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Database: PDB
Entry: 2AZ5
LinkDB: 2AZ5
Original site: 2AZ5 
HEADER    CYTOKINE                                09-SEP-05   2AZ5              
TITLE     CRYSTAL STRUCTURE OF TNF-ALPHA WITH A SMALL MOLECULE                  
TITLE    2 INHIBITOR                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TUMOR NECROSIS FACTOR (TNF-ALPHA) (TUMOR                   
COMPND   3 NECROSIS FACTOR LIGAND SUPERFAMILY MEMBER 2) (TNF-A)                 
COMPND   4 (CACHECTIN) [CONTAINS: TUMOR NECROSIS FACTOR, MEMBRANE               
COMPND   5 FORM; TUMOR NECROSIS FACTOR, SOLUBLE FORM];                          
COMPND   6 CHAIN: A, B, C, D;                                                   
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: TNF, TNFA, TNFSF2;                                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PRSET                                     
KEYWDS    TNF-ALPHA TRIMER DISRUPTION BY BINDING OF A SMALL MOLECULE            
KEYWDS   2 INHIBITOR, CYTOKINE                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.M.HE                                                                
REVDAT   4   24-FEB-09 2AZ5    1       VERSN                                    
REVDAT   3   18-APR-06 2AZ5    1       AUTHOR                                   
REVDAT   2   06-DEC-05 2AZ5    1       AUTHOR                                   
REVDAT   1   29-NOV-05 2AZ5    0                                                
JRNL        AUTH   M.M.HE,A.S.SMITH,J.D.OSLOB,W.M.FLANAGAN,                     
JRNL        AUTH 2 A.C.BRAISTED,A.WHITTY,M.T.CANCILLA,J.WANG,                   
JRNL        AUTH 3 A.A.LUGOVSKOY,J.C.YOBURN,A.D.FUNG,G.FARRINGTON,              
JRNL        AUTH 4 J.K.ELDREDGE,E.S.DAY,L.A.CRUZ,T.G.CACHERO,                   
JRNL        AUTH 5 S.K.MILLER,J.E.FRIEDMAN,I.C.CHOONG,B.C.CUNNINGHAM            
JRNL        TITL   SMALL-MOLECULE INHIBITION OF TNF-ALPHA.                      
JRNL        REF    SCIENCE                       V. 310  1022 2005              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   16284179                                                     
JRNL        DOI    10.1126/SCIENCE.1116304                                      
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 37535                          
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 + TEST SET) : 0.227                           
REMARK   3   R VALUE            (WORKING SET) : 0.220                           
REMARK   3   FREE R VALUE                     : 0.278                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1916                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 15                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.17                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3496                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.95                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2270                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 196                          
REMARK   3   BIN FREE R VALUE                    : 0.2830                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4194                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 80                                      
REMARK   3   SOLVENT ATOMS            : 226                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.78                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.57000                                             
REMARK   3    B22 (A**2) : -0.57000                                             
REMARK   3    B33 (A**2) : 0.86000                                              
REMARK   3    B12 (A**2) : -0.29000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.231         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.212         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.153         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.550         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.940                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.891                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4376 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5968 ; 1.396 ; 1.989       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   531 ; 6.734 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   184 ;39.195 ;24.511       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   684 ;14.902 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;15.132 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   672 ; 0.091 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3302 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1854 ; 0.203 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2908 ; 0.311 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   278 ; 0.139 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    70 ; 0.185 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    12 ; 0.072 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2757 ; 3.420 ; 2.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4319 ; 4.870 ; 5.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1976 ; 3.598 ; 2.500       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1649 ; 5.359 ; 5.000       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2AZ5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-SEP-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB034476.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-MAR-03                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 37559                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY: 1TNF                                      
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.5 M SODIUM FORMATE, PH 7.5, VAPOR      
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 323K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       82.62700            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       47.70472            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       21.24267            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       82.62700            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       47.70472            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       21.24267            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       82.62700            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       47.70472            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       21.24267            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       95.40944            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       42.48533            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       95.40944            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       42.48533            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       95.40944            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       42.48533            
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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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     ARG A    31                                                      
REMARK 465     ARG A    32                                                      
REMARK 465     ALA A    33                                                      
REMARK 465     ASN A    34                                                      
REMARK 465     ALA A    35                                                      
REMARK 465     GLN A   102                                                      
REMARK 465     ARG A   103                                                      
REMARK 465     GLU A   104                                                      
REMARK 465     THR A   105                                                      
REMARK 465     PRO A   106                                                      
REMARK 465     GLU A   107                                                      
REMARK 465     GLY A   108                                                      
REMARK 465     ALA A   109                                                      
REMARK 465     GLU A   110                                                      
REMARK 465     ALA A   111                                                      
REMARK 465     LYS A   112                                                      
REMARK 465     GLU B   104                                                      
REMARK 465     THR B   105                                                      
REMARK 465     PRO B   106                                                      
REMARK 465     GLU B   107                                                      
REMARK 465     GLY B   108                                                      
REMARK 465     ALA B   109                                                      
REMARK 465     GLU B   110                                                      
REMARK 465     ALA B   111                                                      
REMARK 465     ARG C    31                                                      
REMARK 465     ARG C    32                                                      
REMARK 465     ALA C    33                                                      
REMARK 465     ASN C    34                                                      
REMARK 465     ALA C    35                                                      
REMARK 465     SER C    86                                                      
REMARK 465     TYR C    87                                                      
REMARK 465     GLN C    88                                                      
REMARK 465     GLN C   102                                                      
REMARK 465     ARG C   103                                                      
REMARK 465     GLU C   104                                                      
REMARK 465     THR C   105                                                      
REMARK 465     PRO C   106                                                      
REMARK 465     GLU C   107                                                      
REMARK 465     GLY C   108                                                      
REMARK 465     ALA C   109                                                      
REMARK 465     GLU C   110                                                      
REMARK 465     ALA C   111                                                      
REMARK 465     LYS C   112                                                      
REMARK 465     GLU D   104                                                      
REMARK 465     THR D   105                                                      
REMARK 465     PRO D   106                                                      
REMARK 465     GLU D   107                                                      
REMARK 465     GLY D   108                                                      
REMARK 465     ALA D   109                                                      
REMARK 465     GLU D   110                                                      
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     ASP A  10    CG   OD1  OD2                                       
REMARK 470     TYR A  87    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU A 146    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 157    O                                                   
REMARK 470     ASP B  10    CG   OD1  OD2                                       
REMARK 470     GLU B  23    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 103    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 146    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 157    O                                                   
REMARK 470     ASP C  10    CG   OD1  OD2                                       
REMARK 470     LEU C 157    O                                                   
REMARK 470     ASP D  10    CG   OD1  OD2                                       
REMARK 470     GLU D  23    CG   CD   OE1  OE2                                  
REMARK 470     TYR D  87    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG D 103    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 112    CG   CD   CE   NZ                                   
REMARK 470     LEU D 157    O                                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A  37       84.55   -151.55                                   
REMARK 500    PRO A  70     -163.08    -79.33                                   
REMARK 500    ARG B  31       43.78    -86.43                                   
REMARK 500    GLN B  88       -9.14     60.17                                   
REMARK 500    LEU C  37       84.47   -156.29                                   
REMARK 500    PRO C  70     -153.34    -78.81                                   
REMARK 500    ARG D  31       49.70    -83.03                                   
REMARK 500    GLN D  88        5.58    -58.85                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 307 A 1                   
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 307 C 2                   
DBREF  2AZ5 A   10   157  UNP    P01375   TNFA_HUMAN      86    233             
DBREF  2AZ5 B   10   157  UNP    P01375   TNFA_HUMAN      86    233             
DBREF  2AZ5 C   10   157  UNP    P01375   TNFA_HUMAN      86    233             
DBREF  2AZ5 D   10   157  UNP    P01375   TNFA_HUMAN      86    233             
SEQRES   1 A  148  ASP LYS PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA          
SEQRES   2 A  148  GLU GLY GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA          
SEQRES   3 A  148  LEU LEU ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU          
SEQRES   4 A  148  VAL VAL PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN          
SEQRES   5 A  148  VAL LEU PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL          
SEQRES   6 A  148  LEU LEU THR HIS THR ILE SER ARG ILE ALA VAL SER TYR          
SEQRES   7 A  148  GLN THR LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO          
SEQRES   8 A  148  CYS GLN ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO          
SEQRES   9 A  148  TRP TYR GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU          
SEQRES  10 A  148  GLU LYS GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO          
SEQRES  11 A  148  ASP TYR LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE          
SEQRES  12 A  148  GLY ILE ILE ALA LEU                                          
SEQRES   1 B  148  ASP LYS PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA          
SEQRES   2 B  148  GLU GLY GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA          
SEQRES   3 B  148  LEU LEU ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU          
SEQRES   4 B  148  VAL VAL PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN          
SEQRES   5 B  148  VAL LEU PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL          
SEQRES   6 B  148  LEU LEU THR HIS THR ILE SER ARG ILE ALA VAL SER TYR          
SEQRES   7 B  148  GLN THR LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO          
SEQRES   8 B  148  CYS GLN ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO          
SEQRES   9 B  148  TRP TYR GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU          
SEQRES  10 B  148  GLU LYS GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO          
SEQRES  11 B  148  ASP TYR LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE          
SEQRES  12 B  148  GLY ILE ILE ALA LEU                                          
SEQRES   1 C  148  ASP LYS PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA          
SEQRES   2 C  148  GLU GLY GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA          
SEQRES   3 C  148  LEU LEU ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU          
SEQRES   4 C  148  VAL VAL PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN          
SEQRES   5 C  148  VAL LEU PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL          
SEQRES   6 C  148  LEU LEU THR HIS THR ILE SER ARG ILE ALA VAL SER TYR          
SEQRES   7 C  148  GLN THR LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO          
SEQRES   8 C  148  CYS GLN ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO          
SEQRES   9 C  148  TRP TYR GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU          
SEQRES  10 C  148  GLU LYS GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO          
SEQRES  11 C  148  ASP TYR LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE          
SEQRES  12 C  148  GLY ILE ILE ALA LEU                                          
SEQRES   1 D  148  ASP LYS PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA          
SEQRES   2 D  148  GLU GLY GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA          
SEQRES   3 D  148  LEU LEU ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU          
SEQRES   4 D  148  VAL VAL PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN          
SEQRES   5 D  148  VAL LEU PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL          
SEQRES   6 D  148  LEU LEU THR HIS THR ILE SER ARG ILE ALA VAL SER TYR          
SEQRES   7 D  148  GLN THR LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO          
SEQRES   8 D  148  CYS GLN ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO          
SEQRES   9 D  148  TRP TYR GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU          
SEQRES  10 D  148  GLU LYS GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO          
SEQRES  11 D  148  ASP TYR LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE          
SEQRES  12 D  148  GLY ILE ILE ALA LEU                                          
HET    307  A   1      40                                                       
HET    307  C   2      40                                                       
HETNAM     307 6,7-DIMETHYL-3-[(METHYL{2-[METHYL({1-[3-                         
HETNAM   2 307  (TRIFLUOROMETHYL)PHENYL]-1H-INDOL-3-YL}METHYL)                  
HETNAM   3 307  AMINO]ETHYL}AMINO)METHYL]-4H-CHROMEN-4-ONE                      
FORMUL   5  307    2(C32 H32 F3 N3 O2)                                          
FORMUL   7  HOH   *226(H2 O)                                                    
HELIX    1   1 ARG A  138  LEU A  142  5                                   5    
HELIX    2   2 GLU A  146  GLN A  149  5                                   4    
HELIX    3   3 ARG B  138  LEU B  142  5                                   5    
HELIX    4   4 ARG C  138  LEU C  142  5                                   5    
HELIX    5   5 ARG D  138  LEU D  142  5                                   5    
SHEET    1   A 3 TRP A  28  LEU A  29  0                                        
SHEET    2   A 3 VAL A  13  ALA A  18 -1  N  VAL A  17   O  LEU A  29           
SHEET    3   A 3 LEU A  37  ALA A  38 -1  O  ALA A  38   N  VAL A  13           
SHEET    1   B 5 TRP A  28  LEU A  29  0                                        
SHEET    2   B 5 VAL A  13  ALA A  18 -1  N  VAL A  17   O  LEU A  29           
SHEET    3   B 5 TYR A 151  ALA A 156 -1  O  PHE A 152   N  VAL A  16           
SHEET    4   B 5 GLY A  54  GLY A  66 -1  N  TYR A  59   O  GLY A 153           
SHEET    5   B 5 TRP A 114  LEU A 126 -1  O  PHE A 124   N  TYR A  56           
SHEET    1   C 5 GLU A  42  LEU A  43  0                                        
SHEET    2   C 5 LEU A  48  VAL A  49 -1  O  VAL A  49   N  GLU A  42           
SHEET    3   C 5 ARG A 131  ILE A 136 -1  O  LEU A 132   N  LEU A  48           
SHEET    4   C 5 LEU A  76  ILE A  83 -1  N  ILE A  83   O  ARG A 131           
SHEET    5   C 5 LYS A  90  LYS A  98 -1  O  LYS A  98   N  LEU A  76           
SHEET    1   D 3 TRP B  28  LEU B  29  0                                        
SHEET    2   D 3 VAL B  13  ALA B  18 -1  N  VAL B  17   O  LEU B  29           
SHEET    3   D 3 LEU B  36  ALA B  38 -1  O  LEU B  36   N  HIS B  15           
SHEET    1   E 5 TRP B  28  LEU B  29  0                                        
SHEET    2   E 5 VAL B  13  ALA B  18 -1  N  VAL B  17   O  LEU B  29           
SHEET    3   E 5 TYR B 151  ALA B 156 -1  O  PHE B 152   N  VAL B  16           
SHEET    4   E 5 GLY B  54  GLN B  67 -1  N  TYR B  59   O  GLY B 153           
SHEET    5   E 5 PRO B 113  LEU B 126 -1  O  GLY B 122   N  ILE B  58           
SHEET    1   F 5 GLU B  42  ARG B  44  0                                        
SHEET    2   F 5 GLN B  47  VAL B  49 -1  O  VAL B  49   N  GLU B  42           
SHEET    3   F 5 ARG B 131  ILE B 136 -1  O  LEU B 132   N  LEU B  48           
SHEET    4   F 5 LEU B  76  ILE B  83 -1  N  ILE B  83   O  ARG B 131           
SHEET    5   F 5 LYS B  90  LYS B  98 -1  O  LEU B  93   N  ILE B  80           
SHEET    1   G 3 TRP C  28  LEU C  29  0                                        
SHEET    2   G 3 VAL C  13  ALA C  18 -1  N  VAL C  17   O  LEU C  29           
SHEET    3   G 3 LEU C  37  ALA C  38 -1  O  ALA C  38   N  VAL C  13           
SHEET    1   H 5 TRP C  28  LEU C  29  0                                        
SHEET    2   H 5 VAL C  13  ALA C  18 -1  N  VAL C  17   O  LEU C  29           
SHEET    3   H 5 TYR C 151  ALA C 156 -1  O  PHE C 152   N  VAL C  16           
SHEET    4   H 5 GLY C  54  GLY C  66 -1  N  TYR C  59   O  GLY C 153           
SHEET    5   H 5 TRP C 114  LEU C 126 -1  O  PHE C 124   N  TYR C  56           
SHEET    1   I 5 GLU C  42  ARG C  44  0                                        
SHEET    2   I 5 GLN C  47  VAL C  49 -1  O  VAL C  49   N  GLU C  42           
SHEET    3   I 5 ARG C 131  ILE C 136 -1  O  LEU C 132   N  LEU C  48           
SHEET    4   I 5 LEU C  76  ILE C  83 -1  N  ILE C  83   O  ARG C 131           
SHEET    5   I 5 LYS C  90  LYS C  98 -1  O  LEU C  94   N  ILE C  80           
SHEET    1   J 3 TRP D  28  LEU D  29  0                                        
SHEET    2   J 3 VAL D  13  ALA D  18 -1  N  VAL D  17   O  LEU D  29           
SHEET    3   J 3 LEU D  36  ALA D  38 -1  O  LEU D  36   N  HIS D  15           
SHEET    1   K 5 TRP D  28  LEU D  29  0                                        
SHEET    2   K 5 VAL D  13  ALA D  18 -1  N  VAL D  17   O  LEU D  29           
SHEET    3   K 5 TYR D 151  ALA D 156 -1  O  PHE D 152   N  VAL D  16           
SHEET    4   K 5 GLY D  54  GLN D  67 -1  N  TYR D  59   O  GLY D 153           
SHEET    5   K 5 PRO D 113  LEU D 126 -1  O  LEU D 126   N  GLY D  54           
SHEET    1   L 5 GLU D  42  ARG D  44  0                                        
SHEET    2   L 5 GLN D  47  VAL D  49 -1  O  VAL D  49   N  GLU D  42           
SHEET    3   L 5 ARG D 131  ILE D 136 -1  O  LEU D 132   N  LEU D  48           
SHEET    4   L 5 LEU D  76  ALA D  84 -1  N  THR D  79   O  GLU D 135           
SHEET    5   L 5 TYR D  87  LYS D  98 -1  O  LYS D  98   N  LEU D  76           
SSBOND   1 CYS A   69    CYS A  101                          1555   1555  2.04  
SSBOND   2 CYS B   69    CYS B  101                          1555   1555  2.06  
SSBOND   3 CYS C   69    CYS C  101                          1555   1555  2.04  
SSBOND   4 CYS D   69    CYS D  101                          1555   1555  2.06  
SITE     1 AC1 12 LEU A  57  SER A  60  TYR A 119  LEU A 120                    
SITE     2 AC1 12 GLY A 121  GLY A 122  TYR A 151  TYR B  59                    
SITE     3 AC1 12 TYR B 119  LEU B 120  GLY B 121  TYR B 151                    
SITE     1 AC2 12 LEU C  57  SER C  60  TYR C 119  LEU C 120                    
SITE     2 AC2 12 GLY C 121  GLY C 122  TYR C 151  TYR D  59                    
SITE     3 AC2 12 SER D  60  TYR D 119  LEU D 120  GLY D 121                    
CRYST1  165.254  165.254   63.728  90.00  90.00 120.00 H 3          36          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006050  0.003490  0.000000        0.00000                         
SCALE2      0.000000  0.006990  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015690        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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