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Database: PDB
Entry: 3WD5
LinkDB: 3WD5
Original site: 3WD5 
HEADER    IMMUNE SYSTEM                           06-JUN-13   3WD5              
TITLE     CRYSTAL STRUCTURE OF TNFALPHA IN COMPLEX WITH ADALIMUMAB FAB FRAGMENT 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TUMOR NECROSIS FACTOR;                                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: TUMOR NECROSIS FACTOR, SOLUBLE FORM;                       
COMPND   5 SYNONYM: TNFALPHA;                                                   
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: ADALIMUMAB LIGHT CHAIN;                                    
COMPND   9 CHAIN: L;                                                            
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: ADALIMUMAB HEAVY CHAIN;                                    
COMPND  13 CHAIN: H;                                                            
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 GENE: TNFA;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  13 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  17 ORGANISM_COMMON: HUMAN;                                              
SOURCE  18 ORGANISM_TAXID: 9606;                                                
SOURCE  19 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  20 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 10029                                       
KEYWDS    ANTIBODY BINDING EPITOPE, IMMUNE SYSTEM                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.HU,S.Y.LIANG,Y.J.GUO,Z.Y.LOU                                        
REVDAT   2   21-AUG-13 3WD5    1       JRNL                                     
REVDAT   1   14-AUG-13 3WD5    0                                                
JRNL        AUTH   S.HU,S.Y.LIANG,H.GUO,D.ZHANG,H.LI,X.WANG,W.YANG,W.QIAN,      
JRNL        AUTH 2 S.HOU,H.WANG,Y.J.GUO,Z.Y.LOU                                 
JRNL        TITL   COMPARISON OF THE INHIBITION MECHANISMS OF ADALIMUMAB AND    
JRNL        TITL 2 INFLIXIMAB IN TREATING TNFALPHA-ASSOCIATED DISEASES FROM A   
JRNL        TITL 3 MOLECULAR VIEW                                               
JRNL        REF    J.BIOL.CHEM.                               2013              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        DOI    10.1074/JBC.M113.491530                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.1_1168)                   
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) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.26                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 12943                          
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) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.275                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.990                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 646                             
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 43.2602 -  5.3001    1.00     2544   130  0.2131 0.2585        
REMARK   3     2  5.3001 -  4.2080    1.00     2462   124  0.1554 0.2313        
REMARK   3     3  4.2080 -  3.6764    1.00     2429   138  0.1705 0.2515        
REMARK   3     4  3.6764 -  3.3404    1.00     2440   121  0.1899 0.3576        
REMARK   3     5  3.3404 -  3.1010    1.00     2422   133  0.2119 0.3461        
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              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.420            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.200           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 49.23                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 48.06                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  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      :  0.010           4536                                  
REMARK   3   ANGLE     :  1.447           6168                                  
REMARK   3   CHIRALITY :  0.113            697                                  
REMARK   3   PLANARITY :  0.006            795                                  
REMARK   3   DIHEDRAL  : 17.883           1630                                  
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 3WD5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-JUN-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB096185.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 4.6                                
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                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12943                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.300                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 26.100                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
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: PHASES                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.48                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG400, 0.1M SODIUM ACETATE          
REMARK 280  TRIHYDRATE, 0.1M CADMIUM CHLORIDE HYDRATE, PH 4.6, VAPOR            
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 291.0K                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 21 3                           
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290       5555   Z,X,Y                                                   
REMARK 290       6555   Z+1/2,-X+1/2,-Y                                         
REMARK 290       7555   -Z+1/2,-X,Y+1/2                                         
REMARK 290       8555   -Z,X+1/2,-Y+1/2                                         
REMARK 290       9555   Y,Z,X                                                   
REMARK 290      10555   -Y,Z+1/2,-X+1/2                                         
REMARK 290      11555   Y+1/2,-Z+1/2,-X                                         
REMARK 290      12555   -Y+1/2,-Z,X+1/2                                         
REMARK 290      13555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      14555   -X,-Y+1/2,Z                                             
REMARK 290      15555   -X+1/2,Y,-Z                                             
REMARK 290      16555   X,-Y,-Z+1/2                                             
REMARK 290      17555   Z+1/2,X+1/2,Y+1/2                                       
REMARK 290      18555   Z,-X,-Y+1/2                                             
REMARK 290      19555   -Z,-X+1/2,Y                                             
REMARK 290      20555   -Z+1/2,X,-Y                                             
REMARK 290      21555   Y+1/2,Z+1/2,X+1/2                                       
REMARK 290      22555   -Y+1/2,Z,-X                                             
REMARK 290      23555   Y,-Z,-X+1/2                                             
REMARK 290      24555   -Y,-Z+1/2,X                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       80.92450            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       80.92450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       80.92450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       80.92450            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       80.92450            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       80.92450            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000       80.92450            
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000       80.92450            
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000       80.92450            
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000       80.92450            
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000       80.92450            
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000       80.92450            
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000       80.92450            
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000       80.92450            
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000       80.92450            
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000       80.92450            
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000       80.92450            
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000       80.92450            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000       80.92450            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       80.92450            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000       80.92450            
REMARK 290   SMTRY1  14 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       80.92450            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1  15 -1.000000  0.000000  0.000000       80.92450            
REMARK 290   SMTRY2  15  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  16  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  16  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       80.92450            
REMARK 290   SMTRY1  17  0.000000  0.000000  1.000000       80.92450            
REMARK 290   SMTRY2  17  1.000000  0.000000  0.000000       80.92450            
REMARK 290   SMTRY3  17  0.000000  1.000000  0.000000       80.92450            
REMARK 290   SMTRY1  18  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2  18 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  18  0.000000 -1.000000  0.000000       80.92450            
REMARK 290   SMTRY1  19  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2  19 -1.000000  0.000000  0.000000       80.92450            
REMARK 290   SMTRY3  19  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1  20  0.000000  0.000000 -1.000000       80.92450            
REMARK 290   SMTRY2  20  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  20  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1  21  0.000000  1.000000  0.000000       80.92450            
REMARK 290   SMTRY2  21  0.000000  0.000000  1.000000       80.92450            
REMARK 290   SMTRY3  21  1.000000  0.000000  0.000000       80.92450            
REMARK 290   SMTRY1  22  0.000000 -1.000000  0.000000       80.92450            
REMARK 290   SMTRY2  22  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3  22 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  23  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  23  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  23 -1.000000  0.000000  0.000000       80.92450            
REMARK 290   SMTRY1  24  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  24  0.000000  0.000000 -1.000000       80.92450            
REMARK 290   SMTRY3  24  1.000000  0.000000  0.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, L, H                               
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 A 201  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     VAL A     1                                                      
REMARK 465     ARG A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     LYS H   137                                                      
REMARK 465     SER H   138                                                      
REMARK 465     THR H   139                                                      
REMARK 465     SER H   140                                                      
REMARK 465     GLY H   141                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LYS L   45   CE                                                  
REMARK 480     GLU L   81   CG                                                  
REMARK 480     GLN L  100   CG                                                  
REMARK 480     LYS L  126   CE   NZ                                             
REMARK 480     GLN L  147   CG                                                  
REMARK 480     LEU L  154   CD1  CD2                                            
REMARK 480     LYS L  169   CG   CD   CE                                        
REMARK 480     LYS L  188   NZ                                                  
REMARK 480     ARG L  211   NH2                                                 
REMARK 480     GLY L  212   CA                                                  
REMARK 480     GLU L  213   CA   O    CB   CG                                   
REMARK 480     GLU H    1   OE2                                                 
REMARK 480     PRO H   41   CA                                                  
REMARK 480     GLU H   89   CG                                                  
REMARK 480     SER H  135   CA   CB                                             
REMARK 480     SER H  136   CB                                                  
REMARK 480     GLY H  142   CA                                                  
REMARK 480     SER H  196   N                                                   
REMARK 480     GLY H  198   CA                                                  
REMARK 480     LYS H  209   CD   CE   NZ                                        
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   SG   CYS A    69     CB   CYS A   101              1.75            
REMARK 500   OD2  ASP H    59     O    HOH H   303              2.06            
REMARK 500   O    ALA A   145     O    HOH H   303              2.07            
REMARK 500   OD1  ASP H    30     O    HOH H   305              2.15            
REMARK 500   O    ALA H    61     N    SER H    63              2.17            
REMARK 500   O    VAL H    64     N    GLY H    66              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    SER A   9      130.77     95.62                                   
REMARK 500    ALA A  33     -137.08     22.15                                   
REMARK 500    LEU A  37       88.08   -179.36                                   
REMARK 500    ARG A  44      -68.46   -126.68                                   
REMARK 500    ASP A  45       47.82   -106.53                                   
REMARK 500    PRO A  70     -126.32   -106.35                                   
REMARK 500    THR A  72      -46.51      3.53                                   
REMARK 500    SER A  86      -72.99    -86.94                                   
REMARK 500    TYR A  87       80.09    -57.98                                   
REMARK 500    GLN A  88        2.89    -56.83                                   
REMARK 500    ALA A  96      135.95   -175.10                                   
REMARK 500    CYS A 101      104.28      2.31                                   
REMARK 500    ARG A 103      -29.13     41.98                                   
REMARK 500    GLU A 104      -51.90     -4.51                                   
REMARK 500    THR A 105       79.92     37.57                                   
REMARK 500    PRO A 106       49.56    -60.27                                   
REMARK 500    ALA A 109     -173.70   -170.26                                   
REMARK 500    GLU A 110      121.31     69.19                                   
REMARK 500    SER A 147      -79.11    -52.47                                   
REMARK 500    ILE L   2      124.98     75.57                                   
REMARK 500    ARG L  30     -124.49     54.88                                   
REMARK 500    ALA L  51      -30.92     72.77                                   
REMARK 500    SER L  52      -16.77   -140.13                                   
REMARK 500    SER L  77       88.36   -156.66                                   
REMARK 500    ARG L  93      109.62     81.01                                   
REMARK 500    LYS L 107      -89.34    -55.22                                   
REMARK 500    ARG L 108      157.97     30.26                                   
REMARK 500    ASN L 152       14.61     59.68                                   
REMARK 500    ARG H  16     -150.90    -76.16                                   
REMARK 500    ASP H  62       62.12    -43.87                                   
REMARK 500    SER H  63       -8.42    173.48                                   
REMARK 500    VAL H  64      -72.84   -142.46                                   
REMARK 500    GLU H  65      -61.81     35.11                                   
REMARK 500    ARG H  72      114.11   -165.64                                   
REMARK 500    LEU H 102      -81.51     57.26                                   
REMARK 500    ALA H 122     -142.34    -70.77                                   
REMARK 500    ASP H 152       62.54     60.64                                   
REMARK 500    ALA H 166       15.92    -59.81                                   
REMARK 500    LEU H 167      109.15   -160.68                                   
REMARK 500    SER H 194       -6.73    -54.63                                   
REMARK 500    SER H 195      -60.70   -103.32                                   
REMARK 500    SER H 196       45.68    -59.03                                   
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    ASN L  92        16.6      L          L   OUTSIDE RANGE           
REMARK 500    ARG L  93        16.3      L          L   OUTSIDE RANGE           
REMARK 500    ARG L 108        24.2      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4G3Y   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF TNFALPHA IN COMPLEX WITH INFLIXIMAB             
REMARK 900 FAB FRAGMENT                                                         
DBREF  3WD5 A    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  3WD5 L    1   213  PDB    3WD5     3WD5             1    213             
DBREF  3WD5 H    1   219  PDB    3WD5     3WD5             1    219             
SEQADV 3WD5 ASP A   31  UNP  P01375    ARG   107 CONFLICT                       
SEQRES   1 A  157  VAL ARG SER SER SER ARG THR PRO SER ASP LYS PRO VAL          
SEQRES   2 A  157  ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY GLN LEU          
SEQRES   3 A  157  GLN TRP LEU ASN ASP ARG ALA ASN ALA LEU LEU ALA ASN          
SEQRES   4 A  157  GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL PRO SER          
SEQRES   5 A  157  GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU PHE LYS          
SEQRES   6 A  157  GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU THR HIS          
SEQRES   7 A  157  THR ILE SER ARG ILE ALA VAL SER TYR GLN THR LYS VAL          
SEQRES   8 A  157  ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN ARG GLU          
SEQRES   9 A  157  THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR GLU PRO          
SEQRES  10 A  157  ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS GLY ASP          
SEQRES  11 A  157  ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR LEU ASP          
SEQRES  12 A  157  PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA          
SEQRES  13 A  157  LEU                                                          
SEQRES   1 L  213  ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA          
SEQRES   2 L  213  SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER          
SEQRES   3 L  213  GLN GLY ILE ARG ASN TYR LEU ALA TRP TYR GLN GLN LYS          
SEQRES   4 L  213  PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ALA ALA SER          
SEQRES   5 L  213  THR LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER          
SEQRES   6 L  213  GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU          
SEQRES   7 L  213  GLN PRO GLU ASP VAL ALA THR TYR TYR CYS GLN ARG TYR          
SEQRES   8 L  213  ASN ARG ALA PRO TYR THR PHE GLY GLN GLY THR LYS VAL          
SEQRES   9 L  213  GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE          
SEQRES  10 L  213  PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA          
SEQRES  11 L  213  SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU          
SEQRES  12 L  213  ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER          
SEQRES  13 L  213  GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS          
SEQRES  14 L  213  ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER          
SEQRES  15 L  213  LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU          
SEQRES  16 L  213  VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER          
SEQRES  17 L  213  PHE ASN ARG GLY GLU                                          
SEQRES   1 H  219  GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN          
SEQRES   2 H  219  PRO GLY ARG SER LEU ARG LEU SER CYS ALA ALA SER GLY          
SEQRES   3 H  219  PHE THR PHE ASP ASP TYR ALA MET HIS TRP VAL ARG GLN          
SEQRES   4 H  219  ALA PRO GLY LYS GLY LEU GLU TRP VAL SER ALA ILE THR          
SEQRES   5 H  219  TRP ASN SER GLY HIS ILE ASP TYR ALA ASP SER VAL GLU          
SEQRES   6 H  219  GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SER          
SEQRES   7 H  219  LEU TYR LEU ASP MET ASN SER LEU ARG ALA GLU ASP THR          
SEQRES   8 H  219  ALA VAL TYR TYR CYS ALA LYS VAL SER TYR LEU SER THR          
SEQRES   9 H  219  ALA SER SER LEU ASP TYR TRP GLY GLN GLY THR LEU VAL          
SEQRES  10 H  219  THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE          
SEQRES  11 H  219  PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR          
SEQRES  12 H  219  ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU          
SEQRES  13 H  219  PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER          
SEQRES  14 H  219  GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY          
SEQRES  15 H  219  LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER          
SEQRES  16 H  219  SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS          
SEQRES  17 H  219  LYS PRO SER ASN THR LYS VAL ASP LYS LYS ILE                  
FORMUL   4  HOH   *34(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 GLN L   79  VAL L   83  5                                   5    
HELIX    4   4 SER L  121  GLY L  128  1                                   8    
HELIX    5   5 LYS L  183  GLU L  187  1                                   5    
HELIX    6   6 THR H   28  TYR H   32  5                                   5    
HELIX    7   7 ARG H   87  THR H   91  5                                   5    
HELIX    8   8 SER H  164  ALA H  166  5                                   3    
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  36  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  LEU A 157 -1  O  PHE A 152   N  VAL A  16           
SHEET    4   B 5 GLY A  54  GLN A  67 -1  N  TYR A  59   O  GLY A 153           
SHEET    5   B 5 PRO A 113  LEU A 126 -1  O  TRP A 114   N  GLY A  66           
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  LEU A  93   N  ILE A  80           
SHEET    1   D 4 MET L   4  SER L   7  0                                        
SHEET    2   D 4 VAL L  19  ALA L  25 -1  O  THR L  22   N  SER L   7           
SHEET    3   D 4 ASP L  70  ILE L  75 -1  O  LEU L  73   N  ILE L  21           
SHEET    4   D 4 PHE L  62  SER L  63 -1  N  SER L  63   O  THR L  74           
SHEET    1   E 6 SER L  10  ALA L  13  0                                        
SHEET    2   E 6 THR L 102  ILE L 106  1  O  GLU L 105   N  LEU L  11           
SHEET    3   E 6 THR L  85  ARG L  90 -1  N  TYR L  86   O  THR L 102           
SHEET    4   E 6 LEU L  33  GLN L  38 -1  N  TYR L  36   O  TYR L  87           
SHEET    5   E 6 LYS L  45  TYR L  49 -1  O  LYS L  45   N  GLN L  37           
SHEET    6   E 6 THR L  53  LEU L  54 -1  O  THR L  53   N  TYR L  49           
SHEET    1   F 3 SER L 114  PHE L 118  0                                        
SHEET    2   F 3 THR L 129  PHE L 139 -1  O  LEU L 135   N  PHE L 116           
SHEET    3   F 3 TYR L 173  SER L 182 -1  O  TYR L 173   N  PHE L 139           
SHEET    1   G 4 ALA L 153  LEU L 154  0                                        
SHEET    2   G 4 LYS L 145  VAL L 150 -1  N  VAL L 150   O  ALA L 153           
SHEET    3   G 4 VAL L 191  THR L 197 -1  O  ALA L 193   N  LYS L 149           
SHEET    4   G 4 VAL L 205  ASN L 210 -1  O  VAL L 205   N  VAL L 196           
SHEET    1   H 4 GLN H   3  SER H   7  0                                        
SHEET    2   H 4 LEU H  18  SER H  25 -1  O  SER H  21   N  SER H   7           
SHEET    3   H 4 SER H  78  MET H  83 -1  O  MET H  83   N  LEU H  18           
SHEET    4   H 4 PHE H  68  ASP H  73 -1  N  SER H  71   O  TYR H  80           
SHEET    1   I 6 GLY H  10  VAL H  12  0                                        
SHEET    2   I 6 LEU H 116  VAL H 119  1  O  THR H 118   N  GLY H  10           
SHEET    3   I 6 ALA H  92  VAL H  99 -1  N  ALA H  92   O  VAL H 117           
SHEET    4   I 6 MET H  34  GLN H  39 -1  N  VAL H  37   O  TYR H  95           
SHEET    5   I 6 LEU H  45  ILE H  51 -1  O  SER H  49   N  TRP H  36           
SHEET    6   I 6 ILE H  58  TYR H  60 -1  O  ASP H  59   N  ALA H  50           
SHEET    1   J 4 GLY H  10  VAL H  12  0                                        
SHEET    2   J 4 LEU H 116  VAL H 119  1  O  THR H 118   N  GLY H  10           
SHEET    3   J 4 ALA H  92  VAL H  99 -1  N  ALA H  92   O  VAL H 117           
SHEET    4   J 4 LEU H 108  TRP H 111 -1  O  TYR H 110   N  LYS H  98           
SHEET    1   K 4 SER H 128  LEU H 132  0                                        
SHEET    2   K 4 THR H 143  TYR H 153 -1  O  GLY H 147   N  LEU H 132           
SHEET    3   K 4 TYR H 184  PRO H 193 -1  O  VAL H 190   N  LEU H 146           
SHEET    4   K 4 VAL H 171  THR H 173 -1  N  HIS H 172   O  VAL H 189           
SHEET    1   L 4 SER H 128  LEU H 132  0                                        
SHEET    2   L 4 THR H 143  TYR H 153 -1  O  GLY H 147   N  LEU H 132           
SHEET    3   L 4 TYR H 184  PRO H 193 -1  O  VAL H 190   N  LEU H 146           
SHEET    4   L 4 VAL H 177  LEU H 178 -1  N  VAL H 177   O  SER H 185           
SHEET    1   M 3 THR H 159  TRP H 162  0                                        
SHEET    2   M 3 TYR H 202  HIS H 208 -1  O  ASN H 207   N  THR H 159           
SHEET    3   M 3 THR H 213  VAL H 215 -1  O  THR H 213   N  HIS H 208           
SHEET    1   N 3 THR H 159  TRP H 162  0                                        
SHEET    2   N 3 TYR H 202  HIS H 208 -1  O  ASN H 207   N  THR H 159           
SHEET    3   N 3 LYS H 218  ILE H 219 -1  O  ILE H 219   N  TYR H 202           
SSBOND   1 CYS A   69    CYS A  101                          1555   1555  2.05  
SSBOND   2 CYS L   23    CYS L   88                          1555   1555  2.06  
SSBOND   3 CYS L  134    CYS L  194                          1555   1555  2.04  
SSBOND   4 CYS H   22    CYS H   96                          1555   1555  2.05  
SSBOND   5 CYS H  148    CYS H  204                          1555   1555  2.03  
CISPEP   1 ARG A    6    THR A    7          0        13.50                     
CISPEP   2 SER L    7    PRO L    8          0        -2.24                     
CISPEP   3 ASN L   92    ARG L   93          0        -5.94                     
CISPEP   4 ALA L   94    PRO L   95          0        -4.86                     
CISPEP   5 TYR L  140    PRO L  141          0         5.44                     
CISPEP   6 PHE H  154    PRO H  155          0        -4.04                     
CISPEP   7 GLU H  156    PRO H  157          0         3.57                     
CRYST1  161.849  161.849  161.849  90.00  90.00  90.00 I 21 3       24          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006179  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006179  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006179        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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