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Database: PDB
Entry: 2OUH
LinkDB: 2OUH
Original site: 2OUH 
HEADER    CELL ADHESION                           11-FEB-07   2OUH              
TITLE     CRYSTAL STRUCTURE OF THE THROMBOSPONDIN-1 N-TERMINAL DOMAIN           
TITLE    2 IN COMPLEX WITH FRACTIONATED HEPARIN DP10                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: THROMBOSPONDIN-1;                                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: N-TERMINAL DOMAIN;                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: THBS1, TSP, TSP1;                                              
SOURCE   6 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;                          
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FRUIT FLY;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7227;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: DROSOPHILA S2 CELL;                        
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PMT/BIP/V5-HIS A                          
KEYWDS    TSP-1, TSPN-1, HBD, FRACTIONATED HEPARIN, DP10, CELL                  
KEYWDS   2 ADHESION                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.TAN,A.JOACHIMIAK,J.WANG,J.LAWLER                                    
REVDAT   3   24-FEB-09 2OUH    1       VERSN                                    
REVDAT   2   19-FEB-08 2OUH    1       JRNL                                     
REVDAT   1   08-JAN-08 2OUH    0                                                
JRNL        AUTH   K.TAN,M.DUQUETTE,J.H.LIU,K.SHANMUGASUNDARAM,                 
JRNL        AUTH 2 A.JOACHIMIAK,J.T.GALLAGHER,A.C.RIGBY,J.H.WANG,               
JRNL        AUTH 3 J.LAWLER                                                     
JRNL        TITL   HEPARIN-INDUCED CIS- AND TRANS-DIMERIZATION MODES            
JRNL        TITL 2 OF THE THROMBOSPONDIN-1 N-TERMINAL DOMAIN.                   
JRNL        REF    J.BIOL.CHEM.                  V. 283  3932 2008              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   18065761                                                     
JRNL        DOI    10.1074/JBC.M705203200                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
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 : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 100.00                         
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)   (%) : 85.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 14228                          
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 SET) : 0.253                           
REMARK   3   FREE R VALUE                     : 0.296                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1140                            
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) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.48                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3270                       
REMARK   3   BIN FREE R VALUE                    : 0.3690                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 57                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3146                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 30                                      
REMARK   3   SOLVENT ATOMS            : 87                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
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) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : 1.63                            
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: FRACTIONATED HEPARIN DP10 IS              
REMARK   3  CHEMICALLY HETEROGENEOUS AND PARTIALLY DISORDERED IN THE            
REMARK   3  STRUCTURE. AUTHORS WERE ABLE TO IDENTIFY ONLY SOME SO4 GROUPS       
REMARK   3  FROM THE HEPARIN BUT NOT THE HEPARIN BACKBONE DUE TO ITS            
REMARK   3  POSSIBLE MOBILITY. INSTEAD, THERE ARE SEVERAL WATER MOLECULES       
REMARK   3  BEING POSITIONED INTO SOME UNCHARACTERIZED DENSITIES NEAR           
REMARK   3  HEPARIN BINDING SITES. THESE DENSITIES ARE LIKELY FROM              
REMARK   3  PARTIALLY DISORDERED HEPARIN DP10, NOT NECESSARILY FROM WATER       
REMARK   3  MOLECULES. INCLUDING OF THESE WATERS IN THE MODEL WAS JUST FOR      
REMARK   3  THE REFINEMENT PURPOSES.                                            
REMARK   4                                                                      
REMARK   4 2OUH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-FEB-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB041600.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-NOV-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.99187                            
REMARK 200  MONOCHROMATOR                  : SI 111 CRYSTAL                     
REMARK 200  OPTICS                         : MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14771                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.8                               
REMARK 200  DATA REDUNDANCY                : 4.400                              
REMARK 200  R MERGE                    (I) : 0.04600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 29.8700                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 65.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.26800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.630                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1Z78                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 32.24                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.82                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG1500, 0.08M SODIUM ACETATE,       
REMARK 280  PH 4.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K             
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       20.15800            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      120.88950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       20.53450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      120.88950            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       20.15800            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       20.53450            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: TSPN-1 IS A MONOMER BY ITSELF. IN PRESENCE OF DP10, IT       
REMARK 300 FORMS A HEPARIN-LINKED DIMER.                                        
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     ARG A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     PRO A    -1                                                      
REMARK 465     TRP A     0                                                      
REMARK 465     ASN A     1                                                      
REMARK 465     ARG A     2                                                      
REMARK 465     ILE A     3                                                      
REMARK 465     PRO A     4                                                      
REMARK 465     GLU A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     GLY A     7                                                      
REMARK 465     GLY A     8                                                      
REMARK 465     ASP A     9                                                      
REMARK 465     ASN A    10                                                      
REMARK 465     SER A    11                                                      
REMARK 465     SER A   215                                                      
REMARK 465     SER A   216                                                      
REMARK 465     SER A   217                                                      
REMARK 465     THR A   218                                                      
REMARK 465     SER A   219                                                      
REMARK 465     VAL A   220                                                      
REMARK 465     LEU A   221                                                      
REMARK 465     LEU A   222                                                      
REMARK 465     THR A   223                                                      
REMARK 465     LEU A   224                                                      
REMARK 465     ASP A   225                                                      
REMARK 465     ASN A   226                                                      
REMARK 465     ASN A   227                                                      
REMARK 465     VAL A   228                                                      
REMARK 465     VAL A   229                                                      
REMARK 465     ASN A   230                                                      
REMARK 465     GLY A   231                                                      
REMARK 465     SER A   232                                                      
REMARK 465     SER A   233                                                      
REMARK 465     PRO A   234                                                      
REMARK 465     ALA A   235                                                      
REMARK 465     ILE A   236                                                      
REMARK 465     ARG A   237                                                      
REMARK 465     THR A   238                                                      
REMARK 465     ASN A   239                                                      
REMARK 465     THR A   240                                                      
REMARK 465     GLY A   241                                                      
REMARK 465     HIS A   242                                                      
REMARK 465     HIS A   243                                                      
REMARK 465     HIS A   244                                                      
REMARK 465     HIS A   245                                                      
REMARK 465     HIS A   246                                                      
REMARK 465     HIS A   247                                                      
REMARK 465     ARG B    -3                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     PRO B    -1                                                      
REMARK 465     TRP B     0                                                      
REMARK 465     ASN B     1                                                      
REMARK 465     ARG B     2                                                      
REMARK 465     ILE B     3                                                      
REMARK 465     PRO B     4                                                      
REMARK 465     GLU B     5                                                      
REMARK 465     SER B     6                                                      
REMARK 465     GLY B     7                                                      
REMARK 465     GLY B     8                                                      
REMARK 465     ASP B     9                                                      
REMARK 465     ASN B    10                                                      
REMARK 465     SER B    11                                                      
REMARK 465     SER B   215                                                      
REMARK 465     SER B   216                                                      
REMARK 465     SER B   217                                                      
REMARK 465     THR B   218                                                      
REMARK 465     SER B   219                                                      
REMARK 465     VAL B   220                                                      
REMARK 465     LEU B   221                                                      
REMARK 465     LEU B   222                                                      
REMARK 465     THR B   223                                                      
REMARK 465     LEU B   224                                                      
REMARK 465     ASP B   225                                                      
REMARK 465     ASN B   226                                                      
REMARK 465     ASN B   227                                                      
REMARK 465     VAL B   228                                                      
REMARK 465     VAL B   229                                                      
REMARK 465     ASN B   230                                                      
REMARK 465     GLY B   231                                                      
REMARK 465     SER B   232                                                      
REMARK 465     SER B   233                                                      
REMARK 465     PRO B   234                                                      
REMARK 465     ALA B   235                                                      
REMARK 465     ILE B   236                                                      
REMARK 465     ARG B   237                                                      
REMARK 465     THR B   238                                                      
REMARK 465     ASN B   239                                                      
REMARK 465     THR B   240                                                      
REMARK 465     GLY B   241                                                      
REMARK 465     HIS B   242                                                      
REMARK 465     HIS B   243                                                      
REMARK 465     HIS B   244                                                      
REMARK 465     HIS B   245                                                      
REMARK 465     HIS B   246                                                      
REMARK 465     HIS B   247                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A  87   CA  -  CB  -  CG  ANGL. DEV. =  15.4 DEGREES          
REMARK 500    THR A 132   N   -  CA  -  C   ANGL. DEV. = -16.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A  23       52.60   -140.72                                   
REMARK 500    LYS A  24      131.31   -173.00                                   
REMARK 500    SER A  26     -137.33   -126.65                                   
REMARK 500    VAL A  31     -166.96   -129.46                                   
REMARK 500    PRO A  53      154.89    -49.01                                   
REMARK 500    ALA A  74      142.24   -171.08                                   
REMARK 500    HIS A  94       96.48    -12.46                                   
REMARK 500    SER A  95      -47.18   -159.69                                   
REMARK 500    GLN A 117       73.16     48.78                                   
REMARK 500    ALA A 131       42.19    -77.82                                   
REMARK 500    GLU A 144     -126.75     58.25                                   
REMARK 500    ASP A 152     -115.23     52.53                                   
REMARK 500    LEU A 173      -49.13    -26.53                                   
REMARK 500    VAL A 186      -10.78     63.80                                   
REMARK 500    ASN A 187       15.26   -158.99                                   
REMARK 500    ASN A 211        0.60    -58.22                                   
REMARK 500    THR B  19     -136.91   -102.75                                   
REMARK 500    ARG B  23      -17.82     72.97                                   
REMARK 500    LEU B  30      104.33    -55.52                                   
REMARK 500    VAL B  31     -160.89   -118.20                                   
REMARK 500    ALA B  74      139.12   -171.56                                   
REMARK 500    ASP B  93       20.35    -76.95                                   
REMARK 500    HIS B  94       16.38     46.28                                   
REMARK 500    GLU B 144     -115.25     62.30                                   
REMARK 500    ASP B 152     -100.10     71.43                                   
REMARK 500    LYS B 155      132.10    -21.05                                   
REMARK 500    ASP B 172       30.50     71.15                                   
REMARK 500    ALA B 174        7.19    -67.78                                   
REMARK 500    ASN B 211       16.23    -67.64                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 248                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 249                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 250                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 248                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 249                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 250                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1Z78   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE THROMBOSPONDIN-1 N-TERMINAL DOMAIN          
REMARK 900 RELATED ID: 1ZA4   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE THROMBOSPONDIN-1 N-TERMINAL DOMAIN          
REMARK 900 IN COMPLEX WITH ARIXTRA                                              
REMARK 900 RELATED ID: 2OUJ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE THROMBOSPONDIN-1 N-TERMINAL DOMAIN          
REMARK 900 IN COMPLEX WITH FRACTIONATED HEPARIN DP8                             
DBREF  2OUH A    1   239  UNP    P07996   TSP1_HUMAN      19    257             
DBREF  2OUH B    1   239  UNP    P07996   TSP1_HUMAN      19    257             
SEQADV 2OUH ARG A   -3  UNP  P07996              EXPRESSION TAG                 
SEQADV 2OUH SER A   -2  UNP  P07996              EXPRESSION TAG                 
SEQADV 2OUH PRO A   -1  UNP  P07996              EXPRESSION TAG                 
SEQADV 2OUH TRP A    0  UNP  P07996              EXPRESSION TAG                 
SEQADV 2OUH THR A   66  UNP  P07996    ALA    84 VARIANT                        
SEQADV 2OUH THR A  240  UNP  P07996              EXPRESSION TAG                 
SEQADV 2OUH GLY A  241  UNP  P07996              EXPRESSION TAG                 
SEQADV 2OUH HIS A  242  UNP  P07996              EXPRESSION TAG                 
SEQADV 2OUH HIS A  243  UNP  P07996              EXPRESSION TAG                 
SEQADV 2OUH HIS A  244  UNP  P07996              EXPRESSION TAG                 
SEQADV 2OUH HIS A  245  UNP  P07996              EXPRESSION TAG                 
SEQADV 2OUH HIS A  246  UNP  P07996              EXPRESSION TAG                 
SEQADV 2OUH HIS A  247  UNP  P07996              EXPRESSION TAG                 
SEQADV 2OUH ARG B   -3  UNP  P07996              EXPRESSION TAG                 
SEQADV 2OUH SER B   -2  UNP  P07996              EXPRESSION TAG                 
SEQADV 2OUH PRO B   -1  UNP  P07996              EXPRESSION TAG                 
SEQADV 2OUH TRP B    0  UNP  P07996              EXPRESSION TAG                 
SEQADV 2OUH THR B   66  UNP  P07996    ALA    84 VARIANT                        
SEQADV 2OUH THR B  240  UNP  P07996              EXPRESSION TAG                 
SEQADV 2OUH GLY B  241  UNP  P07996              EXPRESSION TAG                 
SEQADV 2OUH HIS B  242  UNP  P07996              EXPRESSION TAG                 
SEQADV 2OUH HIS B  243  UNP  P07996              EXPRESSION TAG                 
SEQADV 2OUH HIS B  244  UNP  P07996              EXPRESSION TAG                 
SEQADV 2OUH HIS B  245  UNP  P07996              EXPRESSION TAG                 
SEQADV 2OUH HIS B  246  UNP  P07996              EXPRESSION TAG                 
SEQADV 2OUH HIS B  247  UNP  P07996              EXPRESSION TAG                 
SEQRES   1 A  251  ARG SER PRO TRP ASN ARG ILE PRO GLU SER GLY GLY ASP          
SEQRES   2 A  251  ASN SER VAL PHE ASP ILE PHE GLU LEU THR GLY ALA ALA          
SEQRES   3 A  251  ARG LYS GLY SER GLY ARG ARG LEU VAL LYS GLY PRO ASP          
SEQRES   4 A  251  PRO SER SER PRO ALA PHE ARG ILE GLU ASP ALA ASN LEU          
SEQRES   5 A  251  ILE PRO PRO VAL PRO ASP ASP LYS PHE GLN ASP LEU VAL          
SEQRES   6 A  251  ASP ALA VAL ARG THR GLU LYS GLY PHE LEU LEU LEU ALA          
SEQRES   7 A  251  SER LEU ARG GLN MET LYS LYS THR ARG GLY THR LEU LEU          
SEQRES   8 A  251  ALA LEU GLU ARG LYS ASP HIS SER GLY GLN VAL PHE SER          
SEQRES   9 A  251  VAL VAL SER ASN GLY LYS ALA GLY THR LEU ASP LEU SER          
SEQRES  10 A  251  LEU THR VAL GLN GLY LYS GLN HIS VAL VAL SER VAL GLU          
SEQRES  11 A  251  GLU ALA LEU LEU ALA THR GLY GLN TRP LYS SER ILE THR          
SEQRES  12 A  251  LEU PHE VAL GLN GLU ASP ARG ALA GLN LEU TYR ILE ASP          
SEQRES  13 A  251  CYS GLU LYS MET GLU ASN ALA GLU LEU ASP VAL PRO ILE          
SEQRES  14 A  251  GLN SER VAL PHE THR ARG ASP LEU ALA SER ILE ALA ARG          
SEQRES  15 A  251  LEU ARG ILE ALA LYS GLY GLY VAL ASN ASP ASN PHE GLN          
SEQRES  16 A  251  GLY VAL LEU GLN ASN VAL ARG PHE VAL PHE GLY THR THR          
SEQRES  17 A  251  PRO GLU ASP ILE LEU ARG ASN LYS GLY CYS SER SER SER          
SEQRES  18 A  251  THR SER VAL LEU LEU THR LEU ASP ASN ASN VAL VAL ASN          
SEQRES  19 A  251  GLY SER SER PRO ALA ILE ARG THR ASN THR GLY HIS HIS          
SEQRES  20 A  251  HIS HIS HIS HIS                                              
SEQRES   1 B  251  ARG SER PRO TRP ASN ARG ILE PRO GLU SER GLY GLY ASP          
SEQRES   2 B  251  ASN SER VAL PHE ASP ILE PHE GLU LEU THR GLY ALA ALA          
SEQRES   3 B  251  ARG LYS GLY SER GLY ARG ARG LEU VAL LYS GLY PRO ASP          
SEQRES   4 B  251  PRO SER SER PRO ALA PHE ARG ILE GLU ASP ALA ASN LEU          
SEQRES   5 B  251  ILE PRO PRO VAL PRO ASP ASP LYS PHE GLN ASP LEU VAL          
SEQRES   6 B  251  ASP ALA VAL ARG THR GLU LYS GLY PHE LEU LEU LEU ALA          
SEQRES   7 B  251  SER LEU ARG GLN MET LYS LYS THR ARG GLY THR LEU LEU          
SEQRES   8 B  251  ALA LEU GLU ARG LYS ASP HIS SER GLY GLN VAL PHE SER          
SEQRES   9 B  251  VAL VAL SER ASN GLY LYS ALA GLY THR LEU ASP LEU SER          
SEQRES  10 B  251  LEU THR VAL GLN GLY LYS GLN HIS VAL VAL SER VAL GLU          
SEQRES  11 B  251  GLU ALA LEU LEU ALA THR GLY GLN TRP LYS SER ILE THR          
SEQRES  12 B  251  LEU PHE VAL GLN GLU ASP ARG ALA GLN LEU TYR ILE ASP          
SEQRES  13 B  251  CYS GLU LYS MET GLU ASN ALA GLU LEU ASP VAL PRO ILE          
SEQRES  14 B  251  GLN SER VAL PHE THR ARG ASP LEU ALA SER ILE ALA ARG          
SEQRES  15 B  251  LEU ARG ILE ALA LYS GLY GLY VAL ASN ASP ASN PHE GLN          
SEQRES  16 B  251  GLY VAL LEU GLN ASN VAL ARG PHE VAL PHE GLY THR THR          
SEQRES  17 B  251  PRO GLU ASP ILE LEU ARG ASN LYS GLY CYS SER SER SER          
SEQRES  18 B  251  THR SER VAL LEU LEU THR LEU ASP ASN ASN VAL VAL ASN          
SEQRES  19 B  251  GLY SER SER PRO ALA ILE ARG THR ASN THR GLY HIS HIS          
SEQRES  20 B  251  HIS HIS HIS HIS                                              
HET    SO4  A 248       5                                                       
HET    SO4  A 249       5                                                       
HET    SO4  A 250       5                                                       
HET    SO4  B 248       5                                                       
HET    SO4  B 249       5                                                       
HET    SO4  B 250       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  SO4    6(O4 S 2-)                                                   
FORMUL   9  HOH   *87(H2 O)                                                     
HELIX    1   1 ILE A   15  GLY A   20  1                                   6    
HELIX    2   2 ALA A   21  LYS A   24  5                                   4    
HELIX    3   3 ASP A   45  ILE A   49  5                                   5    
HELIX    4   4 PRO A   53  LYS A   68  1                                  16    
HELIX    5   5 PRO A  164  PHE A  169  1                                   6    
HELIX    6   6 ASP A  172  ILE A  176  1                                   5    
HELIX    7   7 THR A  204  ASN A  211  1                                   8    
HELIX    8   8 ILE B   15  THR B   19  1                                   5    
HELIX    9   9 ASP B   45  ILE B   49  5                                   5    
HELIX   10  10 PRO B   53  LYS B   68  1                                  16    
HELIX   11  11 PRO B  164  VAL B  168  5                                   5    
HELIX   12  12 ASP B  172  SER B  175  5                                   4    
HELIX   13  13 THR B  204  ASN B  211  1                                   8    
SHEET    1   A 4 PHE A  13  ASP A  14  0                                        
SHEET    2   A 4 GLY A 192  VAL A 200 -1  O  PHE A 199   N  PHE A  13           
SHEET    3   A 4 ALA A  40  ILE A  43 -1  N  ILE A  43   O  GLY A 192           
SHEET    4   A 4 ARG A  28  VAL A  31 -1  N  VAL A  31   O  ALA A  40           
SHEET    1   B 6 PHE A  13  ASP A  14  0                                        
SHEET    2   B 6 GLY A 192  VAL A 200 -1  O  PHE A 199   N  PHE A  13           
SHEET    3   B 6 GLY A  69  GLN A  78 -1  N  LEU A  73   O  ARG A 198           
SHEET    4   B 6 LYS A 136  GLN A 143 -1  O  LEU A 140   N  LEU A  72           
SHEET    5   B 6 ARG A 146  ILE A 151 -1  O  GLN A 148   N  PHE A 141           
SHEET    6   B 6 GLU A 157  GLU A 160 -1  O  GLU A 157   N  LEU A 149           
SHEET    1   C 5 LYS A 119  VAL A 125  0                                        
SHEET    2   C 5 THR A 109  VAL A 116 -1  N  VAL A 116   O  LYS A 119           
SHEET    3   C 5 GLN A  97  ASN A 104 -1  N  VAL A 102   O  ASP A 111           
SHEET    4   C 5 ARG A  83  ARG A  91 -1  N  GLY A  84   O  SER A 103           
SHEET    5   C 5 ALA A 177  ILE A 181 -1  O  ARG A 180   N  ALA A  88           
SHEET    1   D 4 PHE B  13  ASP B  14  0                                        
SHEET    2   D 4 GLY B 192  VAL B 200 -1  O  PHE B 199   N  PHE B  13           
SHEET    3   D 4 ALA B  40  ILE B  43 -1  N  ILE B  43   O  GLY B 192           
SHEET    4   D 4 LEU B  30  VAL B  31 -1  N  VAL B  31   O  ALA B  40           
SHEET    1   E 6 PHE B  13  ASP B  14  0                                        
SHEET    2   E 6 GLY B 192  VAL B 200 -1  O  PHE B 199   N  PHE B  13           
SHEET    3   E 6 GLY B  69  GLN B  78 -1  N  LEU B  73   O  ARG B 198           
SHEET    4   E 6 TRP B 135  GLN B 143 -1  O  LEU B 140   N  LEU B  72           
SHEET    5   E 6 ARG B 146  ILE B 151 -1  O  GLN B 148   N  PHE B 141           
SHEET    6   E 6 MET B 156  GLU B 160 -1  O  GLU B 157   N  LEU B 149           
SHEET    1   F 5 LYS B 119  VAL B 125  0                                        
SHEET    2   F 5 THR B 109  VAL B 116 -1  N  LEU B 114   O  HIS B 121           
SHEET    3   F 5 GLN B  97  ASN B 104 -1  N  VAL B 102   O  ASP B 111           
SHEET    4   F 5 ARG B  83  ARG B  91 -1  N  GLY B  84   O  SER B 103           
SHEET    5   F 5 ALA B 177  ILE B 181 -1  O  ARG B 180   N  ALA B  88           
SSBOND   1 CYS A  153    CYS A  214                          1555   1555  2.03  
SSBOND   2 CYS B  153    CYS B  214                          1555   1555  2.67  
SITE     1 AC1  5 ARG A  29  VAL A  31  ARG A  42  ARG A  77                    
SITE     2 AC1  5 HOH A 281                                                     
SITE     1 AC2  5 ARG A  42  ARG A  77  MET A  79  GLY A 133                    
SITE     2 AC2  5 HOH A 310                                                     
SITE     1 AC3  3 LYS B  24  PRO B  51  HOH B 265                               
SITE     1 AC4  3 VAL B  31  ARG B  42  VAL B 193                               
SITE     1 AC5  2 ARG B  42  GLU B  44                                          
SITE     1 AC6  5 ARG B  42  GLN B  78  MET B  79  GLN B 191                    
SITE     2 AC6  5 GLY B 192                                                     
CRYST1   40.316   41.069  241.779  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.024804  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.024349  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004136        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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