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Database: PDB
Entry: 1A8M
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Original site: 1A8M 
HEADER    LYMPHOKINE                              27-MAR-98   1A8M              
TITLE     TUMOR NECROSIS FACTOR ALPHA, R31D MUTANT                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TUMOR NECROSIS FACTOR ALPHA;                               
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 SYNONYM: TNF-ALPHA;                                                  
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: 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                                         
KEYWDS    LYMPHOKINE, CYTOKINE, CYTOTOXIN                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.REED,Z.-Q.FU,J.WU,Y.-N.XUE,R.W.HARRISON,M.-J.CHEN,                  
AUTHOR   2 I.T.WEBER                                                            
REVDAT   2   24-FEB-09 1A8M    1       VERSN                                    
REVDAT   1   17-JUN-98 1A8M    0                                                
JRNL        AUTH   C.REED,Z.Q.FU,J.WU,Y.N.XUE,R.W.HARRISON,M.J.CHEN,            
JRNL        AUTH 2 I.T.WEBER                                                    
JRNL        TITL   CRYSTAL STRUCTURE OF TNF-ALPHA MUTANT R31D WITH              
JRNL        TITL 2 GREATER AFFINITY FOR RECEPTOR R1 COMPARED WITH R2.           
JRNL        REF    PROTEIN ENG.                  V.  10  1101 1997              
JRNL        REFN                   ISSN 0269-2139                               
JRNL        PMID   9488135                                                      
JRNL        DOI    10.1093/PROTEIN/10.10.1101                                   
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   Z.Q.FU,R.W.HARRISON,C.REED,J.WU,Y.N.XUE,M.J.CHEN,            
REMARK   1  AUTH 2 I.T.WEBER                                                    
REMARK   1  TITL   MODEL COMPLEXES OF TUMOR NECROSIS FACTOR-ALPHA               
REMARK   1  TITL 2 WITH RECEPTORS R1 AND R2                                     
REMARK   1  REF    PROTEIN ENG.                  V.   8  1233 1995              
REMARK   1  REFN                   ISSN 0269-2139                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 21396                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.218                           
REMARK   3   FREE R VALUE                     : 0.240                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 8.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1171                            
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            : 4347                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 69                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.00                          
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) : 0.013                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.30                            
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  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1A8M 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        : JUL-94                             
REMARK 200  TEMPERATURE           (KELVIN) : 290                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RUH2R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NI                                 
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : PROCESS                            
REMARK 200  DATA SCALING SOFTWARE          : PROCESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21396                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 10.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.07800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.40                     
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         : 1.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR 3.1                                            
REMARK 200 STARTING MODEL: PDB ENTRY 1TNF                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALLIZED FROM 88% MGSO4, 1-2%        
REMARK 280  PEG 400, 0.2 M MES, PH 5.5.                                         
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       58.70000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       47.35000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       47.35000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       29.35000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       47.35000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       47.35000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       88.05000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       47.35000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       47.35000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       29.35000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       47.35000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       47.35000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       88.05000            
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       58.70000            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7470 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17930 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NH2  ARG B   131     O    HOH A   212     4454     1.82            
REMARK 500   NE2  GLN A    88     O    ASP B    31     8665     1.90            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A 157   CA  -  CB  -  CG  ANGL. DEV. =  17.8 DEGREES          
REMARK 500    PHE B 144   N   -  CA  -  C   ANGL. DEV. =  21.9 DEGREES          
REMARK 500    SER B 147   N   -  CA  -  C   ANGL. DEV. = -17.7 DEGREES          
REMARK 500    LEU C  37   N   -  CA  -  C   ANGL. DEV. = -17.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A   9      145.47     47.91                                   
REMARK 500    HIS A  15       82.11   -172.50                                   
REMARK 500    PRO A  20       37.07    -77.03                                   
REMARK 500    ALA A  33     -136.42     49.00                                   
REMARK 500    ASN A  34       41.31   -109.91                                   
REMARK 500    ALA A  35       74.47    -61.82                                   
REMARK 500    LEU A  37       61.83   -162.59                                   
REMARK 500    ALA A  38     -159.43    -72.06                                   
REMARK 500    ASN A  39       68.33    -27.60                                   
REMARK 500    ARG A  44     -104.87   -111.60                                   
REMARK 500    ASP A  45       42.80    -81.50                                   
REMARK 500    ASN A  46       28.74     84.43                                   
REMARK 500    GLU A  53      173.99    -56.99                                   
REMARK 500    PRO A  70     -118.76    -89.23                                   
REMARK 500    THR A  72      -29.97    -16.01                                   
REMARK 500    LEU A  75       81.07     68.37                                   
REMARK 500    CYS A 101       90.48     64.72                                   
REMARK 500    ARG A 103      -83.08     61.39                                   
REMARK 500    GLU A 104      -90.22     47.75                                   
REMARK 500    THR A 105       67.88     61.22                                   
REMARK 500    ALA A 109       49.61   -102.35                                   
REMARK 500    LEU A 120      147.04    169.47                                   
REMARK 500    PHE A 144       -0.36   -140.02                                   
REMARK 500    SER A 147      -82.34    -90.56                                   
REMARK 500    GLN A 149      -76.49   -125.59                                   
REMARK 500    PHE A 152      120.25   -175.71                                   
REMARK 500    PRO B   8       30.73    -76.32                                   
REMARK 500    SER B   9     -160.71     48.08                                   
REMARK 500    ALA B  14      129.44    179.53                                   
REMARK 500    ASP B  31       22.33    162.25                                   
REMARK 500    LEU B  37       70.05   -166.04                                   
REMARK 500    ARG B  44      -96.07   -103.89                                   
REMARK 500    THR B  72      111.11     63.62                                   
REMARK 500    SER B  86      -77.44    -65.98                                   
REMARK 500    LEU B  93      -92.09    -81.63                                   
REMARK 500    ALA B  96      140.13   -172.26                                   
REMARK 500    GLN B 102      -50.46   -129.93                                   
REMARK 500    ARG B 103      161.84    -31.01                                   
REMARK 500    THR B 105       95.25     80.71                                   
REMARK 500    PRO B 106      153.96     -1.74                                   
REMARK 500    GLU B 107      -92.08   -158.78                                   
REMARK 500    ALA B 109      119.31   -169.29                                   
REMARK 500    GLU B 110     -168.24    -73.93                                   
REMARK 500    ALA B 111     -139.21     49.74                                   
REMARK 500    LYS B 112       96.21     73.94                                   
REMARK 500    SER B 133      117.83   -171.18                                   
REMARK 500    PHE B 144       45.64   -154.12                                   
REMARK 500    ALA B 145       48.39    -93.56                                   
REMARK 500    GLU B 146      -95.77    -74.54                                   
REMARK 500    SER B 147       94.39     79.66                                   
REMARK 500    SER C   9      115.62     52.80                                   
REMARK 500    ASP C  10     -137.06    -87.99                                   
REMARK 500    LYS C  11      132.53     77.60                                   
REMARK 500    PRO C  20      -87.14    -59.03                                   
REMARK 500    GLN C  21       84.18    -53.57                                   
REMARK 500    ALA C  22       63.73   -165.92                                   
REMARK 500    GLU C  23      109.68    -30.23                                   
REMARK 500    GLN C  25      -30.06   -136.24                                   
REMARK 500    LEU C  26       78.29     61.66                                   
REMARK 500    ASP C  31      -39.42     95.20                                   
REMARK 500    ARG C  32      177.34    -55.96                                   
REMARK 500    ALA C  33     -112.02     15.17                                   
REMARK 500    LEU C  37      119.19   -167.05                                   
REMARK 500    VAL C  41       62.84   -110.30                                   
REMARK 500    GLU C  42      152.08    -47.00                                   
REMARK 500    SER C  52      144.84     88.69                                   
REMARK 500    SER C  60      148.52   -173.20                                   
REMARK 500    SER C  71       47.27   -101.51                                   
REMARK 500    THR C  72       22.42   -144.79                                   
REMARK 500    HIS C  73       99.82     47.78                                   
REMARK 500    SER C  86      -89.51    -70.40                                   
REMARK 500    GLN C  88      -19.78     64.15                                   
REMARK 500    ARG C 103      107.00     34.19                                   
REMARK 500    GLU C 104      -58.01   -124.10                                   
REMARK 500    THR C 105       96.78     64.66                                   
REMARK 500    PRO C 106      109.06    -54.25                                   
REMARK 500    ALA C 111      177.14     97.01                                   
REMARK 500    LYS C 112      108.26    136.15                                   
REMARK 500    LYS C 128      109.96    -33.25                                   
REMARK 500    ARG C 138       75.89   -113.71                                   
REMARK 500    TYR C 141       54.05   -110.30                                   
REMARK 500    GLU C 146       92.26     19.38                                   
REMARK 500    SER C 147      -75.67    -93.86                                   
REMARK 500    ILE C 155      135.87   -175.71                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 200        DISTANCE =  5.23 ANGSTROMS                       
REMARK 525    HOH B 215        DISTANCE =  6.25 ANGSTROMS                       
REMARK 525    HOH C 231        DISTANCE =  6.64 ANGSTROMS                       
REMARK 525    HOH C 232        DISTANCE =  5.19 ANGSTROMS                       
REMARK 525    HOH B 221        DISTANCE =  5.07 ANGSTROMS                       
REMARK 525    HOH C 239        DISTANCE =  5.56 ANGSTROMS                       
REMARK 525    HOH C 241        DISTANCE =  5.16 ANGSTROMS                       
REMARK 525    HOH B 227        DISTANCE =  5.21 ANGSTROMS                       
REMARK 525    HOH B 251        DISTANCE =  5.95 ANGSTROMS                       
REMARK 525    HOH B 252        DISTANCE =  8.20 ANGSTROMS                       
DBREF  1A8M A    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  1A8M B    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  1A8M C    1   157  UNP    P01375   TNFA_HUMAN      77    233             
SEQADV 1A8M ASP A   31  UNP  P01375    ARG   107 ENGINEERED                     
SEQADV 1A8M ASP B   31  UNP  P01375    ARG   107 ENGINEERED                     
SEQADV 1A8M ASP C   31  UNP  P01375    ARG   107 ENGINEERED                     
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 ASP 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 ASP          
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 ASP 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 ASP          
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 ASP 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 ASP          
SEQRES  12 C  157  PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA          
SEQRES  13 C  157  LEU                                                          
FORMUL   4  HOH   *69(H2 O)                                                     
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  2.56  
SSBOND   2 CYS B   69    CYS B  101                          1555   1555  2.40  
SSBOND   3 CYS C   69    CYS C  101                          1555   1555  2.36  
CRYST1   94.700   94.700  117.400  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      0.010560  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010560  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008518        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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