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Database: PDB
Entry: 5XUY
LinkDB: 5XUY
Original site: 5XUY 
HEADER    PROTEIN BINDING                         26-JUN-17   5XUY              
TITLE     CRYSTAL STRUCTURE OF ATG101-ATG13HORMA                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: AUTOPHAGY-RELATED PROTEIN 13;                              
COMPND   3 CHAIN: A, C;                                                         
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, D;                                                         
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 5XUY    1       JRNL                                     
REVDAT   1   04-JUL-18 5XUY    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.    2.20 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) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 31.46                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 53556                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.239                           
REMARK   3   R VALUE            (WORKING SET) : 0.237                           
REMARK   3   FREE R VALUE                     : 0.275                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.730                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1998                            
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 31.4668 -  5.2872    0.90     3422   132  0.2043 0.2451        
REMARK   3     2  5.2872 -  4.1998    0.99     3703   144  0.1832 0.2034        
REMARK   3     3  4.1998 -  3.6698    0.99     3712   144  0.2056 0.2515        
REMARK   3     4  3.6698 -  3.3347    1.00     3734   144  0.2289 0.2426        
REMARK   3     5  3.3347 -  3.0959    1.00     3755   147  0.2481 0.2889        
REMARK   3     6  3.0959 -  2.9135    1.00     3700   143  0.2602 0.3290        
REMARK   3     7  2.9135 -  2.7677    1.00     3730   144  0.2648 0.3414        
REMARK   3     8  2.7677 -  2.6473    1.00     3695   143  0.2748 0.3471        
REMARK   3     9  2.6473 -  2.5454    1.00     3729   145  0.2879 0.3104        
REMARK   3    10  2.5454 -  2.4576    1.00     3710   144  0.3185 0.3850        
REMARK   3    11  2.4576 -  2.3808    1.00     3693   143  0.3521 0.3867        
REMARK   3    12  2.3808 -  2.3128    1.00     3725   145  0.3802 0.4253        
REMARK   3    13  2.3128 -  2.2519    0.99     3678   141  0.4343 0.4954        
REMARK   3    14  2.2519 -  2.1970    0.97     3572   139  0.4716 0.4831        
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)     : 0.430            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 37.040           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 52.95                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 79.47                          
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      :  0.004           6037                                  
REMARK   3   ANGLE     :  0.700           8192                                  
REMARK   3   CHIRALITY :  0.044            974                                  
REMARK   3   PLANARITY :  0.004           1035                                  
REMARK   3   DIHEDRAL  : 14.339           3602                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  63.7379  28.7810 221.3517              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3030 T22:   0.3816                                     
REMARK   3      T33:   0.3846 T12:   0.0008                                     
REMARK   3      T13:  -0.0120 T23:  -0.0114                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2575 L22:   2.2236                                     
REMARK   3      L33:   2.1880 L12:   0.2995                                     
REMARK   3      L13:  -0.4286 L23:  -1.7733                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0010 S12:  -0.0048 S13:  -0.0186                       
REMARK   3      S21:  -0.1928 S22:  -0.0772 S23:  -0.0143                       
REMARK   3      S31:   0.2281 S32:  -0.0440 S33:  -0.0025                       
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 5XUY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-JUL-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300004218.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-OCT-14                          
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               : PAL/PLS                            
REMARK 200  BEAMLINE                       : 5C (4A)                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 53628                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
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     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.06200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.24                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.63600                            
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: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.97                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.93                     
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 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       43.99500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       62.58850            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       43.99500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       62.58850            
REMARK 290   SMTRY3   4  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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2660 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18680 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2600 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19290 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     ASP A     4                                                      
REMARK 465     LEU A     5                                                      
REMARK 465     ASP A    92                                                      
REMARK 465     LYS A   112                                                      
REMARK 465     VAL A   113                                                      
REMARK 465     GLY A   145                                                      
REMARK 465     HIS A   146                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLY B    94                                                      
REMARK 465     MET B   208                                                      
REMARK 465     ARG B   209                                                      
REMARK 465     ARG B   210                                                      
REMARK 465     LEU B   211                                                      
REMARK 465     ILE B   212                                                      
REMARK 465     LYS B   213                                                      
REMARK 465     ASP B   214                                                      
REMARK 465     THR B   215                                                      
REMARK 465     LEU B   216                                                      
REMARK 465     ALA B   217                                                      
REMARK 465     LEU B   218                                                      
REMARK 465     MET C     1                                                      
REMARK 465     GLU C     2                                                      
REMARK 465     THR C     3                                                      
REMARK 465     ASP C     4                                                      
REMARK 465     LEU C     5                                                      
REMARK 465     GLY C   145                                                      
REMARK 465     LEU D   216                                                      
REMARK 465     ALA D   217                                                      
REMARK 465     LEU D   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     LYS A  11    CG   CD   CE   NZ                                   
REMARK 470     ARG A  40    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A  44    OG                                                  
REMARK 470     LYS A  67    CG   CD   CE   NZ                                   
REMARK 470     ARG A  78    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  87    CG   CD   CE   NZ                                   
REMARK 470     GLU A  90    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 105    CG   CD   OE1  OE2                                  
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     SER A 114    OG                                                  
REMARK 470     LEU A 140    CG   CD1  CD2                                       
REMARK 470     LYS A 143    CG   CD   CE   NZ                                   
REMARK 470     GLN A 144    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 147    CG   CD   OE1  OE2                                  
REMARK 470     TYR A 148    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU A 151    CG   CD1  CD2                                       
REMARK 470     GLU A 158    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 160    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 166    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 172    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 190    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B   9    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  18    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  71    CG   CD   OE1  OE2                                  
REMARK 470     ARG B  88    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN B  89    CG   OD1  ND2                                       
REMARK 470     SER B  90    OG                                                  
REMARK 470     ASP B  93    CG   OD1  OD2                                       
REMARK 470     LEU B  95    CG   CD1  CD2                                       
REMARK 470     LYS B 107    CG   CD   CE   NZ                                   
REMARK 470     ARG B 109    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 134    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 161    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 163    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 167    CG   CD   CE   NZ                                   
REMARK 470     LEU B 200    CG   CD1  CD2                                       
REMARK 470     SER B 203    OG                                                  
REMARK 470     THR B 205    OG1  CG2                                            
REMARK 470     LYS C  11    CG   CD   CE   NZ                                   
REMARK 470     SER C  44    OG                                                  
REMARK 470     GLU C  60    CG   CD   OE1  OE2                                  
REMARK 470     LYS C  87    CG   CD   CE   NZ                                   
REMARK 470     GLU C  90    CG   CD   OE1  OE2                                  
REMARK 470     ASP C  92    CG   OD1  OD2                                       
REMARK 470     GLU C 105    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 106    CG   CD   CE   NZ                                   
REMARK 470     LYS C 109    CG   CD   CE   NZ                                   
REMARK 470     GLU C 110    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 112    CG   CD   CE   NZ                                   
REMARK 470     VAL C 113    CG1  CG2                                            
REMARK 470     SER C 114    OG                                                  
REMARK 470     ARG C 139    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 158    CG   CD   OE1  OE2                                  
REMARK 470     SER C 162    OG                                                  
REMARK 470     GLU C 166    CG   CD   OE1  OE2                                  
REMARK 470     MET D   1    CG   SD   CE                                        
REMARK 470     GLU D  18    CG   CD   OE1  OE2                                  
REMARK 470     GLU D  70    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 107    CG   CD   CE   NZ                                   
REMARK 470     ARG D 109    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D 134    CG   CD   OE1  OE2                                  
REMARK 470     GLN D 135    CG   CD   OE1  NE2                                  
REMARK 470     LYS D 167    CG   CD   CE   NZ                                   
REMARK 470     LEU D 200    CG   CD1  CD2                                       
REMARK 470     VAL D 204    CG1  CG2                                            
REMARK 470     THR D 205    OG1  CG2                                            
REMARK 470     MET D 208    CG   SD   CE                                        
REMARK 470     ARG D 209    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D 210    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE D 212    CG1  CG2  CD1                                       
REMARK 470     LYS D 213    CG   CD   CE   NZ                                   
REMARK 470     ASP D 214    CG   OD1  OD2                                       
REMARK 470     THR D 215    OG1  CG2                                            
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   ND2  ASN C   104     OG1  THR C   182              2.05            
REMARK 500   O    TYR D   164     O    HOH D   301              2.14            
REMARK 500   NH1  ARG C   153     O    HOH C   201              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU D 131   CB  -  CG  -  CD1 ANGL. DEV. = -22.6 DEGREES          
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  44       78.61   -118.05                                   
REMARK 500    ARG B  15        4.27    -62.26                                   
REMARK 500    ARG B  32       54.57   -109.02                                   
REMARK 500    VAL B 204       41.53    -97.21                                   
REMARK 500    SER C  44       72.78   -118.71                                   
REMARK 500    SER C 114       73.43    -68.66                                   
REMARK 500    TYR C 115      -13.31     94.04                                   
REMARK 500    GLU C 158       75.19     57.37                                   
REMARK 500    ASN D   2       19.17     59.33                                   
REMARK 500    ARG D  32       55.09   -113.10                                   
REMARK 500    ASP D  61       81.72    -62.67                                   
REMARK 500    ALA D 132      -25.12   -144.66                                   
REMARK 500    THR D 197     -163.40   -122.10                                   
REMARK 500    SER D 203       40.41     75.80                                   
REMARK 500    VAL D 204       17.24     49.71                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 327        DISTANCE =  6.07 ANGSTROMS                       
REMARK 525    HOH D 331        DISTANCE =  7.42 ANGSTROMS                       
DBREF  5XUY A    1   190  UNP    O75143   ATG13_HUMAN      1    190             
DBREF  5XUY B    1   218  UNP    Q9BSB4   ATGA1_HUMAN      1    218             
DBREF  5XUY C    1   190  UNP    O75143   ATG13_HUMAN      1    190             
DBREF  5XUY D    1   218  UNP    Q9BSB4   ATGA1_HUMAN      1    218             
SEQADV 5XUY ALA B   40  UNP  Q9BSB4    LYS    40 ENGINEERED MUTATION            
SEQADV 5XUY ALA B   41  UNP  Q9BSB4    LYS    41 ENGINEERED MUTATION            
SEQADV 5XUY ALA B   42  UNP  Q9BSB4    GLU    42 ENGINEERED MUTATION            
SEQADV 5XUY ALA D   40  UNP  Q9BSB4    LYS    40 ENGINEERED MUTATION            
SEQADV 5XUY ALA D   41  UNP  Q9BSB4    LYS    41 ENGINEERED MUTATION            
SEQADV 5XUY ALA D   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                      
SEQRES   1 C  190  MET GLU THR ASP LEU ASN SER GLN ASP ARG LYS ASP LEU          
SEQRES   2 C  190  ASP LYS PHE ILE LYS PHE PHE ALA LEU LYS THR VAL GLN          
SEQRES   3 C  190  VAL ILE VAL GLN ALA ARG LEU GLY GLU LYS ILE CYS THR          
SEQRES   4 C  190  ARG SER SER SER SER PRO THR GLY SER ASP TRP PHE ASN          
SEQRES   5 C  190  LEU ALA ILE LYS ASP ILE PRO GLU VAL THR HIS GLU ALA          
SEQRES   6 C  190  LYS LYS ALA LEU ALA GLY GLN LEU PRO ALA VAL GLY ARG          
SEQRES   7 C  190  SER MET CYS VAL GLU ILE SER LEU LYS THR SER GLU GLY          
SEQRES   8 C  190  ASP SER MET GLU LEU GLU ILE TRP CYS LEU GLU MET ASN          
SEQRES   9 C  190  GLU LYS CYS ASP LYS GLU ILE LYS VAL SER TYR THR VAL          
SEQRES  10 C  190  TYR ASN ARG LEU SER LEU LEU LEU LYS SER LEU LEU ALA          
SEQRES  11 C  190  ILE THR ARG VAL THR PRO ALA TYR ARG LEU SER ARG LYS          
SEQRES  12 C  190  GLN GLY HIS GLU TYR VAL ILE LEU TYR ARG ILE TYR PHE          
SEQRES  13 C  190  GLY GLU VAL GLN LEU SER GLY LEU GLY GLU GLY PHE GLN          
SEQRES  14 C  190  THR VAL ARG VAL GLY THR VAL GLY THR PRO VAL GLY THR          
SEQRES  15 C  190  ILE THR LEU SER CYS ALA TYR ARG                              
SEQRES   1 D  218  MET ASN CYS ARG SER GLU VAL LEU GLU VAL SER VAL GLU          
SEQRES   2 D  218  GLY ARG GLN VAL GLU GLU ALA MET LEU ALA VAL LEU HIS          
SEQRES   3 D  218  THR VAL LEU LEU HIS ARG SER THR GLY LYS PHE HIS TYR          
SEQRES   4 D  218  ALA ALA ALA GLY THR TYR SER ILE GLY THR VAL GLY THR          
SEQRES   5 D  218  GLN ASP VAL ASP CYS ASP PHE ILE ASP PHE THR TYR VAL          
SEQRES   6 D  218  ARG VAL SER SER GLU GLU LEU ASP ARG ALA LEU ARG LYS          
SEQRES   7 D  218  VAL VAL GLY GLU PHE LYS ASP ALA LEU ARG ASN SER GLY          
SEQRES   8 D  218  GLY ASP GLY LEU GLY GLN MET SER LEU GLU PHE TYR GLN          
SEQRES   9 D  218  LYS LYS LYS SER ARG TRP PRO PHE SER ASP GLU CYS ILE          
SEQRES  10 D  218  PRO TRP GLU VAL TRP THR VAL LYS VAL HIS VAL VAL ALA          
SEQRES  11 D  218  LEU ALA THR GLU GLN GLU ARG GLN ILE CYS ARG GLU LYS          
SEQRES  12 D  218  VAL GLY GLU LYS LEU CYS GLU LYS ILE ILE ASN ILE VAL          
SEQRES  13 D  218  GLU VAL MET ASN ARG HIS GLU TYR LEU PRO LYS MET PRO          
SEQRES  14 D  218  THR GLN SER GLU VAL ASP ASN VAL PHE ASP THR GLY LEU          
SEQRES  15 D  218  ARG ASP VAL GLN PRO TYR LEU TYR LYS ILE SER PHE GLN          
SEQRES  16 D  218  ILE THR ASP ALA LEU GLY THR SER VAL THR THR THR MET          
SEQRES  17 D  218  ARG ARG LEU ILE LYS ASP THR LEU ALA LEU                      
FORMUL   5  HOH   *101(H2 O)                                                    
HELIX    1 AA1 SER A    7  ARG A   32  1                                  26    
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  THR A  132  1                                  18    
HELIX    5 AA5 THR A  135  ARG A  142  1                                   8    
HELIX    6 AA6 GLN B   16  ARG B   32  1                                  17    
HELIX    7 AA7 GLU B   71  GLY B   91  1                                  21    
HELIX    8 AA8 THR B  133  HIS B  162  1                                  30    
HELIX    9 AA9 GLU B  173  VAL B  177  5                                   5    
HELIX   10 AB1 SER C    7  ARG C   32  1                                  26    
HELIX   11 AB2 ASP C   49  LEU C   53  5                                   5    
HELIX   12 AB3 ILE C   58  ALA C   70  1                                  13    
HELIX   13 AB4 TYR C  115  THR C  132  1                                  18    
HELIX   14 AB5 THR C  135  ARG C  142  1                                   8    
HELIX   15 AB6 LEU C  161  GLY C  165  5                                   5    
HELIX   16 AB7 GLN D   16  ARG D   32  1                                  17    
HELIX   17 AB8 SER D   69  SER D   90  1                                  22    
HELIX   18 AB9 THR D  133  ASN D  160  1                                  28    
HELIX   19 AC1 GLU D  173  VAL D  177  5                                   5    
HELIX   20 AC2 THR D  205  THR D  215  1                                  11    
SHEET    1 AA1 5 ILE A 150  GLY A 157  0                                        
SHEET    2 AA1 5 SER A  79  LEU A  86 -1  N  SER A  79   O  GLY A 157           
SHEET    3 AA1 5 MET A  94  MET A 103 -1  O  GLU A  97   N  ILE A  84           
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  GLY A 174   O  LEU A 185           
SHEET    1 AA2 4 ARG B   4  GLU B  13  0                                        
SHEET    2 AA2 4 GLU B 115  VAL B 129  1  O  HIS B 127   N  VAL B  10           
SHEET    3 AA2 4 GLY B  96  LYS B 106 -1  N  PHE B 102   O  GLU B 120           
SHEET    4 AA2 4 TYR B 190  ILE B 196 -1  O  SER B 193   N  SER B  99           
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  TYR B  64   N  VAL B  55           
SHEET    1 AA6 5 TYR C 148  GLY C 157  0                                        
SHEET    2 AA6 5 SER C  79  THR C  88 -1  N  GLU C  83   O  ARG C 153           
SHEET    3 AA6 5 SER C  93  ASN C 104 -1  O  LEU C 101   N  MET C  80           
SHEET    4 AA6 5 GLY C 181  TYR C 189 -1  O  THR C 184   N  GLU C 102           
SHEET    5 AA6 5 GLN C 169  THR C 178 -1  N  GLN C 169   O  TYR C 189           
SHEET    1 AA7 4 ARG D   4  GLU D  13  0                                        
SHEET    2 AA7 4 GLU D 115  VAL D 129  1  O  THR D 123   N  GLU D   6           
SHEET    3 AA7 4 LEU D  95  LYS D 106 -1  N  LEU D 100   O  TRP D 122           
SHEET    4 AA7 4 TYR D 190  ILE D 196 -1  O  SER D 193   N  SER D  99           
SHEET    1 AA8 2 SER D  33  THR D  34  0                                        
SHEET    2 AA8 2 GLN D 186  PRO D 187 -1  O  GLN D 186   N  THR D  34           
SHEET    1 AA9 2 PHE D  37  TYR D  39  0                                        
SHEET    2 AA9 2 TYR D  45  ILE D  47 -1  O  SER D  46   N  HIS D  38           
SHEET    1 AB1 2 THR D  52  ASP D  56  0                                        
SHEET    2 AB1 2 THR D  63  VAL D  67 -1  O  ARG D  66   N  GLN D  53           
CISPEP   1 GLY A  157    GLU A  158          0        -1.35                     
CISPEP   2 TRP B  110    PRO B  111          0         4.41                     
CISPEP   3 GLY C  157    GLU C  158          0        -4.99                     
CISPEP   4 MET D    1    ASN D    2          0        -1.29                     
CISPEP   5 TRP D  110    PRO D  111          0         2.92                     
CISPEP   6 GLY D  201    THR D  202          0        -2.70                     
CRYST1   87.990  125.177  100.760  90.00 102.08  90.00 C 1 2 1       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      0.011365  0.000000  0.002432        0.00000                         
SCALE2      0.000000  0.007989  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010149        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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