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Database: PDB
Entry: 4G3Y
LinkDB: 4G3Y
Original site: 4G3Y 
HEADER    IMMUNE SYSTEM                           15-JUL-12   4G3Y              
TITLE     CRYSTAL STRUCTURE OF TNF-ALPHA IN COMPLEX WITH INFLIXIMAB FAB FRAGMENT
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INFLIXIMAB FAB L;                                          
COMPND   3 CHAIN: L;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: INFLIXIMAB FAB H;                                          
COMPND   7 CHAIN: H;                                                            
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: TUMOR NECROSIS FACTOR;                                     
COMPND  11 CHAIN: C;                                                            
COMPND  12 FRAGMENT: TUMOR NECROSIS FACTOR, SOLUBLE FORM;                       
COMPND  13 SYNONYM: TNF-ALPHA;                                                  
COMPND  14 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 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   9 ORGANISM_COMMON: HUMAN;                                              
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  13 MOL_ID: 3;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  15 ORGANISM_COMMON: HUMAN;                                              
SOURCE  16 ORGANISM_TAXID: 9606;                                                
SOURCE  17 GENE: TNFA;                                                          
SOURCE  18 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TNF, INFLIXIMAB, IMMUNE SYSTEM                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.Y.LIANG,J.X.DAI,Y.J.GUO,Z.Y.LOU                                     
REVDAT   2   07-AUG-13 4G3Y    1       JRNL                                     
REVDAT   1   27-MAR-13 4G3Y    0                                                
JRNL        AUTH   S.Y.LIANG,J.X.DAI,S.HOU,L.SU,D.ZHANG,H.GUO,S.HU,H.WANG,      
JRNL        AUTH 2 Z.RAO,Y.J.GUO,Z.Y.LOU                                        
JRNL        TITL   STRUCTURAL BASIS FOR TREATING TUMOR NECROSIS FACTOR ALPHA    
JRNL        TITL 2 (TNFALPHA)-ASSOCIATED DISEASES WITH THE THERAPEUTIC ANTIBODY 
JRNL        TITL 3 INFLIXIMAB                                                   
JRNL        REF    J.BIOL.CHEM.                  V. 288 13799 2013              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   23504311                                                     
JRNL        DOI    10.1074/JBC.M112.433961                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.1_357)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.54                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.080                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 25400                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.191                           
REMARK   3   R VALUE            (WORKING SET) : 0.189                           
REMARK   3   FREE R VALUE                     : 0.235                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.030                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1278                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 21.5356 -  5.3832    0.99     2828   143  0.1711 0.2087        
REMARK   3     2  5.3832 -  4.2838    0.99     2808   141  0.1316 0.1656        
REMARK   3     3  4.2838 -  3.7456    0.98     2779   161  0.1556 0.1925        
REMARK   3     4  3.7456 -  3.4046    0.98     2787   135  0.1871 0.2389        
REMARK   3     5  3.4046 -  3.1613    0.97     2719   147  0.2152 0.2614        
REMARK   3     6  3.1613 -  2.9755    0.95     2725   161  0.2308 0.3108        
REMARK   3     7  2.9755 -  2.8268    0.93     2627   146  0.2480 0.2942        
REMARK   3     8  2.8268 -  2.7040    0.88     2483   122  0.2452 0.3081        
REMARK   3     9  2.7040 -  2.6001    0.82     2366   122  0.2485 0.3149        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.34                                          
REMARK   3   B_SOL              : 31.58                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.330            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.550           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.91                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.62390                                             
REMARK   3    B22 (A**2) : -1.62390                                             
REMARK   3    B33 (A**2) : 3.24780                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : -0.00000                                             
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008           4576                                  
REMARK   3   ANGLE     :  1.223           6214                                  
REMARK   3   CHIRALITY :  0.079            695                                  
REMARK   3   PLANARITY :  0.005            800                                  
REMARK   3   DIHEDRAL  : 16.588           1647                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4G3Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-JUL-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB073707.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-SEP-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-17A                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27025                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
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: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.45                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0M NA/K PHOSPHATE, PH 8.2, VAPOR       
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 291K                           
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       76.83150            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       44.35869            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       33.09300            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       76.83150            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       44.35869            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       33.09300            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       76.83150            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       44.35869            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       33.09300            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       88.71737            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       66.18600            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       88.71737            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       66.18600            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       88.71737            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       66.18600            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: NONAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, 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 350   BIOMT1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5200 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25300 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, 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     LYS H   221                                                      
REMARK 465     SER H   222                                                      
REMARK 465     CYS H   223                                                      
REMARK 465     ASP H   224                                                      
REMARK 465     LYS H   225                                                      
REMARK 465     THR H   226                                                      
REMARK 465     VAL C     1                                                      
REMARK 465     ARG C     2                                                      
REMARK 465     SER C     3                                                      
REMARK 465     SER C     4                                                      
REMARK 465     SER C     5                                                      
REMARK 465     ARG C     6                                                      
REMARK 465     THR C     7                                                      
REMARK 465     PRO C     8                                                      
REMARK 465     SER C     9                                                      
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     TYR C  87    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU C 157    O                                                   
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    PRO C 106   C   -  N   -  CA  ANGL. DEV. =  11.5 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    ALA L  51      -44.79     71.17                                   
REMARK 500    SER L  52       -7.42   -143.76                                   
REMARK 500    THR L  69      -14.32   -142.08                                   
REMARK 500    SER L 127        3.34    -55.81                                   
REMARK 500    ASP L 151       53.65     39.22                                   
REMARK 500    SER L 171       19.35     59.85                                   
REMARK 500    GLU L 187        1.23    -64.79                                   
REMARK 500    VAL H   2       96.69     57.30                                   
REMARK 500    ASN H  57      176.73     57.25                                   
REMARK 500    ALA H  59       88.96     50.27                                   
REMARK 500    SER H 105      -92.54   -156.37                                   
REMARK 500    SER H 137       58.25    -91.52                                   
REMARK 500    SER H 139       71.16     13.38                                   
REMARK 500    ASP H 151       79.45     48.03                                   
REMARK 500    ASN H 211       29.94     49.89                                   
REMARK 500    ARG C  32     -158.06   -135.79                                   
REMARK 500    SER C  86      -82.78    -70.12                                   
REMARK 500    GLN C  88        3.24     85.23                                   
REMARK 500    GLN C 102     -112.67    123.70                                   
REMARK 500    ARG C 103     -161.83   -126.16                                   
REMARK 500    GLU C 107      135.94     84.72                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ILE H   56     ASN H   57                 -147.45                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    VAL H   2        24.5      L          L   OUTSIDE RANGE           
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 H 311        DISTANCE =  5.06 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4G3Z   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE SEQUENCE DATABASE REFERENCES FOR CHAIN L, H DO NOT CURRENTLY     
REMARK 999 EXIST.                                                               
DBREF  4G3Y L    1   214  PDB    4G3Y     4G3Y             1    214             
DBREF  4G3Y H    1   226  PDB    4G3Y     4G3Y             1    226             
DBREF  4G3Y C    1   157  UNP    P01375   TNFA_HUMAN      77    233             
SEQRES   1 L  214  ASP ILE LEU LEU THR GLN SER PRO ALA ILE LEU SER VAL          
SEQRES   2 L  214  SER PRO GLY GLU ARG VAL SER PHE SER CYS ARG ALA SER          
SEQRES   3 L  214  GLN PHE VAL GLY SER SER ILE HIS TRP TYR GLN GLN ARG          
SEQRES   4 L  214  THR ASN GLY SER PRO ARG LEU LEU ILE LYS TYR ALA SER          
SEQRES   5 L  214  GLU SER MET SER GLY ILE PRO SER ARG PHE SER GLY SER          
SEQRES   6 L  214  GLY SER GLY THR ASP PHE THR LEU SER ILE ASN THR VAL          
SEQRES   7 L  214  GLU SER GLU ASP ILE ALA ASP TYR TYR CYS GLN GLN SER          
SEQRES   8 L  214  HIS SER TRP PRO PHE THR PHE GLY SER GLY THR ASN LEU          
SEQRES   9 L  214  GLU VAL LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE          
SEQRES  10 L  214  PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA          
SEQRES  11 L  214  SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU          
SEQRES  12 L  214  ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER          
SEQRES  13 L  214  GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS          
SEQRES  14 L  214  ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER          
SEQRES  15 L  214  LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU          
SEQRES  16 L  214  VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER          
SEQRES  17 L  214  PHE ASN ARG GLY GLU CYS                                      
SEQRES   1 H  226  GLU VAL LYS LEU GLU GLU SER GLY GLY GLY LEU VAL GLN          
SEQRES   2 H  226  PRO GLY GLY SER MET LYS LEU SER CYS VAL ALA SER GLY          
SEQRES   3 H  226  PHE ILE PHE SER ASN HIS TRP MET ASN TRP VAL ARG GLN          
SEQRES   4 H  226  SER PRO GLU LYS GLY LEU GLU TRP VAL ALA GLU ILE ARG          
SEQRES   5 H  226  SER LYS SER ILE ASN SER ALA THR HIS TYR ALA GLU SER          
SEQRES   6 H  226  VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASP SER LYS          
SEQRES   7 H  226  SER ALA VAL TYR LEU GLN MET THR ASP LEU ARG THR GLU          
SEQRES   8 H  226  ASP THR GLY VAL TYR TYR CYS SER ARG ASN TYR TYR GLY          
SEQRES   9 H  226  SER THR TYR ASP TYR TRP GLY GLN GLY THR THR LEU THR          
SEQRES  10 H  226  VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO          
SEQRES  11 H  226  LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA          
SEQRES  12 H  226  ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO          
SEQRES  13 H  226  VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY          
SEQRES  14 H  226  VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU          
SEQRES  15 H  226  TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER          
SEQRES  16 H  226  LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS          
SEQRES  17 H  226  PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS          
SEQRES  18 H  226  SER CYS ASP LYS THR                                          
SEQRES   1 C  157  VAL ARG SER SER SER ARG THR PRO SER ASP LYS PRO VAL          
SEQRES   2 C  157  ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY GLN LEU          
SEQRES   3 C  157  GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU ALA ASN          
SEQRES   4 C  157  GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL PRO SER          
SEQRES   5 C  157  GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU PHE LYS          
SEQRES   6 C  157  GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU THR HIS          
SEQRES   7 C  157  THR ILE SER ARG ILE ALA VAL SER TYR GLN THR LYS VAL          
SEQRES   8 C  157  ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN ARG GLU          
SEQRES   9 C  157  THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR GLU PRO          
SEQRES  10 C  157  ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS GLY ASP          
SEQRES  11 C  157  ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR LEU 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   *134(H2 O)                                                    
HELIX    1   1 GLU L   79  ILE L   83  5                                   5    
HELIX    2   2 SER L  121  SER L  127  1                                   7    
HELIX    3   3 LYS L  183  GLU L  187  1                                   5    
HELIX    4   4 ILE H   28  HIS H   32  5                                   5    
HELIX    5   5 SER H   53  ASN H   57  5                                   5    
HELIX    6   6 ARG H   89  THR H   93  5                                   5    
HELIX    7   7 SER H  163  ALA H  165  5                                   3    
HELIX    8   8 SER H  194  GLY H  197  5                                   4    
HELIX    9   9 LYS H  208  ASN H  211  5                                   4    
HELIX   10  10 ARG C  138  LEU C  142  5                                   5    
SHEET    1   A 4 LEU L   4  THR L   5  0                                        
SHEET    2   A 4 VAL L  19  ALA L  25 -1  O  ARG L  24   N  THR L   5           
SHEET    3   A 4 ASP L  70  ILE L  75 -1  O  LEU L  73   N  PHE L  21           
SHEET    4   A 4 PHE L  62  SER L  67 -1  N  SER L  63   O  SER L  74           
SHEET    1   B 6 ILE L  10  VAL L  13  0                                        
SHEET    2   B 6 THR L 102  VAL L 106  1  O  GLU L 105   N  VAL L  13           
SHEET    3   B 6 ALA L  84  GLN L  90 -1  N  ALA L  84   O  LEU L 104           
SHEET    4   B 6 ILE L  33  GLN L  38 -1  N  HIS L  34   O  GLN L  89           
SHEET    5   B 6 ARG L  45  LYS L  49 -1  O  LEU L  47   N  TRP L  35           
SHEET    6   B 6 GLU L  53  SER L  54 -1  O  GLU L  53   N  LYS L  49           
SHEET    1   C 4 ILE L  10  VAL L  13  0                                        
SHEET    2   C 4 THR L 102  VAL L 106  1  O  GLU L 105   N  VAL L  13           
SHEET    3   C 4 ALA L  84  GLN L  90 -1  N  ALA L  84   O  LEU L 104           
SHEET    4   C 4 THR L  97  PHE L  98 -1  O  THR L  97   N  GLN L  90           
SHEET    1   D 4 SER L 114  PHE L 118  0                                        
SHEET    2   D 4 THR L 129  PHE L 139 -1  O  VAL L 133   N  PHE L 118           
SHEET    3   D 4 TYR L 173  SER L 182 -1  O  LEU L 179   N  VAL L 132           
SHEET    4   D 4 SER L 159  VAL L 163 -1  N  GLN L 160   O  THR L 178           
SHEET    1   E 4 ALA L 144  LYS L 145  0                                        
SHEET    2   E 4 VAL L 191  HIS L 198 -1  O  THR L 197   N  LYS L 145           
SHEET    3   E 4 TRP L 148  VAL L 150 -1  N  LYS L 149   O  ALA L 193           
SHEET    4   E 4 ALA L 153  LEU L 154 -1  O  ALA L 153   N  VAL L 150           
SHEET    1   F 3 ALA L 144  LYS L 145  0                                        
SHEET    2   F 3 VAL L 191  HIS L 198 -1  O  THR L 197   N  LYS L 145           
SHEET    3   F 3 VAL L 205  ASN L 210 -1  O  LYS L 207   N  CYS L 194           
SHEET    1   G 4 LYS H   3  SER H   7  0                                        
SHEET    2   G 4 MET H  18  SER H  25 -1  O  SER H  21   N  SER H   7           
SHEET    3   G 4 ALA H  80  MET H  85 -1  O  MET H  85   N  MET H  18           
SHEET    4   G 4 PHE H  70  ASP H  75 -1  N  SER H  73   O  TYR H  82           
SHEET    1   H 6 GLY H  10  VAL H  12  0                                        
SHEET    2   H 6 THR H 114  VAL H 118  1  O  THR H 117   N  GLY H  10           
SHEET    3   H 6 GLY H  94  ASN H 101 -1  N  TYR H  96   O  THR H 114           
SHEET    4   H 6 TRP H  33  SER H  40 -1  N  VAL H  37   O  TYR H  97           
SHEET    5   H 6 GLY H  44  ILE H  51 -1  O  GLU H  46   N  ARG H  38           
SHEET    6   H 6 THR H  60  TYR H  62 -1  O  HIS H  61   N  GLU H  50           
SHEET    1   I 4 GLY H  10  VAL H  12  0                                        
SHEET    2   I 4 THR H 114  VAL H 118  1  O  THR H 117   N  GLY H  10           
SHEET    3   I 4 GLY H  94  ASN H 101 -1  N  TYR H  96   O  THR H 114           
SHEET    4   I 4 TYR H 107  TRP H 110 -1  O  TYR H 109   N  ARG H 100           
SHEET    1   J 4 SER H 127  LEU H 131  0                                        
SHEET    2   J 4 THR H 142  TYR H 152 -1  O  GLY H 146   N  LEU H 131           
SHEET    3   J 4 TYR H 183  PRO H 192 -1  O  VAL H 191   N  ALA H 143           
SHEET    4   J 4 VAL H 170  THR H 172 -1  N  HIS H 171   O  VAL H 188           
SHEET    1   K 4 SER H 127  LEU H 131  0                                        
SHEET    2   K 4 THR H 142  TYR H 152 -1  O  GLY H 146   N  LEU H 131           
SHEET    3   K 4 TYR H 183  PRO H 192 -1  O  VAL H 191   N  ALA H 143           
SHEET    4   K 4 VAL H 176  LEU H 177 -1  N  VAL H 176   O  SER H 184           
SHEET    1   L 3 THR H 158  TRP H 161  0                                        
SHEET    2   L 3 TYR H 201  HIS H 207 -1  O  ASN H 206   N  THR H 158           
SHEET    3   L 3 THR H 212  VAL H 214 -1  O  THR H 212   N  HIS H 207           
SHEET    1   M 3 THR H 158  TRP H 161  0                                        
SHEET    2   M 3 TYR H 201  HIS H 207 -1  O  ASN H 206   N  THR H 158           
SHEET    3   M 3 LYS H 217  VAL H 218 -1  O  VAL H 218   N  TYR H 201           
SHEET    1   N 3 TRP C  28  LEU C  29  0                                        
SHEET    2   N 3 VAL C  13  ALA C  18 -1  N  VAL C  17   O  LEU C  29           
SHEET    3   N 3 LEU C  36  ALA C  38 -1  O  LEU C  36   N  HIS C  15           
SHEET    1   O 5 TRP C  28  LEU C  29  0                                        
SHEET    2   O 5 VAL C  13  ALA C  18 -1  N  VAL C  17   O  LEU C  29           
SHEET    3   O 5 TYR C 151  ALA C 156 -1  O  ILE C 154   N  ALA C  14           
SHEET    4   O 5 GLY C  54  GLN C  67 -1  N  TYR C  59   O  GLY C 153           
SHEET    5   O 5 PRO C 113  LEU C 126 -1  O  GLY C 122   N  ILE C  58           
SHEET    1   P 5 GLU C  42  ARG C  44  0                                        
SHEET    2   P 5 GLN C  47  VAL C  49 -1  O  VAL C  49   N  GLU C  42           
SHEET    3   P 5 ARG C 131  ILE C 136 -1  O  LEU C 132   N  LEU C  48           
SHEET    4   P 5 LEU C  76  ILE C  83 -1  N  THR C  79   O  GLU C 135           
SHEET    5   P 5 LYS C  90  LYS C  98 -1  O  LEU C  94   N  ILE C  80           
SSBOND   1 CYS L   23    CYS L   88                          1555   1555  2.05  
SSBOND   2 CYS L  134    CYS L  194                          1555   1555  2.03  
SSBOND   3 CYS H   22    CYS H   98                          1555   1555  2.05  
SSBOND   4 CYS H  147    CYS H  203                          1555   1555  2.03  
SSBOND   5 CYS C   69    CYS C  101                          1555   1555  2.06  
CISPEP   1 SER L    7    PRO L    8          0         2.35                     
CISPEP   2 TRP L   94    PRO L   95          0         6.74                     
CISPEP   3 TYR L  140    PRO L  141          0         1.27                     
CISPEP   4 GLU H    1    VAL H    2          0         3.36                     
CISPEP   5 GLY H  140    GLY H  141          0         9.68                     
CISPEP   6 PHE H  153    PRO H  154          0        -3.35                     
CISPEP   7 GLU H  155    PRO H  156          0         0.91                     
CISPEP   8 CYS C  101    GLN C  102          0        -3.69                     
CRYST1  153.663  153.663   99.279  90.00  90.00 120.00 H 3           9          
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      0.006508  0.003757  0.000000        0.00000                         
SCALE2      0.000000  0.007514  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010073        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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