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Database: PDB
Entry: 6IRD
LinkDB: 6IRD
Original site: 6IRD 
HEADER    HYDROLASE/PROTEIN BINDING               12-NOV-18   6IRD              
TITLE     COMPLEX STRUCTURE OF INADL PDZ89 AND PLCB4 C-TERMINAL CC-PBM          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE; 
COMPND   3 CHAIN: B;                                                            
COMPND   4 FRAGMENT: C-TERMINAL CC-PBM;                                         
COMPND   5 EC: 3.1.4.11;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: INAD-LIKE PROTEIN;                                         
COMPND  10 CHAIN: C;                                                            
COMPND  11 FRAGMENT: PDZ89;                                                     
COMPND  12 SYNONYM: HINADL,PALS1-ASSOCIATED TIGHT JUNCTION PROTEIN,PROTEIN      
COMPND  13 ASSOCIATED TO TIGHT JUNCTIONS;                                       
COMPND  14 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: PLCB4;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: PATJ, INADL;                                                   
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 469008                                      
KEYWDS    PDZ SUPRAMODULE, PHOSPHOLIPASE C BETA, HYDROLASE-PROTEIN BINDING      
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.YE,J.LI,Y.HUANG,W.LIU,M.ZHANG                                       
REVDAT   2   28-OCT-20 6IRD    1       JRNL   LINK                              
REVDAT   1   23-JAN-19 6IRD    0                                                
JRNL        AUTH   F.YE,Y.HUANG,J.LI,Y.MA,C.XIE,Z.LIU,X.DENG,J.WAN,T.XUE,W.LIU, 
JRNL        AUTH 2 M.ZHANG                                                      
JRNL        TITL   AN UNEXPECTED INAD PDZ TANDEM-MEDIATED PLC BETA BINDING IN   
JRNL        TITL 2 DROSOPHILA PHOTO RECEPTORS.                                  
JRNL        REF    ELIFE                         V.   7       2018              
JRNL        REFN                   ESSN 2050-084X                               
JRNL        PMID   30526850                                                     
JRNL        DOI    10.7554/ELIFE.41848                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.81 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.14_3260: ???)                              
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) : 2.81                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.310                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 88.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 12434                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.247                           
REMARK   3   R VALUE            (WORKING SET) : 0.244                           
REMARK   3   FREE R VALUE                     : 0.302                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.860                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 604                             
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  3.0936 -  2.8128    0.54     1757   106  0.3153 0.3287        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
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)     : 0.410            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.500           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.86                          
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      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
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 6IRD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-NOV-18.                  
REMARK 100 THE DEPOSITION ID IS D_1300008898.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-MAR-18                          
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               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97918                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14070                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
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     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 7.200                              
REMARK 200  R MERGE                    (I) : 0.11700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.93800                            
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: AUTOSOL, SHELXD                                       
REMARK 200 STARTING MODEL: 3R0H                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.86                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M MGCL2, 0.1M BIS-TRIS PH6.5, 20%     
REMARK 280  W/V POLYETHYLENE GLYCOL 3350, LIQUID DIFFUSION, TEMPERATURE 289K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       66.79167            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      133.58333            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  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        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      133.58333            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       66.79167            
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: 3210 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24900 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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     GLU B    -1                                                      
REMARK 465     GLY B     0                                                      
REMARK 465     GLU B     1                                                      
REMARK 465     LEU B     2                                                      
REMARK 465     ILE B     3                                                      
REMARK 465     PRO B     4                                                      
REMARK 465     GLN B     5                                                      
REMARK 465     LYS B    75                                                      
REMARK 465     GLY B    76                                                      
REMARK 465     GLY B    77                                                      
REMARK 465     SER B    78                                                      
REMARK 465     ASN B    79                                                      
REMARK 465     LEU C   266                                                      
REMARK 465     SER C   267                                                      
REMARK 465     VAL C   268                                                      
REMARK 465     ASP C   269                                                      
REMARK 465     PRO C   270                                                      
REMARK 465     ASP C   363A                                                     
REMARK 465     GLU C   363B                                                     
REMARK 465     ALA C   363C                                                     
REMARK 465     HIS C   363D                                                     
REMARK 465     TYR C   363E                                                     
REMARK 465     ARG C   363F                                                     
REMARK 465     ASP C   363G                                                     
REMARK 465     GLU C   363H                                                     
REMARK 465     GLU C   363I                                                     
REMARK 465     ASN C   363J                                                     
REMARK 465     ALA C   460                                                      
REMARK 465     GLY C   461                                                      
REMARK 465     SER C   462                                                      
REMARK 465     TRP C   463                                                      
REMARK 465     THR C   464                                                      
REMARK 465     SER C   465                                                      
REMARK 465     ALA C   466                                                      
REMARK 465     ARG C   467                                                      
REMARK 465     THR C   468                                                      
REMARK 465     THR C   469                                                      
REMARK 465     GLY C   470                                                      
REMARK 465     GLY C   471                                                      
REMARK 465     GLY C   472                                                      
REMARK 465     SER C   473                                                      
REMARK 465     GLY C   474                                                      
REMARK 465     GLY C   475                                                      
REMARK 465     GLY C   476                                                      
REMARK 465     GLY C   477                                                      
REMARK 465     SER C   478                                                      
REMARK 465     GLY C   479                                                      
REMARK 465     GLY C   480                                                      
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 B  12    CG   CD   CE   NZ                                   
REMARK 470     GLN B  25    CG   CD   OE1  NE2                                  
REMARK 470     LYS B  32    CG   CD   CE   NZ                                   
REMARK 470     GLU B  65    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  66    CG   CD   CE   NZ                                   
REMARK 470     GLU B  69    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  70    CG   CD   CE   NZ                                   
REMARK 470     MET B  72    CG   SD   CE                                        
REMARK 470     LYS B  73    CG   CD   CE   NZ                                   
REMARK 470     LYS B  74    CG   CD   CE   NZ                                   
REMARK 470     LYS B  84    CG   CD   CE   NZ                                   
REMARK 470     LYS B  85    CG   CD   CE   NZ                                   
REMARK 470     GLU B  86    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  90    CG   CD   CE   NZ                                   
REMARK 470     GLN B  92    CG   CD   OE1  NE2                                  
REMARK 470     LYS B  99    CG   CD   CE   NZ                                   
REMARK 470     LYS B 101    CG   CD   CE   NZ                                   
REMARK 470     GLU B 104    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 128    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 141    CG   CD   CE   NZ                                   
REMARK 470     ARG B 166    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 171    CG   CD   CE   NZ                                   
REMARK 470     GLU B 175    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 178    CG   CD   CE   NZ                                   
REMARK 470     GLN B 182    CG   CD   OE1  NE2                                  
REMARK 470     ASP B 183    CG   OD1  OD2                                       
REMARK 470     LYS B 184    CG   CD   CE   NZ                                   
REMARK 470     LYS B 187    CG   CD   CE   NZ                                   
REMARK 470     LYS B 189    CG   CD   CE   NZ                                   
REMARK 470     LYS B 220    CG   CD   CE   NZ                                   
REMARK 470     LYS B 227    CG   CD   CE   NZ                                   
REMARK 470     GLU B 234    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 238    CG   CD   CE   NZ                                   
REMARK 470     GLU B 255    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 280    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 284    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 287    CG   CD   CE   NZ                                   
REMARK 470     ARG C 289    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 315    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 320    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 332    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 339    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 344    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 345    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 351    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN C 352    CG   CD   OE1  NE2                                  
REMARK 470     GLN C 355    CG   CD   OE1  NE2                                  
REMARK 470     LYS C 356    CG   CD   CE   NZ                                   
REMARK 470     ARG C 358    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 383    CG   CD   CE   NZ                                   
REMARK 470     ARG C 386    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN C 397    CG   OD1  ND2                                       
REMARK 470     LYS C 408    CG   CD   CE   NZ                                   
REMARK 470     GLN C 420    CG   CD   OE1  NE2                                  
REMARK 470     GLN C 423    CG   CD   OE1  NE2                                  
REMARK 470     ARG C 459    CG   CD   NE   CZ   NH1  NH2                        
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 B  81   CA  -  CB  -  CG  ANGL. DEV. =  18.0 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    LEU B  81     -128.84     61.11                                   
REMARK 500    GLN C 352        4.38    -68.14                                   
REMARK 500    PRO C 354     -166.70    -68.08                                   
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                              AU B 303  AU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR C 272   O                                                      
REMARK 620 2 CYS C 273   SG   90.0                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue AU B 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue AU B 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue AU B 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue AU B 304                  
DBREF  6IRD B    1   264  UNP    Q91UZ1   Q91UZ1_MOUSE   912   1175             
DBREF  6IRD C  266   469  UNP    Q8NI35   INADL_HUMAN   1421   1625             
SEQADV 6IRD GLU B   -1  UNP  Q91UZ1              EXPRESSION TAG                 
SEQADV 6IRD GLY B    0  UNP  Q91UZ1              EXPRESSION TAG                 
SEQADV 6IRD ALA B   15  UNP  Q91UZ1    LYS   926 ENGINEERED MUTATION            
SEQADV 6IRD ALA B   19  UNP  Q91UZ1    LYS   930 ENGINEERED MUTATION            
SEQADV 6IRD ALA B   22  UNP  Q91UZ1    LYS   933 ENGINEERED MUTATION            
SEQADV 6IRD ALA B   23  UNP  Q91UZ1    LYS   934 ENGINEERED MUTATION            
SEQADV 6IRD ALA B   26  UNP  Q91UZ1    LYS   937 ENGINEERED MUTATION            
SEQADV 6IRD ALA B   33  UNP  Q91UZ1    LYS   944 ENGINEERED MUTATION            
SEQADV 6IRD ALA B   34  UNP  Q91UZ1    LYS   945 ENGINEERED MUTATION            
SEQADV 6IRD ALA B   37  UNP  Q91UZ1    LYS   948 ENGINEERED MUTATION            
SEQADV 6IRD GLY C  470  UNP  Q8NI35              EXPRESSION TAG                 
SEQADV 6IRD GLY C  471  UNP  Q8NI35              EXPRESSION TAG                 
SEQADV 6IRD GLY C  472  UNP  Q8NI35              EXPRESSION TAG                 
SEQADV 6IRD SER C  473  UNP  Q8NI35              EXPRESSION TAG                 
SEQADV 6IRD GLY C  474  UNP  Q8NI35              EXPRESSION TAG                 
SEQADV 6IRD GLY C  475  UNP  Q8NI35              EXPRESSION TAG                 
SEQADV 6IRD GLY C  476  UNP  Q8NI35              EXPRESSION TAG                 
SEQADV 6IRD GLY C  477  UNP  Q8NI35              EXPRESSION TAG                 
SEQADV 6IRD SER C  478  UNP  Q8NI35              EXPRESSION TAG                 
SEQADV 6IRD GLY C  479  UNP  Q8NI35              EXPRESSION TAG                 
SEQADV 6IRD GLY C  480  UNP  Q8NI35              EXPRESSION TAG                 
SEQRES   1 B  266  GLU GLY GLU LEU ILE PRO GLN VAL ARG ILE GLU ASP LEU          
SEQRES   2 B  266  LYS GLN MET ALA ALA TYR LEU ALA HIS LEU ALA ALA GLN          
SEQRES   3 B  266  GLN ALA GLU LEU ASN SER LEU LYS ALA ALA HIS ALA ALA          
SEQRES   4 B  266  GLU HIS SER THR MET GLN LYS LEU HIS CYS THR GLN VAL          
SEQRES   5 B  266  ASP LYS ILE VAL ALA GLN TYR ASP LYS GLU LYS SER THR          
SEQRES   6 B  266  HIS GLU LYS ILE LEU GLU LYS ALA MET LYS LYS LYS GLY          
SEQRES   7 B  266  GLY SER ASN CYS LEU GLU ILE LYS LYS GLU THR GLU ILE          
SEQRES   8 B  266  LYS ILE GLN THR LEU THR THR ASP HIS LYS SER LYS VAL          
SEQRES   9 B  266  LYS GLU ILE VAL ALA GLN HIS THR LYS GLU TRP SER GLU          
SEQRES  10 B  266  MET ILE ASN THR HIS SER ALA GLU GLU GLN GLU ILE ARG          
SEQRES  11 B  266  ASP LEU HIS LEU SER GLN GLN CYS GLU LEU LEU ARG LYS          
SEQRES  12 B  266  LEU LEU ILE ASN ALA HIS GLU GLN GLN THR GLN GLN LEU          
SEQRES  13 B  266  LYS LEU SER HIS ASP ARG GLU SER LYS GLU MET ARG ALA          
SEQRES  14 B  266  HIS GLN ALA LYS ILE SER MET GLU ASN SER LYS ALA ILE          
SEQRES  15 B  266  SER GLN ASP LYS SER ILE LYS ASN LYS ALA GLU ARG GLU          
SEQRES  16 B  266  ARG ARG VAL ARG GLU LEU ASN SER SER ASN THR LYS LYS          
SEQRES  17 B  266  PHE LEU GLU GLU ARG LYS ARG LEU ALA MET LYS GLN SER          
SEQRES  18 B  266  LYS GLU MET ASP GLN LEU LYS LYS VAL GLN LEU GLU HIS          
SEQRES  19 B  266  LEU GLU PHE LEU GLU LYS GLN ASN GLU GLN ALA LYS GLU          
SEQRES  20 B  266  MET GLN GLN MET VAL LYS LEU GLU ALA GLU MET ASP ARG          
SEQRES  21 B  266  ARG PRO ALA THR VAL VAL                                      
SEQRES   1 C  216  LEU SER VAL ASP PRO ALA THR CYS PRO ILE VAL PRO GLY          
SEQRES   2 C  216  GLN GLU MET ILE ILE GLU ILE SER LYS GLY ARG SER GLY          
SEQRES   3 C  216  LEU GLY LEU SER ILE VAL GLY GLY LYS ASP THR PRO LEU          
SEQRES   4 C  216  ASN ALA ILE VAL ILE HIS GLU VAL TYR GLU GLU GLY ALA          
SEQRES   5 C  216  ALA ALA ARG ASP GLY ARG LEU TRP ALA GLY ASP GLN ILE          
SEQRES   6 C  216  LEU GLU VAL ASN GLY VAL ASP LEU ARG ASN SER SER HIS          
SEQRES   7 C  216  GLU GLU ALA ILE THR ALA LEU ARG GLN THR PRO GLN LYS          
SEQRES   8 C  216  VAL ARG LEU VAL VAL TYR ARG ASP GLU ALA HIS TYR ARG          
SEQRES   9 C  216  ASP GLU GLU ASN LEU GLU ILE PHE PRO VAL ASP LEU GLN          
SEQRES  10 C  216  LYS LYS ALA GLY ARG GLY LEU GLY LEU SER ILE VAL GLY          
SEQRES  11 C  216  LYS ARG ASN GLY SER GLY VAL PHE ILE SER ASP ILE VAL          
SEQRES  12 C  216  LYS GLY GLY ALA ALA ASP LEU ASP GLY ARG LEU ILE GLN          
SEQRES  13 C  216  GLY ASP GLN ILE LEU SER VAL ASN GLY GLU ASP MET ARG          
SEQRES  14 C  216  ASN ALA SER GLN GLU THR VAL ALA THR ILE LEU LYS CYS          
SEQRES  15 C  216  ALA GLN GLY LEU VAL GLN LEU GLU ILE GLY ARG LEU ARG          
SEQRES  16 C  216  ALA GLY SER TRP THR SER ALA ARG THR THR GLY GLY GLY          
SEQRES  17 C  216  SER GLY GLY GLY GLY SER GLY GLY                              
HET     AU  B 301       1                                                       
HET     AU  B 302       1                                                       
HET     AU  B 303       1                                                       
HET     AU  B 304       1                                                       
HET     AU  C 501       1                                                       
HETNAM      AU GOLD ION                                                         
FORMUL   3   AU    5(AU 1+)                                                     
HELIX    1 AA1 VAL B    6  LYS B   12  1                                   7    
HELIX    2 AA2 MET B   14  LYS B   74  1                                  61    
HELIX    3 AA3 LEU B   81  GLN B  182  1                                 102    
HELIX    4 AA4 ASN B  188  ARG B  258  1                                  71    
HELIX    5 AA5 GLY C  316  GLY C  322  1                                   7    
HELIX    6 AA6 SER C  342  GLN C  352  1                                  11    
HELIX    7 AA7 GLY C  410  GLY C  416  1                                   7    
HELIX    8 AA8 SER C  436  ALA C  447  1                                  12    
SHEET    1 AA1 3 THR B 262  VAL B 263  0                                        
SHEET    2 AA1 3 SER C 391  VAL C 393 -1  O  ILE C 392   N  THR B 262           
SHEET    3 AA1 3 PHE C 402  ILE C 403 -1  O  PHE C 402   N  VAL C 393           
SHEET    1 AA2 5 MET C 281  SER C 286  0                                        
SHEET    2 AA2 5 LYS C 356  TYR C 362 -1  O  LEU C 359   N  ILE C 283           
SHEET    3 AA2 5 GLN C 329  VAL C 333 -1  N  LEU C 331   O  VAL C 360           
SHEET    4 AA2 5 ILE C 307  VAL C 312 -1  N  ILE C 307   O  ILE C 330           
SHEET    5 AA2 5 LEU C 294  VAL C 297 -1  N  SER C 295   O  HIS C 310           
SHEET    1 AA3 4 MET C 281  SER C 286  0                                        
SHEET    2 AA3 4 LYS C 356  TYR C 362 -1  O  LEU C 359   N  ILE C 283           
SHEET    3 AA3 4 GLN C 329  VAL C 333 -1  N  LEU C 331   O  VAL C 360           
SHEET    4 AA3 4 VAL C 336  ASP C 337 -1  O  VAL C 336   N  VAL C 333           
SHEET    1 AA4 4 GLU C 374  GLN C 381  0                                        
SHEET    2 AA4 4 LEU C 450  ARG C 457 -1  O  VAL C 451   N  LEU C 380           
SHEET    3 AA4 4 GLN C 423  VAL C 427 -1  N  GLN C 423   O  GLY C 456           
SHEET    4 AA4 4 GLU C 430  ASP C 431 -1  O  GLU C 430   N  VAL C 427           
LINK         SG  CYS B  47                AU    AU B 302     1555   1555  2.48  
LINK         SG  CYS B 136                AU    AU B 301     1555   1555  2.32  
LINK        AU    AU B 303                 O   THR C 272     2555   1555  2.80  
LINK        AU    AU B 303                 SG  CYS C 273     2555   1555  2.23  
SITE     1 AC1  2 CYS B 136  GLU B 137                                          
SITE     1 AC2  3 CYS B  47  THR B  48  ASP B  51                               
SITE     1 AC3  3 THR C 272  CYS C 273  PRO C 274                               
SITE     1 AC4  1 GLN B 239                                                     
CRYST1   69.089   69.089  200.375  90.00  90.00 120.00 P 31 2 1      6          
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      0.014474  0.008357  0.000000        0.00000                         
SCALE2      0.000000  0.016713  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004991        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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