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HEADER BLOOD CLOTTING 17-MAR-04 1SQ0 TITLE CRYSTAL STRUCTURE OF THE COMPLEX OF THE WILD-TYPE VON TITLE 2 WILLEBRAND FACTOR A1 DOMAIN AND GLYCOPROTEIN IB ALPHA AT TITLE 3 2.6 ANGSTROM RESOLUTION COMPND MOL_ID: 1; COMPND 2 MOLECULE: VON WILLEBRAND FACTOR (VWF) [CONTAINS: VON COMPND 3 WILLEBRAND ANTIGEN II]; COMPND 4 CHAIN: A; COMPND 5 FRAGMENT: A1; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: PLATELET GLYCOPROTEIN IB ALPHA CHAIN COMPND 9 (GLYCOPROTEIN IBALPHA) (GP-IB ALPHA) (GPIBA) (GPIB-ALPHA) COMPND 10 (CD42B-ALPHA) (CD42B) [CONTAINS: GLYCOCALICIN]; COMPND 11 CHAIN: B; COMPND 12 FRAGMENT: GLYCOPROTEIN IB-(ALPHA); COMPND 13 ENGINEERED: YES; COMPND 14 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 GENE: VWF, F8VWF; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21DE3; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_COMMON: HUMAN; SOURCE 12 GENE: GP1BA; SOURCE 13 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 14 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 15 EXPRESSION_SYSTEM_CELL: CHO KEYWDS LEUCINE RICH REPEAT (LRR), RIGHT-HANDED BETA-ALPHA KEYWDS 2 SUPERHELIX); INTEGRIN A (OR I) DOMAIN FOLD EXPDTA X-RAY DIFFRACTION AUTHOR J.J.DUMAS,R.KUMAR,T.MCDONAGH,F.SULLIVAN,M.L.STAHL, AUTHOR 2 W.S.SOMERS,L.MOSYAK REVDAT 2 31-AUG-04 1SQ0 1 JRNL REVDAT 1 13-APR-04 1SQ0 0 JRNL AUTH J.J.DUMAS,R.KUMAR,T.MCDONAGH,F.SULLIVAN,M.L.STAHL, JRNL AUTH 2 W.S.SOMERS,L.MOSYAK JRNL TITL CRYSTAL STRUCTURE OF THE WILD-TYPE VON WILLEBRAND JRNL TITL 2 FACTOR A1-GLYCOPROTEIN IBALPHA COMPLEX REVEALS JRNL TITL 3 CONFORMATION DIFFERENCES WITH A COMPLEX BEARING JRNL TITL 4 VON WILLEBRAND DISEASE MUTATIONS JRNL REF J.BIOL.CHEM. V. 279 23327 2004 JRNL REFN ASTM JBCHA3 US ISSN 0021-9258 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH J.J.DUMAS,R.KUMAR,J.SEEHRA,W.S.SOMERS,L.MOSYAK REMARK 1 TITL CRYSTAL STRUCTURE OF THE GPIB(ALPHA)-THROMBIN REMARK 1 TITL 2 COMPLEX ESSENTIAL FOR PLATELET AGGREGATION REMARK 1 REF SCIENCE V. 301 222 2003 REMARK 1 REFN ASTM SCIEAS US ISSN 0036-8075 REMARK 2 REMARK 2 RESOLUTION. 2.60 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) : 2.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.58 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 132767.560 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.9 REMARK 3 NUMBER OF REFLECTIONS : 17150 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) : 0.190 REMARK 3 FREE R VALUE : 0.239 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.800 REMARK 3 FREE R VALUE TEST SET COUNT : 1685 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 6 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.60 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.76 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 84.00 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2261 REMARK 3 BIN R VALUE (WORKING SET) : 0.2810 REMARK 3 BIN FREE R VALUE : 0.3220 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.90 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 248 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.020 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3666 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 318 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 28.50 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.60 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -2.42000 REMARK 3 B22 (A**2) : -10.55000 REMARK 3 B33 (A**2) : 12.98000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.28 REMARK 3 ESD FROM SIGMAA (A) : 0.36 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) : 0.42 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.006 REMARK 3 BOND ANGLES (DEGREES) : 1.30 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 26.00 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.87 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 1.560 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.620 ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 2.340 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.580 ; 2.500 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : FLAT MODEL REMARK 3 KSOL : 0.31 REMARK 3 BSOL : 34.43 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 : PROTEIN_REP.PARAM REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM REMARK 3 PARAMETER FILE 3 : ION.PARAM REMARK 3 PARAMETER FILE 4 : NULL REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : WATER.TOP REMARK 3 TOPOLOGY FILE 3 : ION.TOP REMARK 3 TOPOLOGY FILE 4 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: DISORDERED RESIDUES IN CHAIN A REMARK 3 INCLUDE N-TERMINAL RESIDUES 496-5 AND C-TERMINAL RESIDUES 704- REMARK 3 709. IN CHAIN A, SIDE CHAIN FOR LYS IS DISORDERED. DISORDERED REMARK 3 RESIDUES IN CHAIN B INCLUDE C-TERMINAL RESIDUES 266-288. REMARK 4 REMARK 4 1SQ0 COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 4 REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. REMARK 4 REMEDIATED DATA FILE REVISION 3.101 (2007-05-29) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB . REMARK 100 THE RCSB ID CODE IS RCSB021902. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 31-AUG-2002; 18-MAY-2002 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 8.00 REMARK 200 NUMBER OF CRYSTALS USED : 2 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y; Y REMARK 200 RADIATION SOURCE : ALS; ALS REMARK 200 BEAMLINE : 5.0.2; 5.0.2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97942, 0.97959, 0.9686; 1 REMARK 200 MONOCHROMATOR : DOUBLE-CRYSTAL, SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD; CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4; ADSC QUANTUM 4 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA) REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17150 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600 REMARK 200 RESOLUTION RANGE LOW (A) : 49.580 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : NULL REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.75 REMARK 200 COMPLETENESS FOR SHELL (%) : 84.0 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: MAD REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD REMARK 200 SOFTWARE USED: SHELXS REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 56.50 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG-3350; POTASSIUM THIOCYANATE, PH REMARK 280 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 1/2-X,1/2+Y,-Z REMARK 290 4555 1/2+X,1/2-Y,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 36.24850 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 58.05200 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.24850 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 58.05200 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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). REMARK 350 REMARK 350 GENERATING THE BIOMOLECULE 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 APPLY THE FOLLOWING TO CHAINS: A, 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 MET A 496 REMARK 465 GLU A 497 REMARK 465 ASP A 498 REMARK 465 ILE A 499 REMARK 465 SER A 500 REMARK 465 GLU A 501 REMARK 465 PRO A 502 REMARK 465 PRO A 503 REMARK 465 LEU A 504 REMARK 465 HIS A 505 REMARK 465 PRO A 704 REMARK 465 THR A 705 REMARK 465 LEU A 706 REMARK 465 PRO A 707 REMARK 465 PRO A 708 REMARK 465 HIS A 709 REMARK 465 THR B 266 REMARK 465 LEU B 267 REMARK 465 GLY B 268 REMARK 465 ASP B 269 REMARK 465 GLU B 270 REMARK 465 GLY B 271 REMARK 465 ASP B 272 REMARK 465 THR B 273 REMARK 465 ASP B 274 REMARK 465 LEU B 275 REMARK 465 TYR B 276 REMARK 465 ASP B 277 REMARK 465 TYR B 278 REMARK 465 TYR B 279 REMARK 465 PRO B 280 REMARK 465 GLU B 281 REMARK 465 GLU B 282 REMARK 465 ASP B 283 REMARK 465 THR B 284 REMARK 465 GLU B 285 REMARK 465 GLY B 286 REMARK 465 ASP B 287 REMARK 465 LYS B 288 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI REMARK 500 O HOH 21 O HOH 243 2.17 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 MET A 541 SD MET A 541 CE -0.057 REMARK 500 PRO A 703 CB PRO A 703 CG 0.050 REMARK 500 ARG B 218 CG ARG B 218 CD 0.038 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: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ASP A 514 N - CA - C ANGL. DEV. = -8.4 DEGREES REMARK 500 ARG A 552 N - CA - C ANGL. DEV. = -8.2 DEGREES REMARK 500 GLU A 700 N - CA - C ANGL. DEV. = 9.4 DEGREES REMARK 500 LEU B 76 N - CA - C ANGL. DEV. = -8.3 DEGREES REMARK 500 ASN B 157 N - CA - C ANGL. DEV. = 8.0 DEGREES REMARK 500 ASN B 158 N - CA - C ANGL. DEV. = -8.4 DEGREES REMARK 500 ALA B 238 N - CA - C ANGL. DEV. = 7.6 DEGREES REMARK 500 GLN B 247 N - CA - C ANGL. DEV. = 8.6 DEGREES REMARK 500 GLY B 263 N - CA - C ANGL. DEV. = 10.6 DEGREES REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1M10 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE COMPLEX OF GLYCOPROTEIN IB ALPHA REMARK 900 AND THE VON WILLEBRAND FACTOR A1 DOMAIN WITH GAIN-OF- REMARK 900 FUNCTION MUTATIONS REMARK 900 RELATED ID: 1M0Z RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE VON WILLEBRAND FACTOR BINDING REMARK 900 DOMAIN OF GLYCOPROTEIN IB ALPHA REMARK 900 RELATED ID: 1AUQ RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE A1 DOMAIN OF VON WILLEBRAND FACTOR REMARK 900 RELATED ID: 1P8V RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE COMPLEX OF GLYCOPROTEIN IB-ALPHA REMARK 900 AND ALPHA-THROMBIN REMARK 900 RELATED ID: 1OOK RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE COMPLEX OF GLYCOPROTEIN IB-ALPHA REMARK 900 AND ALPHA-THROMBIN REMARK 999 REMARK 999 SEQUENCE REMARK 999 ASN RESIDUES AT POSITIONS 21 AND 159 OF CHAIN B, WHICH ARE REMARK 999 SITES FOR N-LINKED GLYCOSYLATION, WERE MUTATED TO ASP. DBREF 1SQ0 A 496 709 UNP P04275 VWF_HUMAN 1259 1472 DBREF 1SQ0 B 1 288 UNP P07359 GP1BA_HUMAN 17 304 SEQADV 1SQ0 MET A 496 UNP P04275 VAL 1259 ENGINEERED SEQADV 1SQ0 ASP B 21 UNP P07359 ASN 37 SEE REMARK 999 SEQADV 1SQ0 ASP B 159 UNP P07359 ASN 175 SEE REMARK 999 SEQRES 1 A 214 MET GLU ASP ILE SER GLU PRO PRO LEU HIS ASP PHE TYR SEQRES 2 A 214 CYS SER ARG LEU LEU ASP LEU VAL PHE LEU LEU ASP GLY SEQRES 3 A 214 SER SER ARG LEU SER GLU ALA GLU PHE GLU VAL LEU LYS SEQRES 4 A 214 ALA PHE VAL VAL ASP MET MET GLU ARG LEU ARG ILE SER SEQRES 5 A 214 GLN LYS TRP VAL ARG VAL ALA VAL VAL GLU TYR HIS ASP SEQRES 6 A 214 GLY SER HIS ALA TYR ILE GLY LEU LYS ASP ARG LYS ARG SEQRES 7 A 214 PRO SER GLU LEU ARG ARG ILE ALA SER GLN VAL LYS TYR SEQRES 8 A 214 ALA GLY SER GLN VAL ALA SER THR SER GLU VAL LEU LYS SEQRES 9 A 214 TYR THR LEU PHE GLN ILE PHE SER LYS ILE ASP ARG PRO SEQRES 10 A 214 GLU ALA SER ARG ILE ALA LEU LEU LEU MET ALA SER GLN SEQRES 11 A 214 GLU PRO GLN ARG MET SER ARG ASN PHE VAL ARG TYR VAL SEQRES 12 A 214 GLN GLY LEU LYS LYS LYS LYS VAL ILE VAL ILE PRO VAL SEQRES 13 A 214 GLY ILE GLY PRO HIS ALA ASN LEU LYS GLN ILE ARG LEU SEQRES 14 A 214 ILE GLU LYS GLN ALA PRO GLU ASN LYS ALA PHE VAL LEU SEQRES 15 A 214 SER SER VAL ASP GLU LEU GLU GLN GLN ARG ASP GLU ILE SEQRES 16 A 214 VAL SER TYR LEU CYS ASP LEU ALA PRO GLU ALA PRO PRO SEQRES 17 A 214 PRO THR LEU PRO PRO HIS SEQRES 1 B 288 HIS PRO ILE CYS GLU VAL SER LYS VAL ALA SER HIS LEU SEQRES 2 B 288 GLU VAL ASN CYS ASP LYS ARG ASP LEU THR ALA LEU PRO SEQRES 3 B 288 PRO ASP LEU PRO LYS ASP THR THR ILE LEU HIS LEU SER SEQRES 4 B 288 GLU ASN LEU LEU TYR THR PHE SER LEU ALA THR LEU MET SEQRES 5 B 288 PRO TYR THR ARG LEU THR GLN LEU ASN LEU ASP ARG CYS SEQRES 6 B 288 GLU LEU THR LYS LEU GLN VAL ASP GLY THR LEU PRO VAL SEQRES 7 B 288 LEU GLY THR LEU ASP LEU SER HIS ASN GLN LEU GLN SER SEQRES 8 B 288 LEU PRO LEU LEU GLY GLN THR LEU PRO ALA LEU THR VAL SEQRES 9 B 288 LEU ASP VAL SER PHE ASN ARG LEU THR SER LEU PRO LEU SEQRES 10 B 288 GLY ALA LEU ARG GLY LEU GLY GLU LEU GLN GLU LEU TYR SEQRES 11 B 288 LEU LYS GLY ASN GLU LEU LYS THR LEU PRO PRO GLY LEU SEQRES 12 B 288 LEU THR PRO THR PRO LYS LEU GLU LYS LEU SER LEU ALA SEQRES 13 B 288 ASN ASN ASP LEU THR GLU LEU PRO ALA GLY LEU LEU ASN SEQRES 14 B 288 GLY LEU GLU ASN LEU ASP THR LEU LEU LEU GLN GLU ASN SEQRES 15 B 288 SER LEU TYR THR ILE PRO LYS GLY PHE PHE GLY SER HIS SEQRES 16 B 288 LEU LEU PRO PHE ALA PHE LEU HIS GLY ASN PRO TRP LEU SEQRES 17 B 288 CYS ASN CYS GLU ILE LEU TYR PHE ARG ARG TRP LEU GLN SEQRES 18 B 288 ASP ASN ALA GLU ASN VAL TYR VAL TRP LYS GLN GLY VAL SEQRES 19 B 288 ASP VAL LYS ALA MET THR SER ASN VAL ALA SER VAL GLN SEQRES 20 B 288 CYS ASP ASN SER ASP LYS PHE PRO VAL TYR LYS TYR PRO SEQRES 21 B 288 GLY LYS GLY CYS PRO THR LEU GLY ASP GLU GLY ASP THR SEQRES 22 B 288 ASP LEU TYR ASP TYR TYR PRO GLU GLU ASP THR GLU GLY SEQRES 23 B 288 ASP LYS FORMUL 3 HOH *318(H2 O) HELIX 1 1 SER A 526 LEU A 544 1 19 HELIX 2 2 ARG A 573 VAL A 584 1 12 HELIX 3 3 SER A 593 ILE A 605 1 13 HELIX 4 4 PRO A 627 SER A 631 5 5 HELIX 5 5 ASN A 633 LYS A 644 1 12 HELIX 6 6 ASN A 658 ALA A 669 1 12 HELIX 7 7 SER A 679 LEU A 683 5 5 HELIX 8 8 GLN A 686 ASP A 696 1 11 HELIX 9 9 ALA B 49 MET B 52 5 4 HELIX 10 10 ASN B 210 GLU B 212 5 3 HELIX 11 11 ILE B 213 ASN B 223 1 11 HELIX 12 12 VAL B 243 VAL B 246 5 4 HELIX 13 13 GLN B 247 SER B 251 5 5 HELIX 14 14 PRO B 255 TYR B 259 5 5 SHEET 1 A18 PHE A 675 LEU A 677 0 SHEET 2 A18 VAL A 646 ILE A 653 1 N GLY A 652 O LEU A 677 SHEET 3 A18 SER A 615 MET A 622 1 N ARG A 616 O ILE A 647 SHEET 4 A18 LEU A 513 ASP A 520 1 N VAL A 516 O ILE A 617 SHEET 5 A18 VAL A 551 TYR A 558 1 O VAL A 556 N PHE A 517 SHEET 6 A18 SER A 562 ILE A 566 -1 O HIS A 563 N GLU A 557 SHEET 7 A18 LYS B 237 SER B 241 -1 O MET B 239 N SER A 562 SHEET 8 A18 VAL B 227 GLN B 232 -1 N VAL B 229 O THR B 240 SHEET 9 A18 PHE B 199 PHE B 201 1 N ALA B 200 O TYR B 228 SHEET 10 A18 THR B 176 LEU B 178 1 N LEU B 177 O PHE B 199 SHEET 11 A18 LYS B 152 SER B 154 1 N LEU B 153 O THR B 176 SHEET 12 A18 GLU B 128 TYR B 130 1 N LEU B 129 O LYS B 152 SHEET 13 A18 VAL B 104 ASP B 106 1 N LEU B 105 O TYR B 130 SHEET 14 A18 THR B 81 ASP B 83 1 N LEU B 82 O VAL B 104 SHEET 15 A18 GLN B 59 ASN B 61 1 N LEU B 60 O THR B 81 SHEET 16 A18 ILE B 35 HIS B 37 1 N LEU B 36 O ASN B 61 SHEET 17 A18 HIS B 12 ASN B 16 1 N VAL B 15 O ILE B 35 SHEET 18 A18 GLU B 5 VAL B 9 -1 N VAL B 9 O HIS B 12 SHEET 1 B 2 THR B 45 SER B 47 0 SHEET 2 B 2 LYS B 69 GLN B 71 1 O GLN B 71 N PHE B 46 SSBOND 1 CYS A 509 CYS A 695 SSBOND 2 CYS B 4 CYS B 17 SSBOND 3 CYS B 209 CYS B 248 SSBOND 4 CYS B 211 CYS B 264 CRYST1 72.497 116.104 67.962 90.00 90.00 90.00 P 21 21 2 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 0.013794 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008613 0.000000 0.00000 SCALE3 0.000000 0.000000 0.014714 0.00000