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Database: PDB
Entry: 5DMI
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HEADER    IMMUNE SYSTEM/SIGNALING PROTEIN         08-SEP-15   5DMI              
TITLE     STRUCTURE OF THE EXTRACELLULAR DOMAIN OF THE CD40 IN COMPLEX WITH     
TITLE    2 CHI220 FAB                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TUMOR NECROSIS FACTOR RECEPTOR SUPERFAMILY MEMBER 5;       
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: EXTRACELLULAR DOMAIN RESIDUES 23-193;                      
COMPND   5 SYNONYM: B-CELL SURFACE ANTIGEN CD40,BP50,CD40L RECEPTOR,CDW40;      
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: CHI220 FAB HEAVY CHAIN;                                    
COMPND   9 CHAIN: H;                                                            
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: CHI220 FAB LIGHT CHAIN;                                    
COMPND  13 CHAIN: L;                                                            
COMPND  14 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CD40, TNFRSF5;                                                 
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: HEK293;                                 
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: MUS MUSCULUS, HOMO SAPIENS;                     
SOURCE  12 ORGANISM_TAXID: 10090, 9606;                                         
SOURCE  13 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  14 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  16 MOL_ID: 3;                                                           
SOURCE  17 ORGANISM_SCIENTIFIC: MUS MUSCULUS, HOMO SAPIENS;                     
SOURCE  18 ORGANISM_TAXID: 10090, 9606;                                         
SOURCE  19 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  20 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 10029                                       
KEYWDS    CELL SURFACE RECEPTOR, ANTIBODY-ANTIGEN COMPLEX, ANTITUMOR, IMMUNE    
KEYWDS   2 SYSTEM-SIGNALING PROTEIN COMPLEX                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.SHERIFF                                                             
REVDAT   3   20-JUL-16 5DMI    1       JRNL                                     
REVDAT   2   08-JUN-16 5DMI    1       JRNL                                     
REVDAT   1   01-JUN-16 5DMI    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.    3.69 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) : 3.69                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.64                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 14605                          
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)  : 0.170                          
REMARK   3   R VALUE            (WORKING SET)  : 0.168                          
REMARK   3   FREE R VALUE                      : 0.207                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.030                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 734                            
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               : 7                        
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 3.69                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.98                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 98.89                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2937                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.1750                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2785                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.1720                   
REMARK   3   BIN FREE R VALUE                        : 0.2283                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.18                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 152                      
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            : 4001                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 10                                      
REMARK   3   SOLVENT ATOMS            : 1                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 11.33                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.89                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -8.90030                                             
REMARK   3    B22 (A**2) : -8.90030                                             
REMARK   3    B33 (A**2) : 17.80050                                             
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) : 0.372               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.397               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
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      : 0.900                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.868                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 4115   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 5615   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1329   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 88     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 604    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 4115   ; 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   : 554    ; 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   : 4626   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.39                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.18                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 25.24                    
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 5DMI 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_1000213438.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-JAN-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 4.6                                
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) : 0.97949                            
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 : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14668                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.690                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 201.150                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 15.90                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.24900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.69                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.89                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 16.30                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.49500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.800                              
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; VL FROM 3D85; VH FROM 2ZPK; CL:CH1 FROM 2O5X            
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 74.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.80                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 80MM SODIYM ACETATE, PH 4.6, 1.6 M       
REMARK 280  AMMONIUM SULFATE, 20% (V/V) GLYCEROL, VAPOR DIFFUSION, HANGING      
REMARK 280  DROP, TEMPERATURE 293K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2                        
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   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-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  0.000000 -1.000000  0.000000      100.57600            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000      100.57600            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       31.90450            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000      100.57600            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000      100.57600            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       31.90450            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000      100.57600            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      100.57600            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       31.90450            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000      100.57600            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      100.57600            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       31.90450            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5010 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23780 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, L                               
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     HIS A   122                                                      
REMARK 465     ARG A   123                                                      
REMARK 465     SER A   124                                                      
REMARK 465     CYS A   125                                                      
REMARK 465     SER A   126                                                      
REMARK 465     PRO A   127                                                      
REMARK 465     GLY A   128                                                      
REMARK 465     PHE A   129                                                      
REMARK 465     GLY A   130                                                      
REMARK 465     VAL A   131                                                      
REMARK 465     LYS A   132                                                      
REMARK 465     GLN A   133                                                      
REMARK 465     ILE A   134                                                      
REMARK 465     ALA A   135                                                      
REMARK 465     THR A   136                                                      
REMARK 465     GLY A   137                                                      
REMARK 465     VAL A   138                                                      
REMARK 465     SER A   139                                                      
REMARK 465     ASP A   140                                                      
REMARK 465     THR A   141                                                      
REMARK 465     ILE A   142                                                      
REMARK 465     CYS A   143                                                      
REMARK 465     GLU A   144                                                      
REMARK 465     PRO A   145                                                      
REMARK 465     CYS A   146                                                      
REMARK 465     PRO A   147                                                      
REMARK 465     VAL A   148                                                      
REMARK 465     GLY A   149                                                      
REMARK 465     PHE A   150                                                      
REMARK 465     PHE A   151                                                      
REMARK 465     SER A   152                                                      
REMARK 465     ASP A   153                                                      
REMARK 465     VAL A   154                                                      
REMARK 465     SER A   155                                                      
REMARK 465     SER A   156                                                      
REMARK 465     ALA A   157                                                      
REMARK 465     PHE A   158                                                      
REMARK 465     GLU A   159                                                      
REMARK 465     LYS A   160                                                      
REMARK 465     CYS A   161                                                      
REMARK 465     HIS A   162                                                      
REMARK 465     PRO A   163                                                      
REMARK 465     TRP A   164                                                      
REMARK 465     THR A   165                                                      
REMARK 465     SER A   166                                                      
REMARK 465     CYS A   167                                                      
REMARK 465     GLU A   168                                                      
REMARK 465     THR A   169                                                      
REMARK 465     LYS A   170                                                      
REMARK 465     ASP A   171                                                      
REMARK 465     LEU A   172                                                      
REMARK 465     VAL A   173                                                      
REMARK 465     VAL A   174                                                      
REMARK 465     GLN A   175                                                      
REMARK 465     GLN A   176                                                      
REMARK 465     ALA A   177                                                      
REMARK 465     GLY A   178                                                      
REMARK 465     THR A   179                                                      
REMARK 465     ASP A   180                                                      
REMARK 465     LYS A   181                                                      
REMARK 465     THR A   182                                                      
REMARK 465     ASP A   183                                                      
REMARK 465     VAL A   184                                                      
REMARK 465     VAL A   185                                                      
REMARK 465     CYS A   186                                                      
REMARK 465     GLY A   187                                                      
REMARK 465     PRO A   188                                                      
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 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     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  56    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  58    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  64    CG   CD   OE1  OE2                                  
REMARK 470     GLN A  79    CG   CD   OE1  NE2                                  
REMARK 470     ARG A  90    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  94    CG   CD   CE   NZ                                   
REMARK 470     ILE A 102    CG1  CG2  CD1                                       
REMARK 470     THR A 104    OG1  CG2                                            
REMARK 470     HIS A 110    CG   ND1  CD2  CE1  NE2                             
REMARK 470     THR A 112    OG1  CG2                                            
REMARK 470     SER A 113    OG                                                  
REMARK 470     GLU A 114    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 117    CG   CD   OE1  OE2                                  
REMARK 470     SER A 118    OG                                                  
REMARK 470     LYS H  58    CG   CD   CE   NZ                                   
REMARK 470     SER H 127    OG                                                  
REMARK 470     SER H 128    OG                                                  
REMARK 470     LYS H 129    CG   CD   CE   NZ                                   
REMARK 470     SER H 130    OG                                                  
REMARK 470     LYS H 222    CG   CD   CE   NZ                                   
REMARK 470     VAL H 225    CG1  CG2                                            
REMARK 470     LYS H 228    CG   CD   CE   NZ                                   
REMARK 470     HIS L  41    CG   ND1  CD2  CE1  NE2                             
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    LEU A  32   N   -  CA  -  C   ANGL. DEV. = -20.0 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     -130.39     76.60                                   
REMARK 500    CYS A  26      103.60    101.57                                   
REMARK 500    GLN A  30      -47.94   -150.81                                   
REMARK 500    TYR A  31      107.15    -33.01                                   
REMARK 500    LEU A  32      116.43   -160.96                                   
REMARK 500    ASN A  34       83.86   -158.61                                   
REMARK 500    SER A  35      -37.04     86.87                                   
REMARK 500    PHE A  54       46.43   -140.74                                   
REMARK 500    GLU A  58      -84.62    -78.42                                   
REMARK 500    CYS A  59      125.01     62.88                                   
REMARK 500    SER A  65       -6.98     86.67                                   
REMARK 500    TYR A  82      -75.79     88.74                                   
REMARK 500    CYS A  83       73.70     81.75                                   
REMARK 500    GLU A 107       32.46    -74.39                                   
REMARK 500    GLU A 114       62.70     -3.30                                   
REMARK 500    ALA A 115       99.44     62.83                                   
REMARK 500    CYS A 116       71.89    169.45                                   
REMARK 500    LYS H  43     -176.26    -41.53                                   
REMARK 500    SER H  95      146.10     97.17                                   
REMARK 500    ASN H  99       61.34   -106.02                                   
REMARK 500    ASP H 100A     -83.14    -52.94                                   
REMARK 500    LEU H 100B      99.07     44.66                                   
REMARK 500    SER H 128      -47.78     71.75                                   
REMARK 500    SER H 132      -77.45    -79.49                                   
REMARK 500    ASP H 146       85.50     35.43                                   
REMARK 500    THR H 167      -56.40   -121.24                                   
REMARK 500    SER H 181       -9.83    -54.59                                   
REMARK 500    ASN H 216       56.05     38.66                                   
REMARK 500    VAL H 225      -94.61     51.75                                   
REMARK 500    GLU H 226      131.06     66.69                                   
REMARK 500    SER L  30     -109.87     52.48                                   
REMARK 500    ALA L  51      -45.43     64.05                                   
REMARK 500    VAL L  78      122.20    -22.30                                   
REMARK 500    ASP L  82       15.80    -67.42                                   
REMARK 500    HIS L  92       73.47    -65.01                                   
REMARK 500    SER L  93      138.77    102.92                                   
REMARK 500    THR L 102       89.49     41.54                                   
REMARK 500    ASN L 138       92.47     41.94                                   
REMARK 500    ASN L 152       17.40     53.02                                   
REMARK 500    ASN L 158       25.58   -154.69                                   
REMARK 500    LYS L 169      -64.95   -104.30                                   
REMARK 500    SER L 171       21.71     43.32                                   
REMARK 500    LYS L 190      -42.25   -137.77                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 L 301                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5DMJ   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  5DMI A   23   193  UNP    P25942   TNR5_HUMAN      23    193             
DBREF  5DMI H    1   228  PDB    5DMI     5DMI             1    228             
DBREF  5DMI L    1   213  PDB    5DMI     5DMI             1    213             
SEQADV 5DMI ASP A  153  UNP  P25942    ASN   153 SEE REMARK 999                 
SEQADV 5DMI ASP A  180  UNP  P25942    ASN   180 SEE REMARK 999                 
SEQADV 5DMI ASP A  194  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMI PRO A  195  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMI GLY A  196  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMI GLY A  197  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMI GLY A  198  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMI GLY A  199  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMI GLY A  200  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMI ARG A  201  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMI LEU A  202  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMI VAL A  203  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMI PRO A  204  UNP  P25942              EXPRESSION TAG                 
SEQADV 5DMI ARG A  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 H  223  GLN ILE GLN LEU VAL GLN SER GLY PRO GLU LEU LYS LYS          
SEQRES   2 H  223  PRO GLY GLU THR VAL ARG ILE SER CYS LYS ALA SER GLY          
SEQRES   3 H  223  TYR ALA PHE THR THR THR GLY MET GLN TRP VAL GLN GLU          
SEQRES   4 H  223  MET PRO GLY LYS GLY LEU LYS TRP ILE GLY TRP ILE ASN          
SEQRES   5 H  223  THR HIS SER GLY VAL PRO LYS TYR VAL GLU ASP PHE LYS          
SEQRES   6 H  223  GLY ARG PHE ALA PHE SER LEU GLU THR SER ALA ASN THR          
SEQRES   7 H  223  ALA TYR LEU GLN ILE SER ASN LEU LYS ASN GLU ASP THR          
SEQRES   8 H  223  ALA THR TYR PHE CYS VAL ARG SER GLY ASN GLY ASN TYR          
SEQRES   9 H  223  ASP LEU ALA TYR PHE ALA TYR TRP GLY GLN GLY THR LEU          
SEQRES  10 H  223  VAL THR VAL SER ALA ALA SER THR LYS GLY PRO SER VAL          
SEQRES  11 H  223  PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY          
SEQRES  12 H  223  THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO          
SEQRES  13 H  223  GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR          
SEQRES  14 H  223  SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER          
SEQRES  15 H  223  GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER          
SEQRES  16 H  223  SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN          
SEQRES  17 H  223  HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU          
SEQRES  18 H  223  PRO LYS                                                      
SEQRES   1 L  213  ASP ILE VAL LEU THR GLN SER PRO ALA THR LEU SER VAL          
SEQRES   2 L  213  THR PRO GLY ASP ARG VAL SER LEU SER CYS ARG ALA SER          
SEQRES   3 L  213  GLN SER ILE SER ASP TYR LEU HIS TRP TYR GLN GLN LYS          
SEQRES   4 L  213  SER HIS GLU SER PRO ARG LEU LEU ILE LYS TYR ALA SER          
SEQRES   5 L  213  HIS SER ILE SER GLY ILE PRO SER ARG PHE SER GLY SER          
SEQRES   6 L  213  GLY SER GLY SER ASP PHE THR LEU SER ILE ASN SER VAL          
SEQRES   7 L  213  GLU PRO GLU ASP VAL GLY ILE TYR TYR CYS GLN HIS GLY          
SEQRES   8 L  213  HIS SER PHE PRO TRP THR PHE GLY GLY GLY THR LYS LEU          
SEQRES   9 L  213  GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE          
SEQRES  10 L  213  PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA          
SEQRES  11 L  213  SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU          
SEQRES  12 L  213  ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER          
SEQRES  13 L  213  GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS          
SEQRES  14 L  213  ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER          
SEQRES  15 L  213  LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU          
SEQRES  16 L  213  VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER          
SEQRES  17 L  213  PHE ASN ARG GLY GLU                                          
HET    SO4  H 301       5                                                       
HET    SO4  L 301       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   4  SO4    2(O4 S 2-)                                                   
FORMUL   6  HOH   *(H2 O)                                                       
HELIX    1 AA1 ASP A   84  GLY A   88  5                                   5    
HELIX    2 AA2 THR H   73  ALA H   75  5                                   3    
HELIX    3 AA3 LYS H   83  THR H   87  5                                   5    
HELIX    4 AA4 SER H  196  GLN H  204  1                                   6    
HELIX    5 AA5 LYS H  213  ASN H  216  5                                   4    
HELIX    6 AA6 SER L  121  GLY L  128  1                                   8    
HELIX    7 AA7 LYS L  183  HIS L  189  1                                   7    
SHEET    1 AA1 2 GLN A  45  LYS A  46  0                                        
SHEET    2 AA1 2 LEU A  60  PRO A  61 -1  O  LEU A  60   N  LYS A  46           
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 HIS A 110  CYS A 111  0                                        
SHEET    2 AA3 2 CYS A 119  VAL A 120 -1  O  VAL A 120   N  HIS A 110           
SHEET    1 AA4 4 GLN H   3  GLN H   6  0                                        
SHEET    2 AA4 4 VAL H  18  SER H  25 -1  O  LYS H  23   N  VAL H   5           
SHEET    3 AA4 4 THR H  77  ILE H  82 -1  O  LEU H  80   N  ILE H  20           
SHEET    4 AA4 4 PHE H  67  GLU H  72 -1  N  SER H  70   O  TYR H  79           
SHEET    1 AA5 6 GLU H  10  LYS H  12  0                                        
SHEET    2 AA5 6 THR H 107  VAL H 111  1  O  THR H 110   N  LYS H  12           
SHEET    3 AA5 6 ALA H  88  ARG H  94 -1  N  ALA H  88   O  VAL H 109           
SHEET    4 AA5 6 MET H  34  GLU H  39 -1  N  VAL H  37   O  PHE H  91           
SHEET    5 AA5 6 LEU H  45  ILE H  51 -1  O  ILE H  51   N  MET H  34           
SHEET    6 AA5 6 PRO H  57  TYR H  59 -1  O  LYS H  58   N  TRP H  50           
SHEET    1 AA6 4 GLU H  10  LYS H  12  0                                        
SHEET    2 AA6 4 THR H 107  VAL H 111  1  O  THR H 110   N  LYS H  12           
SHEET    3 AA6 4 ALA H  88  ARG H  94 -1  N  ALA H  88   O  VAL H 109           
SHEET    4 AA6 4 TYR H 102  TRP H 103 -1  O  TYR H 102   N  ARG H  94           
SHEET    1 AA7 4 SER H 120  LEU H 124  0                                        
SHEET    2 AA7 4 THR H 137  TYR H 147 -1  O  LEU H 143   N  PHE H 122           
SHEET    3 AA7 4 TYR H 185  PRO H 194 -1  O  LEU H 187   N  VAL H 144           
SHEET    4 AA7 4 VAL H 171  THR H 173 -1  N  HIS H 172   O  VAL H 190           
SHEET    1 AA8 4 SER H 120  LEU H 124  0                                        
SHEET    2 AA8 4 THR H 137  TYR H 147 -1  O  LEU H 143   N  PHE H 122           
SHEET    3 AA8 4 TYR H 185  PRO H 194 -1  O  LEU H 187   N  VAL H 144           
SHEET    4 AA8 4 VAL H 177  LEU H 178 -1  N  VAL H 177   O  SER H 186           
SHEET    1 AA9 3 THR H 153  TRP H 157  0                                        
SHEET    2 AA9 3 CYS H 208  HIS H 212 -1  O  ASN H 209   N  SER H 156           
SHEET    3 AA9 3 THR H 217  LYS H 221 -1  O  VAL H 219   N  VAL H 210           
SHEET    1 AB1 4 LEU L   4  THR L   5  0                                        
SHEET    2 AB1 4 VAL L  19  ALA L  25 -1  O  ARG L  24   N  THR L   5           
SHEET    3 AB1 4 ASP L  70  ILE L  75 -1  O  PHE L  71   N  CYS L  23           
SHEET    4 AB1 4 PHE L  62  SER L  67 -1  N  SER L  63   O  SER L  74           
SHEET    1 AB2 6 THR L  10  VAL L  13  0                                        
SHEET    2 AB2 6 LYS L 103  ILE L 106  1  O  GLU L 105   N  VAL L  13           
SHEET    3 AB2 6 GLY L  84  HIS L  90 -1  N  GLY L  84   O  LEU L 104           
SHEET    4 AB2 6 LEU L  33  GLN L  38 -1  N  GLN L  38   O  ILE L  85           
SHEET    5 AB2 6 ARG L  45  LYS L  49 -1  O  LEU L  47   N  TRP L  35           
SHEET    6 AB2 6 HIS L  53  SER L  54 -1  O  HIS L  53   N  LYS L  49           
SHEET    1 AB3 4 SER L 114  PHE L 118  0                                        
SHEET    2 AB3 4 THR L 129  PHE L 139 -1  O  VAL L 133   N  PHE L 118           
SHEET    3 AB3 4 TYR L 173  SER L 182 -1  O  LEU L 179   N  VAL L 132           
SHEET    4 AB3 4 SER L 159  VAL L 163 -1  N  SER L 162   O  SER L 176           
SHEET    1 AB4 4 ALA L 153  GLN L 155  0                                        
SHEET    2 AB4 4 LYS L 145  VAL L 150 -1  N  VAL L 150   O  ALA L 153           
SHEET    3 AB4 4 VAL L 191  THR L 197 -1  O  GLU L 195   N  GLN L 147           
SHEET    4 AB4 4 VAL L 205  ASN L 210 -1  O  VAL L 205   N  VAL L 196           
SSBOND   1 CYS A   26    CYS A   37                          1555   1555  2.06  
SSBOND   2 CYS A   38    CYS A   51                          1555   1555  2.03  
SSBOND   3 CYS A   41    CYS A   59                          1555   1555  2.04  
SSBOND   4 CYS A   62    CYS A   77                          1555   1555  2.07  
SSBOND   5 CYS A   83    CYS A  103                          1555   1555  2.05  
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 H   22    CYS H   92                          1555   1555  2.05  
SSBOND   9 CYS H  142    CYS H  208                          1555   1555  2.04  
SSBOND  10 CYS L   23    CYS L   88                          1555   1555  2.05  
SSBOND  11 CYS L  134    CYS L  194                          1555   1555  2.05  
CISPEP   1 ALA A  115    CYS A  116          0         2.30                     
CISPEP   2 SER H   95    GLY H   96          0         4.04                     
CISPEP   3 PHE H  148    PRO H  149          0        -3.31                     
CISPEP   4 GLU H  150    PRO H  151          0        13.90                     
CISPEP   5 SER L    7    PRO L    8          0         3.68                     
CISPEP   6 PHE L   94    PRO L   95          0        -2.37                     
CISPEP   7 TYR L  140    PRO L  141          0        -3.16                     
SITE     1 AC1  2 ASP H  62  ARG H  66                                          
SITE     1 AC2  2 HIS L  53  SER L  54                                          
CRYST1  201.152  201.152   63.809  90.00  90.00  90.00 P 42 21 2     8          
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      0.004971  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004971  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015672        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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