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Database: PDB
Entry: 5JGE
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Original site: 5JGE 
HEADER    PROTEIN TRANSPORT                       20-APR-16   5JGE              
TITLE     CRYSTAL STRUCTURE OF ATG19 COILED-COIL COMPLEXED WITH APE1 PROPEPTIDE 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: AUTOPHAGY-RELATED PROTEIN 19;                              
COMPND   3 CHAIN: A, B, D, E;                                                   
COMPND   4 SYNONYM: CYTOPLASM-TO-VACUOLE TARGETING PROTEIN 19;                  
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: APE1 PROPEPTIDE;                                           
COMPND   8 CHAIN: C, F;                                                         
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   4 ORGANISM_TAXID: 559292;                                              
SOURCE   5 STRAIN: ATCC 204508 / S288C;                                         
SOURCE   6 GENE: ATG19, CVT19, YOL082W, O0980, YOL01;                           
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  11 ORGANISM_TAXID: 4932;                                                
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    RECEPTOR, COMPLEX, PROTEIN TRANSPORT                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.WATANABE,N.N.NODA                                                   
REVDAT   2   13-JUL-16 5JGE    1       JRNL                                     
REVDAT   1   29-JUN-16 5JGE    0                                                
JRNL        AUTH   A.YAMASAKI,Y.WATANABE,W.ADACHI,K.SUZUKI,K.MATOBA,H.KIRISAKO, 
JRNL        AUTH 2 H.KUMETA,H.NAKATOGAWA,Y.OHSUMI,F.INAGAKI,N.N.NODA            
JRNL        TITL   STRUCTURAL BASIS FOR RECEPTOR-MEDIATED SELECTIVE AUTOPHAGY   
JRNL        TITL 2 OF AMINOPEPTIDASE I AGGREGATES                               
JRNL        REF    CELL REP                      V.  16    19 2016              
JRNL        REFN                   ESSN 2211-1247                               
JRNL        PMID   27320913                                                     
JRNL        DOI    10.1016/J.CELREP.2016.05.066                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.91 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0103                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.91                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 55.33                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 12989                          
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) : 0.197                           
REMARK   3   R VALUE            (WORKING SET) : 0.194                           
REMARK   3   FREE R VALUE                     : 0.246                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 686                             
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) : 1.91                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 835                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 82.91                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2570                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 43                           
REMARK   3   BIN FREE R VALUE                    : 0.3120                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1337                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 176                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.72                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.99000                                             
REMARK   3    B22 (A**2) : -1.20000                                             
REMARK   3    B33 (A**2) : 0.99000                                              
REMARK   3    B12 (A**2) : -0.20000                                             
REMARK   3    B13 (A**2) : -1.49000                                             
REMARK   3    B23 (A**2) : 1.72000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.178         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.165         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.124         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.881         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.922                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1346 ; 0.015 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  1399 ; 0.008 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1790 ; 1.633 ; 2.031       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3248 ; 1.775 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   155 ; 4.754 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    65 ;43.373 ;27.846       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   315 ;16.557 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     2 ; 4.213 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   206 ; 0.088 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1438 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   252 ; 0.005 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):   638 ; 1.020 ; 1.819       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   637 ; 1.015 ; 1.818       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):   787 ; 1.627 ; 2.703       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):   788 ; 1.627 ; 2.704       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   708 ; 1.317 ; 1.990       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):   708 ; 1.316 ; 1.990       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  1003 ; 2.166 ; 2.919       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  1678 ; 6.889 ;15.799       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  1586 ; 6.579 ;14.691       
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   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 5                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A   158    181       B   158    181    2078  0.28  0.05     
REMARK   3    2     A   158    184       D   158    184    2700  0.19  0.05     
REMARK   3    3     A   158    184       E   158    184    2324  0.29  0.05     
REMARK   3    4     B   156    181       E   156    181    2580  0.18  0.05     
REMARK   3    5     C    -1     21       F    -1     21    2344  0.14  0.05     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   158        A   185                          
REMARK   3    ORIGIN FOR THE GROUP (A):  28.4950  -4.9490  36.3090              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1286 T22:   0.1759                                     
REMARK   3      T33:   0.0477 T12:  -0.0173                                     
REMARK   3      T13:   0.0256 T23:  -0.0207                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  14.0987 L22:  11.8775                                     
REMARK   3      L33:   7.6859 L12: -10.1275                                     
REMARK   3      L13:   8.6359 L23:  -7.9146                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0030 S12:   0.3991 S13:   0.1645                       
REMARK   3      S21:  -0.3288 S22:   0.0080 S23:  -0.0943                       
REMARK   3      S31:   0.0257 S32:  -0.1472 S33:  -0.0110                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   156        B   182                          
REMARK   3    ORIGIN FOR THE GROUP (A):  24.6690  -7.2590  46.1870              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1022 T22:   0.0592                                     
REMARK   3      T33:   0.1345 T12:  -0.0304                                     
REMARK   3      T13:   0.0137 T23:  -0.0062                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  17.6080 L22:   1.2672                                     
REMARK   3      L33:  10.9057 L12:  -0.5144                                     
REMARK   3      L13:  12.1057 L23:  -0.5658                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0550 S12:   0.5807 S13:  -0.1962                       
REMARK   3      S21:  -0.0313 S22:   0.0598 S23:  -0.1714                       
REMARK   3      S31:  -0.0482 S32:   0.1477 S33:  -0.0048                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    -1        C    21                          
REMARK   3    ORIGIN FOR THE GROUP (A):  31.9380  -0.2140  45.0490              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0670 T22:   0.0871                                     
REMARK   3      T33:   0.0820 T12:  -0.0090                                     
REMARK   3      T13:   0.0296 T23:  -0.0228                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.9108 L22:   3.7002                                     
REMARK   3      L33:   2.1950 L12:  -4.6067                                     
REMARK   3      L13:   3.9001 L23:  -2.5321                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0336 S12:   0.2377 S13:   0.2467                       
REMARK   3      S21:  -0.0207 S22:  -0.0846 S23:   0.0319                       
REMARK   3      S31:  -0.0057 S32:   0.2083 S33:   0.0510                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   156        D   185                          
REMARK   3    ORIGIN FOR THE GROUP (A):  43.9750   7.3560  67.4910              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1362 T22:   0.1584                                     
REMARK   3      T33:   0.0393 T12:   0.0381                                     
REMARK   3      T13:  -0.0220 T23:  -0.0137                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  14.6528 L22:   6.9911                                     
REMARK   3      L33:   5.4330 L12:   8.0723                                     
REMARK   3      L13:  -7.3616 L23:  -4.8604                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1480 S12:  -0.3806 S13:  -0.0094                       
REMARK   3      S21:   0.3481 S22:  -0.0865 S23:   0.0417                       
REMARK   3      S31:  -0.1853 S32:  -0.1321 S33:  -0.0615                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   156        E   185                          
REMARK   3    ORIGIN FOR THE GROUP (A):  37.6820   9.0660  59.1600              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0547 T22:   0.0501                                     
REMARK   3      T33:   0.0573 T12:   0.0149                                     
REMARK   3      T13:  -0.0014 T23:   0.0135                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.7161 L22:   0.4417                                     
REMARK   3      L33:   6.9902 L12:   1.1530                                     
REMARK   3      L13:  -7.0740 L23:  -0.4099                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1348 S12:  -0.3009 S13:  -0.1964                       
REMARK   3      S21:  -0.0683 S22:  -0.0792 S23:  -0.0279                       
REMARK   3      S31:   0.0450 S32:   0.0113 S33:   0.2140                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F    -1        F    21                          
REMARK   3    ORIGIN FOR THE GROUP (A):  46.3020   2.7420  58.6390              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0438 T22:   0.0116                                     
REMARK   3      T33:   0.0476 T12:  -0.0073                                     
REMARK   3      T13:  -0.0271 T23:   0.0067                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.5013 L22:   4.7947                                     
REMARK   3      L33:   1.6402 L12:   5.6535                                     
REMARK   3      L13:  -2.2758 L23:  -1.9229                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0102 S12:  -0.0937 S13:  -0.1059                       
REMARK   3      S21:   0.0002 S22:   0.0095 S23:   0.1549                       
REMARK   3      S31:  -0.0154 S32:  -0.0134 S33:  -0.0197                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5JGE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-APR-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000220544.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-FEB-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 95                                 
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : AR-NE3A                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000, 0.9792                     
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13677                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 55.330                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.4                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.93                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.45800                            
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: SAD                          
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.35                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% (W/V) PEG 4000, 200 MM SODIUM        
REMARK 280  ACETATE, 100 MM TRIS-HCL, PH 8.5, VAPOR DIFFUSION, SITTING DROP,    
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2830 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 6090 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3040 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 6110 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, 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 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   156                                                      
REMARK 465     PRO A   157                                                      
REMARK 465     LYS A   186                                                      
REMARK 465     GLU A   187                                                      
REMARK 465     VAL B   183                                                      
REMARK 465     THR B   184                                                      
REMARK 465     ASN B   185                                                      
REMARK 465     LYS B   186                                                      
REMARK 465     GLU B   187                                                      
REMARK 465     LYS D   186                                                      
REMARK 465     GLU D   187                                                      
REMARK 465     LYS E   186                                                      
REMARK 465     GLU E   187                                                      
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   180     NE2  GLN B   181              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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   O    HOH B   210     O    HOH F   128     1455     2.11            
REMARK 500   O    HOH B   201     O    HOH C   101     1455     2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5JGF   RELATED DB: PDB                                   
DBREF  5JGE A  160   187  UNP    P35193   ATG19_YEAST    160    187             
DBREF  5JGE B  160   187  UNP    P35193   ATG19_YEAST    160    187             
DBREF  5JGE C   -1    21  PDB    5JGE     5JGE            -1     21             
DBREF  5JGE D  160   187  UNP    P35193   ATG19_YEAST    160    187             
DBREF  5JGE E  160   187  UNP    P35193   ATG19_YEAST    160    187             
DBREF  5JGE F   -1    21  PDB    5JGE     5JGE            -1     21             
SEQADV 5JGE GLY A  156  UNP  P35193              EXPRESSION TAG                 
SEQADV 5JGE PRO A  157  UNP  P35193              EXPRESSION TAG                 
SEQADV 5JGE HIS A  158  UNP  P35193              EXPRESSION TAG                 
SEQADV 5JGE MET A  159  UNP  P35193              EXPRESSION TAG                 
SEQADV 5JGE GLY B  156  UNP  P35193              EXPRESSION TAG                 
SEQADV 5JGE PRO B  157  UNP  P35193              EXPRESSION TAG                 
SEQADV 5JGE HIS B  158  UNP  P35193              EXPRESSION TAG                 
SEQADV 5JGE MET B  159  UNP  P35193              EXPRESSION TAG                 
SEQADV 5JGE GLY D  156  UNP  P35193              EXPRESSION TAG                 
SEQADV 5JGE PRO D  157  UNP  P35193              EXPRESSION TAG                 
SEQADV 5JGE HIS D  158  UNP  P35193              EXPRESSION TAG                 
SEQADV 5JGE MET D  159  UNP  P35193              EXPRESSION TAG                 
SEQADV 5JGE GLY E  156  UNP  P35193              EXPRESSION TAG                 
SEQADV 5JGE PRO E  157  UNP  P35193              EXPRESSION TAG                 
SEQADV 5JGE HIS E  158  UNP  P35193              EXPRESSION TAG                 
SEQADV 5JGE MET E  159  UNP  P35193              EXPRESSION TAG                 
SEQRES   1 A   32  GLY PRO HIS MET LEU ASP ASN PHE MET LYS GLN LEU LEU          
SEQRES   2 A   32  LYS LEU GLU GLU SER LEU ASN LYS LEU GLU LEU GLU GLN          
SEQRES   3 A   32  LYS VAL THR ASN LYS GLU                                      
SEQRES   1 B   32  GLY PRO HIS MET LEU ASP ASN PHE MET LYS GLN LEU LEU          
SEQRES   2 B   32  LYS LEU GLU GLU SER LEU ASN LYS LEU GLU LEU GLU GLN          
SEQRES   3 B   32  LYS VAL THR ASN LYS GLU                                      
SEQRES   1 C   23  GLY PRO MET GLU GLU GLN ARG GLU ILE LEU GLU GLN LEU          
SEQRES   2 C   23  LYS LYS THR LEU GLN MET LEU THR VAL TYR                      
SEQRES   1 D   32  GLY PRO HIS MET LEU ASP ASN PHE MET LYS GLN LEU LEU          
SEQRES   2 D   32  LYS LEU GLU GLU SER LEU ASN LYS LEU GLU LEU GLU GLN          
SEQRES   3 D   32  LYS VAL THR ASN LYS GLU                                      
SEQRES   1 E   32  GLY PRO HIS MET LEU ASP ASN PHE MET LYS GLN LEU LEU          
SEQRES   2 E   32  LYS LEU GLU GLU SER LEU ASN LYS LEU GLU LEU GLU GLN          
SEQRES   3 E   32  LYS VAL THR ASN LYS GLU                                      
SEQRES   1 F   23  GLY PRO MET GLU GLU GLN ARG GLU ILE LEU GLU GLN LEU          
SEQRES   2 F   23  LYS LYS THR LEU GLN MET LEU THR VAL TYR                      
FORMUL   7  HOH   *176(H2 O)                                                    
HELIX    1 AA1 LEU A  160  ASN A  185  1                                  26    
HELIX    2 AA2 PRO B  157  LYS B  182  1                                  26    
HELIX    3 AA3 PRO C    0  LEU C   18  1                                  19    
HELIX    4 AA4 MET D  159  ASN D  185  1                                  27    
HELIX    5 AA5 PRO E  157  ASN E  185  1                                  29    
HELIX    6 AA6 PRO F    0  LEU F   18  1                                  19    
CRYST1   27.875   32.921   56.957  87.19  76.52  67.10 P 1           4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.035874 -0.015152 -0.009315        0.00000                         
SCALE2      0.000000  0.032974  0.001536        0.00000                         
SCALE3      0.000000  0.000000  0.018074        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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