILE MET ASN HIS PRO THR          
SEQRES  24 A  383  HIS LYS SER LEU LYS ALA ALA TYR SER PHE TYR ASN VAL          
SEQRES  25 A  383  HIS THR GLN THR PRO LEU LEU ASP LEU MET SER ASP ALA          
SEQRES  26 A  383  LEU VAL LEU ALA LYS MET LYS GLY PHE ASP VAL PHE ASN          
SEQRES  27 A  383  ALA LEU ASP LEU MET GLU ASN LYS THR PHE LEU GLU LYS          
SEQRES  28 A  383  LEU LYS PHE GLY ILE GLY ASP GLY ASN LEU GLN TYR TYR          
SEQRES  29 A  383  LEU TYR ASN TRP LYS CYS PRO SER MET GLY ALA GLU LYS          
SEQRES  30 A  383  VAL GLY LEU VAL LEU GLN                                      
SEQRES   1 B  383  GLY ARG SER TYR GLN PHE TRP ASP THR GLN PRO VAL PRO          
SEQRES   2 B  383  LYS LEU GLY GLU VAL VAL ASN THR HIS GLY PRO VAL GLU          
SEQRES   3 B  383  PRO ASP LYS ASP ASN ILE ARG GLN GLU PRO TYR THR LEU          
SEQRES   4 B  383  PRO GLN GLY PHE THR TRP ASP ALA LEU ASP LEU GLY ASP          
SEQRES   5 B  383  ARG GLY VAL LEU LYS GLU LEU TYR THR LEU LEU ASN GLU          
SEQRES   6 B  383  ASN TYR VAL GLU ASP ASP ASP ASN MET PHE ARG PHE ASP          
SEQRES   7 B  383  TYR SER PRO GLU PHE LEU LEU TRP ALA LEU ARG PRO PRO          
SEQRES   8 B  383  GLY TRP LEU PRO GLN TRP HIS CYS GLY VAL ARG VAL VAL          
SEQRES   9 B  383  SER SER ARG LYS LEU VAL GLY PHE ILE SER ALA ILE PRO          
SEQRES  10 B  383  ALA ASN ILE HIS ILE TYR ASP THR GLU LYS LYS MET VAL          
SEQRES  11 B  383  GLU ILE ASN PHE LEU CYS VAL HIS LYS LYS LEU ARG SER          
SEQRES  12 B  383  LYS ARG VAL ALA PRO VAL LEU ILE ARG GLU ILE THR ARG          
SEQRES  13 B  383  ARG VAL HIS LEU GLU GLY ILE PHE GLN ALA VAL TYR THR          
SEQRES  14 B  383  ALA GLY VAL VAL LEU PRO LYS PRO VAL GLY THR CYS ARG          
SEQRES  15 B  383  TYR TRP HIS ARG SER LEU ASN PRO ARG LYS LEU ILE GLU          
SEQRES  16 B  383  VAL LYS PHE SER HIS LEU SER ARG ASN MET THR MET GLN          
SEQRES  17 B  383  ARG THR MET LYS LEU TYR ARG LEU PRO GLU THR PRO LYS          
SEQRES  18 B  383  THR ALA GLY LEU ARG PRO MET GLU THR LYS ASP ILE PRO          
SEQRES  19 B  383  VAL VAL HIS GLN LEU LEU THR ARG TYR LEU LYS GLN PHE          
SEQRES  20 B  383  HIS LEU THR PRO VAL MET SER GLN GLU GLU VAL GLU HIS          
SEQRES  21 B  383  TRP PHE TYR PRO GLN GLU ASN ILE ILE ASP THR PHE VAL          
SEQRES  22 B  383  VAL GLU ASN ALA ASN GLY GLU VAL THR ASP PHE LEU SER          
SEQRES  23 B  383  PHE TYR THR LEU PRO SER THR ILE MET ASN HIS PRO THR          
SEQRES  24 B  383  HIS LYS SER LEU LYS ALA ALA TYR SER PHE TYR ASN VAL          
SEQRES  25 B  383  HIS THR GLN THR PRO LEU LEU ASP LEU MET SER ASP ALA          
SEQRES  26 B  383  LEU VAL LEU ALA LYS MET LYS GLY PHE ASP VAL PHE ASN          
SEQRES  27 B  383  ALA LEU ASP LEU MET GLU ASN LYS THR PHE LEU GLU LYS          
SEQRES  28 B  383  LEU LYS PHE GLY ILE GLY ASP GLY ASN LEU GLN TYR TYR          
SEQRES  29 B  383  LEU TYR ASN TRP LYS CYS PRO SER MET GLY ALA GLU LYS          
SEQRES  30 B  383  VAL GLY LEU VAL LEU GLN                                      
HET    MYA  A1001      63                                                       
HET    MYA  B2001      63                                                       
HETNAM     MYA TETRADECANOYL-COA                                                
HETSYN     MYA MYRISTOYL-COA                                                    
FORMUL   3  MYA    2(C35 H62 N7 O17 P3 S)                                       
FORMUL   5  HOH   *1233(H2 O)                                                   
HELIX    1   1 PHE A  119  GLN A  123  5                                   5    
HELIX    2   2 ASP A  165  TYR A  180  1                                  16    
HELIX    3   3 SER A  193  ARG A  202  1                                  10    
HELIX    4   4 LEU A  207  GLN A  209  5                                   3    
HELIX    5   5 LYS A  252  ARG A  255  5                                   4    
HELIX    6   6 ARG A  258  LEU A  273  1                                  16    
HELIX    7   7 ASN A  302  VAL A  309  1                                   8    
HELIX    8   8 THR A  319  ARG A  328  1                                  10    
HELIX    9   9 GLU A  342  LYS A  344  5                                   3    
HELIX   10  10 ASP A  345  LEU A  357  1                                  13    
HELIX   11  11 LYS A  358  PHE A  360  5                                   3    
HELIX   12  12 SER A  367  TYR A  376  1                                  10    
HELIX   13  13 PRO A  430  LYS A  445  1                                  16    
HELIX   14  14 GLU A  457  PHE A  461  5                                   5    
HELIX   15  15 GLY A  487  VAL A  491  5                                   5    
HELIX   16  16 PHE B  119  GLN B  123  5                                   5    
HELIX   17  17 ASP B  165  TYR B  180  1                                  16    
HELIX   18  18 SER B  193  ARG B  202  1                                  10    
HELIX   19  19 LEU B  207  GLN B  209  5                                   3    
HELIX   20  20 LYS B  252  ARG B  255  5                                   4    
HELIX   21  21 ARG B  258  LEU B  273  1                                  16    
HELIX   22  22 ASN B  302  VAL B  309  1                                   8    
HELIX   23  23 THR B  319  ARG B  328  1                                  10    
HELIX   24  24 GLU B  342  LYS B  344  5                                   3    
HELIX   25  25 ASP B  345  LYS B  358  1                                  14    
HELIX   26  26 SER B  367  TYR B  376  1                                  10    
HELIX   27  27 PRO B  430  LYS B  445  1                                  16    
HELIX   28  28 GLU B  457  PHE B  461  5                                   5    
HELIX   29  29 GLY B  487  VAL B  491  5                                   5    
SHEET    1   A12 PHE A 156  ALA A 160  0                                        
SHEET    2   A12 HIS A 211  VAL A 216 -1  O  ARG A 215   N  THR A 157           
SHEET    3   A12 LEU A 222  ILE A 235 -1  O  VAL A 223   N  VAL A 214           
SHEET    4   A12 THR A 238  VAL A 250 -1  O  THR A 238   N  ILE A 235           
SHEET    5   A12 ALA A 279  ALA A 283  1  O  VAL A 280   N  VAL A 243           
SHEET    6   A12 GLY A 468  TYR A 479 -1  O  TYR A 477   N  TYR A 281           
SHEET    7   A12 GLY A 292  SER A 300 -1  N  HIS A 298   O  GLY A 468           
SHEET    8   A12 VAL A 449  LEU A 453 -1  O  ALA A 452   N  TRP A 297           
SHEET    9   A12 ALA A 418  SER A 421  1  N  ALA A 419   O  ASN A 451           
SHEET   10   A12 VAL A 394  THR A 402 -1  N  TYR A 401   O  TYR A 420           
SHEET   11   A12 ILE A 382  GLU A 388 -1  N  PHE A 385   O  LEU A 398           
SHEET   12   A12 LEU A 338  PRO A 340 -1  N  ARG A 339   O  VAL A 386           
SHEET    1   B 4 PHE A 156  ALA A 160  0                                        
SHEET    2   B 4 HIS A 211  VAL A 216 -1  O  ARG A 215   N  THR A 157           
SHEET    3   B 4 LEU A 222  ILE A 235 -1  O  VAL A 223   N  VAL A 214           
SHEET    4   B 4 LEU A 362  VAL A 365 -1  O  THR A 363   N  HIS A 234           
SHEET    1   C 3 PHE A 188  PHE A 190  0                                        
SHEET    2   C 3 SER A 405  ILE A 407 -1  O  THR A 406   N  ARG A 189           
SHEET    3   C 3 SER A 415  LEU A 416 -1  O  LEU A 416   N  SER A 405           
SHEET    1   D 7 PHE B 156  ALA B 160  0                                        
SHEET    2   D 7 HIS B 211  VAL B 216 -1  O  ARG B 215   N  THR B 157           
SHEET    3   D 7 LEU B 222  ILE B 235 -1  O  VAL B 223   N  VAL B 214           
SHEET    4   D 7 THR B 238  VAL B 250 -1  O  THR B 238   N  ILE B 235           
SHEET    5   D 7 ALA B 279  ALA B 283  1  O  VAL B 280   N  VAL B 243           
SHEET    6   D 7 LEU B 474  TYR B 479 -1  O  GLN B 475   N  ALA B 283           
SHEET    7   D 7 GLY B 292  CYS B 294 -1  N  GLY B 292   O  TYR B 476           
SHEET    1   E 4 PHE B 156  ALA B 160  0                                        
SHEET    2   E 4 HIS B 211  VAL B 216 -1  O  ARG B 215   N  THR B 157           
SHEET    3   E 4 LEU B 222  ILE B 235 -1  O  VAL B 223   N  VAL B 214           
SHEET    4   E 4 LEU B 362  VAL B 365 -1  O  THR B 363   N  HIS B 234           
SHEET    1   F 2 PHE B 188  PHE B 190  0                                        
SHEET    2   F 2 SER B 405  ILE B 407 -1  O  THR B 406   N  ARG B 189           
SHEET    1   G 4 LEU B 338  PRO B 340  0                                        
SHEET    2   G 4 ILE B 382  GLU B 388 -1  O  VAL B 386   N  ARG B 339           
SHEET    3   G 4 VAL B 394  THR B 402 -1  O  ASP B 396   N  VAL B 387           
SHEET    4   G 4 VAL B 425  HIS B 426 -1  O  VAL B 425   N  PHE B 397           
SHEET    1   H 7 LEU B 338  PRO B 340  0                                        
SHEET    2   H 7 ILE B 382  GLU B 388 -1  O  VAL B 386   N  ARG B 339           
SHEET    3   H 7 VAL B 394  THR B 402 -1  O  ASP B 396   N  VAL B 387           
SHEET    4   H 7 ALA B 418  SER B 421 -1  O  TYR B 420   N  TYR B 401           
SHEET    5   H 7 VAL B 449  LEU B 453  1  O  ASN B 451   N  ALA B 419           
SHEET    6   H 7 TYR B 296  SER B 300 -1  N  ARG B 299   O  PHE B 450           
SHEET    7   H 7 GLY B 468  ILE B 469 -1  O  GLY B 468   N  HIS B 298           
CISPEP   1 PRO A  288    LYS A  289          0       -11.05                     
CISPEP   2 PRO B  288    LYS B  289          0       -14.10                     
SITE     1 AC1 36 TYR A 117  GLN A 118  PHE A 119  TRP A 120                    
SITE     2 AC1 36 ASN A 179  TYR A 180  VAL A 181  ASN A 246                    
SITE     3 AC1 36 PHE A 247  LEU A 248  CYS A 249  VAL A 250                    
SITE     4 AC1 36 ARG A 255  SER A 256  LYS A 257  ARG A 258                    
SITE     5 AC1 36 VAL A 259  ALA A 260  PRO A 261  THR A 268                    
SITE     6 AC1 36 VAL A 271  PHE A 277  TYR A 281  THR A 282                    
SITE     7 AC1 36 LEU A 287  TYR A 479  HOH A 532  HOH A 587                    
SITE     8 AC1 36 HOH A 601  HOH A 607  HOH A 649  HOH A 653                    
SITE     9 AC1 36 HOH A 663  HOH A 696  HOH A 720  HOH A 822                    
SITE     1 AC2 36 HOH B   7  TYR B 117  GLN B 118  PHE B 119                    
SITE     2 AC2 36 TRP B 120  ASN B 179  TYR B 180  VAL B 181                    
SITE     3 AC2 36 ASN B 246  PHE B 247  LEU B 248  CYS B 249                    
SITE     4 AC2 36 VAL B 250  ARG B 255  SER B 256  LYS B 257                    
SITE     5 AC2 36 ARG B 258  VAL B 259  ALA B 260  PRO B 261                    
SITE     6 AC2 36 THR B 268  VAL B 271  PHE B 277  TYR B 281                    
SITE     7 AC2 36 THR B 282  LEU B 287  TYR B 479  HOH B 531                    
SITE     8 AC2 36 HOH B 534  HOH B 545  HOH B 565  HOH B 640                    
SITE     9 AC2 36 HOH B 729  HOH B 734  HOH B 741  HOH B 806                    
CRYST1   58.276   78.060  178.650  90.00  90.00  90.00 P 2 21 21     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      0.017160  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012811  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005598        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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