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Database: PDB
Entry: 3L9J
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Original site: 3L9J 
HEADER    IMMUNE SYSTEM                           05-JAN-10   3L9J              
TITLE     SELECTION OF A NOVEL HIGHLY SPECIFIC TNFALPHA ANTAGONIST: INSIGHT FROM
TITLE    2 THE CRYSTAL STRUCTURE OF THE ANTAGONIST-TNFALPHA COMPLEX             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TNFALPHA;                                                  
COMPND   3 CHAIN: C;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: TUMOR NECROSIS FACTOR, SOLUBLE FORM;                       
COMPND   7 CHAIN: T;                                                            
COMPND   8 FRAGMENT: UNP RESIDUES 85-233;                                       
COMPND   9 SYNONYM: TNF-ALPHA, TUMOR NECROSIS FACTOR LIGAND SUPERFAMILY MEMBER  
COMPND  10 2, TNF-A, CACHECTIN;                                                 
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PT7CIIH6;                                 
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  16 EXPRESSION_SYSTEM_PLASMID: PT7CIIH6                                  
KEYWDS    TNF-ALPHA, ANTAGONIST, IN VITRO SELECTION, CELL MEMBRANE, CYTOKINE,   
KEYWDS   2 DISULFIDE BOND, GLYCOPROTEIN, LIPOPROTEIN, SECRETED, SIGNAL-ANCHOR,  
KEYWDS   3 TRANSMEMBRANE, IMMUNE SYSTEM                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.BYLA,M.H.ANDERSEN,H.C.THOGERSEN,H.H.GAD,R.HARTMANN                  
REVDAT   3   26-FEB-14 3L9J    1       REMARK VERSN                             
REVDAT   2   21-APR-10 3L9J    1       JRNL                                     
REVDAT   1   23-FEB-10 3L9J    0                                                
JRNL        AUTH   P.BYLA,M.H.ANDERSEN,T.L.HOLTET,H.JACOBSEN,M.MUNCH,H.H.GAD,   
JRNL        AUTH 2 H.C.THOGERSEN,R.HARTMANN                                     
JRNL        TITL   SELECTION OF A NOVEL AND HIGHLY SPECIFIC TNF{ALPHA}          
JRNL        TITL 2 ANTAGONIST: INSIGHT FROM THE CRYSTAL STRUCTURE OF THE        
JRNL        TITL 3 ANTAGONIST-TNF{ALPHA} COMPLEX                                
JRNL        REF    J.BIOL.CHEM.                  V. 285 12096 2010              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   20179326                                                     
JRNL        DOI    10.1074/JBC.M109.063305                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 41.95                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 17855                          
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) : 0.175                           
REMARK   3   R VALUE            (WORKING SET) : 0.173                           
REMARK   3   FREE R VALUE                     : 0.217                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 968                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1261                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.85                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1730                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 82                           
REMARK   3   BIN FREE R VALUE                    : 0.2760                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2206                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 246                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.37                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.29000                                              
REMARK   3    B22 (A**2) : 0.29000                                              
REMARK   3    B33 (A**2) : -0.44000                                             
REMARK   3    B12 (A**2) : 0.15000                                              
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): 0.205         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.172         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.104         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.821         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.947                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2267 ; 0.016 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3082 ; 1.475 ; 1.940       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   276 ; 6.420 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   110 ;38.431 ;24.182       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   365 ;13.126 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    14 ;18.222 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   328 ; 0.110 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1756 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   928 ; 0.207 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1543 ; 0.306 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   203 ; 0.191 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     2 ; 0.045 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    62 ; 0.234 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    38 ; 0.319 ; 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):  1417 ; 1.129 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2224 ; 1.977 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   987 ; 2.915 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   858 ; 4.718 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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 : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3L9J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-JAN-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB057003.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL; NULL                         
REMARK 200  TEMPERATURE           (KELVIN) : 100; 100                           
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG; MAX II         
REMARK 200  BEAMLINE                       : X12; I911-3                        
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.81500; 1.0                       
REMARK 200  MONOCHROMATOR                  : NULL; NULL                         
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD                           
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH; MARRESEARCH           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17855                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 74.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
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; SINGLE WAVELENGTH           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASES                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1TNF FOR CHAIN T AND  1TN3 FOR CHAIN C;    
REMARK 200  FOR 1TN3 THE RANDOMIZED LOOPS WAS REMOVED FROM TEH SEARCH MODEL.    
REMARK 200  THESE LOOP IS 116-122 (LOOP 1) AND 145-150 (LOOP 4)                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.37                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS, 0.35M MGAC, 20% 2-PROPANOL,   
REMARK 280  PH 8.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 323K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 2                         
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,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/2                                            
REMARK 290       6555   X-Y,X,Z+1/2                                             
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z                                              
REMARK 290      10555   -Y,-X,-Z+1/2                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-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 -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        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       74.58600            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       74.58600            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       74.58600            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       74.58600            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       74.58600            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       74.58600            
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, T                                  
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH T 200  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH T 284  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH T 283  LIES ON A SPECIAL POSITION.                          
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     LYS C    53                                                      
REMARK 465     GLY C    54                                                      
REMARK 465     THR C    55                                                      
REMARK 465     LYS C    56                                                      
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     LEU C  46    CG   CD1  CD2                                       
REMARK 470     LEU C  51    CG   CD1  CD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH T   174     O    HOH T   244              1.85            
REMARK 500   O    HOH C   226     O    HOH C   227              1.92            
REMARK 500   O    HOH C   224     O    HOH C   225              2.04            
REMARK 500   O    HOH C    10     O    HOH T   257              2.11            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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   O    HOH T   206     O    HOH T   217     2665     1.96            
REMARK 500   O    HOH T   217     O    HOH T   217     2665     1.99            
REMARK 500   O    HOH T   218     O    HOH T   218     2665     2.14            
REMARK 500   O    HOH T   201     O    HOH T   201     2665     2.18            
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    ARG C 120      -50.97     77.62                                   
REMARK 500    ASN C 135       45.41   -140.65                                   
REMARK 500    LEU T  37       79.17   -159.74                                   
REMARK 500    TYR T  87       -6.69     75.37                                   
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 C 188        DISTANCE =  6.68 ANGSTROMS                       
REMARK 525    HOH C 212        DISTANCE =  5.26 ANGSTROMS                       
REMARK 525    HOH C 213        DISTANCE =  5.79 ANGSTROMS                       
REMARK 525    HOH C 262        DISTANCE =  7.03 ANGSTROMS                       
REMARK 525    HOH T 183        DISTANCE =  5.71 ANGSTROMS                       
REMARK 525    HOH T 207        DISTANCE =  6.69 ANGSTROMS                       
REMARK 525    HOH T 216        DISTANCE =  7.65 ANGSTROMS                       
REMARK 525    HOH T 284        DISTANCE =  5.74 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 497  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C 246   O                                                      
REMARK 620 2 HOH C 210   O    92.8                                              
REMARK 620 3 HOH C 251   O   170.4  96.2                                        
REMARK 620 4 HOH C 221   O    95.5  86.1  82.2                                  
REMARK 620 5 HOH C 202   O    92.7  90.2  90.3 171.2                            
REMARK 620 6 HOH C 245   O    81.5 172.3  89.2  89.3  95.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 497                  
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE NUMBER 52 IS SIMPLY SKIPPED IN CHAIN C.                          
DBREF  3L9J C   46   180  PDB    3L9J     3L9J            46    179             
DBREF  3L9J T    9   157  UNP    P01375   TNFA_HUMAN      85    233             
SEQRES   1 C  134  LEU GLN THR VAL CYS LEU LYS GLY THR LYS HIS MET LYS          
SEQRES   2 C  134  CYS PHE LEU ALA PHE THR GLN THR LYS THR PHE HIS GLU          
SEQRES   3 C  134  ALA SER GLU ASP CYS ILE SER ARG GLY GLY THR LEU SER          
SEQRES   4 C  134  THR PRO GLN THR GLY SER GLU ASN ASP ALA LEU TYR GLU          
SEQRES   5 C  134  TYR LEU ARG GLN SER VAL GLY ASN GLU ALA GLU ILE TRP          
SEQRES   6 C  134  LEU GLY LEU ASN LYS ARG TRP SER ARG TYR PHE TRP VAL          
SEQRES   7 C  134  ASP MET THR GLY THR ARG ILE ALA TYR LYS ASN TRP GLU          
SEQRES   8 C  134  HIS SER SER ASP ALA GLN PRO ASP PRO SER ASN TRP GLU          
SEQRES   9 C  134  ASN CYS ALA VAL LEU SER GLY ALA ALA ASN GLY LYS TRP          
SEQRES  10 C  134  PHE GLY LYS ARG CYS ARG ASP GLN LEU PRO TYR ILE CYS          
SEQRES  11 C  134  GLN PHE GLY ILE                                              
SEQRES   1 T  149  SER ASP LYS PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN          
SEQRES   2 T  149  ALA GLU GLY GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN          
SEQRES   3 T  149  ALA LEU LEU ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN          
SEQRES   4 T  149  LEU VAL VAL PRO SER GLU GLY LEU TYR LEU ILE TYR SER          
SEQRES   5 T  149  GLN VAL LEU PHE LYS GLY GLN GLY CYS PRO SER THR HIS          
SEQRES   6 T  149  VAL LEU LEU THR HIS THR ILE SER ARG ILE ALA VAL SER          
SEQRES   7 T  149  TYR GLN THR LYS VAL ASN LEU LEU SER ALA ILE LYS SER          
SEQRES   8 T  149  PRO CYS GLN ARG GLU THR PRO GLU GLY ALA GLU ALA LYS          
SEQRES   9 T  149  PRO TRP TYR GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN          
SEQRES  10 T  149  LEU GLU LYS GLY ASP ARG LEU SER ALA GLU ILE ASN ARG          
SEQRES  11 T  149  PRO ASP TYR LEU ASP PHE ALA GLU SER GLY GLN VAL TYR          
SEQRES  12 T  149  PHE GLY ILE ILE ALA LEU                                      
HET     MG  C 497       1                                                       
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   3   MG    MG 2+                                                        
FORMUL   4  HOH   *246(H2 O)                                                    
HELIX    1   1 THR C   69  ARG C   80  1                                  12    
HELIX    2   2 THR C   89  VAL C  104  1                                  16    
HELIX    3   3 HIS C  138  GLN C  143  1                                   6    
HELIX    4   4 ARG T  138  LEU T  142  5                                   5    
SHEET    1   A 4 VAL C  49  LEU C  51  0                                        
SHEET    2   A 4 MET C  58  LYS C  68 -1  O  PHE C  61   N  VAL C  49           
SHEET    3   A 4 LEU C 172  ILE C 180 -1  O  CYS C 176   N  LEU C  62           
SHEET    4   A 4 THR C  83  LEU C  84 -1  N  THR C  83   O  GLN C 177           
SHEET    1   B 3 GLU C 109  TRP C 111  0                                        
SHEET    2   B 3 CYS C 152  SER C 156 -1  O  LEU C 155   N  ILE C 110           
SHEET    3   B 3 TRP C 163  LYS C 166 -1  O  PHE C 164   N  VAL C 154           
SHEET    1   C 2 LEU C 114  ASN C 115  0                                        
SHEET    2   C 2 VAL C 124  ASP C 125 -1  O  VAL C 124   N  ASN C 115           
SHEET    1   D 3 TRP T  28  LEU T  29  0                                        
SHEET    2   D 3 VAL T  13  ALA T  18 -1  N  VAL T  17   O  LEU T  29           
SHEET    3   D 3 LEU T  36  ALA T  38 -1  O  ALA T  38   N  VAL T  13           
SHEET    1   E 5 TRP T  28  LEU T  29  0                                        
SHEET    2   E 5 VAL T  13  ALA T  18 -1  N  VAL T  17   O  LEU T  29           
SHEET    3   E 5 TYR T 151  ALA T 156 -1  O  PHE T 152   N  VAL T  16           
SHEET    4   E 5 GLY T  54  GLN T  67 -1  N  TYR T  59   O  GLY T 153           
SHEET    5   E 5 PRO T 113  LEU T 126 -1  O  GLY T 122   N  ILE T  58           
SHEET    1   F 5 GLU T  42  ARG T  44  0                                        
SHEET    2   F 5 GLN T  47  VAL T  49 -1  O  VAL T  49   N  GLU T  42           
SHEET    3   F 5 ARG T 131  ILE T 136 -1  O  LEU T 132   N  LEU T  48           
SHEET    4   F 5 LEU T  76  ILE T  83 -1  N  ILE T  83   O  ARG T 131           
SHEET    5   F 5 LYS T  90  LYS T  98 -1  O  LYS T  98   N  LEU T  76           
SSBOND   1 CYS C   50    CYS C   60                          1555   1555  2.08  
SSBOND   2 CYS C   77    CYS C  176                          1555   1555  2.03  
SSBOND   3 CYS C  152    CYS C  168                          1555   1555  2.06  
SSBOND   4 CYS T   69    CYS T  101                          1555   1555  2.09  
LINK        MG    MG C 497                 O   HOH C 246     1555   1555  1.94  
LINK        MG    MG C 497                 O   HOH C 210     1555   1555  1.95  
LINK        MG    MG C 497                 O   HOH C 251     1555   1555  2.07  
LINK        MG    MG C 497                 O   HOH C 221     1555   1555  2.14  
LINK        MG    MG C 497                 O   HOH C 202     1555   1555  2.31  
LINK        MG    MG C 497                 O   HOH C 245     1555   1555  2.63  
SITE     1 AC1  6 HOH C 202  HOH C 210  HOH C 221  HOH C 245                    
SITE     2 AC1  6 HOH C 246  HOH C 251                                          
CRYST1   83.905   83.905  149.172  90.00  90.00 120.00 P 63 2 2     12          
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      0.011918  0.006881  0.000000        0.00000                         
SCALE2      0.000000  0.013762  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006704        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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