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Database: PDB
Entry: 4GDL
LinkDB: 4GDL
Original site: 4GDL 
HEADER    PROTEIN BINDING                         31-JUL-12   4GDL              
TITLE     CRYSTAL STRUCTURE OF HUMAN ATG12~ATG5 CONJUGATE IN COMPLEX WITH AN N- 
TITLE    2 TERMINAL FRAGMENT OF ATG16L1                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UBIQUITIN-LIKE PROTEIN ATG12;                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: AUTOPHAGY-RELATED PROTEIN 12, APG12-LIKE;                   
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: AUTOPHAGY PROTEIN 5;                                       
COMPND   8 CHAIN: B;                                                            
COMPND   9 SYNONYM: APG5-LIKE, APOPTOSIS-SPECIFIC PROTEIN;                      
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: AUTOPHAGY-RELATED PROTEIN 16-1;                            
COMPND  13 CHAIN: C;                                                            
COMPND  14 SYNONYM: APG16-LIKE 1;                                               
COMPND  15 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: APG12, APG12L, ATG12;                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PACYC DUET-1;                             
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: APG5L, ASP, ATG5;                                              
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PACYC DUET-1;                             
SOURCE  21 MOL_ID: 3;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  23 ORGANISM_COMMON: HUMAN;                                              
SOURCE  24 ORGANISM_TAXID: 9606;                                                
SOURCE  25 GENE: APG16L, ATG16L1, UNQ9393/PRO34307;                             
SOURCE  26 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  27 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  28 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  29 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  30 EXPRESSION_SYSTEM_PLASMID: PET                                       
KEYWDS    PROTEIN-PROTEIN CONJUGATE, PROTEIN-PROTEIN COMPLEX, UBIQUITIN-LIKE    
KEYWDS   2 PROTEIN, AUTOPHAGY, E3 LIGASE, UBIQUITIN-LIKE FOLD, STRUCTURAL       
KEYWDS   3 PROTEIN, ISOPEPTIDE BOND, CYTOPLASM AND AUTOPHAGOSOMAL MEMBRANES,    
KEYWDS   4 PROTEIN BINDING                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.OTOMO,Z.METLAGEL,G.TAKAESU,T.OTOMO                                  
REVDAT   4   15-NOV-17 4GDL    1       REMARK                                   
REVDAT   3   16-JAN-13 4GDL    1       JRNL                                     
REVDAT   2   02-JAN-13 4GDL    1       JRNL                                     
REVDAT   1   05-DEC-12 4GDL    0                                                
JRNL        AUTH   C.OTOMO,Z.METLAGEL,G.TAKAESU,T.OTOMO                         
JRNL        TITL   STRUCTURE OF THE HUMAN ATG12~ATG5 CONJUGATE REQUIRED FOR LC3 
JRNL        TITL 2 LIPIDATION IN AUTOPHAGY.                                     
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  20    59 2013              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   23202584                                                     
JRNL        DOI    10.1038/NSMB.2431                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.88 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.8_1069                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.88                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.22                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 12465                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.219                           
REMARK   3   R VALUE            (WORKING SET) : 0.215                           
REMARK   3   FREE R VALUE                     : 0.254                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.130                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1263                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 36.2267 -  5.9729    0.99     1308   151  0.2006 0.2450        
REMARK   3     2  5.9729 -  4.7442    1.00     1287   148  0.2030 0.2265        
REMARK   3     3  4.7442 -  4.1455    1.00     1267   142  0.1802 0.2081        
REMARK   3     4  4.1455 -  3.7669    0.99     1269   141  0.2207 0.2620        
REMARK   3     5  3.7669 -  3.4971    0.99     1258   145  0.2354 0.3062        
REMARK   3     6  3.4971 -  3.2911    0.99     1253   133  0.2514 0.2919        
REMARK   3     7  3.2911 -  3.1264    0.98     1257   141  0.2506 0.2864        
REMARK   3     8  3.1264 -  2.9903    0.97     1222   136  0.3040 0.3126        
REMARK   3     9  2.9903 -  2.8753    0.86     1081   126  0.3301 0.4281        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.00                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.320            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.840           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 138.7                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           3316                                  
REMARK   3   ANGLE     :  0.510           4482                                  
REMARK   3   CHIRALITY :  0.037            479                                  
REMARK   3   PLANARITY :  0.003            566                                  
REMARK   3   DIHEDRAL  :  9.914           1256                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 9                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 53:61)                           
REMARK   3    ORIGIN FOR THE GROUP (A): 131.9098  14.7466  14.7212              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8731 T22:   1.5639                                     
REMARK   3      T33:   1.5721 T12:   0.5559                                     
REMARK   3      T13:   0.1543 T23:   0.5159                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6238 L22:   3.2452                                     
REMARK   3      L33:   6.0662 L12:   2.7977                                     
REMARK   3      L13:   0.6736 L23:   0.8570                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.9306 S12:   1.6393 S13:   1.6291                       
REMARK   3      S21:  -1.4487 S22:   0.1603 S23:   1.6733                       
REMARK   3      S31:  -0.2069 S32:  -1.6583 S33:   0.8281                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 62:91)                           
REMARK   3    ORIGIN FOR THE GROUP (A): 129.9928   6.0654  15.7652              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6716 T22:   1.8883                                     
REMARK   3      T33:   1.1547 T12:   0.1147                                     
REMARK   3      T13:  -0.2917 T23:  -0.1696                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.2938 L22:   3.7272                                     
REMARK   3      L33:   5.8908 L12:  -3.3147                                     
REMARK   3      L13:  -4.1637 L23:  -0.7557                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3887 S12:   1.6713 S13:  -0.3986                       
REMARK   3      S21:  -0.4764 S22:  -0.5727 S23:   0.9357                       
REMARK   3      S31:  -0.0244 S32:  -2.8717 S33:   0.0498                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 92:104)                          
REMARK   3    ORIGIN FOR THE GROUP (A): 133.6834  -2.2909  12.3846              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1311 T22:   1.3008                                     
REMARK   3      T33:   1.5979 T12:  -0.1251                                     
REMARK   3      T13:   0.0261 T23:  -0.1878                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.5054 L22:   3.8222                                     
REMARK   3      L33:   3.2700 L12:   4.9979                                     
REMARK   3      L13:  -2.7965 L23:  -1.8131                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.4633 S12:   0.6937 S13:  -2.0906                       
REMARK   3      S21:  -1.9660 S22:   1.1251 S23:  -0.2622                       
REMARK   3      S31:   1.6633 S32:   0.6728 S33:   0.3787                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 105:134)                         
REMARK   3    ORIGIN FOR THE GROUP (A): 140.0424  11.9384  13.0095              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9782 T22:   1.6464                                     
REMARK   3      T33:   1.2002 T12:   0.2414                                     
REMARK   3      T13:  -0.1224 T23:   0.1838                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.7311 L22:   8.8877                                     
REMARK   3      L33:   3.3538 L12:   7.6172                                     
REMARK   3      L13:  -0.5108 L23:   2.8401                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3554 S12:   1.6975 S13:   0.9582                       
REMARK   3      S21:  -1.0900 S22:   0.8627 S23:   0.3778                       
REMARK   3      S31:  -1.1970 S32:   0.2940 S33:  -0.6039                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 135:140)                         
REMARK   3    ORIGIN FOR THE GROUP (A): 140.1161  -0.3734   4.6258              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5600 T22:   2.3461                                     
REMARK   3      T33:   1.7240 T12:   0.3194                                     
REMARK   3      T13:  -0.2346 T23:  -0.1557                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7752 L22:   9.6962                                     
REMARK   3      L33:   2.3201 L12:   5.6888                                     
REMARK   3      L13:  -0.1132 L23:   1.3887                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0168 S12:   2.3705 S13:   0.7689                       
REMARK   3      S21:  -1.8665 S22:   0.8880 S23:   0.5925                       
REMARK   3      S31:  -0.1597 S32:  -1.8648 S33:   0.0609                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 3:117)                           
REMARK   3    ORIGIN FOR THE GROUP (A): 158.9248  -6.7631  28.9032              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6411 T22:   0.9328                                     
REMARK   3      T33:   0.9535 T12:  -0.0160                                     
REMARK   3      T13:   0.0173 T23:  -0.2245                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.0139 L22:   6.3927                                     
REMARK   3      L33:   7.1094 L12:  -1.4957                                     
REMARK   3      L13:   1.3425 L23:  -2.9860                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2765 S12:   0.2747 S13:  -1.2077                       
REMARK   3      S21:  -0.3156 S22:  -0.0774 S23:   0.9176                       
REMARK   3      S31:   0.7319 S32:  -0.3263 S33:   0.0475                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 118:173)                         
REMARK   3    ORIGIN FOR THE GROUP (A): 157.4494   3.1499   6.6807              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1155 T22:   2.5459                                     
REMARK   3      T33:   0.9501 T12:   0.0125                                     
REMARK   3      T13:  -0.1655 T23:  -0.2036                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2388 L22:   3.7026                                     
REMARK   3      L33:   6.3635 L12:  -2.2128                                     
REMARK   3      L13:   0.0823 L23:  -3.8407                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3081 S12:   3.5878 S13:  -0.2294                       
REMARK   3      S21:  -0.8773 S22:  -0.0315 S23:   0.2101                       
REMARK   3      S31:   0.2615 S32:   1.0743 S33:  -0.4028                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 174:274)                         
REMARK   3    ORIGIN FOR THE GROUP (A): 158.9984  18.7852  20.0348              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8807 T22:   0.9552                                     
REMARK   3      T33:   1.0515 T12:  -0.0844                                     
REMARK   3      T13:  -0.0671 T23:   0.4015                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.8884 L22:   4.0508                                     
REMARK   3      L33:   2.8113 L12:  -0.0630                                     
REMARK   3      L13:   1.7123 L23:   1.5365                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4282 S12:   1.7108 S13:   2.1212                       
REMARK   3      S21:  -0.3057 S22:   0.1234 S23:   0.0233                       
REMARK   3      S31:  -0.6817 S32:   0.4777 S33:   0.2267                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESSEQ 10:43)                           
REMARK   3    ORIGIN FOR THE GROUP (A): 175.8442   3.7178  25.6581              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7444 T22:   1.4281                                     
REMARK   3      T33:   0.7622 T12:  -0.0613                                     
REMARK   3      T13:   0.2367 T23:   0.0818                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.7345 L22:   3.2343                                     
REMARK   3      L33:   4.4717 L12:  -4.1351                                     
REMARK   3      L13:   4.4435 L23:  -2.2397                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0006 S12:   0.9326 S13:   1.0446                       
REMARK   3      S21:  -0.1225 S22:  -0.4194 S23:  -0.4746                       
REMARK   3      S31:  -0.1523 S32:   0.8516 S33:   0.7474                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4GDL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-AUG-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000074049.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-NOV-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0092                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12548                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.875                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : 4.400                              
REMARK 200  R MERGE                    (I) : 0.05600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.54100                            
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.38                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.96                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN: 10 MG/ML IN 0.01M HEPES PH      
REMARK 280  7.0, 0.3 M NACL, 0.001 M DTT; RESERVOIR: 0.1M BICINE PH9.0, 0.2     
REMARK 280  M SODIUM PHOSPHATE DIBASIC, 18% PEG 3350, VAPOR DIFFUSION,          
REMARK 280  HANGING DROP, TEMPERATURE 293K, VAPOR DIFFUSION, HANGING DROP,      
REMARK 280  PH 6.5                                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       68.30050            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       29.19950            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       68.30050            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       29.19950            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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 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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 THERE IS AN ISOPEPTIDE LINKAGE BETWEEN RESIDUE GLY140 OF ATG12 AND   
REMARK 400 LYS130 OF ATG5. THE ATG12~ATG5 CONJUGATE WAS GENERATED BY CO-        
REMARK 400 EXPRESSING ATG12 AND ATG5 FROM PACYC DUET-1 AND ATG7 AND ATG10 FROM  
REMARK 400 PCDF DUET-1 IN E. COLI                                               
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    50                                                      
REMARK 465     SER A    51                                                      
REMARK 465     LYS A    52                                                      
REMARK 465     MET B     1                                                      
REMARK 465     THR B     2                                                      
REMARK 465     ASP B   228                                                      
REMARK 465     PRO B   229                                                      
REMARK 465     GLU B   230                                                      
REMARK 465     ASP B   231                                                      
REMARK 465     GLY B   232                                                      
REMARK 465     GLU B   233                                                      
REMARK 465     LYS B   234                                                      
REMARK 465     ASP B   275                                                      
REMARK 465     SER C     8                                                      
REMARK 465     HIS C     9                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 107      -60.10   -133.91                                   
REMARK 500    SER B  43     -164.54   -107.38                                   
REMARK 500    SER B  66     -144.37   -146.50                                   
REMARK 500    PHE B 104      -38.90   -140.11                                   
REMARK 500    GLN B 191      118.20   -166.06                                   
REMARK 500    CYS B 223       65.91   -156.28                                   
REMARK 500    ALA B 226       17.75   -159.42                                   
REMARK 500    LEU B 265       75.59   -101.67                                   
REMARK 500    PRO B 273     -163.49    -61.62                                   
REMARK 500    GLN C  28      -67.83   -108.70                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 301  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA B  95   O                                                      
REMARK 620 2 ASN B  99   OD1 152.4                                              
REMARK 620 3 PRO B  97   O    82.7  92.8                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 301                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4GDK   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF THE SAME COMPLEX IN A DIFFERENT SPACE GROUP.        
DBREF  4GDL A   52   140  UNP    O94817   ATG12_HUMAN     52    140             
DBREF  4GDL B    1   275  UNP    Q9H1Y0   ATG5_HUMAN       1    275             
DBREF  4GDL C   11    43  UNP    Q676U5   A16L1_HUMAN     11     43             
SEQADV 4GDL GLY A   50  UNP  O94817              EXPRESSION TAG                 
SEQADV 4GDL SER A   51  UNP  O94817              EXPRESSION TAG                 
SEQADV 4GDL SER C    8  UNP  Q676U5              EXPRESSION TAG                 
SEQADV 4GDL HIS C    9  UNP  Q676U5              EXPRESSION TAG                 
SEQADV 4GDL MET C   10  UNP  Q676U5              EXPRESSION TAG                 
SEQRES   1 A   91  GLY SER LYS LYS LYS ILE ASP ILE LEU LEU LYS ALA VAL          
SEQRES   2 A   91  GLY ASP THR PRO ILE MET LYS THR LYS LYS TRP ALA VAL          
SEQRES   3 A   91  GLU ARG THR ARG THR ILE GLN GLY LEU ILE ASP PHE ILE          
SEQRES   4 A   91  LYS LYS PHE LEU LYS LEU VAL ALA SER GLU GLN LEU PHE          
SEQRES   5 A   91  ILE TYR VAL ASN GLN SER PHE ALA PRO SER PRO ASP GLN          
SEQRES   6 A   91  GLU VAL GLY THR LEU TYR GLU CYS PHE GLY SER ASP GLY          
SEQRES   7 A   91  LYS LEU VAL LEU HIS TYR CYS LYS SER GLN ALA TRP GLY          
SEQRES   1 B  275  MET THR ASP ASP LYS ASP VAL LEU ARG ASP VAL TRP PHE          
SEQRES   2 B  275  GLY ARG ILE PRO THR CYS PHE THR LEU TYR GLN ASP GLU          
SEQRES   3 B  275  ILE THR GLU ARG GLU ALA GLU PRO TYR TYR LEU LEU LEU          
SEQRES   4 B  275  PRO ARG VAL SER TYR LEU THR LEU VAL THR ASP LYS VAL          
SEQRES   5 B  275  LYS LYS HIS PHE GLN LYS VAL MET ARG GLN GLU ASP ILE          
SEQRES   6 B  275  SER GLU ILE TRP PHE GLU TYR GLU GLY THR PRO LEU LYS          
SEQRES   7 B  275  TRP HIS TYR PRO ILE GLY LEU LEU PHE ASP LEU LEU ALA          
SEQRES   8 B  275  SER SER SER ALA LEU PRO TRP ASN ILE THR VAL HIS PHE          
SEQRES   9 B  275  LYS SER PHE PRO GLU LYS ASP LEU LEU HIS CYS PRO SER          
SEQRES  10 B  275  LYS ASP ALA ILE GLU ALA HIS PHE MET SER CYS MET LYS          
SEQRES  11 B  275  GLU ALA ASP ALA LEU LYS HIS LYS SER GLN VAL ILE ASN          
SEQRES  12 B  275  GLU MET GLN LYS LYS ASP HIS LYS GLN LEU TRP MET GLY          
SEQRES  13 B  275  LEU GLN ASN ASP ARG PHE ASP GLN PHE TRP ALA ILE ASN          
SEQRES  14 B  275  ARG LYS LEU MET GLU TYR PRO ALA GLU GLU ASN GLY PHE          
SEQRES  15 B  275  ARG TYR ILE PRO PHE ARG ILE TYR GLN THR THR THR GLU          
SEQRES  16 B  275  ARG PRO PHE ILE GLN LYS LEU PHE ARG PRO VAL ALA ALA          
SEQRES  17 B  275  ASP GLY GLN LEU HIS THR LEU GLY ASP LEU LEU LYS GLU          
SEQRES  18 B  275  VAL CYS PRO SER ALA ILE ASP PRO GLU ASP GLY GLU LYS          
SEQRES  19 B  275  LYS ASN GLN VAL MET ILE HIS GLY ILE GLU PRO MET LEU          
SEQRES  20 B  275  GLU THR PRO LEU GLN TRP LEU SER GLU HIS LEU SER TYR          
SEQRES  21 B  275  PRO ASP ASN PHE LEU HIS ILE SER ILE ILE PRO GLN PRO          
SEQRES  22 B  275  THR ASP                                                      
SEQRES   1 C   36  SER HIS MET PRO ARG TRP LYS ARG HIS ILE SER GLU GLN          
SEQRES   2 C   36  LEU ARG ARG ARG ASP ARG LEU GLN ARG GLN ALA PHE GLU          
SEQRES   3 C   36  GLU ILE ILE LEU GLN TYR ASN LYS LEU LEU                      
HET     NA  B 301       1                                                       
HETNAM      NA SODIUM ION                                                       
FORMUL   4   NA    NA 1+                                                        
HELIX    1   1 THR A   80  LEU A   92  1                                  13    
HELIX    2   2 GLU A  115  GLY A  124  1                                  10    
HELIX    3   3 ASP B    4  PHE B   13  1                                  10    
HELIX    4   4 TYR B   44  VAL B   48  5                                   5    
HELIX    5   5 ASP B   50  LYS B   58  1                                   9    
HELIX    6   6 PRO B   82  ALA B   91  1                                  10    
HELIX    7   7 SER B  117  LYS B  138  1                                  22    
HELIX    8   8 GLN B  146  ASN B  159  1                                  14    
HELIX    9   9 ARG B  161  ARG B  170  1                                  10    
HELIX   10  10 LYS B  171  GLU B  174  5                                   4    
HELIX   11  11 THR B  214  CYS B  223  1                                  10    
HELIX   12  12 PRO B  250  LEU B  258  1                                   9    
HELIX   13  13 PRO C   11  GLN C   28  1                                  18    
HELIX   14  14 GLN C   28  LEU C   42  1                                  15    
SHEET    1   A 4 LYS A  72  GLU A  76  0                                        
SHEET    2   A 4 LYS A  54  ALA A  61 -1  N  ILE A  57   O  TRP A  73           
SHEET    3   A 4 LYS A 128  CYS A 134  1  O  LEU A 131   N  LEU A  58           
SHEET    4   A 4 PHE A 101  VAL A 104 -1  N  PHE A 101   O  CYS A 134           
SHEET    1   B 5 TYR B  35  PRO B  40  0                                        
SHEET    2   B 5 ARG B  15  LEU B  22 -1  N  PHE B  20   O  TYR B  35           
SHEET    3   B 5 TRP B  98  HIS B 103  1  O  TRP B  98   N  PRO B  17           
SHEET    4   B 5 TRP B  69  TYR B  72 -1  N  GLU B  71   O  THR B 101           
SHEET    5   B 5 THR B  75  PRO B  76 -1  O  THR B  75   N  TYR B  72           
SHEET    1   C 3 PHE B 187  TYR B 190  0                                        
SHEET    2   C 3 LEU B 265  PRO B 271  1  O  ILE B 267   N  TYR B 190           
SHEET    3   C 3 ASN B 236  MET B 239 -1  N  GLN B 237   O  ILE B 270           
LINK         O   ALA B  95                NA    NA B 301     1555   1555  2.25  
LINK         OD1 ASN B  99                NA    NA B 301     1555   1555  2.41  
LINK         O   PRO B  97                NA    NA B 301     1555   1555  2.68  
LINK         C   GLY A 140                 NZ  LYS B 130     1555   1555  1.33  
CISPEP   1 GLY A   63    ASP A   64          0         2.84                     
CISPEP   2 LEU B   96    PRO B   97          0        -4.26                     
SITE     1 AC1  3 ALA B  95  PRO B  97  ASN B  99                               
CRYST1  136.601   58.399   91.802  90.00 130.04  90.00 C 1 2 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      0.007321  0.000000  0.006151        0.00000                         
SCALE2      0.000000  0.017124  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014228        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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