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Database: PDB
Entry: 1TNF
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Original site: 1TNF 
HEADER    LYMPHOKINE                              25-AUG-89   1TNF              
TITLE     THE STRUCTURE OF TUMOR NECROSIS FACTOR-ALPHA AT 2.6                   
TITLE    2 ANGSTROMS RESOLUTION. IMPLICATIONS FOR RECEPTOR BINDING              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TUMOR NECROSIS FACTOR-ALPHA;                               
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 ENGINEERED: 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    M.J.ECK,S.R.SPRANG                                                    
REVDAT   4   24-FEB-09 1TNF    1       VERSN                                    
REVDAT   3   01-APR-03 1TNF    1       JRNL                                     
REVDAT   2   15-JAN-91 1TNF    1       REMARK                                   
REVDAT   1   15-JAN-90 1TNF    0                                                
JRNL        AUTH   M.J.ECK,S.R.SPRANG                                           
JRNL        TITL   THE STRUCTURE OF TUMOR NECROSIS FACTOR-ALPHA AT              
JRNL        TITL 2 2.6 A RESOLUTION. IMPLICATIONS FOR RECEPTOR                  
JRNL        TITL 3 BINDING.                                                     
JRNL        REF    J.BIOL.CHEM.                  V. 264 17595 1989              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   2551905                                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   M.J.ECK,B.BEUTLER,G.KUO,J.P.MERRYWEATHER,S.R.SPRANG          
REMARK   1  TITL   CRYSTALLIZATION OF TRIMERIC RECOMBINANT HUMAN                
REMARK   1  TITL 2 TUMOR NECROSIS FACTOR (CACHECTIN)                            
REMARK   1  REF    J.BIOL.CHEM.                  V. 263 12816 1988              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL                           
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  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.230                           
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   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            : 3552                                    
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  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) : 0.015                           
REMARK   3   BOND ANGLES            (DEGREES) : 4.10                            
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  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 1TNF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
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: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.41                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       58.50000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       47.50000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       47.50000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       29.25000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       47.50000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       47.50000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       87.75000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       47.50000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       47.50000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       29.25000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       47.50000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       47.50000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       87.75000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       58.50000            
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 300 REMARK:                                                              
REMARK 300 THE MOLECULE EXISTS AS A TRIMER IN WHICH THE THREE SUBUNITS          
REMARK 300 ARE RELATED BY APPROXIMATE THREE-FOLD SYMMETRY.  THE THREE           
REMARK 300 SUBUNITS HAVE BEEN ASSIGNED CHAIN INDICATORS A, B, AND C.            
REMARK 300 THE TRANSFORMATION PRESENTED ON *MTRIX 1* RECORDS BELOW              
REMARK 300 WILL YIELD APPROXIMATE COORDINATES FOR CHAIN B WHEN APPLIED          
REMARK 300 TO CHAIN A.  THE TRANSFORMATION PRESENTED ON *MTRIX 2*               
REMARK 300 RECORDS BELOW WILL YIELD APPROXIMATE COORDINATES FOR CHAIN           
REMARK 300 C WHEN APPLIED TO CHAIN A.  THE TRANSFORMATION PRESENTED ON          
REMARK 300 *MTRIX 3* RECORDS BELOW WILL YIELD APPROXIMATE COORDINATES           
REMARK 300 FOR CHAIN C WHEN APPLIED TO CHAIN B.                                 
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7040 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18400 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 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     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     VAL C     1                                                      
REMARK 465     ARG C     2                                                      
REMARK 465     SER C     3                                                      
REMARK 465     SER C     4                                                      
REMARK 465     SER C     5                                                      
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     ARG A   6    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B   6    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C   6    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    HIS A  15   NE2   HIS A  15   CD2    -0.078                       
REMARK 500    HIS A  73   NE2   HIS A  73   CD2    -0.067                       
REMARK 500    HIS A  78   NE2   HIS A  78   CD2    -0.079                       
REMARK 500    HIS B  15   NE2   HIS B  15   CD2    -0.077                       
REMARK 500    HIS B  73   NE2   HIS B  73   CD2    -0.067                       
REMARK 500    HIS B  78   NE2   HIS B  78   CD2    -0.068                       
REMARK 500    HIS C  15   NE2   HIS C  15   CD2    -0.076                       
REMARK 500    HIS C  73   NE2   HIS C  73   CD2    -0.071                       
REMARK 500    HIS C  78   NE2   HIS C  78   CD2    -0.073                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    TRP A  28   CD1 -  CG  -  CD2 ANGL. DEV. =   7.6 DEGREES          
REMARK 500    TRP A  28   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.8 DEGREES          
REMARK 500    ARG A  32   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG A  32   NE  -  CZ  -  NH2 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    LEU A  37   N   -  CA  -  C   ANGL. DEV. = -18.5 DEGREES          
REMARK 500    LEU A  43   CA  -  CB  -  CG  ANGL. DEV. =  14.5 DEGREES          
REMARK 500    ARG A  44   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG A  44   NE  -  CZ  -  NH2 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    CYS A  69   CA  -  CB  -  SG  ANGL. DEV. = -15.4 DEGREES          
REMARK 500    HIS A  73   CA  -  CB  -  CG  ANGL. DEV. = -13.6 DEGREES          
REMARK 500    ARG A  82   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    ARG A  82   NE  -  CZ  -  NH2 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    VAL A  85   CA  -  CB  -  CG2 ANGL. DEV. = -11.3 DEGREES          
REMARK 500    TYR A  87   CA  -  CB  -  CG  ANGL. DEV. =  13.0 DEGREES          
REMARK 500    CYS A 101   CA  -  CB  -  SG  ANGL. DEV. = -11.3 DEGREES          
REMARK 500    GLN A 102   N   -  CA  -  C   ANGL. DEV. = -19.0 DEGREES          
REMARK 500    ARG A 103   NE  -  CZ  -  NH2 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    TRP A 114   CD1 -  CG  -  CD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    TRP A 114   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ARG A 138   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    ARG A 138   NE  -  CZ  -  NH2 ANGL. DEV. =   8.1 DEGREES          
REMARK 500    THR B   7   N   -  CA  -  CB  ANGL. DEV. = -11.6 DEGREES          
REMARK 500    TRP B  28   CD1 -  CG  -  CD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    TRP B  28   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    LEU B  29   CA  -  CB  -  CG  ANGL. DEV. =  15.1 DEGREES          
REMARK 500    SER B  71   CA  -  C   -  N   ANGL. DEV. = -13.9 DEGREES          
REMARK 500    ARG B  82   CA  -  CB  -  CG  ANGL. DEV. =  14.2 DEGREES          
REMARK 500    GLN B  88   CA  -  CB  -  CG  ANGL. DEV. =  22.2 DEGREES          
REMARK 500    ALA B 111   N   -  CA  -  C   ANGL. DEV. =  17.0 DEGREES          
REMARK 500    TRP B 114   CD1 -  CG  -  CD2 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    TRP B 114   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    ARG B 131   NE  -  CZ  -  NH2 ANGL. DEV. =   5.2 DEGREES          
REMARK 500    ARG B 138   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.8 DEGREES          
REMARK 500    ARG B 138   NE  -  CZ  -  NH2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    TYR B 151   CB  -  CG  -  CD1 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ASP C  10   CA  -  C   -  N   ANGL. DEV. = -14.5 DEGREES          
REMARK 500    TRP C  28   CD1 -  CG  -  CD2 ANGL. DEV. =   5.0 DEGREES          
REMARK 500    TRP C  28   CB  -  CG  -  CD1 ANGL. DEV. =  -7.8 DEGREES          
REMARK 500    TRP C  28   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    TRP C  28   CG  -  CD2 -  CE3 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ARG C  32   NE  -  CZ  -  NH2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ALA C  38   CA  -  C   -  N   ANGL. DEV. = -14.9 DEGREES          
REMARK 500    ALA C  38   O   -  C   -  N   ANGL. DEV. =  10.2 DEGREES          
REMARK 500    ARG C  44   NE  -  CZ  -  NH2 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG C  44   CA  -  C   -  N   ANGL. DEV. =  16.0 DEGREES          
REMARK 500    ARG C  82   NE  -  CZ  -  NH2 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    TYR C  87   CA  -  CB  -  CG  ANGL. DEV. =  11.7 DEGREES          
REMARK 500    TYR C  87   CB  -  CG  -  CD2 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    TYR C  87   N   -  CA  -  C   ANGL. DEV. = -18.8 DEGREES          
REMARK 500    GLN C  88   CA  -  CB  -  CG  ANGL. DEV. = -14.8 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      58 ANGLE DEVIATIONS.                             
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A   9      154.98     58.28                                   
REMARK 500    ASP A  10       55.79    -90.64                                   
REMARK 500    ALA A  22       98.18   -165.86                                   
REMARK 500    ASN A  30     -133.94   -127.53                                   
REMARK 500    ARG A  31      -33.09     60.04                                   
REMARK 500    ARG A  32     -163.66    -65.01                                   
REMARK 500    ALA A  35       78.59   -116.21                                   
REMARK 500    ALA A  38     -131.11   -116.98                                   
REMARK 500    ASN A  39       77.03    -65.69                                   
REMARK 500    ARG A  44     -107.79   -124.84                                   
REMARK 500    PRO A  70     -126.62    -87.44                                   
REMARK 500    THR A  72      -60.61     31.06                                   
REMARK 500    LEU A  75      103.22     55.43                                   
REMARK 500    SER A  86      -60.69   -123.03                                   
REMARK 500    PRO A 100     -110.81    -68.93                                   
REMARK 500    ARG A 103      172.65     59.19                                   
REMARK 500    GLU A 104      -58.23    143.33                                   
REMARK 500    GLU A 107      -31.40     18.65                                   
REMARK 500    GLU A 110      -87.20    -67.71                                   
REMARK 500    GLN A 149      -73.58   -141.29                                   
REMARK 500    ILE A 155      121.56   -174.04                                   
REMARK 500    PRO B   8      -78.54    -50.97                                   
REMARK 500    SER B   9      146.20    167.72                                   
REMARK 500    ASP B  10       64.27   -103.98                                   
REMARK 500    HIS B  15       77.63   -153.63                                   
REMARK 500    GLN B  21       26.68    -73.04                                   
REMARK 500    ASN B  30     -166.03   -107.29                                   
REMARK 500    ASN B  34       42.98   -148.92                                   
REMARK 500    LEU B  37       96.98    174.36                                   
REMARK 500    ARG B  44      -91.17    -99.22                                   
REMARK 500    ASP B  45       55.54    -93.50                                   
REMARK 500    SER B  60      130.97   -171.65                                   
REMARK 500    THR B  72     -123.74     47.18                                   
REMARK 500    LEU B  75      109.50     52.56                                   
REMARK 500    ALA B  84     -151.23    -49.81                                   
REMARK 500    VAL B  85      -31.99   -140.06                                   
REMARK 500    SER B  86     -102.29    -87.76                                   
REMARK 500    GLN B  88       63.62    -57.32                                   
REMARK 500    ARG B 103      163.73     61.78                                   
REMARK 500    GLU B 104      -50.73    153.78                                   
REMARK 500    PRO B 106       87.78    -67.85                                   
REMARK 500    GLU B 107      -71.30    -56.25                                   
REMARK 500    ALA B 109      -48.37   -148.90                                   
REMARK 500    GLU B 110      -26.84     73.32                                   
REMARK 500    ALA B 111      160.41     73.81                                   
REMARK 500    ALA B 145       45.13    -93.71                                   
REMARK 500    SER B 147      -78.36   -112.27                                   
REMARK 500    GLN B 149      -26.37   -144.57                                   
REMARK 500    PRO C   8     -169.31    -72.71                                   
REMARK 500    SER C   9       75.82     53.10                                   
REMARK 500    PRO C  12      127.54    -37.13                                   
REMARK 500    ALA C  18     -164.34    -76.91                                   
REMARK 500    PRO C  20       38.76    -80.12                                   
REMARK 500    GLU C  23      -40.52    -14.82                                   
REMARK 500    GLN C  25      -56.97   -155.27                                   
REMARK 500    LEU C  26       58.28     88.63                                   
REMARK 500    ARG C  31      -27.14    115.06                                   
REMARK 500    ARG C  32      151.06    -43.68                                   
REMARK 500    ALA C  33      -53.20    -16.54                                   
REMARK 500    ASN C  39       76.83     33.42                                   
REMARK 500    ARG C  44     -113.93   -121.98                                   
REMARK 500    PRO C  51     -147.38    -83.35                                   
REMARK 500    SER C  52      -90.56     36.91                                   
REMARK 500    GLU C  53      158.88    136.41                                   
REMARK 500    THR C  72      150.01     72.41                                   
REMARK 500    LEU C  75       95.80     34.05                                   
REMARK 500    SER C  86     -100.31    -93.20                                   
REMARK 500    GLN C  88     -166.00    -69.95                                   
REMARK 500    THR C  89      165.30     84.36                                   
REMARK 500    GLU C 104      -48.98   -137.67                                   
REMARK 500    PRO C 106       70.52    -20.35                                   
REMARK 500    GLU C 107      -85.93    -90.44                                   
REMARK 500    GLU C 110      128.42    -32.37                                   
REMARK 500    ALA C 111       84.81     20.53                                   
REMARK 500    LYS C 128      110.41    -38.55                                   
REMARK 500    TYR C 141       30.61    -84.03                                   
REMARK 500    ALA C 145       58.55   -172.39                                   
REMARK 500    SER C 147      -78.19   -163.32                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 THR A    7     PRO A    8                  117.21                    
REMARK 500 THR A  105     PRO A  106                  -99.71                    
REMARK 500 THR B    7     PRO B    8                  144.02                    
REMARK 500 THR B  105     PRO B  106                 -142.83                    
REMARK 500 THR C    7     PRO C    8                   51.13                    
REMARK 500 LYS C   11     PRO C   12                  135.94                    
REMARK 500 GLU C  146     SER C  147                  141.65                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1TNF A    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  1TNF B    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  1TNF C    1   157  UNP    P01375   TNFA_HUMAN      77    233             
SEQADV 1TNF ASP A   45  UNP  P01375    LEU   219 CONFLICT                       
SEQADV 1TNF ASP B   45  UNP  P01375    LEU   219 CONFLICT                       
SEQADV 1TNF ASP C   45  UNP  P01375    LEU   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 ALA 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 ALA 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 ALA 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                                                          
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    
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  ALA 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  ALA 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  ALA 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           
SSBOND   1 CYS A   69    CYS A  101                          1555   1555  1.99  
SSBOND   2 CYS B   69    CYS B  101                          1555   1555  2.03  
SSBOND   3 CYS C   69    CYS C  101                          1555   1555  2.02  
CRYST1   95.000   95.000  117.000  90.00  90.00  90.00 P 41 21 2    24          
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      0.010526  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010526  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008547        0.00000                         
MTRIX1   1  0.040460 -0.105750  0.993570      -16.17000    1                    
MTRIX2   1 -0.980650  0.186430  0.059780       57.43000    1                    
MTRIX3   1 -0.191550 -0.976760 -0.096160       96.33000    1                    
MTRIX1   2 -0.028960 -0.992710 -0.116990       74.40000    1                    
MTRIX2   2 -0.202020  0.120440 -0.971950       87.33000    1                    
MTRIX3   2  0.978950 -0.004510 -0.204040       28.89000    1                    
MTRIX1   3 -0.012020 -0.163460  0.986460      -11.46000    1                    
MTRIX2   3 -0.986560  0.162730  0.014940       60.62000    1                    
MTRIX3   3 -0.162970 -0.973040 -0.163220       97.89000    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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