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Database: PDB
Entry: 4ZCH
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Original site: 4ZCH 
HEADER    CYTOKINE                                16-APR-15   4ZCH              
TITLE     SINGLE-CHAIN HUMAN APRIL-BAFF-BAFF HETEROTRIMER                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TUMOR NECROSIS FACTOR LIGAND SUPERFAMILY MEMBER 13,TUMOR   
COMPND   3 NECROSIS FACTOR LIGAND SUPERFAMILY MEMBER 13B,TUMOR NECROSIS FACTOR  
COMPND   4 LIGAND SUPERFAMILY MEMBER 13B;                                       
COMPND   5 CHAIN: A, B;                                                         
COMPND   6 SYNONYM: A PROLIFERATION-INDUCING LIGAND,APRIL,TNF- AND APOL-RELATED 
COMPND   7 LEUKOCYTE EXPRESSED LIGAND 2,TALL-2,TNF-RELATED DEATH LIGAND 1,TRDL- 
COMPND   8 1,B LYMPHOCYTE STIMULATOR,BLYS,B-CELL-ACTIVATING FACTOR,BAFF,        
COMPND   9 DENDRITIC CELL-DERIVED TNF-LIKE MOLECULE,TNF- AND APOL-RELATED       
COMPND  10 LEUKOCYTE EXPRESSED LIGAND 1,TALL-1,B LYMPHOCYTE STIMULATOR,BLYS,B-  
COMPND  11 CELL-ACTIVATING FACTOR,BAFF,DENDRITIC CELL-DERIVED TNF-LIKE MOLECULE,
COMPND  12 TNF- AND APOL-RELATED LEUKOCYTE EXPRESSED LIGAND 1,TALL-1;           
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 OTHER_DETAILS: THE COMPOUND IS A SINGLE CHAIN APRIL-BAFF-BAFF        
COMPND  15 HETEROTRIMER FROM THE CONSTRUCT OF HIS-FLAG-TEV-GS-HAPRIL (AA111-250,
COMPND  16 T126A)-GGGGS-HBAFF(AA140-285)-GGGGS-HBAFF(AA140-285) WITH CLEAVED    
COMPND  17 TAGS.                                                                
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: TNFSF13, APRIL, TALL2, ZTNF2, UNQ383/PRO715, TNFSF13B, BAFF,   
SOURCE   6 BLYS, TALL1, TNFSF20, ZTNF4, UNQ401/PRO738;                          
SOURCE   7 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   8 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  10 EXPRESSION_SYSTEM_CELL_LINE: HEK293                                  
KEYWDS    B-CELL ACTIVATING FACTOR, A PROLIFERATION-INDUCING LIGAND, TNF        
KEYWDS   2 SUPERFAMILY; CYTOKINE, PROTEROS BIOSTRUCTURES GMBH, CYTOKINE         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.LAMMENS,X.JIANG,K.MASKOS,P.SCHNEIDER                                
REVDAT   5   16-OCT-19 4ZCH    1       REMARK                                   
REVDAT   4   03-APR-19 4ZCH    1       SOURCE REMARK                            
REVDAT   3   08-JUL-15 4ZCH    1       JRNL                                     
REVDAT   2   20-MAY-15 4ZCH    1       JRNL                                     
REVDAT   1   13-MAY-15 4ZCH    0                                                
JRNL        AUTH   S.SCHUEPBACH-MALLEPELL,D.DAS,L.WILLEN,M.VIGOLO,A.TARDIVEL,   
JRNL        AUTH 2 L.LEBON,C.KOWALCZYK-QUINTAS,J.NYS,C.SMULSKI,T.S.ZHENG,       
JRNL        AUTH 3 K.MASKOS,A.LAMMENS,X.JIANG,H.HESS,S.L.TAN,P.SCHNEIDER        
JRNL        TITL   STOICHIOMETRY OF HETEROMERIC BAFF AND APRIL CYTOKINES        
JRNL        TITL 2 DICTATES THEIR RECEPTOR BINDING AND SIGNALING PROPERTIES.    
JRNL        REF    J.BIOL.CHEM.                  V. 290 16330 2015              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   25953898                                                     
JRNL        DOI    10.1074/JBC.M115.661405                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.43 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER-TNT BUSTER 2.11.5                             
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.43                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.61                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 36894                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.179                          
REMARK   3   R VALUE            (WORKING SET)  : 0.177                          
REMARK   3   FREE R VALUE                      : 0.234                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 3.010                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1111                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 18                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.43                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.50                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 96.72                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 3016                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2742                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2929                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2712                   
REMARK   3   BIN FREE R VALUE                        : 0.3682                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 2.88                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 87                       
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6642                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 8                                       
REMARK   3   SOLVENT ATOMS            : 339                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 54.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 48.37                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.92300                                             
REMARK   3    B22 (A**2) : -2.65760                                             
REMARK   3    B33 (A**2) : 5.58050                                              
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  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.334               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.411               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.250               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.385               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.250               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.918                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 6797   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 9194   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2367   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 170    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 974    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 6797   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 873    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 7336   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.22                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.30                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 19.50                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 14                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|8 - A|142 }                                        
REMARK   3    ORIGIN FOR THE GROUP (A):  -10.6728   27.3095   61.3683           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2253 T22:   -0.0286                                    
REMARK   3     T33:   -0.0876 T12:   -0.1571                                    
REMARK   3     T13:    0.0173 T23:    0.0405                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.8003 L22:    3.9022                                    
REMARK   3     L33:    4.0780 L12:   -0.8758                                    
REMARK   3     L13:   -0.2243 L23:   -0.1159                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0284 S12:   -0.1558 S13:   -0.2671                     
REMARK   3     S21:    0.3107 S22:    0.0097 S23:    0.2280                     
REMARK   3     S31:    0.5453 S32:   -0.6272 S33:    0.0187                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { A|150 - A|221 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):   -3.0503   30.3380   39.2703           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0974 T22:   -0.0255                                    
REMARK   3     T33:   -0.0237 T12:   -0.0755                                    
REMARK   3     T13:   -0.0069 T23:   -0.0205                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.1355 L22:    4.0941                                    
REMARK   3     L33:    2.8982 L12:    0.5297                                    
REMARK   3     L13:   -0.0771 L23:   -1.3909                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0345 S12:    0.1132 S13:    0.0708                     
REMARK   3     S21:   -0.1509 S22:    0.0578 S23:    0.1597                     
REMARK   3     S31:    0.0406 S32:   -0.4485 S33:   -0.0233                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { A|222 - A|235 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):   11.2034   40.6034   31.9199           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0167 T22:   -0.0434                                    
REMARK   3     T33:    0.1057 T12:   -0.0708                                    
REMARK   3     T13:   -0.0136 T23:    0.0993                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0000 L22:    5.3116                                    
REMARK   3     L33:    1.4202 L12:    3.8298                                    
REMARK   3     L13:   -1.7744 L23:   -2.7212                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0015 S12:   -0.1629 S13:   -0.0686                     
REMARK   3     S21:    0.0998 S22:   -0.0035 S23:   -0.0580                     
REMARK   3     S31:    0.0590 S32:   -0.1805 S33:    0.0020                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: { A|236 - A|294 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):    1.5666   27.6338   43.9856           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0969 T22:   -0.0996                                    
REMARK   3     T33:    0.0512 T12:   -0.0423                                    
REMARK   3     T13:   -0.0211 T23:    0.0143                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.2997 L22:    1.0930                                    
REMARK   3     L33:    2.8078 L12:    0.4092                                    
REMARK   3     L13:   -0.4631 L23:    0.4979                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0986 S12:    0.0242 S13:   -0.0996                     
REMARK   3     S21:   -0.1807 S22:    0.0698 S23:   -0.0637                     
REMARK   3     S31:    0.2760 S32:   -0.1649 S33:    0.0287                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: { A|301 - A|372 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):   11.1655   40.1195   58.3562           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0992 T22:   -0.0426                                    
REMARK   3     T33:    0.0198 T12:   -0.0437                                    
REMARK   3     T13:   -0.0228 T23:   -0.0238                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.4499 L22:    2.2528                                    
REMARK   3     L33:    3.4413 L12:    0.2182                                    
REMARK   3     L13:   -0.5583 L23:    0.2619                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0278 S12:   -0.1727 S13:    0.0692                     
REMARK   3     S21:    0.0920 S22:    0.1128 S23:   -0.2606                     
REMARK   3     S31:   -0.1090 S32:    0.2432 S33:   -0.0850                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: { A|373 - A|386 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):   10.9024   47.6302   75.2222           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0074 T22:   -0.0175                                    
REMARK   3     T33:    0.0373 T12:   -0.0824                                    
REMARK   3     T13:    0.0272 T23:   -0.0481                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.8697 L22:    0.0426                                    
REMARK   3     L33:    2.7071 L12:    0.4842                                    
REMARK   3     L13:    2.6271 L23:   -1.9120                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0433 S12:    0.1171 S13:    0.0883                     
REMARK   3     S21:    0.1249 S22:   -0.2033 S23:   -0.1540                     
REMARK   3     S31:   -0.2512 S32:    0.1619 S33:    0.1601                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: { A|387 - A|444 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):    9.1782   33.2707   59.7748           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1050 T22:   -0.0565                                    
REMARK   3     T33:   -0.0042 T12:   -0.0011                                    
REMARK   3     T13:   -0.0593 T23:    0.0263                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.5637 L22:    1.9928                                    
REMARK   3     L33:    3.7063 L12:    0.1492                                    
REMARK   3     L13:   -0.9173 L23:    1.4977                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0275 S12:   -0.1899 S13:    0.0085                     
REMARK   3     S21:    0.2089 S22:    0.1451 S23:   -0.2438                     
REMARK   3     S31:    0.1504 S32:    0.1683 S33:   -0.1176                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: { B|7 - B|142 }                                        
REMARK   3    ORIGIN FOR THE GROUP (A):   -0.0371    9.1433   12.9924           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0847 T22:   -0.1990                                    
REMARK   3     T33:   -0.1756 T12:   -0.0825                                    
REMARK   3     T13:    0.0856 T23:    0.0720                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.0321 L22:    3.5859                                    
REMARK   3     L33:    4.5930 L12:   -0.4892                                    
REMARK   3     L13:    0.7104 L23:   -0.1374                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0124 S12:    0.3214 S13:    0.2161                     
REMARK   3     S21:   -0.3510 S22:   -0.1537 S23:   -0.4998                     
REMARK   3     S31:   -0.7413 S32:    0.5535 S33:    0.1661                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: { B|151 - B|221 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):   -1.4353   -0.1088   34.4642           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0618 T22:   -0.1092                                    
REMARK   3     T33:   -0.0217 T12:   -0.0249                                    
REMARK   3     T13:   -0.0098 T23:    0.0475                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.6709 L22:    2.8155                                    
REMARK   3     L33:    3.7668 L12:    0.0860                                    
REMARK   3     L13:   -0.5513 L23:    0.3638                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0281 S12:   -0.0339 S13:   -0.0820                     
REMARK   3     S21:    0.0765 S22:    0.0764 S23:   -0.1399                     
REMARK   3     S31:   -0.1002 S32:    0.1668 S33:   -0.0483                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: { B|222 - B|235 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):  -12.3408  -14.1397   41.2798           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0030 T22:   -0.0265                                    
REMARK   3     T33:    0.0755 T12:   -0.0507                                    
REMARK   3     T13:    0.0624 T23:    0.0408                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.9874 L22:    0.0000                                    
REMARK   3     L33:    1.8276 L12:    3.8355                                    
REMARK   3     L13:   -3.9732 L23:   -3.9463                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0064 S12:    0.0263 S13:   -0.1023                     
REMARK   3     S21:    0.0065 S22:   -0.0507 S23:    0.0846                     
REMARK   3     S31:    0.2136 S32:   -0.1863 S33:    0.0443                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: { B|236 - B|294 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):    0.5416   -4.3718   29.2771           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1107 T22:   -0.0859                                    
REMARK   3     T33:    0.0001 T12:    0.0242                                    
REMARK   3     T13:    0.0129 T23:    0.0407                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.5426 L22:    2.4754                                    
REMARK   3     L33:    2.9645 L12:    0.5615                                    
REMARK   3     L13:    0.8839 L23:   -0.6514                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1073 S12:    0.1755 S13:   -0.1375                     
REMARK   3     S21:   -0.1966 S22:   -0.0487 S23:   -0.3146                     
REMARK   3     S31:    0.0330 S32:    0.3635 S33:   -0.0586                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: { B|300 - B|372 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):  -13.1419  -12.3378   15.0163           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0906 T22:   -0.2806                                    
REMARK   3     T33:   -0.1686 T12:   -0.0681                                    
REMARK   3     T13:   -0.1387 T23:   -0.0030                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.2446 L22:    3.7523                                    
REMARK   3     L33:    6.8588 L12:   -0.3885                                    
REMARK   3     L13:    0.7357 L23:   -1.4380                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.2011 S12:    0.0561 S13:   -0.2666                     
REMARK   3     S21:   -0.6913 S22:    0.0991 S23:    0.4772                     
REMARK   3     S31:    0.9620 S32:   -0.3333 S33:   -0.3003                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: { B|373 - B|386 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):  -20.0644  -10.8655   -2.0951           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1620 T22:   -0.0283                                    
REMARK   3     T33:   -0.1126 T12:    0.0344                                    
REMARK   3     T13:   -0.1819 T23:   -0.0257                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0000 L22:    0.0000                                    
REMARK   3     L33:    1.0948 L12:    0.6373                                    
REMARK   3     L13:   -2.4279 L23:    1.6214                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0260 S12:   -0.0451 S13:   -0.1535                     
REMARK   3     S21:   -0.0213 S22:    0.0655 S23:    0.1175                     
REMARK   3     S31:    0.0888 S32:   -0.1346 S33:   -0.0394                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: { B|387 - B|444 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):   -6.0912  -10.5306   13.3922           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1396 T22:   -0.2009                                    
REMARK   3     T33:   -0.1895 T12:    0.0545                                    
REMARK   3     T13:    0.0021 T23:   -0.0101                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.3227 L22:    3.3172                                    
REMARK   3     L33:    5.4545 L12:    1.1588                                    
REMARK   3     L13:    0.7912 L23:   -1.2036                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0778 S12:    0.0647 S13:   -0.1096                     
REMARK   3     S21:   -0.8302 S22:   -0.0211 S23:   -0.2381                     
REMARK   3     S31:    0.6218 S32:    0.3315 S33:   -0.0568                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4ZCH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-APR-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000209030.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-NOV-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.99998                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36901                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.430                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 147.760                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.7                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.07900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.4600                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.43                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.68                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.50500                            
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: PHASER                                                
REMARK 200 STARTING MODEL: 1Q5X AND 1KD7                                        
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: RESERVOIR SOLUTION : 14% PEG6000 , 1M    
REMARK 280  LICL , TRIS-HCL PH 8.50, VAPOR DIFFUSION, HANGING DROP,             
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      147.76050            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      147.76050            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       28.52050            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       58.93250            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       28.52050            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       58.93250            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      147.76050            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       28.52050            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       58.93250            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      147.76050            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       28.52050            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       58.93250            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
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 A    20                                                      
REMARK 465     ASP A    21                                                      
REMARK 465     SER A    94                                                      
REMARK 465     GLY A   143                                                      
REMARK 465     GLY A   144                                                      
REMARK 465     GLY A   145                                                      
REMARK 465     GLY A   146                                                      
REMARK 465     SER A   147                                                      
REMARK 465     GLU A   148                                                      
REMARK 465     THR A   149                                                      
REMARK 465     GLY A   295                                                      
REMARK 465     GLY A   296                                                      
REMARK 465     GLY A   297                                                      
REMARK 465     SER A   298                                                      
REMARK 465     GLU A   299                                                      
REMARK 465     THR A   300                                                      
REMARK 465     LYS B    20                                                      
REMARK 465     ASP B    21                                                      
REMARK 465     ASP B    22                                                      
REMARK 465     SER B    23                                                      
REMARK 465     SER B    94                                                      
REMARK 465     HIS B    95                                                      
REMARK 465     GLY B   143                                                      
REMARK 465     GLY B   144                                                      
REMARK 465     GLY B   145                                                      
REMARK 465     GLY B   146                                                      
REMARK 465     SER B   147                                                      
REMARK 465     GLU B   148                                                      
REMARK 465     THR B   149                                                      
REMARK 465     VAL B   150                                                      
REMARK 465     GLY B   295                                                      
REMARK 465     GLY B   296                                                      
REMARK 465     GLY B   297                                                      
REMARK 465     SER B   298                                                      
REMARK 465     GLU B   299                                                      
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     ASP A   22   CB   CG   OD1  OD2                                  
REMARK 480     ASP A   24   CG   OD1  OD2                                       
REMARK 480     GLU A   27   CG   CD   OE1  OE2                                  
REMARK 480     MET A   29   CE                                                  
REMARK 480     ARG A   38   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     VAL A   66   CG1  CG2                                            
REMARK 480     MET A   70   CE                                                  
REMARK 480     HIS A   95   CG   ND1  CD2  CE1  NE2                             
REMARK 480     ARG A   98   CZ   NH1  NH2                                       
REMARK 480     ILE A  120   CD1                                                 
REMARK 480     ARG A  125   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     LYS A  127   CD   CE   NZ                                        
REMARK 480     VAL A  150   CG1  CG2                                            
REMARK 480     THR A  151   OG1  CG2                                            
REMARK 480     ARG A  182   NE   CZ   NH1  NH2                                  
REMARK 480     LYS A  189   CE   NZ                                             
REMARK 480     GLU A  190   CD   OE1  OE2                                       
REMARK 480     LYS A  212   CE   NZ                                             
REMARK 480     LYS A  223   CD   CE   NZ                                        
REMARK 480     GLU A  246   CG   CD   OE1  OE2                                  
REMARK 480     LEU A  248   CD1  CD2                                            
REMARK 480     LYS A  319   CD   CE   NZ                                        
REMARK 480     LYS A  340   NZ                                                  
REMARK 480     GLU A  341   CD   OE1  OE2                                       
REMARK 480     LYS A  343   NZ                                                  
REMARK 480     LYS A  363   CG   CD   CE   NZ                                   
REMARK 480     PHE A  379   CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 480     GLU A  397   CD   OE1  OE2                                       
REMARK 480     LEU A  444   CG   CD1  CD2                                       
REMARK 480     HIS B    7   ND1  CD2  CE1  NE2                                  
REMARK 480     ILE B   15   CD1                                                 
REMARK 480     VAL B   25   CG1  CG2                                            
REMARK 480     GLU B   27   CD   OE1  OE2                                       
REMARK 480     ARG B   38   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     GLN B   41   CG   CD   NE2                                       
REMARK 480     ASP B   51   OD1  OD2                                            
REMARK 480     VAL B   66   CG1  CG2                                            
REMARK 480     THR B   67   OG1  CG2                                            
REMARK 480     ILE B   89   CD1                                                 
REMARK 480     ARG B   98   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     TYR B  100   CD1  CD2  CE1  CE2  CZ   OH                         
REMARK 480     ASN B  101   CG   OD1  ND2                                       
REMARK 480     ILE B  120   CD1                                                 
REMARK 480     ILE B  121   CD1                                                 
REMARK 480     ARG B  123   CZ   NH1  NH2                                       
REMARK 480     ARG B  125   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     LYS B  127   CG   CD   CE   NZ                                   
REMARK 480     LEU B  128   CD1  CD2                                            
REMARK 480     LEU B  130   CG   CD1  CD2                                       
REMARK 480     GLU B  162   CG   CD   OE1  OE2                                  
REMARK 480     LYS B  168   CE   NZ                                             
REMARK 480     LYS B  189   CG   CD   CE   NZ                                   
REMARK 480     GLU B  190   CD   OE1  OE2                                       
REMARK 480     LYS B  192   NZ                                                  
REMARK 480     LYS B  212   CE   NZ                                             
REMARK 480     TYR B  214   CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 480     LYS B  223   CD   CE   NZ                                        
REMARK 480     GLU B  246   CG   CD   OE1  OE2                                  
REMARK 480     THR B  247   OG1  CG2                                            
REMARK 480     LEU B  248   CG   CD1  CD2                                       
REMARK 480     LEU B  293   CD1  CD2                                            
REMARK 480     THR B  300   OG1  CG2                                            
REMARK 480     GLU B  313   CD   OE1  OE2                                       
REMARK 480     LYS B  319   CE   NZ                                             
REMARK 480     SER B  321   OG                                                  
REMARK 480     LYS B  340   CG   CD   CE   NZ                                   
REMARK 480     GLU B  341   CD   OE1  OE2                                       
REMARK 480     LYS B  343   CD   CE   NZ                                        
REMARK 480     LYS B  347   CD   CE   NZ                                        
REMARK 480     LYS B  363   CG   CD   CE   NZ                                   
REMARK 480     TYR B  365   CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 480     LYS B  374   NZ                                                  
REMARK 480     VAL B  378   CG1  CG2                                            
REMARK 480     PHE B  379   CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 480     VAL B  386   CG1  CG2                                            
REMARK 480     ILE B  392   CD1                                                 
REMARK 480     GLU B  397   CG   CD   OE1  OE2                                  
REMARK 480     THR B  398   OG1  CG2                                            
REMARK 480     GLU B  417   CG   CD   OE1  OE2                                  
REMARK 480     ARG B  424   CD   NE   CZ   NH1  NH2                             
REMARK 480     GLU B  425   CG   CD   OE1  OE2                                  
REMARK 480     LEU B  444   CG   CD1  CD2                                       
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  23      -11.72     60.01                                   
REMARK 500    ASP A  24      -15.20     72.10                                   
REMARK 500    THR A  67      -54.00     56.07                                   
REMARK 500    PRO A  96     -168.25    -78.13                                   
REMARK 500    ALA A  99      103.62    -57.99                                   
REMARK 500    LEU A 248       64.71     31.72                                   
REMARK 500    PRO A 272       47.47    -75.87                                   
REMARK 500    LEU A 280       35.39    -96.83                                   
REMARK 500    LYS A 319       71.09   -117.17                                   
REMARK 500    GLU A 341       51.81     39.94                                   
REMARK 500    ASN A 401       86.79   -157.44                                   
REMARK 500    THR B  67      -64.41     55.45                                   
REMARK 500    LEU B 130       34.61    -85.93                                   
REMARK 500    ASN B 250       85.56   -153.17                                   
REMARK 500    LEU B 280       47.06    -85.30                                   
REMARK 500    VAL B 301     -174.16    -69.66                                   
REMARK 500    GLU B 341       60.87     32.39                                   
REMARK 500    TYR B 365      -45.31    -29.35                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 791        DISTANCE =  6.03 ANGSTROMS                       
REMARK 525    HOH A 792        DISTANCE =  6.92 ANGSTROMS                       
REMARK 525    HOH A 793        DISTANCE =  7.97 ANGSTROMS                       
REMARK 525    HOH A 794        DISTANCE =  9.83 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 144 A 501                 
DBREF  4ZCH A    7   142  UNP    O75888   TNF13_HUMAN     87    222             
DBREF  4ZCH A  148   293  UNP    Q9Y275   TN13B_HUMAN    140    285             
DBREF  4ZCH A  299   444  UNP    Q9Y275   TN13B_HUMAN    140    285             
DBREF  4ZCH B    7   142  UNP    O75888   TNF13_HUMAN     87    222             
DBREF  4ZCH B  148   293  UNP    Q9Y275   TN13B_HUMAN    140    285             
DBREF  4ZCH B  299   444  UNP    Q9Y275   TN13B_HUMAN    140    285             
SEQADV 4ZCH ALA A   18  UNP  O75888    THR    98 CONFLICT                       
SEQADV 4ZCH GLY A  143  UNP  O75888              LINKER                         
SEQADV 4ZCH GLY A  144  UNP  O75888              LINKER                         
SEQADV 4ZCH GLY A  145  UNP  O75888              LINKER                         
SEQADV 4ZCH GLY A  146  UNP  O75888              LINKER                         
SEQADV 4ZCH SER A  147  UNP  O75888              LINKER                         
SEQADV 4ZCH GLY A  294  UNP  Q9Y275              LINKER                         
SEQADV 4ZCH GLY A  295  UNP  Q9Y275              LINKER                         
SEQADV 4ZCH GLY A  296  UNP  Q9Y275              LINKER                         
SEQADV 4ZCH GLY A  297  UNP  Q9Y275              LINKER                         
SEQADV 4ZCH SER A  298  UNP  Q9Y275              LINKER                         
SEQADV 4ZCH ALA B   18  UNP  O75888    THR    98 CONFLICT                       
SEQADV 4ZCH GLY B  143  UNP  O75888              LINKER                         
SEQADV 4ZCH GLY B  144  UNP  O75888              LINKER                         
SEQADV 4ZCH GLY B  145  UNP  O75888              LINKER                         
SEQADV 4ZCH GLY B  146  UNP  O75888              LINKER                         
SEQADV 4ZCH SER B  147  UNP  O75888              LINKER                         
SEQADV 4ZCH GLY B  294  UNP  Q9Y275              LINKER                         
SEQADV 4ZCH GLY B  295  UNP  Q9Y275              LINKER                         
SEQADV 4ZCH GLY B  296  UNP  Q9Y275              LINKER                         
SEQADV 4ZCH GLY B  297  UNP  Q9Y275              LINKER                         
SEQADV 4ZCH SER B  298  UNP  Q9Y275              LINKER                         
SEQRES   1 A  438  HIS SER VAL LEU HIS LEU VAL PRO ILE ASN ALA ALA SER          
SEQRES   2 A  438  LYS ASP ASP SER ASP VAL THR GLU VAL MET TRP GLN PRO          
SEQRES   3 A  438  ALA LEU ARG ARG GLY ARG GLY LEU GLN ALA GLN GLY TYR          
SEQRES   4 A  438  GLY VAL ARG ILE GLN ASP ALA GLY VAL TYR LEU LEU TYR          
SEQRES   5 A  438  SER GLN VAL LEU PHE GLN ASP VAL THR PHE THR MET GLY          
SEQRES   6 A  438  GLN VAL VAL SER ARG GLU GLY GLN GLY ARG GLN GLU THR          
SEQRES   7 A  438  LEU PHE ARG CYS ILE ARG SER MET PRO SER HIS PRO ASP          
SEQRES   8 A  438  ARG ALA TYR ASN SER CYS TYR SER ALA GLY VAL PHE HIS          
SEQRES   9 A  438  LEU HIS GLN GLY ASP ILE LEU SER VAL ILE ILE PRO ARG          
SEQRES  10 A  438  ALA ARG ALA LYS LEU ASN LEU SER PRO HIS GLY THR PHE          
SEQRES  11 A  438  LEU GLY PHE VAL LYS LEU GLY GLY GLY GLY SER GLU THR          
SEQRES  12 A  438  VAL THR GLN ASP CYS LEU GLN LEU ILE ALA ASP SER GLU          
SEQRES  13 A  438  THR PRO THR ILE GLN LYS GLY SER TYR THR PHE VAL PRO          
SEQRES  14 A  438  TRP LEU LEU SER PHE LYS ARG GLY SER ALA LEU GLU GLU          
SEQRES  15 A  438  LYS GLU ASN LYS ILE LEU VAL LYS GLU THR GLY TYR PHE          
SEQRES  16 A  438  PHE ILE TYR GLY GLN VAL LEU TYR THR ASP LYS THR TYR          
SEQRES  17 A  438  ALA MET GLY HIS LEU ILE GLN ARG LYS LYS VAL HIS VAL          
SEQRES  18 A  438  PHE GLY ASP GLU LEU SER LEU VAL THR LEU PHE ARG CYS          
SEQRES  19 A  438  ILE GLN ASN MET PRO GLU THR LEU PRO ASN ASN SER CYS          
SEQRES  20 A  438  TYR SER ALA GLY ILE ALA LYS LEU GLU GLU GLY ASP GLU          
SEQRES  21 A  438  LEU GLN LEU ALA ILE PRO ARG GLU ASN ALA GLN ILE SER          
SEQRES  22 A  438  LEU ASP GLY ASP VAL THR PHE PHE GLY ALA LEU LYS LEU          
SEQRES  23 A  438  LEU GLY GLY GLY GLY SER GLU THR VAL THR GLN ASP CYS          
SEQRES  24 A  438  LEU GLN LEU ILE ALA ASP SER GLU THR PRO THR ILE GLN          
SEQRES  25 A  438  LYS GLY SER TYR THR PHE VAL PRO TRP LEU LEU SER PHE          
SEQRES  26 A  438  LYS ARG GLY SER ALA LEU GLU GLU LYS GLU ASN LYS ILE          
SEQRES  27 A  438  LEU VAL LYS GLU THR GLY TYR PHE PHE ILE TYR GLY GLN          
SEQRES  28 A  438  VAL LEU TYR THR ASP LYS THR TYR ALA MET GLY HIS LEU          
SEQRES  29 A  438  ILE GLN ARG LYS LYS VAL HIS VAL PHE GLY ASP GLU LEU          
SEQRES  30 A  438  SER LEU VAL THR LEU PHE ARG CYS ILE GLN ASN MET PRO          
SEQRES  31 A  438  GLU THR LEU PRO ASN ASN SER CYS TYR SER ALA GLY ILE          
SEQRES  32 A  438  ALA LYS LEU GLU GLU GLY ASP GLU LEU GLN LEU ALA ILE          
SEQRES  33 A  438  PRO ARG GLU ASN ALA GLN ILE SER LEU ASP GLY ASP VAL          
SEQRES  34 A  438  THR PHE PHE GLY ALA LEU LYS LEU LEU                          
SEQRES   1 B  438  HIS SER VAL LEU HIS LEU VAL PRO ILE ASN ALA ALA SER          
SEQRES   2 B  438  LYS ASP ASP SER ASP VAL THR GLU VAL MET TRP GLN PRO          
SEQRES   3 B  438  ALA LEU ARG ARG GLY ARG GLY LEU GLN ALA GLN GLY TYR          
SEQRES   4 B  438  GLY VAL ARG ILE GLN ASP ALA GLY VAL TYR LEU LEU TYR          
SEQRES   5 B  438  SER GLN VAL LEU PHE GLN ASP VAL THR PHE THR MET GLY          
SEQRES   6 B  438  GLN VAL VAL SER ARG GLU GLY GLN GLY ARG GLN GLU THR          
SEQRES   7 B  438  LEU PHE ARG CYS ILE ARG SER MET PRO SER HIS PRO ASP          
SEQRES   8 B  438  ARG ALA TYR ASN SER CYS TYR SER ALA GLY VAL PHE HIS          
SEQRES   9 B  438  LEU HIS GLN GLY ASP ILE LEU SER VAL ILE ILE PRO ARG          
SEQRES  10 B  438  ALA ARG ALA LYS LEU ASN LEU SER PRO HIS GLY THR PHE          
SEQRES  11 B  438  LEU GLY PHE VAL LYS LEU GLY GLY GLY GLY SER GLU THR          
SEQRES  12 B  438  VAL THR GLN ASP CYS LEU GLN LEU ILE ALA ASP SER GLU          
SEQRES  13 B  438  THR PRO THR ILE GLN LYS GLY SER TYR THR PHE VAL PRO          
SEQRES  14 B  438  TRP LEU LEU SER PHE LYS ARG GLY SER ALA LEU GLU GLU          
SEQRES  15 B  438  LYS GLU ASN LYS ILE LEU VAL LYS GLU THR GLY TYR PHE          
SEQRES  16 B  438  PHE ILE TYR GLY GLN VAL LEU TYR THR ASP LYS THR TYR          
SEQRES  17 B  438  ALA MET GLY HIS LEU ILE GLN ARG LYS LYS VAL HIS VAL          
SEQRES  18 B  438  PHE GLY ASP GLU LEU SER LEU VAL THR LEU PHE ARG CYS          
SEQRES  19 B  438  ILE GLN ASN MET PRO GLU THR LEU PRO ASN ASN SER CYS          
SEQRES  20 B  438  TYR SER ALA GLY ILE ALA LYS LEU GLU GLU GLY ASP GLU          
SEQRES  21 B  438  LEU GLN LEU ALA ILE PRO ARG GLU ASN ALA GLN ILE SER          
SEQRES  22 B  438  LEU ASP GLY ASP VAL THR PHE PHE GLY ALA LEU LYS LEU          
SEQRES  23 B  438  LEU GLY GLY GLY GLY SER GLU THR VAL THR GLN ASP CYS          
SEQRES  24 B  438  LEU GLN LEU ILE ALA ASP SER GLU THR PRO THR ILE GLN          
SEQRES  25 B  438  LYS GLY SER TYR THR PHE VAL PRO TRP LEU LEU SER PHE          
SEQRES  26 B  438  LYS ARG GLY SER ALA LEU GLU GLU LYS GLU ASN LYS ILE          
SEQRES  27 B  438  LEU VAL LYS GLU THR GLY TYR PHE PHE ILE TYR GLY GLN          
SEQRES  28 B  438  VAL LEU TYR THR ASP LYS THR TYR ALA MET GLY HIS LEU          
SEQRES  29 B  438  ILE GLN ARG LYS LYS VAL HIS VAL PHE GLY ASP GLU LEU          
SEQRES  30 B  438  SER LEU VAL THR LEU PHE ARG CYS ILE GLN ASN MET PRO          
SEQRES  31 B  438  GLU THR LEU PRO ASN ASN SER CYS TYR SER ALA GLY ILE          
SEQRES  32 B  438  ALA LYS LEU GLU GLU GLY ASP GLU LEU GLN LEU ALA ILE          
SEQRES  33 B  438  PRO ARG GLU ASN ALA GLN ILE SER LEU ASP GLY ASP VAL          
SEQRES  34 B  438  THR PHE PHE GLY ALA LEU LYS LEU LEU                          
HET    144  A 501       8                                                       
HETNAM     144 TRIS-HYDROXYMETHYL-METHYL-AMMONIUM                               
FORMUL   3  144    C4 H12 N O3 1+                                               
FORMUL   4  HOH   *339(H2 O)                                                    
SHEET    1 AA1 8 LEU A  40  ALA A  42  0                                        
SHEET    2 AA1 8 VAL A  47  ILE A  49 -1  O  ARG A  48   N  GLN A  41           
SHEET    3 AA1 8 ILE A 116  ILE A 121 -1  O  LEU A 117   N  VAL A  47           
SHEET    4 AA1 8 THR A  26  ARG A  36 -1  N  THR A  26   O  ILE A 121           
SHEET    5 AA1 8 VAL A   9  ALA A  18 -1  N  ASN A  16   O  MET A  29           
SHEET    6 AA1 8 PHE A 136  LYS A 141 -1  O  LEU A 137   N  LEU A  12           
SHEET    7 AA1 8 GLY A  53  PHE A  63 -1  N  TYR A  58   O  GLY A 138           
SHEET    8 AA1 8 ASN A 101  LEU A 111 -1  O  LEU A 111   N  GLY A  53           
SHEET    1 AA2 8 GLN A  82  SER A  91  0                                        
SHEET    2 AA2 8 THR A  69  GLU A  77 -1  N  ARG A  76   O  GLU A  83           
SHEET    3 AA2 8 ILE A 116  ILE A 121 -1  O  ILE A 120   N  VAL A  73           
SHEET    4 AA2 8 THR A  26  ARG A  36 -1  N  THR A  26   O  ILE A 121           
SHEET    5 AA2 8 VAL A   9  ALA A  18 -1  N  ASN A  16   O  MET A  29           
SHEET    6 AA2 8 PHE A 136  LYS A 141 -1  O  LEU A 137   N  LEU A  12           
SHEET    7 AA2 8 GLY A  53  PHE A  63 -1  N  TYR A  58   O  GLY A 138           
SHEET    8 AA2 8 LEU A 128  ASN A 129 -1  O  ASN A 129   N  LEU A  62           
SHEET    1 AA3 5 TRP A 176  ARG A 182  0                                        
SHEET    2 AA3 5 CYS A 154  ALA A 159 -1  N  GLN A 156   O  PHE A 180           
SHEET    3 AA3 5 PHE A 286  LYS A 291 -1  O  PHE A 287   N  LEU A 157           
SHEET    4 AA3 5 GLY A 199  TYR A 209 -1  N  GLN A 206   O  PHE A 286           
SHEET    5 AA3 5 ASN A 251  LEU A 261 -1  O  LEU A 261   N  GLY A 199           
SHEET    1 AA4 5 ILE A 166  LYS A 168  0                                        
SHEET    2 AA4 5 TYR A 171  PHE A 173 -1  O  PHE A 173   N  ILE A 166           
SHEET    3 AA4 5 GLU A 266  ILE A 271 -1  O  ILE A 271   N  THR A 172           
SHEET    4 AA4 5 LYS A 192  VAL A 195 -1  N  ILE A 193   O  LEU A 267           
SHEET    5 AA4 5 LEU A 186  LYS A 189 -1  N  GLU A 187   O  LEU A 194           
SHEET    1 AA5 5 ILE A 166  LYS A 168  0                                        
SHEET    2 AA5 5 TYR A 171  PHE A 173 -1  O  PHE A 173   N  ILE A 166           
SHEET    3 AA5 5 GLU A 266  ILE A 271 -1  O  ILE A 271   N  THR A 172           
SHEET    4 AA5 5 ALA A 215  LYS A 223 -1  N  LYS A 223   O  GLU A 266           
SHEET    5 AA5 5 LEU A 234  ASN A 243 -1  O  VAL A 235   N  ARG A 222           
SHEET    1 AA6 5 TRP A 327  ARG A 333  0                                        
SHEET    2 AA6 5 CYS A 305  ALA A 310 -1  N  CYS A 305   O  ARG A 333           
SHEET    3 AA6 5 PHE A 437  LEU A 443 -1  O  PHE A 438   N  LEU A 308           
SHEET    4 AA6 5 GLY A 350  TYR A 360 -1  N  TYR A 355   O  GLY A 439           
SHEET    5 AA6 5 ASN A 402  LEU A 412 -1  O  GLY A 408   N  ILE A 354           
SHEET    1 AA7 5 ILE A 317  LYS A 319  0                                        
SHEET    2 AA7 5 TYR A 322  PHE A 324 -1  O  PHE A 324   N  ILE A 317           
SHEET    3 AA7 5 GLU A 417  ILE A 422 -1  O  ILE A 422   N  THR A 323           
SHEET    4 AA7 5 LYS A 343  VAL A 346 -1  N  ILE A 344   O  LEU A 418           
SHEET    5 AA7 5 LEU A 337  LYS A 340 -1  N  GLU A 338   O  LEU A 345           
SHEET    1 AA8 5 ILE A 317  LYS A 319  0                                        
SHEET    2 AA8 5 TYR A 322  PHE A 324 -1  O  PHE A 324   N  ILE A 317           
SHEET    3 AA8 5 GLU A 417  ILE A 422 -1  O  ILE A 422   N  THR A 323           
SHEET    4 AA8 5 ALA A 366  HIS A 377 -1  N  LYS A 374   O  GLU A 417           
SHEET    5 AA8 5 GLU A 382  ASN A 394 -1  O  LEU A 388   N  ILE A 371           
SHEET    1 AA9 5 LEU B  40  GLN B  43  0                                        
SHEET    2 AA9 5 GLY B  46  ILE B  49 -1  O  ARG B  48   N  GLN B  41           
SHEET    3 AA9 5 ILE B 116  ILE B 121 -1  O  LEU B 117   N  VAL B  47           
SHEET    4 AA9 5 VAL B  73  GLY B  78 -1  N  VAL B  73   O  ILE B 120           
SHEET    5 AA9 5 ARG B  81  ARG B  87 -1  O  LEU B  85   N  VAL B  74           
SHEET    1 AB1 8 LEU B  40  GLN B  43  0                                        
SHEET    2 AB1 8 GLY B  46  ILE B  49 -1  O  ARG B  48   N  GLN B  41           
SHEET    3 AB1 8 ILE B 116  ILE B 121 -1  O  LEU B 117   N  VAL B  47           
SHEET    4 AB1 8 THR B  26  ARG B  36 -1  N  THR B  26   O  ILE B 121           
SHEET    5 AB1 8 VAL B   9  ALA B  18 -1  N  HIS B  11   O  ALA B  33           
SHEET    6 AB1 8 PHE B 136  LYS B 141 -1  O  LEU B 137   N  LEU B  12           
SHEET    7 AB1 8 GLY B  53  PHE B  63 -1  N  LEU B  56   O  VAL B 140           
SHEET    8 AB1 8 ASN B 101  LEU B 111 -1  O  LEU B 111   N  GLY B  53           
SHEET    1 AB2 5 TRP B 176  ARG B 182  0                                        
SHEET    2 AB2 5 CYS B 154  ALA B 159 -1  N  GLN B 156   O  PHE B 180           
SHEET    3 AB2 5 PHE B 286  LYS B 291 -1  O  PHE B 287   N  LEU B 157           
SHEET    4 AB2 5 GLY B 199  TYR B 209 -1  N  PHE B 202   O  LEU B 290           
SHEET    5 AB2 5 ASN B 251  LEU B 261 -1  O  GLY B 257   N  ILE B 203           
SHEET    1 AB3 5 ILE B 166  LYS B 168  0                                        
SHEET    2 AB3 5 TYR B 171  PHE B 173 -1  O  PHE B 173   N  ILE B 166           
SHEET    3 AB3 5 GLU B 266  ILE B 271 -1  O  ILE B 271   N  THR B 172           
SHEET    4 AB3 5 LYS B 192  VAL B 195 -1  N  ILE B 193   O  LEU B 267           
SHEET    5 AB3 5 LEU B 186  LYS B 189 -1  N  LYS B 189   O  LYS B 192           
SHEET    1 AB4 5 ILE B 166  LYS B 168  0                                        
SHEET    2 AB4 5 TYR B 171  PHE B 173 -1  O  PHE B 173   N  ILE B 166           
SHEET    3 AB4 5 GLU B 266  ILE B 271 -1  O  ILE B 271   N  THR B 172           
SHEET    4 AB4 5 ALA B 215  LYS B 223 -1  N  GLN B 221   O  GLN B 268           
SHEET    5 AB4 5 LEU B 234  ASN B 243 -1  O  VAL B 235   N  ARG B 222           
SHEET    1 AB5 5 TRP B 327  ARG B 333  0                                        
SHEET    2 AB5 5 CYS B 305  ALA B 310 -1  N  ILE B 309   O  LEU B 328           
SHEET    3 AB5 5 PHE B 437  LYS B 442 -1  O  PHE B 438   N  LEU B 308           
SHEET    4 AB5 5 GLY B 350  TYR B 360 -1  N  PHE B 353   O  LEU B 441           
SHEET    5 AB5 5 ASN B 402  LEU B 412 -1  O  ALA B 410   N  PHE B 352           
SHEET    1 AB6 5 TRP B 327  ARG B 333  0                                        
SHEET    2 AB6 5 CYS B 305  ALA B 310 -1  N  ILE B 309   O  LEU B 328           
SHEET    3 AB6 5 PHE B 437  LYS B 442 -1  O  PHE B 438   N  LEU B 308           
SHEET    4 AB6 5 GLY B 350  TYR B 360 -1  N  PHE B 353   O  LEU B 441           
SHEET    5 AB6 5 ILE B 429  SER B 430 -1  O  SER B 430   N  LEU B 359           
SHEET    1 AB7 5 ILE B 317  GLN B 318  0                                        
SHEET    2 AB7 5 THR B 323  PHE B 324 -1  O  PHE B 324   N  ILE B 317           
SHEET    3 AB7 5 GLU B 417  ILE B 422 -1  O  ILE B 422   N  THR B 323           
SHEET    4 AB7 5 LYS B 343  VAL B 346 -1  N  ILE B 344   O  LEU B 418           
SHEET    5 AB7 5 LEU B 337  LYS B 340 -1  N  GLU B 338   O  LEU B 345           
SHEET    1 AB8 5 ILE B 317  GLN B 318  0                                        
SHEET    2 AB8 5 THR B 323  PHE B 324 -1  O  PHE B 324   N  ILE B 317           
SHEET    3 AB8 5 GLU B 417  ILE B 422 -1  O  ILE B 422   N  THR B 323           
SHEET    4 AB8 5 ALA B 366  HIS B 377 -1  N  GLN B 372   O  GLN B 419           
SHEET    5 AB8 5 GLU B 382  ASN B 394 -1  O  LEU B 388   N  ILE B 371           
SSBOND   1 CYS A   88    CYS A  103                          1555   1555  2.03  
SSBOND   2 CYS A  240    CYS A  253                          1555   1555  2.06  
SSBOND   3 CYS A  391    CYS A  404                          1555   1555  2.05  
SSBOND   4 CYS B   88    CYS B  103                          1555   1555  2.04  
SSBOND   5 CYS B  240    CYS B  253                          1555   1555  2.04  
SSBOND   6 CYS B  391    CYS B  404                          1555   1555  2.05  
SITE     1 AC1  6 GLU A  83  THR A  84  LEU A  85  PHE A 109                    
SITE     2 AC1  6 GLY A 282  ASP A 283                                          
CRYST1   57.041  117.865  295.521  90.00  90.00  90.00 C 2 2 21     16          
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      0.017531  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008484  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003384        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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