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Database: PDB
Entry: 2TUN
LinkDB: 2TUN
Original site: 2TUN 
HEADER    LYMPHOKINE                              06-OCT-93   2TUN              
TITLE     CONFORMATIONAL CHANGES IN THE (ALA-84-VAL) MUTANT OF TUMOR NECROSIS   
TITLE    2 FACTOR                                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TUMOR NECROSIS FACTOR-ALPHA;                               
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606                                                 
KEYWDS    LYMPHOKINE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.SALUDJIAN,T.PRANGE                                                  
REVDAT   4   19-JUN-13 2TUN    1       REMARK SEQADV                            
REVDAT   3   13-JUL-11 2TUN    1       VERSN                                    
REVDAT   2   24-FEB-09 2TUN    1       VERSN                                    
REVDAT   1   31-JAN-94 2TUN    0                                                
JRNL        AUTH   P.SALUDJIAN,T.PRANGE,R.KAHN,R.FOURME,J.TAVERNIER,            
JRNL        AUTH 2 X.VAN-OOSTADE,W.FIERS,G.NAVAZA                               
JRNL        TITL   CONFORMATIONAL CHANGES IN THE (ALA-84-VAL) MUTANT OF TUMOR   
JRNL        TITL 2 NECROSIS FACTOR                                              
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   E.Y.JONES,N.P.WALKER,D.I.STUART                              
REMARK   1  TITL   METHODOLOGY EMPLOYED FOR THE STRUCTURE DETERMINATION OF      
REMARK   1  TITL 2 TUMOR NECROSIS FACTOR, A CASE OF HIGH NON-CRYSTALLOGRAPHIC   
REMARK   1  TITL 3 SYMMETRY                                                     
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.A      V.  47   753 1991              
REMARK   1  REFN                   ISSN 0108-7673                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   M.J.ECK,S.R.SPRANG                                           
REMARK   1  TITL   THE STRUCTURE OF TUMOR NECROSIS FACTOR-ALPHA AT 2.6          
REMARK   1  TITL 2 ANGSTROMS RESOLUTION. IMPLICATIONS FOR RECEPTOR BINDING      
REMARK   1  REF    J.BIOL.CHEM.                  V. 264 17595 1989              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   E.Y.JONES,D.I.STUART,N.P.WALKER                              
REMARK   1  TITL   STRUCTURE OF TUMOR NECROSIS FACTOR                           
REMARK   1  REF    NATURE                        V. 338   225 1989              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   A.LEWITT-BENTLEY,R.FOURME,R.KAHN,T.PRANGE,P.VACHETTE,        
REMARK   1  AUTH 2 J.TAVERNIER,G.HAUQUIER,W.FIERS                               
REMARK   1  TITL   STRUCTURE OF TUMOR NECROSIS FACTOR BY X-RAY SOLUTION         
REMARK   1  TITL 2 SCATTERING AND PRELIMINARY STUDIES BY SINGLE CRYSTAL X-RAY   
REMARK   1  TITL 3 DIFFRACTION                                                  
REMARK   1  REF    J.MOL.BIOL.                   V. 199   389 1988              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PROLSQ                                               
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 9.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 3.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 15325                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.198                           
REMARK   3   R VALUE            (WORKING SET) : NULL                            
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7086                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
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  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.018 ; 0.020               
REMARK   3    ANGLE DISTANCE                  (A) : 0.037 ; 0.030               
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.070 ; 0.040               
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : 0.007 ; 0.010               
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.050 ; 0.030               
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : 0.230 ; 0.300               
REMARK   3    MULTIPLE TORSION                (A) : 0.290 ; 0.300               
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : 0.180 ; 0.300               
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : 7.300 ; 2.000               
REMARK   3    STAGGERED                 (DEGREES) : 17.700; 10.000              
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND               (A**2) : 1.807 ; 2.000               
REMARK   3   MAIN-CHAIN ANGLE              (A**2) : 3.210 ; 3.000               
REMARK   3   SIDE-CHAIN BOND               (A**2) : 1.837 ; 2.000               
REMARK   3   SIDE-CHAIN ANGLE              (A**2) : 3.301 ; 3.000               
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  THE STRUCTURE WAS SOLVED BY MOLECULAR REPLACEMENT (PROGRAM          
REMARK   3  *AMORE*) STARTING FROM THE COORDINATES IN PROTEIN DATA BANK         
REMARK   3  ENTRY 1TNF.                                                         
REMARK   3                                                                      
REMARK   3  ONLY FAINT ELECTRON DENSITY IS OBSERVED FOR RESIDUES 1 - 6          
REMARK   3  AT THE N-TERMINUS OF EACH CHAIN AND, THEREFORE, NO                  
REMARK   3  COORDINATES FOR THESE RESIDUES ARE PRESENT IN THIS ENTRY.           
REMARK   3  ELECTRON DENSITY FOR THE LOOP 103 - 110 IS ALSO RATHER WEAK         
REMARK   3  IN CHAINS A, B, D, AND F.   SEVERE DISTORSIONS ARE ALSO             
REMARK   3  OBSERVED IN THE SEGMENTS 7-9                                        
REMARK   4                                                                      
REMARK   4 2TUN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
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: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.53                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.57                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
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       31.23333            
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       62.46667            
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       62.46667            
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       31.23333            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F                      
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6930 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18470 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, F, 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7010 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18070 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     VAL A     1                                                      
REMARK 465     ARG A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     ARG A     6                                                      
REMARK 465     VAL B     1                                                      
REMARK 465     ARG B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     SER B     4                                                      
REMARK 465     SER B     5                                                      
REMARK 465     ARG B     6                                                      
REMARK 465     VAL C     1                                                      
REMARK 465     ARG C     2                                                      
REMARK 465     SER C     3                                                      
REMARK 465     SER C     4                                                      
REMARK 465     SER C     5                                                      
REMARK 465     ARG C     6                                                      
REMARK 465     VAL D     1                                                      
REMARK 465     ARG D     2                                                      
REMARK 465     SER D     3                                                      
REMARK 465     SER D     4                                                      
REMARK 465     SER D     5                                                      
REMARK 465     ARG D     6                                                      
REMARK 465     VAL E     1                                                      
REMARK 465     ARG E     2                                                      
REMARK 465     SER E     3                                                      
REMARK 465     SER E     4                                                      
REMARK 465     SER E     5                                                      
REMARK 465     ARG E     6                                                      
REMARK 465     VAL F     1                                                      
REMARK 465     ARG F     2                                                      
REMARK 465     SER F     3                                                      
REMARK 465     SER F     4                                                      
REMARK 465     SER F     5                                                      
REMARK 465     ARG F     6                                                      
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 PROTEIN DATA BANK ADVISORY NOTICE:                                   
REMARK 999      DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE.                 
REMARK 999                                                                      
REMARK 999      SWISS-PROT ENTRY NAME: TNFA_HUMAN                               
REMARK 999                                                                      
REMARK 999      SWISS-PROT RESIDUE      PDB SEQRES                              
REMARK 999        NAME   NUMBER         NAME  CHAIN  SEQ/INSERT CODE            
REMARK 999        ASP    220            LEU          137                        
DBREF  2TUN A    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  2TUN B    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  2TUN C    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  2TUN D    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  2TUN E    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  2TUN F    1   157  UNP    P01375   TNFA_HUMAN      77    233             
SEQADV 2TUN VAL A   84  UNP  P01375    ALA   160 ENGINEERED MUTATION            
SEQADV 2TUN LEU A  143  UNP  P01375    ASP   219 CONFLICT                       
SEQADV 2TUN VAL B   84  UNP  P01375    ALA   160 ENGINEERED MUTATION            
SEQADV 2TUN LEU B  143  UNP  P01375    ASP   219 CONFLICT                       
SEQADV 2TUN VAL C   84  UNP  P01375    ALA   160 ENGINEERED MUTATION            
SEQADV 2TUN LEU C  143  UNP  P01375    ASP   219 CONFLICT                       
SEQADV 2TUN VAL D   84  UNP  P01375    ALA   160 ENGINEERED MUTATION            
SEQADV 2TUN LEU D  143  UNP  P01375    ASP   219 CONFLICT                       
SEQADV 2TUN VAL E   84  UNP  P01375    ALA   160 ENGINEERED MUTATION            
SEQADV 2TUN LEU E  143  UNP  P01375    ASP   219 CONFLICT                       
SEQADV 2TUN VAL F   84  UNP  P01375    ALA   160 ENGINEERED MUTATION            
SEQADV 2TUN LEU F  143  UNP  P01375    ASP   219 CONFLICT                       
SEQRES   1 A  157  VAL ARG SER SER SER ARG THR PRO SER ASP LYS PRO VAL          
SEQRES   2 A  157  ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY GLN LEU          
SEQRES   3 A  157  GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU ALA ASN          
SEQRES   4 A  157  GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL PRO SER          
SEQRES   5 A  157  GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU PHE LYS          
SEQRES   6 A  157  GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU THR HIS          
SEQRES   7 A  157  THR ILE SER ARG ILE VAL VAL SER TYR GLN THR LYS VAL          
SEQRES   8 A  157  ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN ARG GLU          
SEQRES   9 A  157  THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR GLU PRO          
SEQRES  10 A  157  ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS GLY ASP          
SEQRES  11 A  157  ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR LEU LEU          
SEQRES  12 A  157  PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA          
SEQRES  13 A  157  LEU                                                          
SEQRES   1 B  157  VAL ARG SER SER SER ARG THR PRO SER ASP LYS PRO VAL          
SEQRES   2 B  157  ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY GLN LEU          
SEQRES   3 B  157  GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU ALA ASN          
SEQRES   4 B  157  GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL PRO SER          
SEQRES   5 B  157  GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU PHE LYS          
SEQRES   6 B  157  GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU THR HIS          
SEQRES   7 B  157  THR ILE SER ARG ILE VAL VAL SER TYR GLN THR LYS VAL          
SEQRES   8 B  157  ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN ARG GLU          
SEQRES   9 B  157  THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR GLU PRO          
SEQRES  10 B  157  ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS GLY ASP          
SEQRES  11 B  157  ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR LEU LEU          
SEQRES  12 B  157  PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA          
SEQRES  13 B  157  LEU                                                          
SEQRES   1 C  157  VAL ARG SER SER SER ARG THR PRO SER ASP LYS PRO VAL          
SEQRES   2 C  157  ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY GLN LEU          
SEQRES   3 C  157  GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU ALA ASN          
SEQRES   4 C  157  GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL PRO SER          
SEQRES   5 C  157  GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU PHE LYS          
SEQRES   6 C  157  GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU THR HIS          
SEQRES   7 C  157  THR ILE SER ARG ILE VAL VAL SER TYR GLN THR LYS VAL          
SEQRES   8 C  157  ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN ARG GLU          
SEQRES   9 C  157  THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR GLU PRO          
SEQRES  10 C  157  ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS GLY ASP          
SEQRES  11 C  157  ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR LEU LEU          
SEQRES  12 C  157  PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA          
SEQRES  13 C  157  LEU                                                          
SEQRES   1 D  157  VAL ARG SER SER SER ARG THR PRO SER ASP LYS PRO VAL          
SEQRES   2 D  157  ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY GLN LEU          
SEQRES   3 D  157  GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU ALA ASN          
SEQRES   4 D  157  GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL PRO SER          
SEQRES   5 D  157  GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU PHE LYS          
SEQRES   6 D  157  GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU THR HIS          
SEQRES   7 D  157  THR ILE SER ARG ILE VAL VAL SER TYR GLN THR LYS VAL          
SEQRES   8 D  157  ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN ARG GLU          
SEQRES   9 D  157  THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR GLU PRO          
SEQRES  10 D  157  ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS GLY ASP          
SEQRES  11 D  157  ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR LEU LEU          
SEQRES  12 D  157  PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA          
SEQRES  13 D  157  LEU                                                          
SEQRES   1 E  157  VAL ARG SER SER SER ARG THR PRO SER ASP LYS PRO VAL          
SEQRES   2 E  157  ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY GLN LEU          
SEQRES   3 E  157  GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU ALA ASN          
SEQRES   4 E  157  GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL PRO SER          
SEQRES   5 E  157  GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU PHE LYS          
SEQRES   6 E  157  GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU THR HIS          
SEQRES   7 E  157  THR ILE SER ARG ILE VAL VAL SER TYR GLN THR LYS VAL          
SEQRES   8 E  157  ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN ARG GLU          
SEQRES   9 E  157  THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR GLU PRO          
SEQRES  10 E  157  ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS GLY ASP          
SEQRES  11 E  157  ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR LEU LEU          
SEQRES  12 E  157  PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA          
SEQRES  13 E  157  LEU                                                          
SEQRES   1 F  157  VAL ARG SER SER SER ARG THR PRO SER ASP LYS PRO VAL          
SEQRES   2 F  157  ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY GLN LEU          
SEQRES   3 F  157  GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU ALA ASN          
SEQRES   4 F  157  GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL PRO SER          
SEQRES   5 F  157  GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU PHE LYS          
SEQRES   6 F  157  GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU THR HIS          
SEQRES   7 F  157  THR ILE SER ARG ILE VAL VAL SER TYR GLN THR LYS VAL          
SEQRES   8 F  157  ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN ARG GLU          
SEQRES   9 F  157  THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR GLU PRO          
SEQRES  10 F  157  ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS GLY ASP          
SEQRES  11 F  157  ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR LEU LEU          
SEQRES  12 F  157  PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA          
SEQRES  13 F  157  LEU                                                          
HELIX    1 H1A ARG A  138  LEU A  142  5                                   5    
HELIX    2 H1B ARG B  138  LEU B  142  5                                   5    
HELIX    3 H1C ARG C  138  LEU C  142  5                                   5    
HELIX    4 H1D ARG D  138  LEU D  142  5                                   5    
HELIX    5 H1E ARG E  138  LEU E  142  5                                   5    
HELIX    6 H1F ARG F  138  LEU F  142  5                                   5    
SHEET    1 S1A 5 LEU A  36  ALA A  38  0                                        
SHEET    2 S1A 5 PRO A  12  ALA A  18 -1  N  HIS A  15   O  LEU A  36           
SHEET    3 S1A 5 VAL A 150  LEU A 157 -1  O  VAL A 150   N  ALA A  18           
SHEET    4 S1A 5 GLY A  54  GLY A  68 -1  O  GLN A  61   N  TYR A 151           
SHEET    5 S1A 5 LYS A 112  LEU A 126 -1  N  LEU A 126   O  GLY A  54           
SHEET    1 S2A 5 GLU A  42  ARG A  44  0                                        
SHEET    2 S2A 5 GLN A  47  VAL A  50 -1  O  GLN A  47   N  ARG A  44           
SHEET    3 S2A 5 GLY A 129  ILE A 136 -1  N  GLY A 129   O  VAL A  50           
SHEET    4 S2A 5 LEU A  76  VAL A  84 -1  N  THR A  79   O  GLU A 135           
SHEET    5 S2A 5 GLN A  88  LYS A  98 -1  N  VAL A  91   O  ARG A  82           
SHEET    1 S1B 5 LEU B  36  ALA B  38  0                                        
SHEET    2 S1B 5 PRO B  12  ALA B  18 -1  N  HIS B  15   O  LEU B  36           
SHEET    3 S1B 5 VAL B 150  LEU B 157 -1  O  VAL B 150   N  ALA B  18           
SHEET    4 S1B 5 GLY B  54  GLY B  68 -1  O  GLN B  61   N  TYR B 151           
SHEET    5 S1B 5 LYS B 112  LEU B 126 -1  N  LEU B 126   O  GLY B  54           
SHEET    1 S2B 5 GLU B  42  ARG B  44  0                                        
SHEET    2 S2B 5 GLN B  47  VAL B  50 -1  O  GLN B  47   N  ARG B  44           
SHEET    3 S2B 5 GLY B 129  ILE B 136 -1  N  GLY B 129   O  VAL B  50           
SHEET    4 S2B 5 LEU B  76  VAL B  84 -1  N  THR B  79   O  GLU B 135           
SHEET    5 S2B 5 GLN B  88  LYS B  98 -1  N  VAL B  91   O  ARG B  82           
SHEET    1 S1C 5 LEU C  36  ALA C  38  0                                        
SHEET    2 S1C 5 PRO C  12  ALA C  18 -1  N  HIS C  15   O  LEU C  36           
SHEET    3 S1C 5 VAL C 150  LEU C 157 -1  O  VAL C 150   N  ALA C  18           
SHEET    4 S1C 5 GLY C  54  GLY C  68 -1  O  GLN C  61   N  TYR C 151           
SHEET    5 S1C 5 LYS C 112  LEU C 126 -1  N  LEU C 126   O  GLY C  54           
SHEET    1 S2C 5 GLU C  42  ARG C  44  0                                        
SHEET    2 S2C 5 GLN C  47  VAL C  50 -1  O  GLN C  47   N  ARG C  44           
SHEET    3 S2C 5 GLY C 129  ILE C 136 -1  N  GLY C 129   O  VAL C  50           
SHEET    4 S2C 5 LEU C  76  VAL C  84 -1  N  THR C  79   O  GLU C 135           
SHEET    5 S2C 5 GLN C  88  LYS C  98 -1  N  VAL C  91   O  ARG C  82           
SHEET    1 S1D 5 LEU D  36  ALA D  38  0                                        
SHEET    2 S1D 5 PRO D  12  ALA D  18 -1  N  HIS D  15   O  LEU D  36           
SHEET    3 S1D 5 VAL D 150  LEU D 157 -1  O  VAL D 150   N  ALA D  18           
SHEET    4 S1D 5 GLY D  54  GLY D  68 -1  O  GLN D  61   N  TYR D 151           
SHEET    5 S1D 5 LYS D 112  LEU D 126 -1  N  LEU D 126   O  GLY D  54           
SHEET    1 S2D 5 GLU D  42  ARG D  44  0                                        
SHEET    2 S2D 5 GLN D  47  VAL D  50 -1  O  GLN D  47   N  ARG D  44           
SHEET    3 S2D 5 GLY D 129  ILE D 136 -1  N  GLY D 129   O  VAL D  50           
SHEET    4 S2D 5 LEU D  76  VAL D  84 -1  N  THR D  79   O  GLU D 135           
SHEET    5 S2D 5 GLN D  88  LYS D  98 -1  N  VAL D  91   O  ARG D  82           
SHEET    1 S1E 5 LEU E  36  ALA E  38  0                                        
SHEET    2 S1E 5 PRO E  12  ALA E  18 -1  N  HIS E  15   O  LEU E  36           
SHEET    3 S1E 5 VAL E 150  LEU E 157 -1  O  VAL E 150   N  ALA E  18           
SHEET    4 S1E 5 GLY E  54  GLY E  68 -1  O  GLN E  61   N  TYR E 151           
SHEET    5 S1E 5 LYS E 112  LEU E 126 -1  N  LEU E 126   O  GLY E  54           
SHEET    1 S2E 5 GLU E  42  ARG E  44  0                                        
SHEET    2 S2E 5 GLN E  47  VAL E  50 -1  O  GLN E  47   N  ARG E  44           
SHEET    3 S2E 5 GLY E 129  ILE E 136 -1  N  GLY E 129   O  VAL E  50           
SHEET    4 S2E 5 LEU E  76  VAL E  84 -1  N  THR E  79   O  GLU E 135           
SHEET    5 S2E 5 GLN E  88  LYS E  98 -1  N  VAL E  91   O  ARG E  82           
SHEET    1 S1F 5 LEU F  36  ALA F  38  0                                        
SHEET    2 S1F 5 PRO F  12  ALA F  18 -1  N  HIS F  15   O  LEU F  36           
SHEET    3 S1F 5 VAL F 150  LEU F 157 -1  O  VAL F 150   N  ALA F  18           
SHEET    4 S1F 5 GLY F  54  GLY F  68 -1  O  GLN F  61   N  TYR F 151           
SHEET    5 S1F 5 LYS F 112  LEU F 126 -1  N  LEU F 126   O  GLY F  54           
SHEET    1 S2F 5 GLU F  42  ARG F  44  0                                        
SHEET    2 S2F 5 GLN F  47  VAL F  50 -1  O  GLN F  47   N  ARG F  44           
SHEET    3 S2F 5 GLY F 129  ILE F 136 -1  N  GLY F 129   O  VAL F  50           
SHEET    4 S2F 5 LEU F  76  VAL F  84 -1  N  THR F  79   O  GLU F 135           
SHEET    5 S2F 5 GLN F  88  LYS F  98 -1  N  VAL F  91   O  ARG F  82           
SSBOND   1 CYS A   69    CYS A  101                          1555   1555  2.07  
SSBOND   2 CYS B   69    CYS B  101                          1555   1555  2.08  
SSBOND   3 CYS C   69    CYS C  101                          1555   1555  2.07  
SSBOND   4 CYS D   69    CYS D  101                          1555   1555  2.07  
SSBOND   5 CYS E   69    CYS E  101                          1555   1555  2.09  
SSBOND   6 CYS F   69    CYS F  101                          1555   1555  2.08  
CISPEP   1 THR B    7    PRO B    8          0        27.64                     
CRYST1  166.000  166.000   93.700  90.00  90.00 120.00 P 31 2 1     36          
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      0.006024  0.003478  0.000000        0.00000                         
SCALE2      0.000000  0.006956  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010672        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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