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Database: PDB
Entry: 5XV6
LinkDB: 5XV6
Original site: 5XV6 
HEADER    PROTEIN BINDING                         26-JUN-17   5XV6              
TITLE     CRYSTAL STRUCTURE OF ATG101-ATG13HORMA                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: AUTOPHAGY-RELATED PROTEIN 13;                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 1-190;                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: AUTOPHAGY-RELATED PROTEIN 101;                             
COMPND   8 CHAIN: B;                                                            
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ATG13, KIAA0652;                                               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: ATG101, C12ORF44, PP894;                                       
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    AUTOPHAGY, ATG101, ATG13, HORMA, PROTEIN BINDING                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.-W.KIM,H.K.SONG                                                     
REVDAT   2   16-JAN-19 5XV6    1       JRNL                                     
REVDAT   1   04-JUL-18 5XV6    0                                                
JRNL        AUTH   B.-W.KIM,Y.JIN,J.KIM,J.H.KIM,J.JUNG,S.KANG,I.Y.KIM,J.KIM,    
JRNL        AUTH 2 H.CHEONG,H.K.SONG                                            
JRNL        TITL   THE C-TERMINAL REGION OF ATG101 BRIDGES ULK1 AND PTDINS3K    
JRNL        TITL 2 COMPLEX IN AUTOPHAGY INITIATION.                             
JRNL        REF    AUTOPHAGY                     V.  14  2104 2018              
JRNL        REFN                   ESSN 1554-8635                               
JRNL        PMID   30081750                                                     
JRNL        DOI    10.1080/15548627.2018.1504716                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.46 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.10.1_2155                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.46                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.90                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 19189                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.229                           
REMARK   3   R VALUE            (WORKING SET) : 0.225                           
REMARK   3   FREE R VALUE                     : 0.271                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1918                            
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 49.9093 -  5.9139    0.98     1302   144  0.1967 0.2279        
REMARK   3     2  5.9139 -  4.6951    0.99     1255   141  0.2094 0.2877        
REMARK   3     3  4.6951 -  4.1020    0.98     1238   137  0.1916 0.2126        
REMARK   3     4  4.1020 -  3.7270    0.99     1231   135  0.2087 0.2590        
REMARK   3     5  3.7270 -  3.4600    1.00     1244   140  0.2471 0.2937        
REMARK   3     6  3.4600 -  3.2560    1.00     1222   135  0.2318 0.2537        
REMARK   3     7  3.2560 -  3.0930    1.00     1243   138  0.2570 0.2895        
REMARK   3     8  3.0930 -  2.9584    1.00     1234   138  0.2801 0.3722        
REMARK   3     9  2.9584 -  2.8445    1.00     1232   137  0.2752 0.3822        
REMARK   3    10  2.8445 -  2.7463    1.00     1230   135  0.2889 0.3381        
REMARK   3    11  2.7463 -  2.6605    1.00     1217   135  0.2828 0.3426        
REMARK   3    12  2.6605 -  2.5844    1.00     1229   137  0.2798 0.3638        
REMARK   3    13  2.5844 -  2.5164    1.00     1220   136  0.2892 0.3171        
REMARK   3    14  2.5164 -  2.4550    0.96     1174   130  0.3051 0.3525        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.350            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.120           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 64.06                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 77.54                          
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      :  0.009           3068                                  
REMARK   3   ANGLE     :  1.100           4167                                  
REMARK   3   CHIRALITY :  0.062            498                                  
REMARK   3   PLANARITY :  0.006            526                                  
REMARK   3   DIHEDRAL  : 17.388           1831                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5XV6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-JUL-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300004228.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-DEC-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-17A                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9800                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19228                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.440                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 7.100                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.44                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.48                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.91200                            
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: 5XUY                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.95                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.79                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES (PH7.5), 0.2M MGCL2, 6-8%     
REMARK 280  (W/V) PEG 3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
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   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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       49.89900            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       49.89900            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       42.00950            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       61.74250            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       42.00950            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       61.74250            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       49.89900            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       42.00950            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       61.74250            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       49.89900            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       42.00950            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       61.74250            
REMARK 290   SMTRY3   8  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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2630 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18840 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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 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     MET A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     THR A     3                                                      
REMARK 465     GLY A   145                                                      
REMARK 465     HIS A   146                                                      
REMARK 465     THR B   215                                                      
REMARK 465     LEU B   216                                                      
REMARK 465     ALA B   217                                                      
REMARK 465     LEU B   218                                                      
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     ASP A   4    CG   OD1  OD2                                       
REMARK 470     ASN A   6    CG   OD1  ND2                                       
REMARK 470     SER A   7    OG                                                  
REMARK 470     ARG A  10    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A  40    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A  44    OG                                                  
REMARK 470     ARG A  78    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A  90    CG   CD   OE1  OE2                                  
REMARK 470     ASP A  92    CG   OD1  OD2                                       
REMARK 470     MET A  94    CG   SD   CE                                        
REMARK 470     LYS A 106    CG   CD   CE   NZ                                   
REMARK 470     LYS A 109    CG   CD   CE   NZ                                   
REMARK 470     GLU A 110    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 112    CG   CD   CE   NZ                                   
REMARK 470     ARG A 139    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 143    CG   CD   CE   NZ                                   
REMARK 470     LEU A 151    CG   CD1  CD2                                       
REMARK 470     GLU A 158    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 166    CG   CD   OE1  OE2                                  
REMARK 470     MET B   1    CG   SD   CE                                        
REMARK 470     ARG B   4    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B  18    CG   CD   OE1  OE2                                  
REMARK 470     ARG B  74    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER B  90    OG                                                  
REMARK 470     ASP B  93    CG   OD1  OD2                                       
REMARK 470     LYS B 107    CG   CD   CE   NZ                                   
REMARK 470     ARG B 109    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 137    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 141    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 163    CG   CD   OE1  OE2                                  
REMARK 470     MET B 208    CG   SD   CE                                        
REMARK 470     ARG B 209    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 210    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B 211    CG   CD1  CD2                                       
REMARK 470     ILE B 212    CG1  CG2  CD1                                       
REMARK 470     LYS B 213    CG   CD   CE   NZ                                   
REMARK 470     ASP B 214    CG   OD1  OD2                                       
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   OG1  THR A    46     OD2  ASP A    49              2.17            
REMARK 500   NH2  ARG A   120     OD1  ASN B   160              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  42      119.06   -162.50                                   
REMARK 500    GLU A  90        8.69    -66.26                                   
REMARK 500    LYS A 106       96.16    -64.32                                   
REMARK 500    ASP A 108       95.86   -176.26                                   
REMARK 500    GLU A 158       88.25     59.42                                   
REMARK 500    SER B  68       42.15    -84.26                                   
REMARK 500    ALA B 132      -63.07    -93.93                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 THR B  202     SER B  203                  136.41                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5XV6 A    1   190  UNP    O75143   ATG13_HUMAN      1    190             
DBREF  5XV6 B    1   218  UNP    Q9BSB4   ATGA1_HUMAN      1    218             
SEQADV 5XV6 ALA B   40  UNP  Q9BSB4    LYS    40 ENGINEERED MUTATION            
SEQADV 5XV6 ALA B   41  UNP  Q9BSB4    LYS    41 ENGINEERED MUTATION            
SEQADV 5XV6 ALA B   42  UNP  Q9BSB4    GLU    42 ENGINEERED MUTATION            
SEQRES   1 A  190  MET GLU THR ASP LEU ASN SER GLN ASP ARG LYS ASP LEU          
SEQRES   2 A  190  ASP LYS PHE ILE LYS PHE PHE ALA LEU LYS THR VAL GLN          
SEQRES   3 A  190  VAL ILE VAL GLN ALA ARG LEU GLY GLU LYS ILE CYS THR          
SEQRES   4 A  190  ARG SER SER SER SER PRO THR GLY SER ASP TRP PHE ASN          
SEQRES   5 A  190  LEU ALA ILE LYS ASP ILE PRO GLU VAL THR HIS GLU ALA          
SEQRES   6 A  190  LYS LYS ALA LEU ALA GLY GLN LEU PRO ALA VAL GLY ARG          
SEQRES   7 A  190  SER MET CYS VAL GLU ILE SER LEU LYS THR SER GLU GLY          
SEQRES   8 A  190  ASP SER MET GLU LEU GLU ILE TRP CYS LEU GLU MET ASN          
SEQRES   9 A  190  GLU LYS CYS ASP LYS GLU ILE LYS VAL SER TYR THR VAL          
SEQRES  10 A  190  TYR ASN ARG LEU SER LEU LEU LEU LYS SER LEU LEU ALA          
SEQRES  11 A  190  ILE THR ARG VAL THR PRO ALA TYR ARG LEU SER ARG LYS          
SEQRES  12 A  190  GLN GLY HIS GLU TYR VAL ILE LEU TYR ARG ILE TYR PHE          
SEQRES  13 A  190  GLY GLU VAL GLN LEU SER GLY LEU GLY GLU GLY PHE GLN          
SEQRES  14 A  190  THR VAL ARG VAL GLY THR VAL GLY THR PRO VAL GLY THR          
SEQRES  15 A  190  ILE THR LEU SER CYS ALA TYR ARG                              
SEQRES   1 B  218  MET ASN CYS ARG SER GLU VAL LEU GLU VAL SER VAL GLU          
SEQRES   2 B  218  GLY ARG GLN VAL GLU GLU ALA MET LEU ALA VAL LEU HIS          
SEQRES   3 B  218  THR VAL LEU LEU HIS ARG SER THR GLY LYS PHE HIS TYR          
SEQRES   4 B  218  ALA ALA ALA GLY THR TYR SER ILE GLY THR VAL GLY THR          
SEQRES   5 B  218  GLN ASP VAL ASP CYS ASP PHE ILE ASP PHE THR TYR VAL          
SEQRES   6 B  218  ARG VAL SER SER GLU GLU LEU ASP ARG ALA LEU ARG LYS          
SEQRES   7 B  218  VAL VAL GLY GLU PHE LYS ASP ALA LEU ARG ASN SER GLY          
SEQRES   8 B  218  GLY ASP GLY LEU GLY GLN MET SER LEU GLU PHE TYR GLN          
SEQRES   9 B  218  LYS LYS LYS SER ARG TRP PRO PHE SER ASP GLU CYS ILE          
SEQRES  10 B  218  PRO TRP GLU VAL TRP THR VAL LYS VAL HIS VAL VAL ALA          
SEQRES  11 B  218  LEU ALA THR GLU GLN GLU ARG GLN ILE CYS ARG GLU LYS          
SEQRES  12 B  218  VAL GLY GLU LYS LEU CYS GLU LYS ILE ILE ASN ILE VAL          
SEQRES  13 B  218  GLU VAL MET ASN ARG HIS GLU TYR LEU PRO LYS MET PRO          
SEQRES  14 B  218  THR GLN SER GLU VAL ASP ASN VAL PHE ASP THR GLY LEU          
SEQRES  15 B  218  ARG ASP VAL GLN PRO TYR LEU TYR LYS ILE SER PHE GLN          
SEQRES  16 B  218  ILE THR ASP ALA LEU GLY THR SER VAL THR THR THR MET          
SEQRES  17 B  218  ARG ARG LEU ILE LYS ASP THR LEU ALA LEU                      
HELIX    1 AA1 ASN A    6  ARG A   32  1                                  27    
HELIX    2 AA2 ASP A   49  LEU A   53  5                                   5    
HELIX    3 AA3 ILE A   58  ALA A   70  1                                  13    
HELIX    4 AA4 TYR A  115  VAL A  134  1                                  20    
HELIX    5 AA5 THR A  135  LYS A  143  1                                   9    
HELIX    6 AA6 LEU A  161  GLY A  165  5                                   5    
HELIX    7 AA7 GLN B   16  ARG B   32  1                                  17    
HELIX    8 AA8 SER B   69  ASN B   89  1                                  21    
HELIX    9 AA9 GLU B  134  HIS B  162  1                                  29    
HELIX   10 AB1 GLU B  173  VAL B  177  5                                   5    
HELIX   11 AB2 THR B  205  ASP B  214  1                                  10    
SHEET    1 AA1 5 TYR A 148  GLY A 157  0                                        
SHEET    2 AA1 5 SER A  79  THR A  88 -1  N  GLU A  83   O  ARG A 153           
SHEET    3 AA1 5 SER A  93  ASN A 104 -1  O  LEU A 101   N  MET A  80           
SHEET    4 AA1 5 GLY A 181  TYR A 189 -1  O  THR A 184   N  GLU A 102           
SHEET    5 AA1 5 GLN A 169  THR A 178 -1  N  VAL A 176   O  ILE A 183           
SHEET    1 AA2 4 ARG B   4  GLU B  13  0                                        
SHEET    2 AA2 4 GLU B 115  VAL B 129  1  O  THR B 123   N  LEU B   8           
SHEET    3 AA2 4 LEU B  95  LYS B 106 -1  N  LEU B 100   O  TRP B 122           
SHEET    4 AA2 4 TYR B 190  THR B 197 -1  O  LYS B 191   N  GLU B 101           
SHEET    1 AA3 2 SER B  33  THR B  34  0                                        
SHEET    2 AA3 2 GLN B 186  PRO B 187 -1  O  GLN B 186   N  THR B  34           
SHEET    1 AA4 2 PHE B  37  TYR B  39  0                                        
SHEET    2 AA4 2 TYR B  45  ILE B  47 -1  O  SER B  46   N  HIS B  38           
SHEET    1 AA5 2 THR B  52  ASP B  56  0                                        
SHEET    2 AA5 2 THR B  63  VAL B  67 -1  O  ARG B  66   N  GLN B  53           
CISPEP   1 GLY A  157    GLU A  158          0        -6.40                     
CISPEP   2 TRP B  110    PRO B  111          0        -0.54                     
CRYST1   84.019  123.485   99.798  90.00  90.00  90.00 C 2 2 21      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011902  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008098  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010020        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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