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Database: PDB
Entry: 3A7O
LinkDB: 3A7O
Original site: 3A7O 
HEADER    PROTEIN TRANSPORT                       01-OCT-09   3A7O              
TITLE     THE CRYSTAL STRUCTURE OF THE COILED-COIL DOMAIN OF SACCHAROMYCES      
TITLE    2 CEREVISIAE ATG16                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: AUTOPHAGY PROTEIN 16;                                      
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 FRAGMENT: COILED-COIL DOMAIN;                                        
COMPND   5 SYNONYM: ATG16, CYTOPLASM TO VACUOLE TARGETING PROTEIN 11, SAP18     
COMPND   6 HOMOLOG;                                                             
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: YEAST;                                              
SOURCE   4 ORGANISM_TAXID: 4932;                                                
SOURCE   5 GENE: ATG16;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX6P                                    
KEYWDS    COILED-COIL, AUTOPHAGY, COILED COIL, CYTOPLASMIC VESICLE, PROTEIN     
KEYWDS   2 TRANSPORT, TRANSPORT, VACUOLE                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.FUJIOKA,N.N.NODA,F.INAGAKI                                          
REVDAT   2   18-OCT-23 3A7O    1       JRNL   SEQADV                            
REVDAT   1   03-NOV-09 3A7O    0                                                
JRNL        AUTH   Y.FUJIOKA,N.N.NODA,H.NAKATOGAWA,Y.OHSUMI,F.INAGAKI           
JRNL        TITL   DIMERIC COILED-COIL STRUCTURE OF SACCHAROMYCES CEREVISIAE    
JRNL        TITL 2 ATG16 AND ITS FUNCTIONAL SIGNIFICANCE IN AUTOPHAGY.          
JRNL        REF    J.BIOL.CHEM.                  V. 285  1508 2010              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   19889643                                                     
JRNL        DOI    10.1074/JBC.M109.053520                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.08                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 22516                          
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 SET) : 0.272                           
REMARK   3   FREE R VALUE                     : 0.299                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1094                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.66                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.70                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3460                       
REMARK   3   BIN FREE R VALUE                    : 0.4310                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 160                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.034                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2662                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 82                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 56.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 5.66000                                              
REMARK   3    B22 (A**2) : 5.66000                                              
REMARK   3    B33 (A**2) : -11.32000                                            
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.000                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 16.20                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.660                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.530 ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3A7O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-OCT-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000028914.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-JUL-08; 23-JUL-08               
REMARK 200  TEMPERATURE           (KELVIN) : 95; 110                            
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; N                               
REMARK 200  RADIATION SOURCE               : SPRING-8; ROTATING ANODE           
REMARK 200  BEAMLINE                       : BL41XU; NULL                       
REMARK 200  X-RAY GENERATOR MODEL          : NULL; RIGAKU MICROMAX-007          
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1000; 1.5418                     
REMARK 200  MONOCHROMATOR                  : NULL; NULL                         
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; IMAGE PLATE                   
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-225; RIGAKU RAXIS VII   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22847                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 17.90                              
REMARK 200  R MERGE                    (I) : 0.06900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.28200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.26                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.18                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.8M AMMONIUM CHLORIDE, 0.1M SODIUM      
REMARK 280  ACETATE, PH 5.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-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       38.90400            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       63.94550            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       63.94550            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       58.35600            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       63.94550            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       63.94550            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       19.45200            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       63.94550            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       63.94550            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       58.35600            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       63.94550            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       63.94550            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       19.45200            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       38.90400            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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: 2560 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8350 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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: 2470 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8130 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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: 2590 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8700 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH F 130  LIES ON A SPECIAL POSITION.                          
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    49                                                      
REMARK 465     SER A    50                                                      
REMARK 465     GLY A    51                                                      
REMARK 465     ALA A    52                                                      
REMARK 465     ILE A    53                                                      
REMARK 465     GLY A    54                                                      
REMARK 465     GLY A    55                                                      
REMARK 465     ASN A    56                                                      
REMARK 465     ILE A    57                                                      
REMARK 465     VAL A    58                                                      
REMARK 465     SER A    59                                                      
REMARK 465     ASP A   119                                                      
REMARK 465     LEU A   120                                                      
REMARK 465     LYS A   121                                                      
REMARK 465     LYS A   122                                                      
REMARK 465     GLU A   123                                                      
REMARK 465     GLY B    49                                                      
REMARK 465     SER B    50                                                      
REMARK 465     GLY B    51                                                      
REMARK 465     ALA B    52                                                      
REMARK 465     ILE B    53                                                      
REMARK 465     GLY B    54                                                      
REMARK 465     GLY B    55                                                      
REMARK 465     ASN B    56                                                      
REMARK 465     ILE B    57                                                      
REMARK 465     VAL B    58                                                      
REMARK 465     SER B    59                                                      
REMARK 465     HIS B    60                                                      
REMARK 465     GLN B   115                                                      
REMARK 465     LYS B   116                                                      
REMARK 465     LEU B   117                                                      
REMARK 465     SER B   118                                                      
REMARK 465     ASP B   119                                                      
REMARK 465     LEU B   120                                                      
REMARK 465     LYS B   121                                                      
REMARK 465     LYS B   122                                                      
REMARK 465     GLU B   123                                                      
REMARK 465     GLY C    49                                                      
REMARK 465     SER C    50                                                      
REMARK 465     GLY C    51                                                      
REMARK 465     ALA C    52                                                      
REMARK 465     ILE C    53                                                      
REMARK 465     GLY C    54                                                      
REMARK 465     GLY C    55                                                      
REMARK 465     ASN C    56                                                      
REMARK 465     ILE C    57                                                      
REMARK 465     VAL C    58                                                      
REMARK 465     SER C    59                                                      
REMARK 465     LEU C   113                                                      
REMARK 465     GLN C   114                                                      
REMARK 465     GLN C   115                                                      
REMARK 465     LYS C   116                                                      
REMARK 465     LEU C   117                                                      
REMARK 465     SER C   118                                                      
REMARK 465     ASP C   119                                                      
REMARK 465     LEU C   120                                                      
REMARK 465     LYS C   121                                                      
REMARK 465     LYS C   122                                                      
REMARK 465     GLU C   123                                                      
REMARK 465     GLY D    49                                                      
REMARK 465     SER D    50                                                      
REMARK 465     GLY D    51                                                      
REMARK 465     ALA D    52                                                      
REMARK 465     ILE D    53                                                      
REMARK 465     GLY D    54                                                      
REMARK 465     GLY D    55                                                      
REMARK 465     ASN D    56                                                      
REMARK 465     ILE D    57                                                      
REMARK 465     VAL D    58                                                      
REMARK 465     LEU D   117                                                      
REMARK 465     SER D   118                                                      
REMARK 465     ASP D   119                                                      
REMARK 465     LEU D   120                                                      
REMARK 465     LYS D   121                                                      
REMARK 465     LYS D   122                                                      
REMARK 465     GLU D   123                                                      
REMARK 465     GLY E    49                                                      
REMARK 465     SER E    50                                                      
REMARK 465     GLY E    51                                                      
REMARK 465     ALA E    52                                                      
REMARK 465     ILE E    53                                                      
REMARK 465     GLY E    54                                                      
REMARK 465     GLY E    55                                                      
REMARK 465     ASN E    56                                                      
REMARK 465     ILE E    57                                                      
REMARK 465     VAL E    58                                                      
REMARK 465     SER E    59                                                      
REMARK 465     LEU E   120                                                      
REMARK 465     LYS E   121                                                      
REMARK 465     LYS E   122                                                      
REMARK 465     GLU E   123                                                      
REMARK 465     GLY F    49                                                      
REMARK 465     SER F    50                                                      
REMARK 465     GLY F    51                                                      
REMARK 465     ALA F    52                                                      
REMARK 465     ILE F    53                                                      
REMARK 465     GLY F    54                                                      
REMARK 465     GLY F    55                                                      
REMARK 465     ASN F    56                                                      
REMARK 465     ILE F    57                                                      
REMARK 465     VAL F    58                                                      
REMARK 465     SER F    59                                                      
REMARK 465     HIS F    60                                                      
REMARK 465     ASP F   119                                                      
REMARK 465     LEU F   120                                                      
REMARK 465     LYS F   121                                                      
REMARK 465     LYS F   122                                                      
REMARK 465     GLU F   123                                                      
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     HIS A  60    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS A  94    CG   CD   CE   NZ                                   
REMARK 470     GLN A 114    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 115    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 116    CG   CD   CE   NZ                                   
REMARK 470     SER A 118    OG                                                  
REMARK 470     LYS B  73    CG   CD   CE   NZ                                   
REMARK 470     LYS B  94    CG   CD   CE   NZ                                   
REMARK 470     GLN C  80    CG   CD   OE1  NE2                                  
REMARK 470     ARG C  83    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C  94    CG   CD   CE   NZ                                   
REMARK 470     SER D  59    OG                                                  
REMARK 470     HIS D  60    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS D  76    CG   CD   CE   NZ                                   
REMARK 470     GLN D 115    CG   CD   OE1  NE2                                  
REMARK 470     LYS D 116    CG   CD   CE   NZ                                   
REMARK 470     HIS E  60    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS E  73    CG   CD   CE   NZ                                   
REMARK 470     ARG E  83    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN E 114    CG   CD   OE1  NE2                                  
REMARK 470     GLN E 115    CG   CD   OE1  NE2                                  
REMARK 470     LYS E 116    CG   CD   CE   NZ                                   
REMARK 470     LEU E 117    CG   CD1  CD2                                       
REMARK 470     ASP E 119    CG   OD1  OD2                                       
REMARK 470     LYS F 116    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OE1  GLN D   114     OE1  GLN D   114     7556     2.03            
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    LEU F 113      -71.81    -61.75                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3A7P   RELATED DB: PDB                                   
DBREF  3A7O A   50   123  UNP    Q03818   ATG16_YEAST     50    123             
DBREF  3A7O B   50   123  UNP    Q03818   ATG16_YEAST     50    123             
DBREF  3A7O C   50   123  UNP    Q03818   ATG16_YEAST     50    123             
DBREF  3A7O D   50   123  UNP    Q03818   ATG16_YEAST     50    123             
DBREF  3A7O E   50   123  UNP    Q03818   ATG16_YEAST     50    123             
DBREF  3A7O F   50   123  UNP    Q03818   ATG16_YEAST     50    123             
SEQADV 3A7O GLY A   49  UNP  Q03818              EXPRESSION TAG                 
SEQADV 3A7O GLY B   49  UNP  Q03818              EXPRESSION TAG                 
SEQADV 3A7O GLY C   49  UNP  Q03818              EXPRESSION TAG                 
SEQADV 3A7O GLY D   49  UNP  Q03818              EXPRESSION TAG                 
SEQADV 3A7O GLY E   49  UNP  Q03818              EXPRESSION TAG                 
SEQADV 3A7O GLY F   49  UNP  Q03818              EXPRESSION TAG                 
SEQRES   1 A   75  GLY SER GLY ALA ILE GLY GLY ASN ILE VAL SER HIS ASP          
SEQRES   2 A   75  ASP ALA LEU LEU ASN THR LEU ALA ILE LEU GLN LYS GLU          
SEQRES   3 A   75  LEU LYS SER LYS GLU GLN GLU ILE ARG ARG LEU LYS GLU          
SEQRES   4 A   75  VAL ILE ALA LEU LYS ASN LYS ASN THR GLU ARG LEU ASN          
SEQRES   5 A   75  ASP GLU LEU ILE SER GLY THR ILE GLU ASN ASN VAL LEU          
SEQRES   6 A   75  GLN GLN LYS LEU SER ASP LEU LYS LYS GLU                      
SEQRES   1 B   75  GLY SER GLY ALA ILE GLY GLY ASN ILE VAL SER HIS ASP          
SEQRES   2 B   75  ASP ALA LEU LEU ASN THR LEU ALA ILE LEU GLN LYS GLU          
SEQRES   3 B   75  LEU LYS SER LYS GLU GLN GLU ILE ARG ARG LEU LYS GLU          
SEQRES   4 B   75  VAL ILE ALA LEU LYS ASN LYS ASN THR GLU ARG LEU ASN          
SEQRES   5 B   75  ASP GLU LEU ILE SER GLY THR ILE GLU ASN ASN VAL LEU          
SEQRES   6 B   75  GLN GLN LYS LEU SER ASP LEU LYS LYS GLU                      
SEQRES   1 C   75  GLY SER GLY ALA ILE GLY GLY ASN ILE VAL SER HIS ASP          
SEQRES   2 C   75  ASP ALA LEU LEU ASN THR LEU ALA ILE LEU GLN LYS GLU          
SEQRES   3 C   75  LEU LYS SER LYS GLU GLN GLU ILE ARG ARG LEU LYS GLU          
SEQRES   4 C   75  VAL ILE ALA LEU LYS ASN LYS ASN THR GLU ARG LEU ASN          
SEQRES   5 C   75  ASP GLU LEU ILE SER GLY THR ILE GLU ASN ASN VAL LEU          
SEQRES   6 C   75  GLN GLN LYS LEU SER ASP LEU LYS LYS GLU                      
SEQRES   1 D   75  GLY SER GLY ALA ILE GLY GLY ASN ILE VAL SER HIS ASP          
SEQRES   2 D   75  ASP ALA LEU LEU ASN THR LEU ALA ILE LEU GLN LYS GLU          
SEQRES   3 D   75  LEU LYS SER LYS GLU GLN GLU ILE ARG ARG LEU LYS GLU          
SEQRES   4 D   75  VAL ILE ALA LEU LYS ASN LYS ASN THR GLU ARG LEU ASN          
SEQRES   5 D   75  ASP GLU LEU ILE SER GLY THR ILE GLU ASN ASN VAL LEU          
SEQRES   6 D   75  GLN GLN LYS LEU SER ASP LEU LYS LYS GLU                      
SEQRES   1 E   75  GLY SER GLY ALA ILE GLY GLY ASN ILE VAL SER HIS ASP          
SEQRES   2 E   75  ASP ALA LEU LEU ASN THR LEU ALA ILE LEU GLN LYS GLU          
SEQRES   3 E   75  LEU LYS SER LYS GLU GLN GLU ILE ARG ARG LEU LYS GLU          
SEQRES   4 E   75  VAL ILE ALA LEU LYS ASN LYS ASN THR GLU ARG LEU ASN          
SEQRES   5 E   75  ASP GLU LEU ILE SER GLY THR ILE GLU ASN ASN VAL LEU          
SEQRES   6 E   75  GLN GLN LYS LEU SER ASP LEU LYS LYS GLU                      
SEQRES   1 F   75  GLY SER GLY ALA ILE GLY GLY ASN ILE VAL SER HIS ASP          
SEQRES   2 F   75  ASP ALA LEU LEU ASN THR LEU ALA ILE LEU GLN LYS GLU          
SEQRES   3 F   75  LEU LYS SER LYS GLU GLN GLU ILE ARG ARG LEU LYS GLU          
SEQRES   4 F   75  VAL ILE ALA LEU LYS ASN LYS ASN THR GLU ARG LEU ASN          
SEQRES   5 F   75  ASP GLU LEU ILE SER GLY THR ILE GLU ASN ASN VAL LEU          
SEQRES   6 F   75  GLN GLN LYS LEU SER ASP LEU LYS LYS GLU                      
FORMUL   7  HOH   *82(H2 O)                                                     
HELIX    1   1 HIS A   60  SER A  118  1                                  59    
HELIX    2   2 ASP B   61  LEU B  113  1                                  53    
HELIX    3   3 HIS C   60  GLU C  109  1                                  50    
HELIX    4   4 SER D   59  LYS D  116  1                                  58    
HELIX    5   5 HIS E   60  ASP E  119  1                                  60    
HELIX    6   6 ASP F   61  LEU F  117  1                                  57    
CRYST1  127.891  127.891   77.808  90.00  90.00  90.00 P 43 21 2    48          
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      0.007819  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007819  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012852        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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