HEADER CELL ADHESION 11-FEB-07 2OUH
TITLE CRYSTAL STRUCTURE OF THE THROMBOSPONDIN-1 N-TERMINAL DOMAIN IN COMPLEX
TITLE 2 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 ADHESION
EXPDTA X-RAY DIFFRACTION
AUTHOR K.TAN,A.JOACHIMIAK,J.WANG,J.LAWLER
REVDAT 4 30-AUG-23 2OUH 1 REMARK SEQADV
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,A.JOACHIMIAK,
JRNL AUTH 2 J.T.GALLAGHER,A.C.RIGBY,J.H.WANG,J.LAWLER
JRNL TITL HEPARIN-INDUCED CIS- AND TRANS-DIMERIZATION MODES OF THE
JRNL TITL 2 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 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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) : 1.629
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 CHEMICALLY
REMARK 3 HETEROGENEOUS AND PARTIALLY DISORDERED IN THE STRUCTURE. AUTHORS
REMARK 3 WERE ABLE TO IDENTIFY ONLY SOME SO4 GROUPS FROM THE HEPARIN BUT
REMARK 3 NOT THE HEPARIN BACKBONE DUE TO ITS POSSIBLE MOBILITY. INSTEAD,
REMARK 3 THERE ARE SEVERAL WATER MOLECULES BEING POSITIONED INTO SOME
REMARK 3 UNCHARACTERIZED DENSITIES NEAR HEPARIN BINDING SITES. THESE
REMARK 3 DENSITIES ARE LIKELY FROM PARTIALLY DISORDERED HEPARIN DP10, NOT
REMARK 3 NECESSARILY FROM WATER MOLECULES. INCLUDING OF THESE WATERS IN
REMARK 3 THE MODEL WAS JUST FOR THE REFINEMENT PURPOSES.
REMARK 4
REMARK 4 2OUH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-FEB-07.
REMARK 100 THE DEPOSITION ID IS D_1000041600.
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, PH
REMARK 280 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
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 249
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 250
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 248
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 249
REMARK 800
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 IN
REMARK 900 COMPLEX WITH ARIXTRA
REMARK 900 RELATED ID: 2OUJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE THROMBOSPONDIN-1 N-TERMINAL DOMAIN IN
REMARK 900 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
