GenomeNet

Database: PDB
Entry: 1CZY
LinkDB: 1CZY
Original site: 1CZY 
HEADER    APOPTOSIS                               07-SEP-99   1CZY              
TITLE     CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE TRAF DOMAIN OF HUMAN     
TITLE    2 TRAF2 AND AN LMP1 BINDING PEPTIDE                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED PROTEIN 2;       
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 FRAGMENT: TRAF DOMAIN;                                               
COMPND   5 SYNONYM: TRAF2;                                                      
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: LATENT MEMBRANE PROTEIN 1;                                 
COMPND   9 CHAIN: D, E;                                                         
COMPND  10 FRAGMENT: TRAF2-BINDING REGION;                                      
COMPND  11 SYNONYM: LMP1;                                                       
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET24D;                                   
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 SYNTHETIC: YES;                                                      
SOURCE  11 OTHER_DETAILS: THIS PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE 
SOURCE  12 OF THIS PEPTIDE NATURALLY OCCURS IN HUMANS (HOMO SAPIENS)            
KEYWDS    BETA SANDWICH, PROTEIN-PEPTIDE COMPLEX, SIGNALING PROTEIN, APOPTOSIS  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.YE,Y.C.PARK,M.KREISHMAN,E.KIEFF,H.WU                                
REVDAT   5   31-JAN-18 1CZY    1       REMARK                                   
REVDAT   4   04-OCT-17 1CZY    1       REMARK                                   
REVDAT   3   24-FEB-09 1CZY    1       VERSN                                    
REVDAT   2   01-APR-03 1CZY    1       JRNL                                     
REVDAT   1   08-MAR-00 1CZY    0                                                
JRNL        AUTH   H.YE,Y.C.PARK,M.KREISHMAN,E.KIEFF,H.WU                       
JRNL        TITL   THE STRUCTURAL BASIS FOR THE RECOGNITION OF DIVERSE RECEPTOR 
JRNL        TITL 2 SEQUENCES BY TRAF2.                                          
JRNL        REF    MOL.CELL                      V.   4   321 1999              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   10518213                                                     
JRNL        DOI    10.1016/S1097-2765(00)80334-2                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   Y.C.PARK,V.BURKITT,A.R.VILLA,L.TONG,H.WU                     
REMARK   1  TITL   STRUCTURAL BASIS FOR SELF-ASSOCIATION AND RECEPTOR           
REMARK   1  TITL 2 RECOGNITION OF HUMAN TRAF2                                   
REMARK   1  REF    NATURE                        V. 398   533 1999              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   1  DOI    10.1038/19110                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : NULL                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : 6%                              
REMARK   3   R VALUE            (WORKING SET) : 0.206                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3957                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 391                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1CZY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-SEP-99.                  
REMARK 100 THE DEPOSITION ID IS D_1000009661.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X4A                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.018                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : SOFTWARE AT SYNCHROTRON            
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: NULL                         
REMARK 200 SOFTWARE USED: REPLACE                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.89                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4K, MES BUFFER, PH 6.00, VAPOR        
REMARK 280  DIFFUSION, TEMPERATURE 20K, TEMPERATURE 293.0K                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       38.40000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5450 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22680 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 THE DEPOSITED TRAF2-RECEPTOR PEPTIDE COMPLEX                         
REMARK 400 CONTAINS 3 TRAF2 PER ASYMMETRIC UNIT,                                
REMARK 400 ONE OF WHICH DOES NOT HAVE THE PEPTIDE BOUND                         
REMARK 400 DUE TO CONFLICT WITH CRYSTAL PACKING.                                
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     ACE E   203                                                      
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     MET A 335    CG   SD   CE                                        
REMARK 470     ASP A 337    CG   OD1  OD2                                       
REMARK 470     GLU A 339    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 340    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 341    CG   CD   CE   NZ                                   
REMARK 470     GLU A 344    CG   CD   OE1  OE2                                  
REMARK 470     PRO A 362    CG   CD                                             
REMARK 470     ARG A 403    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 423    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 440    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 441    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 479    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 481    CG   CD   CE   NZ                                   
REMARK 470     MET B 335    CG   SD   CE                                        
REMARK 470     ASP B 337    CG   OD1  OD2                                       
REMARK 470     GLU B 339    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 340    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 341    CG   CD   CE   NZ                                   
REMARK 470     GLU B 344    CG   CD   OE1  OE2                                  
REMARK 470     PRO B 362    CG   CD                                             
REMARK 470     ARG B 403    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 423    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 440    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 441    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 479    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 481    CG   CD   CE   NZ                                   
REMARK 470     MET C 335    CG   SD   CE                                        
REMARK 470     ASP C 337    CG   OD1  OD2                                       
REMARK 470     GLU C 339    CG   CD   OE1  OE2                                  
REMARK 470     GLN C 340    CG   CD   OE1  NE2                                  
REMARK 470     LYS C 341    CG   CD   CE   NZ                                   
REMARK 470     GLU C 344    CG   CD   OE1  OE2                                  
REMARK 470     PRO C 362    CG   CD                                             
REMARK 470     ARG C 403    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C 423    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C 440    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 441    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 479    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 481    CG   CD   CE   NZ                                   
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   OD1  ASP E   210     O    HOH E  6233              1.98            
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    MET A 335      -16.11    -44.36                                   
REMARK 500    ASN A 427       43.98   -140.29                                   
REMARK 500    ARG A 440      -89.91    -91.67                                   
REMARK 500    VAL A 451      -19.04    -47.52                                   
REMARK 500    MET A 478     -123.32    -90.90                                   
REMARK 500    GLU A 479      -69.02      7.71                                   
REMARK 500    ALA A 480      -81.73    -30.31                                   
REMARK 500    LYS A 481     -118.77   -145.82                                   
REMARK 500    ASN A 482     -168.41     58.97                                   
REMARK 500    ASN B 427       43.22   -140.52                                   
REMARK 500    LEU B 471       51.15   -117.77                                   
REMARK 500    MET B 478     -122.53    -78.70                                   
REMARK 500    GLU B 479      -75.51      7.93                                   
REMARK 500    ALA B 480      -84.32    -21.65                                   
REMARK 500    LYS B 481     -109.54   -145.92                                   
REMARK 500    ASN B 482     -165.17     55.97                                   
REMARK 500    ASN C 427       42.85   -140.95                                   
REMARK 500    LEU C 471       44.66   -109.56                                   
REMARK 500    MET C 478     -130.24    -73.26                                   
REMARK 500    GLU C 479      -81.44     13.71                                   
REMARK 500    ALA C 480      -90.21    -18.06                                   
REMARK 500    LYS C 481     -121.55   -138.72                                   
REMARK 500    ASN C 482     -167.00     63.32                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACE D 203                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1CA4   RELATED DB: PDB                                   
REMARK 900 1CA4 CONTAINS THE SAME PROTEIN IN UNCOMPLEXED FORM                   
REMARK 900 RELATED ID: 1CA9   RELATED DB: PDB                                   
REMARK 900 1CA9 CONTAINS A LONGER CONSTRUCT OF THE SAME PROTEIN IN COMPLEX      
REMARK 900 WITH TNF-R2 PEPTIDE                                                  
REMARK 900 RELATED ID: 1CZZ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1D00   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1D01   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1D0J   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1D0A   RELATED DB: PDB                                   
DBREF  1CZY A  334   501  UNP    Q12933   TRAF2_HUMAN    334    501             
DBREF  1CZY B  334   501  UNP    Q12933   TRAF2_HUMAN    334    501             
DBREF  1CZY C  334   501  UNP    Q12933   TRAF2_HUMAN    334    501             
DBREF  1CZY D  204   210  UNP    P03230   LMP1_EBV       204    210             
DBREF  1CZY E  204   210  UNP    P03230   LMP1_EBV       204    210             
SEQADV 1CZY ARG A  365  UNP  Q12933    LEU   365 CONFLICT                       
SEQADV 1CZY ARG B  365  UNP  Q12933    LEU   365 CONFLICT                       
SEQADV 1CZY ARG C  365  UNP  Q12933    LEU   365 CONFLICT                       
SEQRES   1 A  168  ALA MET ALA ASP LEU GLU GLN LYS VAL LEU GLU MET GLU          
SEQRES   2 A  168  ALA SER THR TYR ASP GLY VAL PHE ILE TRP LYS ILE SER          
SEQRES   3 A  168  ASP PHE PRO ARG LYS ARG GLN GLU ALA VAL ALA GLY ARG          
SEQRES   4 A  168  ILE PRO ALA ILE PHE SER PRO ALA PHE TYR THR SER ARG          
SEQRES   5 A  168  TYR GLY TYR LYS MET CYS LEU ARG ILE TYR LEU ASN GLY          
SEQRES   6 A  168  ASP GLY THR GLY ARG GLY THR HIS LEU SER LEU PHE PHE          
SEQRES   7 A  168  VAL VAL MET LYS GLY PRO ASN ASP ALA LEU LEU ARG TRP          
SEQRES   8 A  168  PRO PHE ASN GLN LYS VAL THR LEU MET LEU LEU ASP GLN          
SEQRES   9 A  168  ASN ASN ARG GLU HIS VAL ILE ASP ALA PHE ARG PRO ASP          
SEQRES  10 A  168  VAL THR SER SER SER PHE GLN ARG PRO VAL ASN ASP MET          
SEQRES  11 A  168  ASN ILE ALA SER GLY CYS PRO LEU PHE CYS PRO VAL SER          
SEQRES  12 A  168  LYS MET GLU ALA LYS ASN SER TYR VAL ARG ASP ASP ALA          
SEQRES  13 A  168  ILE PHE ILE LYS ALA ILE VAL ASP LEU THR GLY LEU              
SEQRES   1 B  168  ALA MET ALA ASP LEU GLU GLN LYS VAL LEU GLU MET GLU          
SEQRES   2 B  168  ALA SER THR TYR ASP GLY VAL PHE ILE TRP LYS ILE SER          
SEQRES   3 B  168  ASP PHE PRO ARG LYS ARG GLN GLU ALA VAL ALA GLY ARG          
SEQRES   4 B  168  ILE PRO ALA ILE PHE SER PRO ALA PHE TYR THR SER ARG          
SEQRES   5 B  168  TYR GLY TYR LYS MET CYS LEU ARG ILE TYR LEU ASN GLY          
SEQRES   6 B  168  ASP GLY THR GLY ARG GLY THR HIS LEU SER LEU PHE PHE          
SEQRES   7 B  168  VAL VAL MET LYS GLY PRO ASN ASP ALA LEU LEU ARG TRP          
SEQRES   8 B  168  PRO PHE ASN GLN LYS VAL THR LEU MET LEU LEU ASP GLN          
SEQRES   9 B  168  ASN ASN ARG GLU HIS VAL ILE ASP ALA PHE ARG PRO ASP          
SEQRES  10 B  168  VAL THR SER SER SER PHE GLN ARG PRO VAL ASN ASP MET          
SEQRES  11 B  168  ASN ILE ALA SER GLY CYS PRO LEU PHE CYS PRO VAL SER          
SEQRES  12 B  168  LYS MET GLU ALA LYS ASN SER TYR VAL ARG ASP ASP ALA          
SEQRES  13 B  168  ILE PHE ILE LYS ALA ILE VAL ASP LEU THR GLY LEU              
SEQRES   1 C  168  ALA MET ALA ASP LEU GLU GLN LYS VAL LEU GLU MET GLU          
SEQRES   2 C  168  ALA SER THR TYR ASP GLY VAL PHE ILE TRP LYS ILE SER          
SEQRES   3 C  168  ASP PHE PRO ARG LYS ARG GLN GLU ALA VAL ALA GLY ARG          
SEQRES   4 C  168  ILE PRO ALA ILE PHE SER PRO ALA PHE TYR THR SER ARG          
SEQRES   5 C  168  TYR GLY TYR LYS MET CYS LEU ARG ILE TYR LEU ASN GLY          
SEQRES   6 C  168  ASP GLY THR GLY ARG GLY THR HIS LEU SER LEU PHE PHE          
SEQRES   7 C  168  VAL VAL MET LYS GLY PRO ASN ASP ALA LEU LEU ARG TRP          
SEQRES   8 C  168  PRO PHE ASN GLN LYS VAL THR LEU MET LEU LEU ASP GLN          
SEQRES   9 C  168  ASN ASN ARG GLU HIS VAL ILE ASP ALA PHE ARG PRO ASP          
SEQRES  10 C  168  VAL THR SER SER SER PHE GLN ARG PRO VAL ASN ASP MET          
SEQRES  11 C  168  ASN ILE ALA SER GLY CYS PRO LEU PHE CYS PRO VAL SER          
SEQRES  12 C  168  LYS MET GLU ALA LYS ASN SER TYR VAL ARG ASP ASP ALA          
SEQRES  13 C  168  ILE PHE ILE LYS ALA ILE VAL ASP LEU THR GLY LEU              
SEQRES   1 D    8  ACE PRO GLN GLN ALA THR ASP ASP                              
SEQRES   1 E    8  ACE PRO GLN GLN ALA THR ASP ASP                              
HET    ACE  D 203       3                                                       
HETNAM     ACE ACETYL GROUP                                                     
FORMUL   4  ACE    C2 H4 O                                                      
FORMUL   6  HOH   *391(H2 O)                                                    
HELIX    1   1 ALA A  334  SER A  348  1                                  15    
HELIX    2   2 ASP A  360  ALA A  370  1                                  11    
HELIX    3   4 ASN A  418  LEU A  422  5                                   5    
HELIX    4   5 SER A  453  GLN A  457  5                                   5    
HELIX    5   6 ALA B  334  SER B  348  1                                  15    
HELIX    6   7 ASP B  360  ALA B  370  1                                  11    
HELIX    7   9 ASN B  418  LEU B  422  5                                   5    
HELIX    8  10 SER B  453  GLN B  457  5                                   5    
HELIX    9  11 ALA C  334  SER C  348  1                                  15    
HELIX   10  12 ASP C  360  ALA C  370  1                                  11    
HELIX   11  14 ASN C  418  LEU C  422  5                                   5    
HELIX   12  15 SER C  453  GLN C  457  5                                   5    
SHEET    1   A 4 VAL A 353  ILE A 358  0                                        
SHEET    2   A 4 ILE A 490  VAL A 496 -1  O  ILE A 490   N  ILE A 358           
SHEET    3   A 4 VAL A 430  LEU A 434 -1  N  THR A 431   O  ILE A 495           
SHEET    4   A 4 VAL A 443  PHE A 447 -1  N  VAL A 443   O  LEU A 434           
SHEET    1   B 5 GLN D 205  GLN D 206  0                                        
SHEET    2   B 5 SER A 467  PRO A 474 -1  N  GLY A 468   O  GLN D 205           
SHEET    3   B 5 HIS A 406  MET A 414 -1  N  LEU A 407   O  CYS A 473           
SHEET    4   B 5 LYS A 389  TYR A 395 -1  O  LYS A 389   N  MET A 414           
SHEET    5   B 5 ILE A 376  PHE A 377 -1  O  ILE A 376   N  ILE A 394           
SHEET    1   C 5 GLN D 205  GLN D 206  0                                        
SHEET    2   C 5 SER A 467  PRO A 474 -1  N  GLY A 468   O  GLN D 205           
SHEET    3   C 5 HIS A 406  MET A 414 -1  N  LEU A 407   O  CYS A 473           
SHEET    4   C 5 LYS A 389  TYR A 395 -1  O  LYS A 389   N  MET A 414           
SHEET    5   C 5 PHE A 381  TYR A 382 -1  O  PHE A 381   N  MET A 390           
SHEET    1   D 4 VAL B 353  SER B 359  0                                        
SHEET    2   D 4 ALA B 489  VAL B 496 -1  O  ILE B 490   N  ILE B 358           
SHEET    3   D 4 VAL B 430  LEU B 434 -1  N  THR B 431   O  ILE B 495           
SHEET    4   D 4 VAL B 443  PHE B 447 -1  N  VAL B 443   O  LEU B 434           
SHEET    1   E 4 SER B 467  PRO B 474  0                                        
SHEET    2   E 4 HIS B 406  MET B 414 -1  N  LEU B 407   O  CYS B 473           
SHEET    3   E 4 LYS B 389  TYR B 395 -1  O  LYS B 389   N  MET B 414           
SHEET    4   E 4 ILE B 376  PHE B 377 -1  O  ILE B 376   N  ILE B 394           
SHEET    1   F 4 SER B 467  PRO B 474  0                                        
SHEET    2   F 4 HIS B 406  MET B 414 -1  N  LEU B 407   O  CYS B 473           
SHEET    3   F 4 LYS B 389  TYR B 395 -1  O  LYS B 389   N  MET B 414           
SHEET    4   F 4 PHE B 381  TYR B 382 -1  O  PHE B 381   N  MET B 390           
SHEET    1   G 4 VAL C 353  ILE C 358  0                                        
SHEET    2   G 4 ILE C 490  VAL C 496 -1  O  ILE C 490   N  ILE C 358           
SHEET    3   G 4 VAL C 430  LEU C 434 -1  N  THR C 431   O  ILE C 495           
SHEET    4   G 4 VAL C 443  PHE C 447 -1  N  VAL C 443   O  LEU C 434           
SHEET    1   H 5 GLN E 205  GLN E 206  0                                        
SHEET    2   H 5 SER C 467  PRO C 474 -1  N  GLY C 468   O  GLN E 205           
SHEET    3   H 5 HIS C 406  MET C 414 -1  N  LEU C 407   O  CYS C 473           
SHEET    4   H 5 LYS C 389  TYR C 395 -1  O  LYS C 389   N  MET C 414           
SHEET    5   H 5 ILE C 376  PHE C 377 -1  O  ILE C 376   N  ILE C 394           
SHEET    1   I 5 GLN E 205  GLN E 206  0                                        
SHEET    2   I 5 SER C 467  PRO C 474 -1  N  GLY C 468   O  GLN E 205           
SHEET    3   I 5 HIS C 406  MET C 414 -1  N  LEU C 407   O  CYS C 473           
SHEET    4   I 5 LYS C 389  TYR C 395 -1  O  LYS C 389   N  MET C 414           
SHEET    5   I 5 PHE C 381  TYR C 382 -1  O  PHE C 381   N  MET C 390           
LINK         C   ACE D 203                 N   PRO D 204     1555   1555  1.34  
CISPEP   1 TRP A  424    PRO A  425          0        -0.23                     
CISPEP   2 TRP B  424    PRO B  425          0        -0.04                     
CISPEP   3 TRP C  424    PRO C  425          0        -0.02                     
SITE     1 AC1  1 HOH D6225                                                     
CRYST1   56.200   76.800   66.900  90.00  93.20  90.00 P 1 21 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      0.017794  0.000000  0.000995        0.00000                         
SCALE2      0.000000  0.013021  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014971        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system