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HEADER MEMBRANE PROTEIN/HYDROLASE 07-MAY-03 1P8V TITLE CRYSTAL STRUCTURE OF THE COMPLEX OF PLATELET RECEPTOR GPIB- TITLE 2 ALPHA AND ALPHA-THROMBIN AT 2.6A COMPND MOL_ID: 1; COMPND 2 MOLECULE: PLATELET GLYCOPROTEIN IB ALPHA CHAIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: GLYCOPROTEIN 1B ALPHA; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: PROTHROMBIN; COMPND 9 CHAIN: B; COMPND 10 FRAGMENT: ALPHA THROMBIN, LIGHT CHAIN; COMPND 11 SYNONYM: COAGULATION FACTOR II; COMPND 12 EC: 3.4.21.5; COMPND 13 MOL_ID: 3; COMPND 14 MOLECULE: PROTHROMBIN; COMPND 15 CHAIN: C; COMPND 16 FRAGMENT: ALPHA THROMBIN, HEAVY CHAIN; COMPND 17 SYNONYM: COAGULATION FACTOR II; COMPND 18 EC: 3.4.21.5 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 GENE: GP1BA; SOURCE 5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 7 EXPRESSION_SYSTEM_ORGAN: OVARY CELLS; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 OTHER_DETAILS: ISOLATED FROM HUMAN PLASMA; SOURCE 12 MOL_ID: 3; SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 14 ORGANISM_COMMON: HUMAN; SOURCE 15 OTHER_DETAILS: ISOLATED FROM HUMAN PLASMA KEYWDS PLATELET GLYCOPROTEIN RECEPTOR, LEUCINE RICH REPEAT DOMAIN EXPDTA X-RAY DIFFRACTION AUTHOR J.J.DUMAS,R.KUMAR,J.SEEHRA,W.S.SOMERS,L.MOSYAK REVDAT 1 22-JUL-03 1P8V 0 JRNL AUTH J.J.DUMAS,R.KUMAR,J.SEEHRA,W.S.SOMERS,L.MOSYAK JRNL TITL CRYSTAL STRUCTURE OF THE GPIBALPHA-THROMBIN JRNL TITL 2 COMPLEX ESSENTIAL FOR PLATELET AGGREGATION JRNL REF SCIENCE V. 301 222 2003 JRNL REFN ASTM SCIEAS US ISSN 0036-8075 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.60 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) : 2.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00 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) (%) : 97.7 REMARK 3 NUMBER OF REFLECTIONS : 27605 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) : 0.207 REMARK 3 FREE R VALUE : 0.238 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.400 REMARK 3 FREE R VALUE TEST SET COUNT : 1903 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) (%) : 95.00 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1903 REMARK 3 BIN R VALUE (WORKING SET) : 0.2810 REMARK 3 BIN FREE R VALUE : 0.3070 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 6.90 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 284 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.018 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4449 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 36 REMARK 3 SOLVENT ATOMS : 217 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 41.30 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.40 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -10.09000 REMARK 3 B22 (A**2) : -0.51000 REMARK 3 B33 (A**2) : 10.59000 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) : 0.30 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) : 0.35 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.37 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.007 REMARK 3 BOND ANGLES (DEGREES) : 1.40 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.90 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.90 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) : 1.437 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.351 ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 2.349 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.522 ; 2.500 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : NULL REMARK 3 KSOL : 0.34 REMARK 3 BSOL : 37.85 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 1P8V 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 RCSB019153. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 11-DEC-2002 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 6.00 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ALS REMARK 200 BEAMLINE : 5.0.1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.000 REMARK 200 MONOCHROMATOR : SI(220) REMARK 200 OPTICS : MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA) REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28711 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.07100 REMARK 200 FOR THE DATA SET : 9.0000 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) : 2.74 REMARK 200 COMPLETENESS FOR SHELL (%) : 95.0 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.39200 REMARK 200 FOR SHELL : 1.900 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: AMORE REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 65.24 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.57 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 14% PEG 400, PH 6.0, VAPOR REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 291K, PH 6.00 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 1/2-X,-Y,1/2+Z REMARK 290 3555 -X,1/2+Y,1/2-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 23.54750 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 88.12550 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.88500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 88.12550 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.54750 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.88500 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 3 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, C 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 BIOMT1 2 -1.000000 0.000000 0.000000 47.09500 REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 55.88500 REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 88.12550 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 C 147 REMARK 465 TRP C 148 REMARK 465 THR C 149 REMARK 465 ALA C 150 REMARK 465 ASN C 151 REMARK 465 VAL C 152 REMARK 465 GLY C 153 REMARK 465 LYS C 154 REMARK 465 GLU C 259 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 ASP A 272 CG OD1 OD2 REMARK 470 LYS C 145 CG CD CE NZ 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 ASP B 17 CB ASP B 17 CG -0.038 REMARK 500 ARG B 21 CG ARG B 21 CD 0.037 REMARK 500 MET C 11 SD MET C 11 CE -0.051 REMARK 500 PRO C 208 CG PRO C 208 CD 0.038 REMARK 500 MET C 211 SD MET C 211 CE -0.044 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 LEU A 13 N - CA - C ANGL. DEV. = -9.1 DEGREES REMARK 500 LEU A 76 N - CA - C ANGL. DEV. = -9.5 DEGREES REMARK 500 PRO A 77 N - CA - C ANGL. DEV. = 8.1 DEGREES REMARK 500 LEU A 168 N - CA - C ANGL. DEV. = 8.4 DEGREES REMARK 500 TYR A 278 N - CA - C ANGL. DEV. =-13.5 DEGREES REMARK 500 GLY B 5 N - CA - C ANGL. DEV. = 9.8 DEGREES REMARK 500 THR B 19 N - CA - C ANGL. DEV. = 8.1 DEGREES REMARK 500 LEU C 59 N - CA - C ANGL. DEV. = 8.7 DEGREES REMARK 500 LEU C 60 CA - CB - CG ANGL. DEV. = 8.5 DEGREES REMARK 500 LEU C 129 N - CA - C ANGL. DEV. = 8.9 DEGREES REMARK 500 PHE C 209 N - CA - C ANGL. DEV. =-11.7 DEGREES REMARK 525 REMARK 525 SOLVENT REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH 167 DISTANCE = 5.02 ANGSTROMS REMARK 525 HOH 180 DISTANCE = 5.40 ANGSTROMS DBREF 1P8V A 1 278 UNP P07359 GP1BA_HUMAN 17 294 DBREF 1P8V B 1 29 UNP P00734 THRB_HUMAN 333 361 DBREF 1P8V C 1 258 UNP P00734 THRB_HUMAN 364 621 SEQADV 1P8V ASP A 21 UNP P07359 ASN 37 ENGINEERED SEQADV 1P8V TYS A 276 UNP P07359 TYR 292 MODIFIED RESIDUE SEQADV 1P8V TYS A 279 UNP P07359 CLONING ARTIFACT SEQADV 1P8V GLU C 259 UNP P00734 CLONING ARTIFACT SEQRES 1 A 279 HIS PRO ILE CYS GLU VAL SER LYS VAL ALA SER HIS LEU SEQRES 2 A 279 GLU VAL ASN CYS ASP LYS ARG ASP LEU THR ALA LEU PRO SEQRES 3 A 279 PRO ASP LEU PRO LYS ASP THR THR ILE LEU HIS LEU SER SEQRES 4 A 279 GLU ASN LEU LEU TYR THR PHE SER LEU ALA THR LEU MET SEQRES 5 A 279 PRO TYR THR ARG LEU THR GLN LEU ASN LEU ASP ARG CYS SEQRES 6 A 279 GLU LEU THR LYS LEU GLN VAL ASP GLY THR LEU PRO VAL SEQRES 7 A 279 LEU GLY THR LEU ASP LEU SER HIS ASN GLN LEU GLN SER SEQRES 8 A 279 LEU PRO LEU LEU GLY GLN THR LEU PRO ALA LEU THR VAL SEQRES 9 A 279 LEU ASP VAL SER PHE ASN ARG LEU THR SER LEU PRO LEU SEQRES 10 A 279 GLY ALA LEU ARG GLY LEU GLY GLU LEU GLN GLU LEU TYR SEQRES 11 A 279 LEU LYS GLY ASN GLU LEU LYS THR LEU PRO PRO GLY LEU SEQRES 12 A 279 LEU THR PRO THR PRO LYS LEU GLU LYS LEU SER LEU ALA SEQRES 13 A 279 ASN ASN ASN LEU THR GLU LEU PRO ALA GLY LEU LEU ASN SEQRES 14 A 279 GLY LEU GLU ASN LEU ASP THR LEU LEU LEU GLN GLU ASN SEQRES 15 A 279 SER LEU TYR THR ILE PRO LYS GLY PHE PHE GLY SER HIS SEQRES 16 A 279 LEU LEU PRO PHE ALA PHE LEU HIS GLY ASN PRO TRP LEU SEQRES 17 A 279 CYS ASN CYS GLU ILE LEU TYR PHE ARG ARG TRP LEU GLN SEQRES 18 A 279 ASP ASN ALA GLU ASN VAL TYR VAL TRP LYS GLN GLY VAL SEQRES 19 A 279 ASP VAL LYS ALA MET THR SER ASN VAL ALA SER VAL GLN SEQRES 20 A 279 CYS ASP ASN SER ASP LYS PHE PRO VAL TYR LYS TYR PRO SEQRES 21 A 279 GLY LYS GLY CYS PRO THR LEU GLY ASP GLU GLY ASP THR SEQRES 22 A 279 ASP LEU TYS ASP TYR TYS SEQRES 1 B 29 GLU ALA ASP CYS GLY LEU ARG PRO LEU PHE GLU LYS LYS SEQRES 2 B 29 SER LEU GLU ASP LYS THR GLU ARG GLU LEU LEU GLU SER SEQRES 3 B 29 TYR ILE ASP SEQRES 1 C 259 ILE VAL GLU GLY SER ASP ALA GLU ILE GLY MET SER PRO SEQRES 2 C 259 TRP GLN VAL MET LEU PHE ARG LYS SER PRO GLN GLU LEU SEQRES 3 C 259 LEU CYS GLY ALA SER LEU ILE SER ASP ARG TRP VAL LEU SEQRES 4 C 259 THR ALA ALA HIS CYS LEU LEU TYR PRO PRO TRP ASP LYS SEQRES 5 C 259 ASN PHE THR GLU ASN ASP LEU LEU VAL ARG ILE GLY LYS SEQRES 6 C 259 HIS SER ARG THR ARG TYR GLU ARG ASN ILE GLU LYS ILE SEQRES 7 C 259 SER MET LEU GLU LYS ILE TYR ILE HIS PRO ARG TYR ASN SEQRES 8 C 259 TRP ARG GLU ASN LEU ASP ARG ASP ILE ALA LEU MET LYS SEQRES 9 C 259 LEU LYS LYS PRO VAL ALA PHE SER ASP TYR ILE HIS PRO SEQRES 10 C 259 VAL CYS LEU PRO ASP ARG GLU THR ALA ALA SER LEU LEU SEQRES 11 C 259 GLN ALA GLY TYR LYS GLY ARG VAL THR GLY TRP GLY ASN SEQRES 12 C 259 LEU LYS GLU THR TRP THR ALA ASN VAL GLY LYS GLY GLN SEQRES 13 C 259 PRO SER VAL LEU GLN VAL VAL ASN LEU PRO ILE VAL GLU SEQRES 14 C 259 ARG PRO VAL CYS LYS ASP SER THR ARG ILE ARG ILE THR SEQRES 15 C 259 ASP ASN MET PHE CYS ALA GLY TYR LYS PRO ASP GLU GLY SEQRES 16 C 259 LYS ARG GLY ASP ALA CYS GLU GLY ASP SER GLY GLY PRO SEQRES 17 C 259 PHE VAL MET LYS SER PRO PHE ASN ASN ARG TRP TYR GLN SEQRES 18 C 259 MET GLY ILE VAL SER TRP GLY GLU GLY CYS ASP ARG ASP SEQRES 19 C 259 GLY LYS TYR GLY PHE TYR THR HIS VAL PHE ARG LEU LYS SEQRES 20 C 259 LYS TRP ILE GLN LYS VAL ILE ASP GLN PHE GLY GLU MODRES 1P8V TYS A 276 TYR SULFONATED TYROSINE MODRES 1P8V TYS A 279 TYR SULFONATED TYROSINE MODRES 1P8V ASN C 53 ASN GLYCOSYLATION SITE HET TYS A 276 16 HET TYS A 279 17 HET NAG C 300 14 HET MES 400 12 HET DFP C 500 10 HETNAM TYS SULFONATED TYROSINE HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID HETNAM DFP DIISOPROPYL PHOSPHONATE HETSYN NAG NAG FORMUL 1 TYS 2(C9 H11 N O6 S) FORMUL 4 NAG C8 H15 N O6 FORMUL 5 MES C6 H13 N O4 S FORMUL 6 DFP C6 H15 O3 P FORMUL 7 HOH *217(H2 O) HELIX 1 1 ALA A 49 MET A 52 5 4 HELIX 2 2 ASN A 210 GLU A 212 5 3 HELIX 3 3 ILE A 213 ASN A 223 1 11 HELIX 4 4 ALA A 224 VAL A 227 5 4 HELIX 5 5 ASP A 235 MET A 239 5 5 HELIX 6 6 ASN A 242 VAL A 246 5 5 HELIX 7 7 GLN A 247 SER A 251 5 5 HELIX 8 8 PRO A 255 TYR A 259 5 5 HELIX 9 9 PHE B 10 SER B 14 5 5 HELIX 10 10 THR B 19 GLU B 25 1 7 HELIX 11 11 SER B 26 ILE B 28 5 3 HELIX 12 12 ALA C 41 CYS C 44 5 4 HELIX 13 13 PRO C 48 ASP C 51 5 4 HELIX 14 14 THR C 55 ASN C 57 5 3 HELIX 15 15 ASP C 122 LEU C 130 1 9 HELIX 16 16 GLU C 169 ASP C 175 1 7 HELIX 17 17 LYS C 191 GLY C 195 5 5 HELIX 18 18 LEU C 246 GLY C 258 1 13 SHEET 1 A10 GLU A 5 VAL A 9 0 SHEET 2 A10 HIS A 12 ASN A 16 -1 O ASN A 16 N GLU A 5 SHEET 3 A10 ILE A 35 HIS A 37 1 O ILE A 35 N VAL A 15 SHEET 4 A10 GLN A 59 ASN A 61 1 O GLN A 59 N LEU A 36 SHEET 5 A10 THR A 81 ASP A 83 1 O THR A 81 N LEU A 60 SHEET 6 A10 VAL A 104 ASP A 106 1 O ASP A 106 N LEU A 82 SHEET 7 A10 GLU A 128 TYR A 130 1 O GLU A 128 N LEU A 105 SHEET 8 A10 LYS A 152 SER A 154 1 O SER A 154 N LEU A 129 SHEET 9 A10 THR A 176 LEU A 178 1 O LEU A 178 N LEU A 153 SHEET 10 A10 PHE A 199 PHE A 201 1 O PHE A 199 N LEU A 177 SHEET 1 B 2 THR A 45 SER A 47 0 SHEET 2 B 2 LYS A 69 GLN A 71 1 O GLN A 71 N PHE A 46 SHEET 1 C 8 SER C 5 ASP C 6 0 SHEET 2 C 8 GLN C 161 VAL C 168 -1 O VAL C 162 N SER C 5 SHEET 3 C 8 MET C 185 ALA C 188 -1 O CYS C 187 N VAL C 168 SHEET 4 C 8 GLY C 238 HIS C 242 -1 O TYR C 240 N PHE C 186 SHEET 5 C 8 TRP C 219 TRP C 227 -1 N TRP C 227 O PHE C 239 SHEET 6 C 8 PRO C 208 LYS C 212 -1 N MET C 211 O TYR C 220 SHEET 7 C 8 LYS C 135 GLY C 140 -1 N ARG C 137 O VAL C 210 SHEET 8 C 8 GLN C 161 VAL C 168 -1 O VAL C 163 N VAL C 138 SHEET 1 D 7 LYS C 77 SER C 79 0 SHEET 2 D 7 LEU C 59 ILE C 63 -1 N ILE C 63 O LYS C 77 SHEET 3 D 7 GLN C 15 ARG C 20 -1 N PHE C 19 O LEU C 60 SHEET 4 D 7 GLU C 25 LEU C 32 -1 O GLU C 25 N ARG C 20 SHEET 5 D 7 TRP C 37 THR C 40 -1 O LEU C 39 N SER C 31 SHEET 6 D 7 ALA C 101 LEU C 105 -1 O MET C 103 N VAL C 38 SHEET 7 D 7 LEU C 81 ILE C 86 -1 N TYR C 85 O LEU C 102 SHEET 1 E 2 LEU C 46 TYR C 47 0 SHEET 2 E 2 LYS C 52 ASN C 53 -1 O LYS C 52 N TYR C 47 SSBOND 1 CYS A 4 CYS A 17 SSBOND 2 CYS A 209 CYS A 248 SSBOND 3 CYS A 211 CYS A 264 SSBOND 4 CYS B 4 CYS C 119 SSBOND 5 CYS C 28 CYS C 44 SSBOND 6 CYS C 173 CYS C 187 SSBOND 7 CYS C 201 CYS C 231 LINK ND2 ASN C 53 C1 NAG C 300 LINK OG SER C 205 P DFP C 500 LINK OG SER C 205 O3P DFP C 500 CISPEP 1 SER C 22 PRO C 23 0 0.94 CRYST1 47.095 111.770 176.251 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 0.021234 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008947 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005674 0.00000