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Database: PDB
Entry: 1TB6
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Original site: 1TB6 
HEADER    HYDROLASE/BLOOD CLOTTING                19-MAY-04   1TB6              
TITLE     2.5A CRYSTAL STRUCTURE OF THE ANTITHROMBIN-THROMBIN-HEPARIN TERNARY   
TITLE    2 COMPLEX                                                              
CAVEAT     1TB6    NAG A 1 HAS WRONG CHIRALITY AT ATOM C1 GU6 B 15 HAS WRONG    
CAVEAT   2 1TB6    CHIRALITY AT ATOM C2 GU6 B 15 HAS WRONG CHIRALITY AT ATOM    
CAVEAT   3 1TB6    C3 GU6 B 15 HAS WRONG CHIRALITY AT ATOM C4 GU6 B 15 HAS      
CAVEAT   4 1TB6    WRONG CHIRALITY AT ATOM C5 NAG I 801 HAS WRONG CHIRALITY AT  
CAVEAT   5 1TB6    ATOM C1                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: THROMBIN;                                                  
COMPND   3 CHAIN: L;                                                            
COMPND   4 FRAGMENT: THROMBIN LIGHT CHAIN;                                      
COMPND   5 SYNONYM: COAGULATION FACTOR II;                                      
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: THROMBIN;                                                  
COMPND  10 CHAIN: H;                                                            
COMPND  11 FRAGMENT: THROMBIN HEAVY CHAIN, SERINE PROTEASE;                     
COMPND  12 SYNONYM: COAGULATION FACTOR II;                                      
COMPND  13 EC: 3.4.21.5;                                                        
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MOL_ID: 3;                                                           
COMPND  16 MOLECULE: ANTITHROMBIN-III;                                          
COMPND  17 CHAIN: I;                                                            
COMPND  18 SYNONYM: ATIII, PRO0309;                                             
COMPND  19 ENGINEERED: YES;                                                     
COMPND  20 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: F2;                                                            
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: F2;                                                            
SOURCE  14 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  15 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  17 MOL_ID: 3;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  19 ORGANISM_COMMON: HUMAN;                                              
SOURCE  20 ORGANISM_TAXID: 9606;                                                
SOURCE  21 GENE: SERPINC1, AT3;                                                 
SOURCE  22 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  23 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE  24 EXPRESSION_SYSTEM_TAXID: 10029                                       
KEYWDS    HEPARIN, HYDROLASE-BLOOD CLOTTING COMPLEX                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.LI,D.J.JOHNSON,C.T.ESMON,J.A.HUNTINGTON                             
REVDAT   5   29-JUL-20 1TB6    1       CAVEAT COMPND REMARK HET                 
REVDAT   5 2                   1       HETNAM FORMUL LINK   SITE                
REVDAT   5 3                   1       ATOM                                     
REVDAT   4   13-JUL-11 1TB6    1       VERSN                                    
REVDAT   3   24-FEB-09 1TB6    1       VERSN                                    
REVDAT   2   21-SEP-04 1TB6    1       JRNL                                     
REVDAT   1   17-AUG-04 1TB6    0                                                
JRNL        AUTH   W.LI,D.J.JOHNSON,C.T.ESMON,J.A.HUNTINGTON                    
JRNL        TITL   STRUCTURE OF THE ANTITHROMBIN-THROMBIN-HEPARIN TERNARY       
JRNL        TITL 2 COMPLEX REVEALS THE ANTITHROMBOTIC MECHANISM OF HEPARIN.     
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  11   857 2004              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   15311269                                                     
JRNL        DOI    10.1038/NSMB811                                              
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.46                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 32246                          
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) : 0.208                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1301                            
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           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.66                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.70                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3170                       
REMARK   3   BIN FREE R VALUE                    : 0.3470                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 208                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.024                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5684                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 494                                     
REMARK   3   SOLVENT ATOMS            : 146                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 55.51                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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) : 0.31                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.35                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.37                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.41                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.400                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : 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  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1TB6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUN-04.                  
REMARK 100 THE DEPOSITION ID IS D_1000022521.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-MAY-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX14.1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.488                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA, CCP4 (SCALA)                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32296                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 62.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.08600                            
REMARK 200  R SYM                      (I) : 0.08600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.56100                            
REMARK 200  R SYM FOR SHELL            (I) : 0.56100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRIES 1E03 AND 1PPB                            
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, LITHIUM CITRATE, PH 7.4,       
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 296K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       44.20450            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       58.60900            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       44.20200            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       58.60900            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       44.20450            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       44.20200            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 16710 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 31450 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, I, A, B, C, D                   
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     THR L     1U                                                     
REMARK 465     ALA L     1T                                                     
REMARK 465     THR L     1S                                                     
REMARK 465     ASP L    14L                                                     
REMARK 465     GLY L    14M                                                     
REMARK 465     ARG L    15                                                      
REMARK 465     HIS I     1                                                      
REMARK 465     GLY I     2                                                      
REMARK 465     SER I     3                                                      
REMARK 465     GLU I    27                                                      
REMARK 465     LYS I    28                                                      
REMARK 465     LYS I    29                                                      
REMARK 465     ALA I    30                                                      
REMARK 465     THR I    31                                                      
REMARK 465     GLU I    32                                                      
REMARK 465     ASP I    33                                                      
REMARK 465     GLU I    34                                                      
REMARK 465     GLY I    35                                                      
REMARK 465     SER I    36                                                      
REMARK 465     SER I   380                                                      
REMARK 465     GLU I   381                                                      
REMARK 465     ALA I   382                                                      
REMARK 465     ALA I   383                                                      
REMARK 465     ALA I   384                                                      
REMARK 465     SER I   385                                                      
REMARK 465     LYS I   432                                                      
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     GLN L   1O   CG   CD   OE1  NE2                                  
REMARK 470     LYS L  14A   CE   NZ                                             
REMARK 470     ARG L  14D   CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG H  75    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS H 110    CD   CE   NZ                                        
REMARK 470     GLU H 127    CG   CD   OE1  OE2                                  
REMARK 470     ARG H 173    NE   CZ   NH1  NH2                                  
REMARK 470     LYS H 240    CE   NZ                                             
REMARK 470     GLU H 247    CG   CD   OE1  OE2                                  
REMARK 470     GLU I  37    CG   CD   OE1  OE2                                  
REMARK 470     GLN I  38    CG   CD   OE1  NE2                                  
REMARK 470     LYS I 133    CE   NZ                                             
REMARK 470     LYS I 188    CD   CE   NZ                                        
REMARK 470     GLU I 195    CD   OE1  OE2                                       
REMARK 470     GLU I 205    CD   OE1  OE2                                       
REMARK 470     LYS I 228    CD   CE   NZ                                        
REMARK 470     GLU I 245    CG   CD   OE1  OE2                                  
REMARK 470     LYS I 294    CD   CE   NZ                                        
REMARK 470     GLU I 310    CG   CD   OE1  OE2                                  
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    ILE I   207     NH2  ARG I   399     4455     2.19            
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    CYS I 317   CA  -  CB  -  SG  ANGL. DEV. =  10.9 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    GLU L   1Q     -48.05   -143.82                                   
REMARK 500    PHE L   1M     -37.66   -136.43                                   
REMARK 500    PHE L   7     -104.26   -137.12                                   
REMARK 500    TYR H  60A      84.47   -154.61                                   
REMARK 500    LEU H  65      148.32   -171.83                                   
REMARK 500    HIS H  71      -59.33   -123.47                                   
REMARK 500    GLU H  77       76.02   -101.93                                   
REMARK 500    GLU H  97A     -67.93   -157.83                                   
REMARK 500    ASN H 147D      31.39   -143.25                                   
REMARK 500    ARG H 175      107.03    -46.67                                   
REMARK 500    ASP H 186A      34.00    -83.65                                   
REMARK 500    SER H 214      -58.98   -121.38                                   
REMARK 500    ASP H 243       46.98    -82.02                                   
REMARK 500    GLN H 244      -30.08   -149.63                                   
REMARK 500    ASP I  14      -38.91    -38.52                                   
REMARK 500    MET I  17       47.61   -150.94                                   
REMARK 500    ASN I  96     -138.48     50.92                                   
REMARK 500    ILE I 111      172.27    -50.40                                   
REMARK 500    ALA I 137      -40.36   -137.83                                   
REMARK 500    GLU I 205      -25.58    100.08                                   
REMARK 500    ASN I 208     -164.75   -129.29                                   
REMARK 500    LYS I 222       92.13   -166.12                                   
REMARK 500    SER I 246     -155.57    -77.54                                   
REMARK 500    CYS I 247      124.17    163.29                                   
REMARK 500    ARG I 261      131.59   -172.53                                   
REMARK 500    VAL I 263     -158.39    -98.62                                   
REMARK 500    ASP I 277      -14.88     78.22                                   
REMARK 500    ALA I 356     -176.31    -69.37                                   
REMARK 500    ARG I 359      113.85    156.71                                   
REMARK 500    ALA I 387      144.26    -19.20                                   
REMARK 500    ASN I 428      104.86   -162.92                                   
REMARK 500    CYS I 430     -173.18    -62.93                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1TB6 I    1   432  UNP    P01008   ANT3_HUMAN      33    464             
DBREF  1TB6 L    1U   15  UNP    P00734   THRB_HUMAN     315    363             
DBREF  1TB6 H   16   247  UNP    P00734   THRB_HUMAN     364    622             
SEQADV 1TB6 ALA I  137  UNP  P01008    SER   169 ENGINEERED                     
SEQADV 1TB6 CYS I  317  UNP  P01008    VAL   349 ENGINEERED                     
SEQADV 1TB6 CYS I  401  UNP  P01008    THR   433 ENGINEERED                     
SEQADV 1TB6 ALA H  195  UNP  P00734    SER   568 ENGINEERED                     
SEQRES   1 L   49  THR ALA THR SER GLU TYR GLN THR PHE PHE ASN PRO ARG          
SEQRES   2 L   49  THR PHE GLY SER GLY GLU ALA ASP CYS GLY LEU ARG PRO          
SEQRES   3 L   49  LEU PHE GLU LYS LYS SER LEU GLU ASP LYS THR GLU ARG          
SEQRES   4 L   49  GLU LEU LEU GLU SER TYR ILE ASP GLY ARG                      
SEQRES   1 H  259  ILE VAL GLU GLY SER ASP ALA GLU ILE GLY MET SER PRO          
SEQRES   2 H  259  TRP GLN VAL MET LEU PHE ARG LYS SER PRO GLN GLU LEU          
SEQRES   3 H  259  LEU CYS GLY ALA SER LEU ILE SER ASP ARG TRP VAL LEU          
SEQRES   4 H  259  THR ALA ALA HIS CYS LEU LEU TYR PRO PRO TRP ASP LYS          
SEQRES   5 H  259  ASN PHE THR GLU ASN ASP LEU LEU VAL ARG ILE GLY LYS          
SEQRES   6 H  259  HIS SER ARG THR ARG TYR GLU ARG ASN ILE GLU LYS ILE          
SEQRES   7 H  259  SER MET LEU GLU LYS ILE TYR ILE HIS PRO ARG TYR ASN          
SEQRES   8 H  259  TRP ARG GLU ASN LEU ASP ARG ASP ILE ALA LEU MET LYS          
SEQRES   9 H  259  LEU LYS LYS PRO VAL ALA PHE SER ASP TYR ILE HIS PRO          
SEQRES  10 H  259  VAL CYS LEU PRO ASP ARG GLU THR ALA ALA SER LEU LEU          
SEQRES  11 H  259  GLN ALA GLY TYR LYS GLY ARG VAL THR GLY TRP GLY ASN          
SEQRES  12 H  259  LEU LYS GLU THR TRP THR ALA ASN VAL GLY LYS GLY GLN          
SEQRES  13 H  259  PRO SER VAL LEU GLN VAL VAL ASN LEU PRO ILE VAL GLU          
SEQRES  14 H  259  ARG PRO VAL CYS LYS ASP SER THR ARG ILE ARG ILE THR          
SEQRES  15 H  259  ASP ASN MET PHE CYS ALA GLY TYR LYS PRO ASP GLU GLY          
SEQRES  16 H  259  LYS ARG GLY ASP ALA CYS GLU GLY ASP ALA GLY GLY PRO          
SEQRES  17 H  259  PHE VAL MET LYS SER PRO PHE ASN ASN ARG TRP TYR GLN          
SEQRES  18 H  259  MET GLY ILE VAL SER TRP GLY GLU GLY CYS ASP ARG ASP          
SEQRES  19 H  259  GLY LYS TYR GLY PHE TYR THR HIS VAL PHE ARG LEU LYS          
SEQRES  20 H  259  LYS TRP ILE GLN LYS VAL ILE ASP GLN PHE GLY GLU              
SEQRES   1 I  432  HIS GLY SER PRO VAL ASP ILE CYS THR ALA LYS PRO ARG          
SEQRES   2 I  432  ASP ILE PRO MET ASN PRO MET CYS ILE TYR ARG SER PRO          
SEQRES   3 I  432  GLU LYS LYS ALA THR GLU ASP GLU GLY SER GLU GLN LYS          
SEQRES   4 I  432  ILE PRO GLU ALA THR ASN ARG ARG VAL TRP GLU LEU SER          
SEQRES   5 I  432  LYS ALA ASN SER ARG PHE ALA THR THR PHE TYR GLN HIS          
SEQRES   6 I  432  LEU ALA ASP SER LYS ASN ASP ASN ASP ASN ILE PHE LEU          
SEQRES   7 I  432  SER PRO LEU SER ILE SER THR ALA PHE ALA MET THR LYS          
SEQRES   8 I  432  LEU GLY ALA CYS ASN ASP THR LEU GLN GLN LEU MET GLU          
SEQRES   9 I  432  VAL PHE LYS PHE ASP THR ILE SER GLU LYS THR SER ASP          
SEQRES  10 I  432  GLN ILE HIS PHE PHE PHE ALA LYS LEU ASN CYS ARG LEU          
SEQRES  11 I  432  TYR ARG LYS ALA ASN LYS ALA SER LYS LEU VAL SER ALA          
SEQRES  12 I  432  ASN ARG LEU PHE GLY ASP LYS SER LEU THR PHE ASN GLU          
SEQRES  13 I  432  THR TYR GLN ASP ILE SER GLU LEU VAL TYR GLY ALA LYS          
SEQRES  14 I  432  LEU GLN PRO LEU ASP PHE LYS GLU ASN ALA GLU GLN SER          
SEQRES  15 I  432  ARG ALA ALA ILE ASN LYS TRP VAL SER ASN LYS THR GLU          
SEQRES  16 I  432  GLY ARG ILE THR ASP VAL ILE PRO SER GLU ALA ILE ASN          
SEQRES  17 I  432  GLU LEU THR VAL LEU VAL LEU VAL ASN THR ILE TYR PHE          
SEQRES  18 I  432  LYS GLY LEU TRP LYS SER LYS PHE SER PRO GLU ASN THR          
SEQRES  19 I  432  ARG LYS GLU LEU PHE TYR LYS ALA ASP GLY GLU SER CYS          
SEQRES  20 I  432  SER ALA SER MET MET TYR GLN GLU GLY LYS PHE ARG TYR          
SEQRES  21 I  432  ARG ARG VAL ALA GLU GLY THR GLN VAL LEU GLU LEU PRO          
SEQRES  22 I  432  PHE LYS GLY ASP ASP ILE THR MET VAL LEU ILE LEU PRO          
SEQRES  23 I  432  LYS PRO GLU LYS SER LEU ALA LYS VAL GLU LYS GLU LEU          
SEQRES  24 I  432  THR PRO GLU VAL LEU GLN GLU TRP LEU ASP GLU LEU GLU          
SEQRES  25 I  432  GLU MET MET LEU CYS VAL HIS MET PRO ARG PHE ARG ILE          
SEQRES  26 I  432  GLU ASP GLY PHE SER LEU LYS GLU GLN LEU GLN ASP MET          
SEQRES  27 I  432  GLY LEU VAL ASP LEU PHE SER PRO GLU LYS SER LYS LEU          
SEQRES  28 I  432  PRO GLY ILE VAL ALA GLU GLY ARG ASP ASP LEU TYR VAL          
SEQRES  29 I  432  SER ASP ALA PHE HIS LYS ALA PHE LEU GLU VAL ASN GLU          
SEQRES  30 I  432  GLU GLY SER GLU ALA ALA ALA SER THR ALA VAL VAL ILE          
SEQRES  31 I  432  ALA GLY ARG SER LEU ASN PRO ASN ARG VAL CYS PHE LYS          
SEQRES  32 I  432  ALA ASN ARG PRO PHE LEU VAL PHE ILE ARG GLU VAL PRO          
SEQRES  33 I  432  LEU ASN THR ILE ILE PHE MET GLY ARG VAL ALA ASN PRO          
SEQRES  34 I  432  CYS VAL LYS                                                  
MODRES 1TB6 ASN H   60G ASN  GLYCOSYLATION SITE                                 
MODRES 1TB6 ASN I   96  ASN  GLYCOSYLATION SITE                                 
MODRES 1TB6 ASN I  155  ASN  GLYCOSYLATION SITE                                 
MODRES 1TB6 ASN I  192  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A   1      14                                                       
HET    NAG  A   2      14                                                       
HET    FUC  A   3      10                                                       
HET    GU3  B   1      22                                                       
HET    GU2  B   2      14                                                       
HET    GU6  B   3      23                                                       
HET    GU1  B   4      14                                                       
HET    GU5  B   5      17                                                       
HET    GU8  B   6      14                                                       
HET    GU9  B   7      14                                                       
HET    GU8  B   8      14                                                       
HET    GU9  B   9      14                                                       
HET    GU8  B  10      14                                                       
HET    GU9  B  11      14                                                       
HET    GU8  B  12      14                                                       
HET    GU5  B  13      17                                                       
HET    GU0  B  14      23                                                       
HET    GU6  B  15      23                                                       
HET    GU4  B  16      27                                                       
HET    NAG  C   1      14                                                       
HET    NAG  C   2      14                                                       
HET    BMA  C   3      11                                                       
HET    MAN  C   4      11                                                       
HET    MAN  C   5      11                                                       
HET    NAG  D   1      14                                                       
HET    NAG  D   2      14                                                       
HET    BMA  D   3      11                                                       
HET    MPD  H 781       8                                                       
HET    MPD  H 782       8                                                       
HET    MPD  H 783       8                                                       
HET    MPD  H 784       8                                                       
HET    NAG  I 801      14                                                       
HET    MPD  I 864       8                                                       
HET    MPD  I 865       8                                                       
HET    MPD  I 866       8                                                       
HET    MPD  I 867       8                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     FUC ALPHA-L-FUCOPYRANOSE                                             
HETNAM     GU3 METHYL 3-O-METHYL-2,6-DI-O-SULFO-ALPHA-D-                        
HETNAM   2 GU3  GLUCOPYRANOSIDE                                                 
HETNAM     GU2 2,3-DI-O-METHYL-ALPHA-L-IDOPYRANURONIC ACID                      
HETNAM     GU6 2,3,6-TRI-O-SULFO-ALPHA-D-GLUCOPYRANOSE                          
HETNAM     GU1 2,3-DI-O-METHYL-BETA-D-GLUCOPYRANURONIC ACID                     
HETNAM     GU5 2,3-DI-O-METHYL-6-O-SULFONATO-ALPHA-D-GLUCOPYRANOSE              
HETNAM     GU8 2,3,6-TRI-O-METHYL-BETA-D-GLUCOPYRANOSE                          
HETNAM     GU9 2,3,6-TRI-O-METHYL-ALPHA-D-GLUCOPYRANOSE                         
HETNAM     GU0 2,3,6-TRI-O-SULFONATO-BETA-D-GLUCOPYRANOSE                       
HETNAM     GU4 2,3,4,6-TETRA-O-SULFONATO-ALPHA-D-GLUCOPYRANOSE                  
HETNAM     BMA BETA-D-MANNOPYRANOSE                                             
HETNAM     MAN ALPHA-D-MANNOPYRANOSE                                            
HETNAM     MPD (4S)-2-METHYL-2,4-PENTANEDIOL                                    
FORMUL   4  NAG    7(C8 H15 N O6)                                               
FORMUL   4  FUC    C6 H12 O5                                                    
FORMUL   5  GU3    C8 H16 O12 S2                                                
FORMUL   5  GU2    C8 H14 O7                                                    
FORMUL   5  GU6    2(C6 H12 O15 S3)                                             
FORMUL   5  GU1    C8 H14 O7                                                    
FORMUL   5  GU5    2(C8 H15 O9 S 1-)                                            
FORMUL   5  GU8    4(C9 H18 O6)                                                 
FORMUL   5  GU9    3(C9 H18 O6)                                                 
FORMUL   5  GU0    C6 H9 O15 S3 3-                                              
FORMUL   5  GU4    C6 H12 O18 S4                                                
FORMUL   6  BMA    2(C6 H12 O6)                                                 
FORMUL   6  MAN    2(C6 H12 O6)                                                 
FORMUL   8  MPD    8(C6 H14 O2)                                                 
FORMUL  17  HOH   *146(H2 O)                                                    
HELIX    1   1 ASN L    1K GLY L    1F 1                                   6    
HELIX    2   2 PHE L    7  SER L   11  5                                   5    
HELIX    3   3 GLU L   14C TYR L   14J 1                                   8    
HELIX    4   4 ALA H   55  CYS H   58  5                                   4    
HELIX    5   5 PRO H   60B ASP H   60E 5                                   4    
HELIX    6   6 THR H   60I ASN H   62  5                                   3    
HELIX    7   7 ASP H  125  LEU H  130  1                                   9    
HELIX    8   8 GLU H  164  THR H  172  1                                   9    
HELIX    9   9 LYS H  185  GLY H  186C 5                                   5    
HELIX   10  10 LEU H  234  GLY H  246  1                                  13    
HELIX   11  11 LYS I   11  ILE I   15  5                                   5    
HELIX   12  12 ASN I   45  ASP I   68  1                                  24    
HELIX   13  13 SER I   79  LEU I   92  1                                  14    
HELIX   14  14 CYS I   95  PHE I  106  1                                  12    
HELIX   15  15 SER I  112  GLN I  118  1                                   7    
HELIX   16  16 GLN I  118  ASN I  135  1                                  18    
HELIX   17  17 ASN I  155  TYR I  166  1                                  12    
HELIX   18  18 ASN I  178  THR I  194  1                                  17    
HELIX   19  19 SER I  230  THR I  234  5                                   5    
HELIX   20  20 ALA I  264  GLY I  266  5                                   3    
HELIX   21  21 SER I  291  LEU I  299  1                                   9    
HELIX   22  22 THR I  300  LEU I  311  1                                  12    
HELIX   23  23 LEU I  331  MET I  338  1                                   8    
HELIX   24  24 VAL I  341  SER I  345  5                                   5    
SHEET    1   A 7 SER H  20  ASP H  21  0                                        
SHEET    2   A 7 GLN H 156  PRO H 161 -1  O  VAL H 157   N  SER H  20           
SHEET    3   A 7 LYS H 135  GLY H 140 -1  N  GLY H 136   O  LEU H 160           
SHEET    4   A 7 PRO H 198  LYS H 202 -1  O  VAL H 200   N  ARG H 137           
SHEET    5   A 7 TRP H 207  TRP H 215 -1  O  GLY H 211   N  PHE H 199           
SHEET    6   A 7 GLY H 226  HIS H 230 -1  O  PHE H 227   N  TRP H 215           
SHEET    7   A 7 MET H 180  ALA H 183 -1  N  PHE H 181   O  TYR H 228           
SHEET    1   B 7 LYS H  81  SER H  83  0                                        
SHEET    2   B 7 LEU H  64  ILE H  68 -1  N  ILE H  68   O  LYS H  81           
SHEET    3   B 7 GLN H  30  ARG H  35 -1  N  PHE H  34   O  LEU H  65           
SHEET    4   B 7 GLU H  39  LEU H  46 -1  O  ALA H  44   N  VAL H  31           
SHEET    5   B 7 TRP H  51  THR H  54 -1  O  LEU H  53   N  SER H  45           
SHEET    6   B 7 ALA H 104  LEU H 108 -1  O  MET H 106   N  VAL H  52           
SHEET    7   B 7 LEU H  85  ILE H  90 -1  N  TYR H  89   O  LEU H 105           
SHEET    1   C 2 LEU H  60  TYR H  60A 0                                        
SHEET    2   C 2 LYS H  60F ASN H  60G-1  O  LYS H  60F  N  TYR H  60A          
SHEET    1   D 7 ILE I  76  LEU I  78  0                                        
SHEET    2   D 7 THR I 419  VAL I 426 -1  O  MET I 423   N  LEU I  78           
SHEET    3   D 7 PHE I 408  GLU I 414 -1  N  PHE I 408   O  VAL I 426           
SHEET    4   D 7 ILE I 279  LEU I 285 -1  N  VAL I 282   O  PHE I 411           
SHEET    5   D 7 GLN I 268  PRO I 273 -1  N  GLN I 268   O  LEU I 285           
SHEET    6   D 7 SER I 248  ARG I 262 -1  N  ARG I 261   O  VAL I 269           
SHEET    7   D 7 ARG I 235  LEU I 238 -1  N  ARG I 235   O  MET I 251           
SHEET    1   E 8 ILE I  76  LEU I  78  0                                        
SHEET    2   E 8 THR I 419  VAL I 426 -1  O  MET I 423   N  LEU I  78           
SHEET    3   E 8 PHE I 408  GLU I 414 -1  N  PHE I 408   O  VAL I 426           
SHEET    4   E 8 ILE I 279  LEU I 285 -1  N  VAL I 282   O  PHE I 411           
SHEET    5   E 8 GLN I 268  PRO I 273 -1  N  GLN I 268   O  LEU I 285           
SHEET    6   E 8 SER I 248  ARG I 262 -1  N  ARG I 261   O  VAL I 269           
SHEET    7   E 8 GLU I 312  PRO I 321 -1  O  MET I 320   N  MET I 252           
SHEET    8   E 8 VAL I 400  LYS I 403  1  O  PHE I 402   N  HIS I 319           
SHEET    1   F 5 GLN I 171  LEU I 173  0                                        
SHEET    2   F 5 LYS I 139  ASP I 149  1  N  GLY I 148   O  LEU I 173           
SHEET    3   F 5 LEU I 213  LYS I 222 -1  O  TYR I 220   N  VAL I 141           
SHEET    4   F 5 ASP I 366  VAL I 375  1  O  PHE I 368   N  LEU I 215           
SHEET    5   F 5 PHE I 323  SER I 330 -1  N  PHE I 323   O  VAL I 375           
SSBOND   1 CYS L    1    CYS H  122                          1555   1555  2.03  
SSBOND   2 CYS H   42    CYS H   58                          1555   1555  2.03  
SSBOND   3 CYS H  168    CYS H  182                          1555   1555  2.04  
SSBOND   4 CYS H  191    CYS H  220                          1555   1555  2.05  
SSBOND   5 CYS I    8    CYS I  128                          1555   1555  2.04  
SSBOND   6 CYS I   21    CYS I   95                          1555   1555  2.04  
SSBOND   7 CYS I  247    CYS I  430                          1555   1555  2.03  
SSBOND   8 CYS I  317    CYS I  401                          1555   1555  2.06  
LINK         ND2 ASN H  60G                C1  NAG A   1     1555   1555  1.45  
LINK         ND2 ASN I  96                 C1  NAG I 801     1555   1555  1.46  
LINK         ND2 ASN I 155                 C1  NAG C   1     1555   1555  1.45  
LINK         ND2 ASN I 192                 C1  NAG D   1     1555   1555  1.45  
LINK         O4  NAG A   1                 C1  NAG A   2     1555   1555  1.40  
LINK         O6  NAG A   1                 C1  FUC A   3     1555   1555  1.41  
LINK         O4  GU3 B   1                 C1  GU2 B   2     1555   1555  1.44  
LINK         O4  GU2 B   2                 C1  GU6 B   3     1555   1555  1.44  
LINK         O4  GU6 B   3                 C1  GU1 B   4     1555   1555  1.44  
LINK         O4  GU1 B   4                 C1  GU5 B   5     1555   1555  1.44  
LINK         O4  GU5 B   5                 C1  GU8 B   6     1555   1555  1.43  
LINK         O4  GU8 B   6                 C1  GU9 B   7     1555   1555  1.44  
LINK         O4  GU9 B   7                 C1  GU8 B   8     1555   1555  1.44  
LINK         O4  GU8 B   8                 C1  GU9 B   9     1555   1555  1.44  
LINK         O4  GU9 B   9                 C1  GU8 B  10     1555   1555  1.44  
LINK         O4  GU8 B  10                 C1  GU9 B  11     1555   1555  1.44  
LINK         O4  GU9 B  11                 C1  GU8 B  12     1555   1555  1.43  
LINK         O4  GU8 B  12                 C1  GU5 B  13     1555   1555  1.44  
LINK         O4  GU5 B  13                 C1  GU0 B  14     1555   1555  1.44  
LINK         O4  GU0 B  14                 C1  GU6 B  15     1555   1555  1.44  
LINK         O4  GU6 B  15                 C1  GU4 B  16     1555   1555  1.44  
LINK         O4  NAG C   1                 C1  NAG C   2     1555   1555  1.38  
LINK         O4  NAG C   2                 C1  BMA C   3     1555   1555  1.38  
LINK         O3  BMA C   3                 C1  MAN C   4     1555   1555  1.41  
LINK         O6  BMA C   3                 C1  MAN C   5     1555   1555  1.40  
LINK         O4  NAG D   1                 C1  NAG D   2     1555   1555  1.39  
LINK         O4  NAG D   2                 C1  BMA D   3     1555   1555  1.40  
CISPEP   1 SER H   36A   PRO H   37          0        -0.14                     
CRYST1   88.409   88.404  117.218  90.00  90.00  90.00 P 21 21 21    4          
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      0.011311  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011312  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008531        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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