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Database: PDB
Entry: 1XDT
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Original site: 1XDT 
HEADER    COMPLEX (TOXIN/GROWTH FACTOR)           18-NOV-97   1XDT              
TITLE     COMPLEX OF DIPHTHERIA TOXIN AND HEPARIN-BINDING EPIDERMAL GROWTH      
TITLE    2 FACTOR                                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIPHTHERIA TOXIN;                                          
COMPND   3 CHAIN: T;                                                            
COMPND   4 SYNONYM: DT;                                                         
COMPND   5 EC: 2.4.2.36;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: HEPARIN-BINDING EPIDERMAL GROWTH FACTOR;                   
COMPND   9 CHAIN: R;                                                            
COMPND  10 FRAGMENT: EXTRACELLULAR DOMAIN;                                      
COMPND  11 SYNONYM: HBEGF;                                                      
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CORYNEBACTERIUM DIPHTHERIAE;                    
SOURCE   3 ORGANISM_TAXID: 1717;                                                
SOURCE   4 VARIANT: LYSOGENIZED BY THE CORYNEPHAGE BETA;                        
SOURCE   5 CELLULAR_LOCATION: EXTRACELLULAR;                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 CELLULAR_LOCATION: MEMBRANE-ANCHORED OR EXTRACELLULARLY-RELEASED;    
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE  17 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE  18 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;                      
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_VECTOR: PET28A                                     
KEYWDS    COMPLEX (TOXIN-GROWTH FACTOR), DIPHTHERIA TOXIN, RECEPTOR, HEPARIN-   
KEYWDS   2 BINDING EPIDERMAL GROWTH FACTOR, EPIDERMAL GROWTH FACTOR, COMPLEX    
KEYWDS   3 (TOXIN-GROWTH FACTOR) COMPLEX                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.V.LOUIE,W.YANG,M.E.BOWMAN,S.CHOE                                    
REVDAT   4   13-JUL-11 1XDT    1       VERSN                                    
REVDAT   3   24-FEB-09 1XDT    1       VERSN                                    
REVDAT   2   01-APR-03 1XDT    1       JRNL                                     
REVDAT   1   25-FEB-98 1XDT    0                                                
JRNL        AUTH   G.V.LOUIE,W.YANG,M.E.BOWMAN,S.CHOE                           
JRNL        TITL   CRYSTAL STRUCTURE OF THE COMPLEX OF DIPHTHERIA TOXIN WITH AN 
JRNL        TITL 2 EXTRACELLULAR FRAGMENT OF ITS RECEPTOR.                      
JRNL        REF    MOL.CELL                      V.   1    67 1997              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   9659904                                                      
JRNL        DOI    10.1016/S1097-2765(00)80008-8                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.851                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 100000.000                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.1000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 88.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 15511                          
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 SET) : 0.172                           
REMARK   3   FREE R VALUE                     : 0.290                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 750                             
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           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.65                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.77                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 80.30                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1627                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2450                       
REMARK   3   BIN FREE R VALUE                    : 0.3670                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.20                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 90                           
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            : 4306                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 48                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.50                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.34                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 3.450 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 5.210 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 5.230 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 7.350 ; 2.500                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : PARAM19.SOL                                    
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : TOPH19.SOL                                     
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1XDT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : OCT-96                             
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NI FILTER                          
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MACSCIENCE                         
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 54532                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.5                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.05200                            
REMARK 200  R SYM                      (I) : 0.05200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 27.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 79.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.15200                            
REMARK 200  R SYM FOR SHELL            (I) : 0.15200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1MDT                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN (15 MG/ML) IN 10 MM TRIS-HCL     
REMARK 280  (PH 7.5), 0.15 M NACL MIXED WITH AN EQUAL VOLUME OF PRECIPITANT     
REMARK 280  CONTAINING 50 MM TRIS-HCL (PH 7.5), 0.15 M NACL, 5% (V/V)           
REMARK 280  GLYCEROL, 22-30% (W/V) POLYETHYLENE GLYCOL 3350; AND EQUILIBRATED   
REMARK 280  BY VAPOR DIFFUSION AGAINST PRECIPITANT, VAPOR DIFFUSION             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       63.85000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       63.85000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       44.70000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       51.85000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       44.70000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       51.85000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       63.85000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       44.70000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       51.85000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       63.85000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       44.70000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       51.85000            
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 300 REMARK: DIPHTHERIA TOXIN MOLECULE HAS THE OPEN CONFORMATION, AND     
REMARK 300 DIMERIZES WITH ANOTHER DIPHTHERIA TOXIN MOLECULE.                    
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 12640 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 43090 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: T, R                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      103.70000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      127.70000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LYS T    39                                                      
REMARK 465     SER T    40                                                      
REMARK 465     GLY T    41                                                      
REMARK 465     THR T    42                                                      
REMARK 465     GLN T    43                                                      
REMARK 465     GLY T    44                                                      
REMARK 465     ASN T   189                                                      
REMARK 465     ARG T   190                                                      
REMARK 465     VAL T   191                                                      
REMARK 465     ARG T   192                                                      
REMARK 465     ARG T   193                                                      
REMARK 465     SER T   194                                                      
REMARK 465     VAL T   195                                                      
REMARK 465     GLY T   196                                                      
REMARK 465     SER T   197                                                      
REMARK 465     SER T   198                                                      
REMARK 465     LEU T   199                                                      
REMARK 465     GLY R    69                                                      
REMARK 465     SER R    70                                                      
REMARK 465     HIS R    71                                                      
REMARK 465     MET R    72                                                      
REMARK 465     ARG R    73                                                      
REMARK 465     VAL R    74                                                      
REMARK 465     THR R    75                                                      
REMARK 465     LEU R    76                                                      
REMARK 465     SER R    77                                                      
REMARK 465     SER R    78                                                      
REMARK 465     LYS R    79                                                      
REMARK 465     PRO R    80                                                      
REMARK 465     GLN R    81                                                      
REMARK 465     ALA R    82                                                      
REMARK 465     LEU R    83                                                      
REMARK 465     ALA R    84                                                      
REMARK 465     THR R    85                                                      
REMARK 465     PRO R    86                                                      
REMARK 465     ASN R    87                                                      
REMARK 465     LYS R    88                                                      
REMARK 465     GLU R    89                                                      
REMARK 465     GLU R    90                                                      
REMARK 465     HIS R    91                                                      
REMARK 465     GLY R    92                                                      
REMARK 465     LYS R    93                                                      
REMARK 465     ARG R    94                                                      
REMARK 465     LYS R    95                                                      
REMARK 465     LYS R    96                                                      
REMARK 465     LYS R    97                                                      
REMARK 465     GLY R    98                                                      
REMARK 465     LYS R    99                                                      
REMARK 465     GLY R   100                                                      
REMARK 465     LEU R   101                                                      
REMARK 465     GLY R   102                                                      
REMARK 465     LYS R   103                                                      
REMARK 465     LYS R   104                                                      
REMARK 465     ARG R   105                                                      
REMARK 465     ASP R   106                                                      
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 T  70    CD   OE1  OE2                                       
REMARK 470     LYS R 113    CG   CD   CE   NZ                                   
REMARK 470     ARG R 128    NH1  NH2                                            
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ALA T  379   O                                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ARG R 128   NE    ARG R 128   CZ      0.169                       
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    ARG R 128   CD  -  NE  -  CZ  ANGL. DEV. = -12.7 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    CYS T 201       93.66   -160.77                                   
REMARK 500    ASN T 235       -3.21     53.42                                   
REMARK 500    THR T 269      -62.16    -91.57                                   
REMARK 500    ALA T 317      148.81   -175.01                                   
REMARK 500    VAL T 347        0.19   -163.14                                   
REMARK 500    GLU T 349       54.98   -172.35                                   
REMARK 500    LEU T 350     -158.89   -152.70                                   
REMARK 500    ASP T 352      -44.59     12.07                                   
REMARK 500    ILE T 353      -39.02   -133.50                                   
REMARK 500    TYR T 358      -95.73    -95.79                                   
REMARK 500    LYS T 385     -128.96     41.93                                   
REMARK 500    ASP T 392       25.39     45.81                                   
REMARK 500    ASN T 424      -93.77   -152.43                                   
REMARK 500    HIS T 520       -4.04     75.83                                   
REMARK 500    ARG R 110      -96.05    -77.57                                   
REMARK 500    TYR R 112       39.47    -89.82                                   
REMARK 500    ASP R 114       -1.14     67.04                                   
REMARK 500    ILE R 117      -82.78    -85.55                                   
REMARK 500    HIS R 118       48.82    -95.85                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ASN T 235        24.0      L          L   OUTSIDE RANGE           
REMARK 500    ASP T 352        22.8      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1XDT T    1   535  UNP    P00588   DTX_CORBE       33    567             
DBREF  1XDT R   73   147  UNP    Q99075   HBEGF_HUMAN     73    147             
SEQRES   1 T  535  GLY ALA ASP ASP VAL VAL ASP SER SER LYS SER PHE VAL          
SEQRES   2 T  535  MET GLU ASN PHE SER SER TYR HIS GLY THR LYS PRO GLY          
SEQRES   3 T  535  TYR VAL ASP SER ILE GLN LYS GLY ILE GLN LYS PRO LYS          
SEQRES   4 T  535  SER GLY THR GLN GLY ASN TYR ASP ASP ASP TRP LYS GLY          
SEQRES   5 T  535  PHE TYR SER THR ASP ASN LYS TYR ASP ALA ALA GLY TYR          
SEQRES   6 T  535  SER VAL ASP ASN GLU ASN PRO LEU SER GLY LYS ALA GLY          
SEQRES   7 T  535  GLY VAL VAL LYS VAL THR TYR PRO GLY LEU THR LYS VAL          
SEQRES   8 T  535  LEU ALA LEU LYS VAL ASP ASN ALA GLU THR ILE LYS LYS          
SEQRES   9 T  535  GLU LEU GLY LEU SER LEU THR GLU PRO LEU MET GLU GLN          
SEQRES  10 T  535  VAL GLY THR GLU GLU PHE ILE LYS ARG PHE GLY ASP GLY          
SEQRES  11 T  535  ALA SER ARG VAL VAL LEU SER LEU PRO PHE ALA GLU GLY          
SEQRES  12 T  535  SER SER SER VAL GLU TYR ILE ASN ASN TRP GLU GLN ALA          
SEQRES  13 T  535  LYS ALA LEU SER VAL GLU LEU GLU ILE ASN PHE GLU THR          
SEQRES  14 T  535  ARG GLY LYS ARG GLY GLN ASP ALA MET TYR GLU TYR MET          
SEQRES  15 T  535  ALA GLN ALA CYS ALA GLY ASN ARG VAL ARG ARG SER VAL          
SEQRES  16 T  535  GLY SER SER LEU SER CYS ILE ASN LEU ASP TRP ASP VAL          
SEQRES  17 T  535  ILE ARG ASP LYS THR LYS THR LYS ILE GLU SER LEU LYS          
SEQRES  18 T  535  GLU HIS GLY PRO ILE LYS ASN LYS MET SER GLU SER PRO          
SEQRES  19 T  535  ASN LYS THR VAL SER GLU GLU LYS ALA LYS GLN TYR LEU          
SEQRES  20 T  535  GLU GLU PHE HIS GLN THR ALA LEU GLU HIS PRO GLU LEU          
SEQRES  21 T  535  SER GLU LEU LYS THR VAL THR GLY THR ASN PRO VAL PHE          
SEQRES  22 T  535  ALA GLY ALA ASN TYR ALA ALA TRP ALA VAL ASN VAL ALA          
SEQRES  23 T  535  GLN VAL ILE ASP SER GLU THR ALA ASP ASN LEU GLU LYS          
SEQRES  24 T  535  THR THR ALA ALA LEU SER ILE LEU PRO GLY ILE GLY SER          
SEQRES  25 T  535  VAL MET GLY ILE ALA ASP GLY ALA VAL HIS HIS ASN THR          
SEQRES  26 T  535  GLU GLU ILE VAL ALA GLN SER ILE ALA LEU SER SER LEU          
SEQRES  27 T  535  MET VAL ALA GLN ALA ILE PRO LEU VAL GLY GLU LEU VAL          
SEQRES  28 T  535  ASP ILE GLY PHE ALA ALA TYR ASN PHE VAL GLU SER ILE          
SEQRES  29 T  535  ILE ASN LEU PHE GLN VAL VAL HIS ASN SER TYR ASN ARG          
SEQRES  30 T  535  PRO ALA TYR SER PRO GLY HIS LYS THR GLN PRO PHE LEU          
SEQRES  31 T  535  HIS ASP GLY TYR ALA VAL SER TRP ASN THR VAL GLU ASP          
SEQRES  32 T  535  SER ILE ILE ARG THR GLY PHE GLN GLY GLU SER GLY HIS          
SEQRES  33 T  535  ASP ILE LYS ILE THR ALA GLU ASN THR PRO LEU PRO ILE          
SEQRES  34 T  535  ALA GLY VAL LEU LEU PRO THR ILE PRO GLY LYS LEU ASP          
SEQRES  35 T  535  VAL ASN LYS SER LYS THR HIS ILE SER VAL ASN GLY ARG          
SEQRES  36 T  535  LYS ILE ARG MET ARG CYS ARG ALA ILE ASP GLY ASP VAL          
SEQRES  37 T  535  THR PHE CYS ARG PRO LYS SER PRO VAL TYR VAL GLY ASN          
SEQRES  38 T  535  GLY VAL HIS ALA ASN LEU HIS VAL ALA PHE HIS ARG SER          
SEQRES  39 T  535  SER SER GLU LYS ILE HIS SER ASN GLU ILE SER SER ASP          
SEQRES  40 T  535  SER ILE GLY VAL LEU GLY TYR GLN LYS THR VAL ASP HIS          
SEQRES  41 T  535  THR LYS VAL ASN SER LYS LEU SER LEU PHE PHE GLU ILE          
SEQRES  42 T  535  LYS SER                                                      
SEQRES   1 R   79  GLY SER HIS MET ARG VAL THR LEU SER SER LYS PRO GLN          
SEQRES   2 R   79  ALA LEU ALA THR PRO ASN LYS GLU GLU HIS GLY LYS ARG          
SEQRES   3 R   79  LYS LYS LYS GLY LYS GLY LEU GLY LYS LYS ARG ASP PRO          
SEQRES   4 R   79  CYS LEU ARG LYS TYR LYS ASP PHE CYS ILE HIS GLY GLU          
SEQRES   5 R   79  CYS LYS TYR VAL LYS GLU LEU ARG ALA PRO SER CYS ILE          
SEQRES   6 R   79  CYS HIS PRO GLY TYR HIS GLY GLU ARG CYS HIS GLY LEU          
SEQRES   7 R   79  SER                                                          
FORMUL   3  HOH   *48(H2 O)                                                     
HELIX    1   3 VAL T   28  LYS T   33  1                                   6    
HELIX    2   5 LYS T   59  SER T   66  1                                   8    
HELIX    3   6 ALA T   99  GLU T  105  1                                   7    
HELIX    4   7 LEU T  114  GLN T  117  1                                   4    
HELIX    5   8 GLU T  121  ARG T  126  1                                   6    
HELIX    6   9 GLN T  155  ALA T  158  5                                   4    
HELIX    7  11 ASP T  176  ALA T  185  1                                  10    
HELIX    8  12 TRP T  206  LYS T  221  1                                  16    
HELIX    9  13 GLY T  224  GLU T  232  1                                   9    
HELIX   10  14 GLU T  240  GLU T  256  1                                  17    
HELIX   11  15 PRO T  258  THR T  267  5                                  10    
HELIX   12  17 GLY T  275  VAL T  288  1                                  14    
HELIX   13  18 SER T  291  ASP T  295  1                                   5    
HELIX   14  19 LEU T  297  ILE T  306  1                                  10    
HELIX   15  20 ILE T  310  MET T  314  1                                   5    
HELIX   16  21 GLU T  326  VAL T  347  1                                  22    
HELIX   17  22 GLY T  354  ALA T  357  1                                   4    
HELIX   18  23 ASN T  359  ASN T  376  1                                  18    
HELIX   19  24 VAL T  401  SER T  404  5                                   4    
HELIX   20  26 LYS R  125  LEU R  127  5                                   3    
SHEET    1   A 5 PHE T  12  GLU T  15  0                                        
SHEET    2   A 5 LEU T  88  ALA T  93 -1  N  VAL T  91   O  PHE T  12           
SHEET    3   A 5 ARG T 133  PRO T 139  1  N  ARG T 133   O  LYS T  90           
SHEET    4   A 5 VAL T 147  ASN T 151 -1  N  ILE T 150   O  LEU T 136           
SHEET    5   A 5 PHE T  53  THR T  56 -1  N  SER T  55   O  TYR T 149           
SHEET    1   B 3 SER T  18  THR T  23  0                                        
SHEET    2   B 3 GLY T  79  TYR T  85 -1  N  VAL T  83   O  SER T  19           
SHEET    3   B 3 LEU T 159  ASN T 166 -1  N  ILE T 165   O  VAL T  80           
SHEET    1   C 6 PHE T 389  HIS T 391  0                                        
SHEET    2   C 6 TYR T 394  TRP T 398 -1  N  VAL T 396   O  PHE T 389           
SHEET    3   C 6 GLY T 412  ALA T 422 -1  N  THR T 421   O  ALA T 395           
SHEET    4   C 6 ALA T 485  ARG T 493 -1  N  ARG T 493   O  GLY T 412           
SHEET    5   C 6 HIS T 449  VAL T 452 -1  N  SER T 451   O  ASN T 486           
SHEET    6   C 6 ARG T 455  ARG T 458 -1  N  ILE T 457   O  ILE T 450           
SHEET    1   D 2 ILE T 405  ARG T 407  0                                        
SHEET    2   D 2 GLU T 532  LYS T 534  1  N  GLU T 532   O  ILE T 406           
SHEET    1   E 5 MET T 459  ALA T 463  0                                        
SHEET    2   E 5 VAL T 468  PRO T 473 -1  N  ARG T 472   O  ARG T 460           
SHEET    3   E 5 GLY T 431  PRO T 435 -1  N  LEU T 434   O  THR T 469           
SHEET    4   E 5 SER T 508  LEU T 512 -1  N  LEU T 512   O  GLY T 431           
SHEET    5   E 5 LYS T 526  PHE T 530 -1  N  LEU T 529   O  ILE T 509           
SHEET    1   F 2 GLN T 515  VAL T 518  0                                        
SHEET    2   F 2 THR T 521  ASN T 524 -1  N  VAL T 523   O  LYS T 516           
SHEET    1   G 2 GLY R 119  CYS R 121  0                                        
SHEET    2   G 2 CYS R 132  CYS R 134 -1  N  ILE R 133   O  GLU R 120           
SSBOND   1 CYS T  186    CYS T  201                          1555   1555  2.04  
SSBOND   2 CYS T  461    CYS T  471                          1555   1555  2.04  
SSBOND   3 CYS R  108    CYS R  121                          1555   1555  2.03  
SSBOND   4 CYS R  116    CYS R  132                          1555   1555  2.04  
SSBOND   5 CYS R  134    CYS R  143                          1555   1555  2.03  
CRYST1   89.400  103.700  127.700  90.00  90.00  90.00 C 2 2 21      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      0.011186  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009643  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007831        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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