GenomeNet

Database: PDB
Entry: 1XTC
LinkDB: 1XTC
Original site: 1XTC 
HEADER    TOXIN                                   10-JAN-96   1XTC              
TITLE     CHOLERA TOXIN                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHOLERA TOXIN;                                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CTX, CHOLERAGEN;                                            
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: CHOLERA TOXIN;                                             
COMPND   7 CHAIN: C;                                                            
COMPND   8 SYNONYM: CTX, CHOLERAGEN;                                            
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: CHOLERA TOXIN;                                             
COMPND  11 CHAIN: D, E, F, G, H;                                                
COMPND  12 SYNONYM: CTX, CHOLERAGEN                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE;                                
SOURCE   3 ORGANISM_TAXID: 44104;                                               
SOURCE   4 STRAIN: 569B;                                                        
SOURCE   5 OTHER_DETAILS: COMMERCIALLY OBTAINED FROM LIST BIOLOGICAL            
SOURCE   6 LABORATORY, CAMPBER CA95008;                                         
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE;                                
SOURCE   9 ORGANISM_TAXID: 44104;                                               
SOURCE  10 STRAIN: 569B;                                                        
SOURCE  11 OTHER_DETAILS: COMMERCIALLY OBTAINED FROM LIST BIOLOGICAL            
SOURCE  12 LABORATORY, CAMPBER CA95008;                                         
SOURCE  13 MOL_ID: 3;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE;                                
SOURCE  15 ORGANISM_TAXID: 44104;                                               
SOURCE  16 STRAIN: 569B;                                                        
SOURCE  17 OTHER_DETAILS: COMMERCIALLY OBTAINED FROM LIST BIOLOGICAL            
SOURCE  18 LABORATORY, CAMPBER CA95008                                          
KEYWDS    ENTEROTOXIN, TOXIN                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.-G.ZHANG,E.WESTBROOK                                                
REVDAT   3   13-JUL-11 1XTC    1       VERSN                                    
REVDAT   2   24-FEB-09 1XTC    1       VERSN                                    
REVDAT   1   01-AUG-96 1XTC    0                                                
JRNL        AUTH   R.G.ZHANG,D.L.SCOTT,M.L.WESTBROOK,S.NANCE,B.D.SPANGLER,      
JRNL        AUTH 2 G.G.SHIPLEY,E.M.WESTBROOK                                    
JRNL        TITL   THE THREE-DIMENSIONAL CRYSTAL STRUCTURE OF CHOLERA TOXIN.    
JRNL        REF    J.MOL.BIOL.                   V. 251   563 1995              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   7658473                                                      
JRNL        DOI    10.1006/JMBI.1995.0456                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   R.G.ZHANG,M.L.WESTBROOK,E.M.WESTBROOK,D.L.SCOTT,             
REMARK   1  AUTH 2 Z.OTWINOWSKI,P.R.MAULIK,R.A.REED,G.G.SHIPLEY                 
REMARK   1  TITL   THE 2.4 A CRYSTAL STRUCTURE OF CHOLERA TOXIN B SUBUNIT       
REMARK   1  TITL 2 PENTAMER: CHOLERAGENOID                                      
REMARK   1  REF    J.MOL.BIOL.                   V. 251   550 1995              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PROFFT, X-PLOR                                       
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON,FINZEL,BRUNGER                   
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.500                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 26200                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.185                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5997                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 138                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.37                          
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  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.015 ; 0.020               
REMARK   3    ANGLE DISTANCE                  (A) : 0.032 ; 0.040               
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.045 ; 0.060               
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND               (A**2) : NULL  ; NULL                
REMARK   3   MAIN-CHAIN ANGLE              (A**2) : NULL  ; NULL                
REMARK   3   SIDE-CHAIN BOND               (A**2) : NULL  ; NULL                
REMARK   3   SIDE-CHAIN ANGLE              (A**2) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1XTC 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        : 15-AUG-89                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
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                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : SIEMENS-NICOLET X100               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XENGEN                             
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26200                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.4                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.04800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       46.10000            
REMARK 290   SMTRY3   2  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: HEPTAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEPTAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 19330 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 27960 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -67.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, D, E, F, G, H                   
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 CHOLERA TOXIN CONTAINS 3 KINDS OF CHAINS: AN ALPHA                   
REMARK 400 AND A GAMMA CHAIN (FROM THE SAME PRECURSOR MOLECULE),                
REMARK 400 LINKED BY AN INTERCHAIN DISULFIDE BOND, ASSOCIATED                   
REMARK 400 NONCOVALENTLY WITH AN AGGREGATE OF 4 TO 6 BETA CHAINS.               
REMARK 400 CHAIN A IS THE A1 OR ALPHA CHAIN, CHAIN C IS THE A2 OR               
REMARK 400 GAMMA CHAIN, AND CHAINS D, E, F, G, AND H ARE THE FIVE               
REMARK 400 ASSOCIATED BETA CHAINS.                                              
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     SER A   193                                                      
REMARK 465     SER A   194                                                      
REMARK 465     MET C   195                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   207     O    HOH A   212              0.24            
REMARK 500   O    HOH A   210     O    HOH A   220              0.76            
REMARK 500   O    ILE A    76     N    SER A    78              1.76            
REMARK 500   OG   SER F    30     O    ARG F    35              1.87            
REMARK 500   NH2  ARG C   235     CB   GLU C   239              1.90            
REMARK 500   O    ASP E    22     CA   LYS E    81              1.93            
REMARK 500   NH1  ARG A   143     NH2  ARG A   146              1.95            
REMARK 500   OG   SER C   228     CG1  ILE D    74              1.98            
REMARK 500   NZ   LYS C   217     O    HOH C   106              2.00            
REMARK 500   O    ALA D    32     O    ARG D    35              2.04            
REMARK 500   OD2  ASP C   229     NH1  ARG D    73              2.06            
REMARK 500   NZ   LYS D    91     OG1  THR E     1              2.07            
REMARK 500   OD2  ASP A    14     O    HOH A   197              2.09            
REMARK 500   O    CYS A   187     N    ASN A   189              2.10            
REMARK 500   CE1  PHE F    25     OXT  ASN G   103              2.10            
REMARK 500   O    ASP F    70     CG2  ILE F    74              2.11            
REMARK 500   NH2  ARG A   129     CB   HIS A   131              2.12            
REMARK 500   O    TYR D    76     N    THR D    78              2.14            
REMARK 500   O    LEU A   139     NH2  ARG A   141              2.14            
REMARK 500   OH   TYR E    76     O    MET F   101              2.14            
REMARK 500   ND2  ASN F    90     O    HOH F   111              2.14            
REMARK 500   OD1  ASP E    59     NZ   LYS E    62              2.17            
REMARK 500   OH   TYR G    18     NE2  HIS G    94              2.18            
REMARK 500   O    GLN E    61     N    ALA E    64              2.18            
REMARK 500   O    THR D    92     OG1  THR E     1              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    ARG A   192     ND2  ASN E    14     1655     1.74            
REMARK 500   CD   ARG A   192     NE2  HIS E    13     1655     2.11            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    SER A  19   C     GLY A  20   N       0.177                       
REMARK 500    THR G   1   C     PRO G   2   N       0.243                       
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    ASP A   3   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ARG A  11   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    PRO A  13   C   -  N   -  CA  ANGL. DEV. =   9.3 DEGREES          
REMARK 500    PRO A  13   CA  -  C   -  N   ANGL. DEV. =  16.5 DEGREES          
REMARK 500    PRO A  13   O   -  C   -  N   ANGL. DEV. = -16.6 DEGREES          
REMARK 500    ASP A  14   C   -  N   -  CA  ANGL. DEV. =  36.2 DEGREES          
REMARK 500    ASP A  14   O   -  C   -  N   ANGL. DEV. = -14.4 DEGREES          
REMARK 500    GLU A  15   CA  -  C   -  N   ANGL. DEV. =  25.1 DEGREES          
REMARK 500    GLU A  15   O   -  C   -  N   ANGL. DEV. = -27.8 DEGREES          
REMARK 500    ILE A  16   C   -  N   -  CA  ANGL. DEV. =  15.6 DEGREES          
REMARK 500    ILE A  16   O   -  C   -  N   ANGL. DEV. = -15.0 DEGREES          
REMARK 500    GLN A  18   CA  -  C   -  N   ANGL. DEV. = -13.2 DEGREES          
REMARK 500    ASP A  32   CB  -  CG  -  OD2 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    ARG A  67   CD  -  NE  -  CZ  ANGL. DEV. =  11.7 DEGREES          
REMARK 500    ARG A  67   NE  -  CZ  -  NH1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASN A  96   CB  -  CA  -  C   ANGL. DEV. =  12.6 DEGREES          
REMARK 500    ASP A  99   CB  -  CG  -  OD1 ANGL. DEV. =   7.2 DEGREES          
REMARK 500    ASP A 109   CB  -  CG  -  OD2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    LEU A 116   CB  -  CA  -  C   ANGL. DEV. =  11.4 DEGREES          
REMARK 500    ARG A 129   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG A 129   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ASP A 154   CB  -  CA  -  C   ANGL. DEV. =  14.2 DEGREES          
REMARK 500    ASP A 154   CB  -  CG  -  OD1 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ARG A 175   NE  -  CZ  -  NH1 ANGL. DEV. =   5.2 DEGREES          
REMARK 500    ARG A 192   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG C 220   NE  -  CZ  -  NH2 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    ARG C 235   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ASP D  22   CB  -  CG  -  OD1 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    ARG D  67   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    ASP D  70   CB  -  CG  -  OD1 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    ARG D  73   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    LYS D  84   N   -  CA  -  CB  ANGL. DEV. =  12.0 DEGREES          
REMARK 500    GLU E  36   N   -  CA  -  CB  ANGL. DEV. =  11.4 DEGREES          
REMARK 500    SER E  54   C   -  N   -  CA  ANGL. DEV. =  19.8 DEGREES          
REMARK 500    ARG E  67   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ARG E  73   CD  -  NE  -  CZ  ANGL. DEV. =  14.6 DEGREES          
REMARK 500    ARG E  73   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500    ARG E  73   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    ALA E  80   C   -  N   -  CA  ANGL. DEV. =  26.9 DEGREES          
REMARK 500    ARG F  35   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    LYS F  62   CA  -  CB  -  CG  ANGL. DEV. =  15.3 DEGREES          
REMARK 500    THR F  71   CA  -  CB  -  CG2 ANGL. DEV. =   9.5 DEGREES          
REMARK 500    ARG F  73   CD  -  NE  -  CZ  ANGL. DEV. =  22.0 DEGREES          
REMARK 500    ARG F  73   NE  -  CZ  -  NH1 ANGL. DEV. =   4.9 DEGREES          
REMARK 500    PRO G   2   CB  -  CA  -  C   ANGL. DEV. =  13.4 DEGREES          
REMARK 500    THR G   1   O   -  C   -  N   ANGL. DEV. = -19.9 DEGREES          
REMARK 500    PRO G   2   C   -  N   -  CA  ANGL. DEV. =  11.5 DEGREES          
REMARK 500    PRO G   2   C   -  N   -  CD  ANGL. DEV. = -22.3 DEGREES          
REMARK 500    THR G   6   CA  -  CB  -  CG2 ANGL. DEV. =   8.5 DEGREES          
REMARK 500    THR G  41   CA  -  CB  -  CG2 ANGL. DEV. =  10.6 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      63 ANGLE DEVIATIONS.                             
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    ARG A  11      132.89    -31.64                                   
REMARK 500    ASP A  14      -53.41    -22.85                                   
REMARK 500    THR A  35       77.49    174.24                                   
REMARK 500    GLN A  49       85.14    100.99                                   
REMARK 500    ARG A  54      116.67    -35.65                                   
REMARK 500    HIS A  55       30.43   -148.37                                   
REMARK 500    ASP A  57       60.07     30.56                                   
REMARK 500    ILE A  64       21.18    -79.11                                   
REMARK 500    SER A  65        8.60   -170.06                                   
REMARK 500    LEU A  66      -90.11     85.33                                   
REMARK 500    ILE A  76     -110.57    -98.27                                   
REMARK 500    LEU A  77       11.16    -31.51                                   
REMARK 500    ALA A  89      156.21    -36.29                                   
REMARK 500    PRO A  92       18.03    -67.46                                   
REMARK 500    TYR A 104       22.59    -73.45                                   
REMARK 500    HIS A 107       51.75   -164.36                                   
REMARK 500    PRO A 108      -75.29    -32.61                                   
REMARK 500    ASP A 109      -58.27    -15.87                                   
REMARK 500    GLN A 111       95.15     14.48                                   
REMARK 500    TYR A 121      -37.96    -27.46                                   
REMARK 500    ILE A 124      107.21    -56.80                                   
REMARK 500    PHE A 132       56.58     32.90                                   
REMARK 500    GLU A 137        2.37    -61.76                                   
REMARK 500    SER A 151       15.02    -66.53                                   
REMARK 500    ILE A 155       19.22    -45.92                                   
REMARK 500    ALA A 156      117.49     71.30                                   
REMARK 500    PRO A 184      171.88    -47.55                                   
REMARK 500    ASN A 189     -158.27     97.85                                   
REMARK 500    SER C 228     -111.43    -35.55                                   
REMARK 500    ARG C 235      -82.41    -86.33                                   
REMARK 500    ASN D   4      161.30    176.24                                   
REMARK 500    ASP D   7      -86.81    -49.87                                   
REMARK 500    LEU D   8      -67.24     -9.61                                   
REMARK 500    ASN D  14       13.99     88.16                                   
REMARK 500    GLN D  16      134.49    179.93                                   
REMARK 500    ASN D  21       46.49     36.37                                   
REMARK 500    LEU D  31       -9.42   -140.60                                   
REMARK 500    LYS D  34       18.61     95.97                                   
REMARK 500    ARG D  35       85.48   -153.64                                   
REMARK 500    PRO D  53       80.76    -51.06                                   
REMARK 500    SER D  55       -6.50    -46.44                                   
REMARK 500    ASP D  59      -51.53    -20.93                                   
REMARK 500    LYS D  69       -2.58    -50.64                                   
REMARK 500    TYR D  76      -71.31    -66.43                                   
REMARK 500    LEU D  77       -3.11    -44.44                                   
REMARK 500    LYS D  81      106.24     77.69                                   
REMARK 500    GLU D  83      -74.82    -93.64                                   
REMARK 500    HIS D  94      100.38    -40.02                                   
REMARK 500    GLN E  16      126.73    178.46                                   
REMARK 500    LEU E  20      -31.81   -150.43                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     109 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 PRO A   13     ASP A   14                  141.05                    
REMARK 500 PRO H   53     SER H   54                   87.96                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A  11         0.20    SIDE CHAIN                              
REMARK 500    TYR A 121         0.07    SIDE CHAIN                              
REMARK 500    TYR A 125         0.07    SIDE CHAIN                              
REMARK 500    ARG A 148         0.12    SIDE CHAIN                              
REMARK 500    ASN A 152         0.10    SIDE CHAIN                              
REMARK 500    ARG C 235         0.19    SIDE CHAIN                              
REMARK 500    ARG D  67         0.17    SIDE CHAIN                              
REMARK 500    TYR F  76         0.07    SIDE CHAIN                              
REMARK 500    GLU G  11         0.07    SIDE CHAIN                              
REMARK 500    ARG H  73         0.11    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    ASP A  14        -25.33                                           
REMARK 500    ILE A  16         11.63                                           
REMARK 500    LYS A  17        -13.50                                           
REMARK 500    GLN A  18        -15.96                                           
REMARK 500    THR A  35         14.96                                           
REMARK 500    PHE A  52        -10.46                                           
REMARK 500    LEU A  88        -16.07                                           
REMARK 500    ASP A 109         14.62                                           
REMARK 500    TRP A 127        -10.41                                           
REMARK 500    GLU C 239        -20.80                                           
REMARK 500    TYR D  18        -12.34                                           
REMARK 500    ARG D  35         11.18                                           
REMARK 500    ILE D  40         11.23                                           
REMARK 500    PHE D  48        -11.08                                           
REMARK 500    THR D  71        -10.38                                           
REMARK 500    LYS D  81        -10.84                                           
REMARK 500    LEU D  85         10.19                                           
REMARK 500    ILE E  65         12.19                                           
REMARK 500    LYS E  81         14.01                                           
REMARK 500    HIS F  13         14.14                                           
REMARK 500    GLN F  61         10.83                                           
REMARK 500    ASP F  70         12.05                                           
REMARK 500    THR G   1         28.95                                           
REMARK 500    LEU G   8         10.11                                           
REMARK 500    TYR G  27         10.56                                           
REMARK 500    ASN G  44         10.53                                           
REMARK 500    VAL G  50         13.98                                           
REMARK 500    GLU G  66        -13.07                                           
REMARK 500    ALA G  80        -10.09                                           
REMARK 500    HIS G  94        -10.16                                           
REMARK 500    ASN H   4        -24.66                                           
REMARK 500    ILE H  39         14.59                                           
REMARK 500    ILE H  47        -11.90                                           
REMARK 500    VAL H  50         13.62                                           
REMARK 500    PRO H  53        -19.52                                           
REMARK 500    SER H  54         11.54                                           
REMARK 500    ASP H  70         10.61                                           
REMARK 500    LYS H  81         11.78                                           
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    THR A  48        18.8      L          L   OUTSIDE RANGE           
REMARK 500    GLN A 111        23.3      L          L   OUTSIDE RANGE           
REMARK 500    ASP A 147        24.6      L          L   OUTSIDE RANGE           
REMARK 500    TYR A 150        23.0      L          L   OUTSIDE RANGE           
REMARK 500    ILE A 155        20.1      L          L   OUTSIDE RANGE           
REMARK 500    ARG A 172        23.4      L          L   OUTSIDE RANGE           
REMARK 500    ARG D  73        24.9      L          L   OUTSIDE RANGE           
REMARK 500    GLN E   3        24.8      L          L   OUTSIDE RANGE           
REMARK 500    SER E  54        18.9      L          L   OUTSIDE RANGE           
REMARK 500    LYS E  62        22.8      L          L   OUTSIDE RANGE           
REMARK 500    ILE E  74        22.4      L          L   OUTSIDE RANGE           
REMARK 500    ILE F  17        23.2      L          L   OUTSIDE RANGE           
REMARK 500    GLN G   3        20.0      L          L   OUTSIDE RANGE           
REMARK 500    LYS G  62        24.7      L          L   OUTSIDE RANGE           
REMARK 500    ILE G  74        22.0      L          L   OUTSIDE RANGE           
REMARK 500    HIS H  13        21.6      L          L   OUTSIDE RANGE           
REMARK 500    GLU H  79        12.9      L          L   OUTSIDE RANGE           
REMARK 500    LYS H  91        22.4      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH D 114        DISTANCE =  5.50 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: CAT                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: CATALYTIC SITE                                     
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GAD                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: GANGLIOSIDE BINDING SITE IN CHAIN D                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GAE                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: GANGLIOSIDE BINDING SITE IN CHAIN E                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GAF                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: GANGLIOSIDE BINDING SITE IN CHAIN F                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GAG                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: GANGLIOSIDE BINDING SITE IN CHAIN G                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GAH                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: GANGLIOSIDE BINDING SITE IN CHAIN H                
DBREF  1XTC A    1   194  UNP    P01555   CHTA_VIBCH      19    212             
DBREF  1XTC C  195   240  UNP    P01555   CHTA_VIBCH     213    258             
DBREF  1XTC D    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1XTC E    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1XTC F    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1XTC G    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1XTC H    1   103  UNP    P01556   CHTB_VIBCH      22    124             
SEQADV 1XTC LEU A   85  UNP  P01555    ILE   103 CONFLICT                       
SEQADV 1XTC LEU A   88  UNP  P01555    ILE   106 CONFLICT                       
SEQADV 1XTC SER D   54  UNP  P01556    GLY    75 CONFLICT                       
SEQADV 1XTC THR D   87  UNP  P01556    VAL   108 CONFLICT                       
SEQADV 1XTC SER E   54  UNP  P01556    GLY    75 CONFLICT                       
SEQADV 1XTC THR E   87  UNP  P01556    VAL   108 CONFLICT                       
SEQADV 1XTC SER F   54  UNP  P01556    GLY    75 CONFLICT                       
SEQADV 1XTC THR F   87  UNP  P01556    VAL   108 CONFLICT                       
SEQADV 1XTC SER G   54  UNP  P01556    GLY    75 CONFLICT                       
SEQADV 1XTC THR G   87  UNP  P01556    VAL   108 CONFLICT                       
SEQADV 1XTC SER H   54  UNP  P01556    GLY    75 CONFLICT                       
SEQADV 1XTC THR H   87  UNP  P01556    VAL   108 CONFLICT                       
SEQRES   1 A  194  ASN ASP ASP LYS LEU TYR ARG ALA ASP SER ARG PRO PRO          
SEQRES   2 A  194  ASP GLU ILE LYS GLN SER GLY GLY LEU MET PRO ARG GLY          
SEQRES   3 A  194  GLN SER GLU TYR PHE ASP ARG GLY THR GLN MET ASN ILE          
SEQRES   4 A  194  ASN LEU TYR ASP HIS ALA ARG GLY THR GLN THR GLY PHE          
SEQRES   5 A  194  VAL ARG HIS ASP ASP GLY TYR VAL SER THR SER ILE SER          
SEQRES   6 A  194  LEU ARG SER ALA HIS LEU VAL GLY GLN THR ILE LEU SER          
SEQRES   7 A  194  GLY HIS SER THR TYR TYR LEU TYR VAL LEU ALA THR ALA          
SEQRES   8 A  194  PRO ASN MET PHE ASN VAL ASN ASP VAL LEU GLY ALA TYR          
SEQRES   9 A  194  SER PRO HIS PRO ASP GLU GLN GLU VAL SER ALA LEU GLY          
SEQRES  10 A  194  GLY ILE PRO TYR SER GLN ILE TYR GLY TRP TYR ARG VAL          
SEQRES  11 A  194  HIS PHE GLY VAL LEU ASP GLU GLN LEU HIS ARG ASN ARG          
SEQRES  12 A  194  GLY TYR ARG ASP ARG TYR TYR SER ASN LEU ASP ILE ALA          
SEQRES  13 A  194  PRO ALA ALA ASP GLY TYR GLY LEU ALA GLY PHE PRO PRO          
SEQRES  14 A  194  GLU HIS ARG ALA TRP ARG GLU GLU PRO TRP ILE HIS HIS          
SEQRES  15 A  194  ALA PRO PRO GLY CYS GLY ASN ALA PRO ARG SER SER              
SEQRES   1 C   46  MET SER ASN THR CYS ASP GLU LYS THR GLN SER LEU GLY          
SEQRES   2 C   46  VAL LYS PHE LEU ASP GLU TYR GLN SER LYS VAL LYS ARG          
SEQRES   3 C   46  GLN ILE PHE SER GLY TYR GLN SER ASP ILE ASP THR HIS          
SEQRES   4 C   46  ASN ARG ILE LYS ASP GLU LEU                                  
SEQRES   1 D  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 D  103  ASN THR GLN ILE TYR THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 D  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 D  103  ILE THR PHE LYS ASN GLY ALA ILE PHE GLN VAL GLU VAL          
SEQRES   5 D  103  PRO SER SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 D  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 D  103  GLU ALA LYS VAL GLU LYS LEU CYS THR TRP ASN ASN LYS          
SEQRES   8 D  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 E  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 E  103  ASN THR GLN ILE TYR THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 E  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 E  103  ILE THR PHE LYS ASN GLY ALA ILE PHE GLN VAL GLU VAL          
SEQRES   5 E  103  PRO SER SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 E  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 E  103  GLU ALA LYS VAL GLU LYS LEU CYS THR TRP ASN ASN LYS          
SEQRES   8 E  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 F  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 F  103  ASN THR GLN ILE TYR THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 F  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 F  103  ILE THR PHE LYS ASN GLY ALA ILE PHE GLN VAL GLU VAL          
SEQRES   5 F  103  PRO SER SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 F  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 F  103  GLU ALA LYS VAL GLU LYS LEU CYS THR TRP ASN ASN LYS          
SEQRES   8 F  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 G  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 G  103  ASN THR GLN ILE TYR THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 G  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 G  103  ILE THR PHE LYS ASN GLY ALA ILE PHE GLN VAL GLU VAL          
SEQRES   5 G  103  PRO SER SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 G  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 G  103  GLU ALA LYS VAL GLU LYS LEU CYS THR TRP ASN ASN LYS          
SEQRES   8 G  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 H  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 H  103  ASN THR GLN ILE TYR THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 H  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 H  103  ILE THR PHE LYS ASN GLY ALA ILE PHE GLN VAL GLU VAL          
SEQRES   5 H  103  PRO SER SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 H  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 H  103  GLU ALA LYS VAL GLU LYS LEU CYS THR TRP ASN ASN LYS          
SEQRES   8 H  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
FORMUL   8  HOH   *138(H2 O)                                                    
HELIX    1   1 PRO A   13  SER A   19  1                                   7    
HELIX    2   2 LEU A   41  ARG A   46  1                                   6    
HELIX    3   3 ARG A   67  LEU A   71  1                                   5    
HELIX    4   4 VAL A   97  TYR A  104  1                                   8    
HELIX    5   5 PRO A  108  GLU A  110  5                                   3    
HELIX    6   6 ASP A  147  ASN A  152  1                                   6    
HELIX    7   7 ALA A  158  ASP A  160  5                                   3    
HELIX    8   8 ARG A  172  ARG A  175  5                                   4    
HELIX    9   9 TRP A  179  HIS A  181  5                                   3    
HELIX   10  10 ASN C  197  HIS C  233  1                                  37    
HELIX   11  11 ILE D    5  GLU D   11  1                                   7    
HELIX   12  12 ASP D   59  LYS D   62  1                                   4    
HELIX   13  13 ALA D   64  TYR D   76  1                                  13    
HELIX   14  14 ILE E    5  GLU E   11  1                                   7    
HELIX   15  15 ASP E   59  TYR E   76  1                                  18    
HELIX   16  16 ILE F    5  ALA F   10  1                                   6    
HELIX   17  17 ASP F   59  LYS F   62  1                                   4    
HELIX   18  18 ALA F   64  LEU F   77  1                                  14    
HELIX   19  19 ILE G    5  CYS G    9  1                                   5    
HELIX   20  20 SER G   60  LEU G   77  1                                  18    
HELIX   21  21 ILE H    5  GLU H   11  1                                   7    
HELIX   22  22 LYS H   62  LEU H   77  1                                  16    
SHEET    1   A 3 TYR A   6  ASP A   9  0                                        
SHEET    2   A 3 TYR A  83  LEU A  88 -1  N  TYR A  86   O  ARG A   7           
SHEET    3   A 3 ILE A 124  VAL A 130 -1  N  VAL A 130   O  TYR A  83           
SHEET    1   B 3 TYR A  59  SER A  63  0                                        
SHEET    2   B 3 GLU A 112  LEU A 116 -1  N  ALA A 115   O  VAL A  60           
SHEET    3   B 3 MET A  94  ASN A  96 -1  N  PHE A  95   O  SER A 114           
SHEET    1   C 3 THR D  15  THR D  19  0                                        
SHEET    2   C 3 LYS D  84  TRP D  88 -1  N  THR D  87   O  GLN D  16           
SHEET    3   C 3 ILE D  96  ILE D  99 -1  N  ALA D  98   O  CYS D  86           
SHEET    1   D 4 ALA E  98  ALA E 102  0                                        
SHEET    2   D 4 SER D  26  SER D  30 -1  N  GLU D  29   O  ILE E  99           
SHEET    3   D 4 ALA D  38  THR D  41 -1  N  THR D  41   O  SER D  26           
SHEET    4   D 4 PHE D  48  VAL D  50 -1  N  VAL D  50   O  ALA D  38           
SHEET    1   E 6 ILE E  47  VAL E  50  0                                        
SHEET    2   E 6 ALA E  38  PHE E  42 -1  N  ILE E  40   O  PHE E  48           
SHEET    3   E 6 ILE E  24  SER E  30 -1  N  THR E  28   O  ILE E  39           
SHEET    4   E 6 ALA F  95  SER F 100 -1  N  ILE F  99   O  GLU E  29           
SHEET    5   E 6 LYS F  84  TRP F  88 -1  N  TRP F  88   O  ALA F  95           
SHEET    6   E 6 THR F  15  THR F  19 -1  N  TYR F  18   O  LEU F  85           
SHEET    1   F 6 THR G  15  THR G  19  0                                        
SHEET    2   F 6 VAL G  82  TRP G  88 -1  N  THR G  87   O  GLN G  16           
SHEET    3   F 6 ALA G  98  ALA G 102 -1  N  SER G 100   O  GLU G  83           
SHEET    4   F 6 SER F  26  SER F  30 -1  N  GLU F  29   O  ILE G  99           
SHEET    5   F 6 ALA F  38  THR F  41 -1  N  THR F  41   O  SER F  26           
SHEET    6   F 6 ILE F  47  VAL F  50 -1  N  VAL F  50   O  ALA F  38           
SHEET    1   G 6 PHE G  48  VAL G  50  0                                        
SHEET    2   G 6 ALA G  38  ILE G  40 -1  N  ILE G  40   O  PHE G  48           
SHEET    3   G 6 SER G  26  SER G  30 -1  N  THR G  28   O  ILE G  39           
SHEET    4   G 6 ALA H  95  ALA H 102 -1  N  MET H 101   O  TYR G  27           
SHEET    5   G 6 LYS H  84  TRP H  88 -1  N  TRP H  88   O  ALA H  95           
SHEET    6   G 6 THR H  15  THR H  19 -1  N  TYR H  18   O  LEU H  85           
SHEET    1   H 3 SER H  26  GLU H  29  0                                        
SHEET    2   H 3 ALA H  38  THR H  41 -1  N  THR H  41   O  SER H  26           
SHEET    3   H 3 ILE H  47  VAL H  50 -1  N  VAL H  50   O  ALA H  38           
SSBOND   1 CYS A  187    CYS C  199                          1555   1555  2.10  
SSBOND   2 CYS D    9    CYS D   86                          1555   1555  2.07  
SSBOND   3 CYS E    9    CYS E   86                          1555   1555  2.06  
SSBOND   4 CYS F    9    CYS F   86                          1555   1555  2.03  
SSBOND   5 CYS G    9    CYS G   86                          1555   1555  2.03  
SSBOND   6 CYS H    9    CYS H   86                          1555   1555  2.12  
CISPEP   1 GLU A  177    PRO A  178          0         3.74                     
CISPEP   2 THR D   92    PRO D   93          0        -1.90                     
CISPEP   3 THR E   92    PRO E   93          0         1.68                     
CISPEP   4 THR F   92    PRO F   93          0         2.74                     
CISPEP   5 THR G   92    PRO G   93          0        -2.15                     
CISPEP   6 THR H   92    PRO H   93          0         4.84                     
SITE     1 CAT  3 ARG A   7  SER A  61  GLU A 112                               
SITE     1 GAD  7 ALA D  46  GLU D  51  GLN D  56  GLN D  61                    
SITE     2 GAD  7 TRP D  88  ASN D  90  LYS D  91                               
SITE     1 GAE  7 ALA E  46  GLU E  51  GLN E  56  GLN E  61                    
SITE     2 GAE  7 TRP E  88  ASN E  90  LYS E  91                               
SITE     1 GAF  7 ALA F  46  GLU F  51  GLN F  56  GLN F  61                    
SITE     2 GAF  7 TRP F  88  ASN F  90  LYS F  91                               
SITE     1 GAG  7 ALA G  46  GLU G  51  GLN G  56  GLN G  61                    
SITE     2 GAG  7 TRP G  88  ASN G  90  LYS G  91                               
SITE     1 GAH  7 ALA H  46  GLU H  51  GLN H  56  GLN H  61                    
SITE     2 GAH  7 TRP H  88  ASN H  90  LYS H  91                               
CRYST1   73.000   92.200   60.600  90.00 106.40  90.00 P 1 21 1     10          
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      0.013699  0.000000  0.004032        0.00000                         
SCALE2      0.000000  0.010846  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017202        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system