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Database: PDB
Entry: 5DMJ
LinkDB: 5DMJ
Original site: 5DMJ 
HEADER    IMMUNE SYSTEM/SIGNALING PROTEIN         08-SEP-15   5DMJ              
TITLE     STRUCTURE OF THE EXTRACELLULAR DOMAIN OF THE CD40 IN COMPLEX WITH     
TITLE    2 3H56-5 DAB                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TUMOR NECROSIS FACTOR RECEPTOR SUPERFAMILY MEMBER 5;       
COMPND   3 CHAIN: A, D, F;                                                      
COMPND   4 SYNONYM: B-CELL SURFACE ANTIGEN CD40,BP50,CD40L RECEPTOR,CDW40;      
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES;                                                       
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: 3H65-5 DOMAIN ANTIBODY (DAB);                              
COMPND   9 CHAIN: B, E, G;                                                      
COMPND  10 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: CD40, TNFRSF5;                                                 
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: HEK293;                                 
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 EXPRESSION_SYSTEM_STRAIN: HB2151;                                    
SOURCE  16 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  17 EXPRESSION_SYSTEM_PLASMID: PDOM13                                    
KEYWDS    CELL SURFACE RECEPTOR, DOMAIN ANTIBODY, PROTEIN/PROTEIN INTERACTION,  
KEYWDS   2 IMMUNE SYSTEM-SIGNALING PROTEIN COMPLEX                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.SHERIFF                                                             
REVDAT   3   20-JUL-16 5DMJ    1       JRNL                                     
REVDAT   2   08-JUN-16 5DMJ    1       JRNL                                     
REVDAT   1   01-JUN-16 5DMJ    0                                                
JRNL        AUTH   A.P.YAMNIUK,A.SURI,S.R.KRYSTEK,J.TAMURA,V.RAMAMURTHY,R.KUHN, 
JRNL        AUTH 2 K.CARROLL,C.FLEENER,R.RYSECK,L.CHENG,Y.AN,P.DREW,S.GRANT,    
JRNL        AUTH 3 S.J.SUCHARD,S.G.NADLER,J.W.BRYSON,S.SHERIFF                  
JRNL        TITL   FUNCTIONAL ANTAGONISM OF HUMAN CD40 ACHIEVED BY TARGETING A  
JRNL        TITL 2 UNIQUE SPECIES-SPECIFIC EPITOPE.                             
JRNL        REF    J.MOL.BIOL.                   V. 428  2860 2016              
JRNL        REFN                   ESSN 1089-8638                               
JRNL        PMID   27216500                                                     
JRNL        DOI    10.1016/J.JMB.2016.05.014                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.79 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.6                                        
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) : 2.79                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.26                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 29299                          
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)  : 0.230                          
REMARK   3   R VALUE            (WORKING SET)  : 0.229                          
REMARK   3   FREE R VALUE                      : 0.258                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 3.540                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1036                           
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               : 15                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.79                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.89                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 92.74                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2717                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2835                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2610                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2827                   
REMARK   3   BIN FREE R VALUE                        : 0.3047                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 3.94                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 107                      
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            : 6137                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 3                                       
REMARK   3   SOLVENT ATOMS            : 13                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 66.59                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 56.91                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -9.77520                                             
REMARK   3    B22 (A**2) : -1.44440                                             
REMARK   3    B33 (A**2) : 11.21960                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -20.46080                                            
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.430               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.698               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.324               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.734               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.330               
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      : 0.864                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.851                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 6315   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 8637   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1993   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 138    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 955    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 6315   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 2      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 858    ; 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   : 6927   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.36                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.44                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 22.05                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5DMJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-SEP-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000213439.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-SEP-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 3.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CLSI                               
REMARK 200  BEAMLINE                       : 08ID-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9793                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-225                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29303                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.790                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : 0.09100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.42100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.400                              
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: CD40 ENSEMBLE FROM 1JMA, 2UWI, 2AW2, 1NCF, 1TNR,     
REMARK 200  2HEV, 2HEY; DAB FROM 2VYR                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.53                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.97                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM CITRIC ACID, PH 3.5, 20% (W/V)     
REMARK 280  PEG 4000, 200 MM POTASSIUM FORMATE, VAPOR DIFFUSION, HANGING        
REMARK 280  DROP, TEMPERATURE 293K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -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        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       99.65000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       24.35000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       99.65000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       24.35000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1900 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14670 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1860 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14980 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E                                  
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: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1720 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14480 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, G                                  
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     PRO A    23                                                      
REMARK 465     GLN A   189                                                      
REMARK 465     ASP A   190                                                      
REMARK 465     ARG A   191                                                      
REMARK 465     LEU A   192                                                      
REMARK 465     ARG A   193                                                      
REMARK 465     ASP A   194                                                      
REMARK 465     PRO A   195                                                      
REMARK 465     GLY A   196                                                      
REMARK 465     GLY A   197                                                      
REMARK 465     GLY A   198                                                      
REMARK 465     GLY A   199                                                      
REMARK 465     GLY A   200                                                      
REMARK 465     ARG A   201                                                      
REMARK 465     LEU A   202                                                      
REMARK 465     VAL A   203                                                      
REMARK 465     PRO A   204                                                      
REMARK 465     ARG A   205                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     THR B     0                                                      
REMARK 465     ALA B   115                                                      
REMARK 465     ALA B   116                                                      
REMARK 465     PRO D    23                                                      
REMARK 465     ARG D   191                                                      
REMARK 465     LEU D   192                                                      
REMARK 465     ARG D   193                                                      
REMARK 465     ASP D   194                                                      
REMARK 465     PRO D   195                                                      
REMARK 465     GLY D   196                                                      
REMARK 465     GLY D   197                                                      
REMARK 465     GLY D   198                                                      
REMARK 465     GLY D   199                                                      
REMARK 465     GLY D   200                                                      
REMARK 465     ARG D   201                                                      
REMARK 465     LEU D   202                                                      
REMARK 465     VAL D   203                                                      
REMARK 465     PRO D   204                                                      
REMARK 465     ARG D   205                                                      
REMARK 465     SER E    -2                                                      
REMARK 465     SER E   113                                                      
REMARK 465     ALA E   114                                                      
REMARK 465     ALA E   115                                                      
REMARK 465     ALA E   116                                                      
REMARK 465     PRO F    23                                                      
REMARK 465     THR F    24                                                      
REMARK 465     ALA F    25                                                      
REMARK 465     GLN F   189                                                      
REMARK 465     ASP F   190                                                      
REMARK 465     ARG F   191                                                      
REMARK 465     LEU F   192                                                      
REMARK 465     ARG F   193                                                      
REMARK 465     ASP F   194                                                      
REMARK 465     PRO F   195                                                      
REMARK 465     GLY F   196                                                      
REMARK 465     GLY F   197                                                      
REMARK 465     GLY F   198                                                      
REMARK 465     GLY F   199                                                      
REMARK 465     GLY F   200                                                      
REMARK 465     ARG F   201                                                      
REMARK 465     LEU F   202                                                      
REMARK 465     VAL F   203                                                      
REMARK 465     PRO F   204                                                      
REMARK 465     ARG F   205                                                      
REMARK 465     SER G    -1                                                      
REMARK 465     THR G     0                                                      
REMARK 465     ALA G   114                                                      
REMARK 465     ALA G   115                                                      
REMARK 465     ALA G   116                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A  27    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A  28    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  29    CG   CD   CE   NZ                                   
REMARK 470     TYR A  31    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU A  53    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  64    CG   CD   OE1  OE2                                  
REMARK 470     TYR A  82    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG A  90    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A  93    CG   CD   OE1  NE2                                  
REMARK 470     LYS A  94    CG   CD   CE   NZ                                   
REMARK 470     SER A 113    OG                                                  
REMARK 470     LYS A 132    NZ                                                  
REMARK 470     ILE A 134    CG1  CG2  CD1                                       
REMARK 470     THR A 136    OG1  CG2                                            
REMARK 470     VAL A 138    CG1  CG2                                            
REMARK 470     SER A 139    OG                                                  
REMARK 470     LYS A 160    CG   CD   CE   NZ                                   
REMARK 470     THR A 165    OG1  CG2                                            
REMARK 470     SER A 166    OG                                                  
REMARK 470     GLU A 168    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 170    CG   CD   CE   NZ                                   
REMARK 470     ASP A 171    CG   OD1  OD2                                       
REMARK 470     LEU A 172    CG   CD1  CD2                                       
REMARK 470     VAL A 173    CG1  CG2                                            
REMARK 470     GLN A 175    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 181    NZ                                                  
REMARK 470     THR A 182    OG1  CG2                                            
REMARK 470     LYS B  43    CG   CD   CE   NZ                                   
REMARK 470     THR D  24    OG1  CG2                                            
REMARK 470     ARG D  27    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D  28    CG   CD   OE1  OE2                                  
REMARK 470     LYS D  29    CD   CE   NZ                                        
REMARK 470     TYR D  31    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU D  56    CG   CD   OE1  OE2                                  
REMARK 470     LYS D  81    CD   CE   NZ                                        
REMARK 470     LYS D  94    NZ                                                  
REMARK 470     GLU D 106    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 107    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 114    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 117    CG   CD   OE1  OE2                                  
REMARK 470     SER D 118    OG                                                  
REMARK 470     SER D 126    OG                                                  
REMARK 470     LYS D 132    CE   NZ                                             
REMARK 470     ILE D 134    CG1  CG2  CD1                                       
REMARK 470     THR D 136    OG1  CG2                                            
REMARK 470     VAL D 138    CG1  CG2                                            
REMARK 470     SER D 139    OG                                                  
REMARK 470     GLU D 144    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 160    NZ                                                  
REMARK 470     GLU D 168    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 170    CG   CD   CE   NZ                                   
REMARK 470     ASP D 171    CG   OD1  OD2                                       
REMARK 470     LEU D 172    CG   CD1  CD2                                       
REMARK 470     VAL D 174    CG1  CG2                                            
REMARK 470     GLN D 175    CG   CD   OE1  NE2                                  
REMARK 470     THR D 182    OG1  CG2                                            
REMARK 470     GLN D 189    CG   CD   OE1  NE2                                  
REMARK 470     ASP D 190    CG   OD1  OD2                                       
REMARK 470     THR E  -1    OG1  CG2                                            
REMARK 470     GLU E   1    CG   CD   OE1  OE2                                  
REMARK 470     ARG E  19    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS E  43    CG   CD   CE   NZ                                   
REMARK 470     ARG E  83    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG F  27    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU F  28    CG   CD   OE1  OE2                                  
REMARK 470     LYS F  29    CG   CD   CE   NZ                                   
REMARK 470     TYR F  31    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS F  46    CE   NZ                                             
REMARK 470     ASP F  50    CG   OD1  OD2                                       
REMARK 470     GLU F  53    CG   CD   OE1  OE2                                  
REMARK 470     PHE F  54    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU F  56    CG   CD   OE1  OE2                                  
REMARK 470     LEU F  60    CG   CD1  CD2                                       
REMARK 470     GLU F  64    CG   CD   OE1  OE2                                  
REMARK 470     GLU F  66    CD   OE1  OE2                                       
REMARK 470     ARG F  73    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG F  90    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN F  93    CG   CD   OE1  NE2                                  
REMARK 470     ILE F 102    CG1  CG2  CD1                                       
REMARK 470     GLU F 107    CD   OE1  OE2                                       
REMARK 470     GLU F 114    CG   CD   OE1  OE2                                  
REMARK 470     SER F 124    OG                                                  
REMARK 470     LYS F 132    CD   CE   NZ                                        
REMARK 470     ILE F 134    CD1                                                 
REMARK 470     THR F 136    OG1  CG2                                            
REMARK 470     VAL F 138    CG1  CG2                                            
REMARK 470     SER F 139    OG                                                  
REMARK 470     GLU F 144    CG   CD   OE1  OE2                                  
REMARK 470     LYS F 160    CG   CD   CE   NZ                                   
REMARK 470     THR F 165    OG1  CG2                                            
REMARK 470     GLU F 168    CG   CD   OE1  OE2                                  
REMARK 470     LYS F 170    CG   CD   CE   NZ                                   
REMARK 470     ASP F 171    CG   OD1  OD2                                       
REMARK 470     LEU F 172    CG   CD1  CD2                                       
REMARK 470     VAL F 173    CG1  CG2                                            
REMARK 470     GLN F 175    CG   CD   OE1  NE2                                  
REMARK 470     GLN F 176    CG   CD   OE1  NE2                                  
REMARK 470     ASP F 180    CG   OD1  OD2                                       
REMARK 470     LYS F 181    CG   CD   CE   NZ                                   
REMARK 470     GLN G  13    CG   CD   OE1  NE2                                  
REMARK 470     ARG G  30    NE   CZ   NH1  NH2                                  
REMARK 470     ARG G  47    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN G  53    CG   CD   OE1  NE2                                  
REMARK 470     MET G  64    CG   SD   CE                                        
REMARK 470     GLN G 105    CG   CD   OE1  NE2                                  
REMARK 470     SER G 113    OG                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    VAL A   174     O    VAL A   185              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PHE D 129   C   -  N   -  CA  ANGL. DEV. =  19.6 DEGREES          
REMARK 500    LYS D 160   C   -  N   -  CA  ANGL. DEV. =  21.0 DEGREES          
REMARK 500    PHE F 129   C   -  N   -  CA  ANGL. DEV. =  16.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A  25      -69.50     54.30                                   
REMARK 500    CYS A  26      127.33     75.22                                   
REMARK 500    LYS A  29       17.04     55.86                                   
REMARK 500    GLN A  30      -51.29   -132.18                                   
REMARK 500    TYR A  31     -130.12     35.34                                   
REMARK 500    LEU A  32       98.98     43.46                                   
REMARK 500    ASN A  34       63.45   -174.95                                   
REMARK 500    SER A  35      -23.89     89.27                                   
REMARK 500    THR A  96     -167.46   -118.88                                   
REMARK 500    GLU A 107      121.91     87.40                                   
REMARK 500    LYS A 132       34.99   -142.93                                   
REMARK 500    GLN A 133      169.50     69.20                                   
REMARK 500    THR A 136      152.16     58.53                                   
REMARK 500    VAL A 138      -35.06     71.06                                   
REMARK 500    SER A 139       74.09    -69.32                                   
REMARK 500    PRO A 145       31.10    -86.18                                   
REMARK 500    CYS A 146      102.72     57.32                                   
REMARK 500    VAL A 154      147.72     46.67                                   
REMARK 500    PHE A 158      -36.93   -133.87                                   
REMARK 500    THR A 165      -90.70    -39.07                                   
REMARK 500    SER A 166      -75.33   -179.28                                   
REMARK 500    GLU A 168      -15.02   -156.69                                   
REMARK 500    THR A 169      -76.89    -69.78                                   
REMARK 500    LYS A 170       20.84    -78.06                                   
REMARK 500    VAL A 173     -108.12    -67.29                                   
REMARK 500    VAL A 174      -46.80   -178.57                                   
REMARK 500    GLN A 175      -59.35     47.14                                   
REMARK 500    ALA D  25       33.72    110.45                                   
REMARK 500    CYS D  26      139.44    152.75                                   
REMARK 500    GLN D  30      -58.05   -137.08                                   
REMARK 500    TYR D  31      105.66     -7.14                                   
REMARK 500    ASN D  34       65.06   -179.56                                   
REMARK 500    SER D  65       -2.75     77.72                                   
REMARK 500    TYR D  82      110.77     65.95                                   
REMARK 500    ALA D 115       80.59     59.27                                   
REMARK 500    CYS D 116       63.99    144.00                                   
REMARK 500    PHE D 129      102.84    115.33                                   
REMARK 500    LYS D 132       35.94   -144.70                                   
REMARK 500    GLN D 133      171.38     69.27                                   
REMARK 500    THR D 136      144.09    -12.89                                   
REMARK 500    VAL D 138      -78.04    -66.98                                   
REMARK 500    PHE D 158      -36.27   -134.55                                   
REMARK 500    LYS D 160      -51.37    143.90                                   
REMARK 500    CYS D 161      103.08     66.88                                   
REMARK 500    CYS D 167      -64.52     77.18                                   
REMARK 500    LYS D 170       79.41     59.91                                   
REMARK 500    ASP D 171      108.04     35.59                                   
REMARK 500    LEU D 172     -131.29    -60.58                                   
REMARK 500    VAL D 173      120.45     73.22                                   
REMARK 500    ALA D 177      -70.69    -41.08                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      82 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A 301   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 125   O                                                      
REMARK 620 2 SER A 126   O    62.5                                              
REMARK 620 3 PHE A 129   O    95.6  72.2                                        
REMARK 620 4 SER A 152   OG  170.2 120.7  77.6                                  
REMARK 620 5 ASP A 153   O   128.9 103.0 128.2  60.5                            
REMARK 620 6 VAL A 154   O    86.9  90.0 158.1 102.0  42.4                      
REMARK 620 7 HOH A 401   O    74.6 126.7  82.7  97.5 128.9 118.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K D 301   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 125   O                                                      
REMARK 620 2 SER D 126   O    72.0                                              
REMARK 620 3 PHE D 129   O   118.7  76.1                                        
REMARK 620 4 VAL D 154   O    84.1  84.1 142.1                                  
REMARK 620 5 HOH D 403   O    83.0 147.2  98.7 114.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K F 301   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS F 125   O                                                      
REMARK 620 2 SER F 126   O    71.4                                              
REMARK 620 3 PHE F 129   O   116.9  76.6                                        
REMARK 620 4 SER F 152   OG  159.1 125.0  81.7                                  
REMARK 620 5 VAL F 154   O    79.8  96.6 157.5  85.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K A 301                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K D 301                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K F 301                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5DMI   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE AUTHOR STATES THAT THE PROTEIN WAS EXPRESSED WITH ASN153 AND     
REMARK 999 ASN180 (AND POST-TRANSLATIONAL CARBOHYDRATE) AND THEN SUBJECTED TO   
REMARK 999 PNGASE F CLEAVAGE WHICH REMOVES THE CARBOHYDRATE AND LEAVES ASP153   
REMARK 999 AND ASP180 RATHER THAN ASN.                                          
DBREF  5DMJ A   23   193  UNP    P25942   TNR5_HUMAN      23    193             
DBREF  5DMJ B   -1   116  PDB    5DMJ     5DMJ            -1    116             
DBREF  5DMJ D   23   193  UNP    P25942   TNR5_HUMAN      23    193             
DBREF  5DMJ E   -2   116  PDB    5DMJ     5DMJ            -2    116             
DBREF  5DMJ F   23   193  UNP    P25942   TNR5_HUMAN      23    193             
DBREF  5DMJ G   -1   116  PDB    5DMJ     5DMJ            -1    116             
SEQADV 5DMJ ASP A  153  UNP  P25942    ASN   153 SEE REMARK 999                 
SEQADV 5DMJ ASP A  180  UNP  P25942    ASN   180 SEE REMARK 999                 
SEQADV 5DMJ ASP A  194  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMJ PRO A  195  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMJ GLY A  196  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMJ GLY A  197  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMJ GLY A  198  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMJ GLY A  199  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMJ GLY A  200  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMJ ARG A  201  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMJ LEU A  202  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMJ VAL A  203  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMJ PRO A  204  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMJ ARG A  205  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMJ ASP D  153  UNP  P25942    ASN   153 SEE REMARK 999                 
SEQADV 5DMJ ASP D  180  UNP  P25942    ASN   180 SEE REMARK 999                 
SEQADV 5DMJ ASP D  194  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMJ PRO D  195  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMJ GLY D  196  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMJ GLY D  197  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMJ GLY D  198  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMJ GLY D  199  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMJ GLY D  200  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMJ ARG D  201  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMJ LEU D  202  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMJ VAL D  203  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMJ PRO D  204  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMJ ARG D  205  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMJ ASP F  153  UNP  P25942    ASN   153 SEE REMARK 999                 
SEQADV 5DMJ ASP F  180  UNP  P25942    ASN   180 SEE REMARK 999                 
SEQADV 5DMJ ASP F  194  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMJ PRO F  195  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMJ GLY F  196  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMJ GLY F  197  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMJ GLY F  198  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMJ GLY F  199  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMJ GLY F  200  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMJ ARG F  201  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMJ LEU F  202  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMJ VAL F  203  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMJ PRO F  204  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMJ ARG F  205  UNP  P25942              EXPRESSION TAG                 
SEQRES   1 A  183  PRO THR ALA CYS ARG GLU LYS GLN TYR LEU ILE ASN SER          
SEQRES   2 A  183  GLN CYS CYS SER LEU CYS GLN PRO GLY GLN LYS LEU VAL          
SEQRES   3 A  183  SER ASP CYS THR GLU PHE THR GLU THR GLU CYS LEU PRO          
SEQRES   4 A  183  CYS GLY GLU SER GLU PHE LEU ASP THR TRP ASN ARG GLU          
SEQRES   5 A  183  THR HIS CYS HIS GLN HIS LYS TYR CYS ASP PRO ASN LEU          
SEQRES   6 A  183  GLY LEU ARG VAL GLN GLN LYS GLY THR SER GLU THR ASP          
SEQRES   7 A  183  THR ILE CYS THR CYS GLU GLU GLY TRP HIS CYS THR SER          
SEQRES   8 A  183  GLU ALA CYS GLU SER CYS VAL LEU HIS ARG SER CYS SER          
SEQRES   9 A  183  PRO GLY PHE GLY VAL LYS GLN ILE ALA THR GLY VAL SER          
SEQRES  10 A  183  ASP THR ILE CYS GLU PRO CYS PRO VAL GLY PHE PHE SER          
SEQRES  11 A  183  ASP VAL SER SER ALA PHE GLU LYS CYS HIS PRO TRP THR          
SEQRES  12 A  183  SER CYS GLU THR LYS ASP LEU VAL VAL GLN GLN ALA GLY          
SEQRES  13 A  183  THR ASP LYS THR ASP VAL VAL CYS GLY PRO GLN ASP ARG          
SEQRES  14 A  183  LEU ARG ASP PRO GLY GLY GLY GLY GLY ARG LEU VAL PRO          
SEQRES  15 A  183  ARG                                                          
SEQRES   1 B  121  SER THR GLU VAL GLN LEU LEU GLU SER GLY GLY GLY LEU          
SEQRES   2 B  121  VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA          
SEQRES   3 B  121  SER GLY PHE THR PHE ARG ASP TYR GLU MET TRP TRP VAL          
SEQRES   4 B  121  ARG GLN ALA PRO GLY LYS GLY LEU GLU ARG VAL SER ALA          
SEQRES   5 B  121  ILE ASN PRO GLN GLY THR ARG THR TYR TYR ALA ASP SER          
SEQRES   6 B  121  VAL MET GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS          
SEQRES   7 B  121  ASN THR LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU          
SEQRES   8 B  121  ASP THR ALA VAL TYR TYR CYS ALA LYS LEU PRO PHE THR          
SEQRES   9 B  121  PHE ASP ASP TRP GLY GLN GLY THR LEU VAL THR VAL SER          
SEQRES  10 B  121  SER ALA ALA ALA                                              
SEQRES   1 D  183  PRO THR ALA CYS ARG GLU LYS GLN TYR LEU ILE ASN SER          
SEQRES   2 D  183  GLN CYS CYS SER LEU CYS GLN PRO GLY GLN LYS LEU VAL          
SEQRES   3 D  183  SER ASP CYS THR GLU PHE THR GLU THR GLU CYS LEU PRO          
SEQRES   4 D  183  CYS GLY GLU SER GLU PHE LEU ASP THR TRP ASN ARG GLU          
SEQRES   5 D  183  THR HIS CYS HIS GLN HIS LYS TYR CYS ASP PRO ASN LEU          
SEQRES   6 D  183  GLY LEU ARG VAL GLN GLN LYS GLY THR SER GLU THR ASP          
SEQRES   7 D  183  THR ILE CYS THR CYS GLU GLU GLY TRP HIS CYS THR SER          
SEQRES   8 D  183  GLU ALA CYS GLU SER CYS VAL LEU HIS ARG SER CYS SER          
SEQRES   9 D  183  PRO GLY PHE GLY VAL LYS GLN ILE ALA THR GLY VAL SER          
SEQRES  10 D  183  ASP THR ILE CYS GLU PRO CYS PRO VAL GLY PHE PHE SER          
SEQRES  11 D  183  ASP VAL SER SER ALA PHE GLU LYS CYS HIS PRO TRP THR          
SEQRES  12 D  183  SER CYS GLU THR LYS ASP LEU VAL VAL GLN GLN ALA GLY          
SEQRES  13 D  183  THR ASP LYS THR ASP VAL VAL CYS GLY PRO GLN ASP ARG          
SEQRES  14 D  183  LEU ARG ASP PRO GLY GLY GLY GLY GLY ARG LEU VAL PRO          
SEQRES  15 D  183  ARG                                                          
SEQRES   1 E  121  SER THR GLU VAL GLN LEU LEU GLU SER GLY GLY GLY LEU          
SEQRES   2 E  121  VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA          
SEQRES   3 E  121  SER GLY PHE THR PHE ARG ASP TYR GLU MET TRP TRP VAL          
SEQRES   4 E  121  ARG GLN ALA PRO GLY LYS GLY LEU GLU ARG VAL SER ALA          
SEQRES   5 E  121  ILE ASN PRO GLN GLY THR ARG THR TYR TYR ALA ASP SER          
SEQRES   6 E  121  VAL MET GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS          
SEQRES   7 E  121  ASN THR LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU          
SEQRES   8 E  121  ASP THR ALA VAL TYR TYR CYS ALA LYS LEU PRO PHE THR          
SEQRES   9 E  121  PHE ASP ASP TRP GLY GLN GLY THR LEU VAL THR VAL SER          
SEQRES  10 E  121  SER ALA ALA ALA                                              
SEQRES   1 F  183  PRO THR ALA CYS ARG GLU LYS GLN TYR LEU ILE ASN SER          
SEQRES   2 F  183  GLN CYS CYS SER LEU CYS GLN PRO GLY GLN LYS LEU VAL          
SEQRES   3 F  183  SER ASP CYS THR GLU PHE THR GLU THR GLU CYS LEU PRO          
SEQRES   4 F  183  CYS GLY GLU SER GLU PHE LEU ASP THR TRP ASN ARG GLU          
SEQRES   5 F  183  THR HIS CYS HIS GLN HIS LYS TYR CYS ASP PRO ASN LEU          
SEQRES   6 F  183  GLY LEU ARG VAL GLN GLN LYS GLY THR SER GLU THR ASP          
SEQRES   7 F  183  THR ILE CYS THR CYS GLU GLU GLY TRP HIS CYS THR SER          
SEQRES   8 F  183  GLU ALA CYS GLU SER CYS VAL LEU HIS ARG SER CYS SER          
SEQRES   9 F  183  PRO GLY PHE GLY VAL LYS GLN ILE ALA THR GLY VAL SER          
SEQRES  10 F  183  ASP THR ILE CYS GLU PRO CYS PRO VAL GLY PHE PHE SER          
SEQRES  11 F  183  ASP VAL SER SER ALA PHE GLU LYS CYS HIS PRO TRP THR          
SEQRES  12 F  183  SER CYS GLU THR LYS ASP LEU VAL VAL GLN GLN ALA GLY          
SEQRES  13 F  183  THR ASP LYS THR ASP VAL VAL CYS GLY PRO GLN ASP ARG          
SEQRES  14 F  183  LEU ARG ASP PRO GLY GLY GLY GLY GLY ARG LEU VAL PRO          
SEQRES  15 F  183  ARG                                                          
SEQRES   1 G  121  SER THR GLU VAL GLN LEU LEU GLU SER GLY GLY GLY LEU          
SEQRES   2 G  121  VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA          
SEQRES   3 G  121  SER GLY PHE THR PHE ARG ASP TYR GLU MET TRP TRP VAL          
SEQRES   4 G  121  ARG GLN ALA PRO GLY LYS GLY LEU GLU ARG VAL SER ALA          
SEQRES   5 G  121  ILE ASN PRO GLN GLY THR ARG THR TYR TYR ALA ASP SER          
SEQRES   6 G  121  VAL MET GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS          
SEQRES   7 G  121  ASN THR LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU          
SEQRES   8 G  121  ASP THR ALA VAL TYR TYR CYS ALA LYS LEU PRO PHE THR          
SEQRES   9 G  121  PHE ASP ASP TRP GLY GLN GLY THR LEU VAL THR VAL SER          
SEQRES  10 G  121  SER ALA ALA ALA                                              
HET      K  A 301       1                                                       
HET      K  D 301       1                                                       
HET      K  F 301       1                                                       
HETNAM       K POTASSIUM ION                                                    
FORMUL   7    K    3(K 1+)                                                      
FORMUL  10  HOH   *13(H2 O)                                                     
HELIX    1 AA1 ASP A   84  LEU A   87  5                                   4    
HELIX    2 AA2 THR B   28  TYR B   32  5                                   5    
HELIX    3 AA3 ARG B   83  THR B   87  5                                   5    
HELIX    4 AA4 ASP D   84  LEU D   87  5                                   4    
HELIX    5 AA5 THR E   28  TYR E   32  5                                   5    
HELIX    6 AA6 ARG E   83  THR E   87  5                                   5    
HELIX    7 AA7 ASP F   84  LEU F   87  5                                   4    
HELIX    8 AA8 CYS F  167  ASP F  171  5                                   5    
HELIX    9 AA9 THR G   28  TYR G   32  5                                   5    
HELIX   10 AB1 ARG G   83  THR G   87  5                                   5    
SHEET    1 AA1 2 GLN A  45  SER A  49  0                                        
SHEET    2 AA1 2 GLU A  58  PRO A  61 -1  O  GLU A  58   N  SER A  49           
SHEET    1 AA2 2 GLU A  66  PHE A  67  0                                        
SHEET    2 AA2 2 HIS A  78  GLN A  79 -1  O  HIS A  78   N  PHE A  67           
SHEET    1 AA3 2 LEU A  89  GLN A  93  0                                        
SHEET    2 AA3 2 ILE A 102  CYS A 105 -1  O  THR A 104   N  ARG A  90           
SHEET    1 AA4 2 HIS A 110  CYS A 111  0                                        
SHEET    2 AA4 2 CYS A 119  VAL A 120 -1  O  VAL A 120   N  HIS A 110           
SHEET    1 AA5 2 GLY A 130  VAL A 131  0                                        
SHEET    2 AA5 2 CYS A 143  GLU A 144 -1  O  GLU A 144   N  GLY A 130           
SHEET    1 AA6 2 PHE A 150  PHE A 151  0                                        
SHEET    2 AA6 2 HIS A 162  PRO A 163 -1  O  HIS A 162   N  PHE A 151           
SHEET    1 AA7 4 GLN B   3  SER B   7  0                                        
SHEET    2 AA7 4 LEU B  18  SER B  25 -1  O  SER B  25   N  GLN B   3           
SHEET    3 AA7 4 THR B  77  MET B  82 -1  O  MET B  82   N  LEU B  18           
SHEET    4 AA7 4 PHE B  67  ASP B  72 -1  N  ASP B  72   O  THR B  77           
SHEET    1 AA8 6 LEU B  11  VAL B  12  0                                        
SHEET    2 AA8 6 THR B 107  VAL B 111  1  O  THR B 110   N  VAL B  12           
SHEET    3 AA8 6 ALA B  88  LYS B  94 -1  N  ALA B  88   O  VAL B 109           
SHEET    4 AA8 6 MET B  34  GLN B  39 -1  N  VAL B  37   O  TYR B  91           
SHEET    5 AA8 6 LEU B  45  ILE B  51 -1  O  GLU B  46   N  ARG B  38           
SHEET    6 AA8 6 THR B  57  TYR B  59 -1  O  TYR B  58   N  ALA B  50           
SHEET    1 AA9 2 GLN D  45  SER D  49  0                                        
SHEET    2 AA9 2 GLU D  58  PRO D  61 -1  O  GLU D  58   N  VAL D  48           
SHEET    1 AB1 2 GLU D  66  PHE D  67  0                                        
SHEET    2 AB1 2 HIS D  78  GLN D  79 -1  O  HIS D  78   N  PHE D  67           
SHEET    1 AB2 2 LEU D  89  GLN D  93  0                                        
SHEET    2 AB2 2 ILE D 102  CYS D 105 -1  O  THR D 104   N  ARG D  90           
SHEET    1 AB3 2 HIS D 110  CYS D 111  0                                        
SHEET    2 AB3 2 CYS D 119  VAL D 120 -1  O  VAL D 120   N  HIS D 110           
SHEET    1 AB4 2 GLY D 130  ILE D 134  0                                        
SHEET    2 AB4 2 THR D 141  GLU D 144 -1  O  GLU D 144   N  GLY D 130           
SHEET    1 AB5 2 PHE D 150  PHE D 151  0                                        
SHEET    2 AB5 2 HIS D 162  PRO D 163 -1  O  HIS D 162   N  PHE D 151           
SHEET    1 AB6 2 VAL D 174  GLN D 176  0                                        
SHEET    2 AB6 2 VAL D 185  CYS D 186 -1  O  VAL D 185   N  GLN D 175           
SHEET    1 AB7 4 GLN E   3  SER E   7  0                                        
SHEET    2 AB7 4 LEU E  18  SER E  25 -1  O  SER E  25   N  GLN E   3           
SHEET    3 AB7 4 THR E  77  MET E  82 -1  O  MET E  82   N  LEU E  18           
SHEET    4 AB7 4 PHE E  67  ASP E  72 -1  N  SER E  70   O  TYR E  79           
SHEET    1 AB8 6 LEU E  11  VAL E  12  0                                        
SHEET    2 AB8 6 THR E 107  VAL E 111  1  O  THR E 110   N  VAL E  12           
SHEET    3 AB8 6 ALA E  88  LYS E  94 -1  N  TYR E  90   O  THR E 107           
SHEET    4 AB8 6 MET E  34  GLN E  39 -1  N  VAL E  37   O  TYR E  91           
SHEET    5 AB8 6 LEU E  45  ILE E  51 -1  O  SER E  49   N  TRP E  36           
SHEET    6 AB8 6 THR E  57  TYR E  59 -1  O  TYR E  58   N  ALA E  50           
SHEET    1 AB9 2 GLN F  45  LYS F  46  0                                        
SHEET    2 AB9 2 LEU F  60  PRO F  61 -1  O  LEU F  60   N  LYS F  46           
SHEET    1 AC1 2 GLU F  66  PHE F  67  0                                        
SHEET    2 AC1 2 HIS F  78  GLN F  79 -1  O  HIS F  78   N  PHE F  67           
SHEET    1 AC2 2 LEU F  89  GLN F  93  0                                        
SHEET    2 AC2 2 ILE F 102  CYS F 105 -1  O  ILE F 102   N  GLN F  92           
SHEET    1 AC3 2 HIS F 110  CYS F 111  0                                        
SHEET    2 AC3 2 CYS F 119  VAL F 120 -1  O  VAL F 120   N  HIS F 110           
SHEET    1 AC4 2 GLY F 130  VAL F 131  0                                        
SHEET    2 AC4 2 CYS F 143  GLU F 144 -1  O  GLU F 144   N  GLY F 130           
SHEET    1 AC5 2 PHE F 150  PHE F 151  0                                        
SHEET    2 AC5 2 HIS F 162  PRO F 163 -1  O  HIS F 162   N  PHE F 151           
SHEET    1 AC6 4 GLN G   3  SER G   7  0                                        
SHEET    2 AC6 4 LEU G  18  SER G  25 -1  O  SER G  25   N  GLN G   3           
SHEET    3 AC6 4 THR G  77  MET G  82 -1  O  MET G  82   N  LEU G  18           
SHEET    4 AC6 4 PHE G  67  ASP G  72 -1  N  SER G  70   O  TYR G  79           
SHEET    1 AC7 6 LEU G  11  VAL G  12  0                                        
SHEET    2 AC7 6 THR G 107  VAL G 111  1  O  THR G 110   N  VAL G  12           
SHEET    3 AC7 6 ALA G  88  LYS G  94 -1  N  ALA G  88   O  VAL G 109           
SHEET    4 AC7 6 MET G  34  GLN G  39 -1  N  VAL G  37   O  TYR G  91           
SHEET    5 AC7 6 LEU G  45  ILE G  51 -1  O  GLU G  46   N  ARG G  38           
SHEET    6 AC7 6 THR G  57  TYR G  59 -1  O  TYR G  58   N  ALA G  50           
SSBOND   1 CYS A   26    CYS A   37                          1555   1555  2.04  
SSBOND   2 CYS A   38    CYS A   51                          1555   1555  2.04  
SSBOND   3 CYS A   41    CYS A   59                          1555   1555  2.04  
SSBOND   4 CYS A   62    CYS A   77                          1555   1555  2.03  
SSBOND   5 CYS A   83    CYS A  103                          1555   1555  2.04  
SSBOND   6 CYS A  105    CYS A  119                          1555   1555  2.04  
SSBOND   7 CYS A  111    CYS A  116                          1555   1555  2.05  
SSBOND   8 CYS A  125    CYS A  143                          1555   1555  2.06  
SSBOND   9 CYS A  146    CYS A  161                          1555   1555  2.07  
SSBOND  10 CYS A  167    CYS A  186                          1555   1555  2.04  
SSBOND  11 CYS B   22    CYS B   92                          1555   1555  2.03  
SSBOND  12 CYS D   26    CYS D   37                          1555   1555  2.04  
SSBOND  13 CYS D   38    CYS D   51                          1555   1555  2.03  
SSBOND  14 CYS D   41    CYS D   59                          1555   1555  2.03  
SSBOND  15 CYS D   62    CYS D   77                          1555   1555  2.07  
SSBOND  16 CYS D   83    CYS D  103                          1555   1555  2.04  
SSBOND  17 CYS D  105    CYS D  119                          1555   1555  2.06  
SSBOND  18 CYS D  111    CYS D  116                          1555   1555  2.05  
SSBOND  19 CYS D  125    CYS D  143                          1555   1555  2.05  
SSBOND  20 CYS D  146    CYS D  161                          1555   1555  2.04  
SSBOND  21 CYS D  167    CYS D  186                          1555   1555  2.05  
SSBOND  22 CYS E   22    CYS E   92                          1555   1555  2.04  
SSBOND  23 CYS F   26    CYS F   37                          1555   1555  2.04  
SSBOND  24 CYS F   38    CYS F   51                          1555   1555  2.04  
SSBOND  25 CYS F   41    CYS F   59                          1555   1555  2.04  
SSBOND  26 CYS F   62    CYS F   77                          1555   1555  2.05  
SSBOND  27 CYS F   83    CYS F  103                          1555   1555  2.03  
SSBOND  28 CYS F  105    CYS F  119                          1555   1555  2.05  
SSBOND  29 CYS F  111    CYS F  116                          1555   1555  2.05  
SSBOND  30 CYS F  125    CYS F  143                          1555   1555  2.04  
SSBOND  31 CYS F  146    CYS F  161                          1555   1555  2.04  
SSBOND  32 CYS F  167    CYS F  186                          1555   1555  2.03  
SSBOND  33 CYS G   22    CYS G   92                          1555   1555  2.04  
LINK         O   CYS A 125                 K     K A 301     1555   1555  2.86  
LINK         O   SER A 126                 K     K A 301     1555   1555  3.18  
LINK         O   PHE A 129                 K     K A 301     1555   1555  2.53  
LINK         OG  SER A 152                 K     K A 301     1555   1555  2.57  
LINK         O   ASP A 153                 K     K A 301     1555   1555  3.46  
LINK         O   VAL A 154                 K     K A 301     1555   1555  2.71  
LINK         O   CYS D 125                 K     K D 301     1555   1555  2.62  
LINK         O   SER D 126                 K     K D 301     1555   1555  3.07  
LINK         O   PHE D 129                 K     K D 301     1555   1555  2.37  
LINK         O   VAL D 154                 K     K D 301     1555   1555  2.66  
LINK         O   CYS F 125                 K     K F 301     1555   1555  2.81  
LINK         O   SER F 126                 K     K F 301     1555   1555  2.96  
LINK         O   PHE F 129                 K     K F 301     1555   1555  2.40  
LINK         OG  SER F 152                 K     K F 301     1555   1555  2.70  
LINK         O   VAL F 154                 K     K F 301     1555   1555  2.67  
LINK         K     K A 301                 O   HOH A 401     1555   1555  2.75  
LINK         K     K D 301                 O   HOH D 403     1555   1555  2.45  
CISPEP   1 GLU A  107    GLY A  108          0         4.54                     
CISPEP   2 LEU B   95    PRO B   96          0         8.62                     
CISPEP   3 ASN D   34    SER D   35          0       -17.38                     
CISPEP   4 ALA D  115    CYS D  116          0         4.13                     
CISPEP   5 GLY D  128    PHE D  129          0        -2.67                     
CISPEP   6 GLU D  159    LYS D  160          0         5.68                     
CISPEP   7 LEU E   95    PRO E   96          0         6.80                     
CISPEP   8 ALA F  115    CYS F  116          0        -7.58                     
CISPEP   9 GLY F  128    PHE F  129          0        -6.68                     
CISPEP  10 THR F  136    GLY F  137          0         0.35                     
CISPEP  11 LEU G   95    PRO G   96          0         5.91                     
SITE     1 AC1  7 CYS A 125  SER A 126  PHE A 129  SER A 152                    
SITE     2 AC1  7 ASP A 153  VAL A 154  HOH A 401                               
SITE     1 AC2  6 CYS D 125  SER D 126  PHE D 129  SER D 152                    
SITE     2 AC2  6 VAL D 154  HOH D 403                                          
SITE     1 AC3  5 CYS F 125  SER F 126  PHE F 129  SER F 152                    
SITE     2 AC3  5 VAL F 154                                                     
CRYST1  199.300   48.700  138.800  90.00 118.20  90.00 C 1 2 1      12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.005018  0.000000  0.002690        0.00000                         
SCALE2      0.000000  0.020534  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008175        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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