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HEADER HYDROLASE 03-MAR-03 1OOK TITLE CRYSTAL STRUCTURE OF THE COMPLEX OF PLATELET RECEPTOR GPIB- TITLE 2 ALPHA AND HUMAN ALPHA-THROMBIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: HUMAN ALPHA THROMBIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: THROMBIN A CHAIN; COMPND 5 SYNONYM: COAGULATION FACTOR II; COMPND 6 EC: 3.4.21.5; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: HUMAN ALPHA THROMBIN; COMPND 9 CHAIN: B; COMPND 10 FRAGMENT: THROMBIN B CHAIN; COMPND 11 SYNONYM: COAGULATION FACTOR II; COMPND 12 EC: 3.4.21.5; COMPND 13 MOL_ID: 3; COMPND 14 MOLECULE: PHE-PRO-ARG-CHLOROMETHYLKETONE; COMPND 15 CHAIN: P; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 4; COMPND 18 MOLECULE: PLATELET GLYCOPROTEIN IB ALPHA CHAIN PRECURSOR; COMPND 19 CHAIN: G; COMPND 20 FRAGMENT: N-TERMINAL DOMAIN; COMPND 21 SYNONYM: GLYCOPROTEIN IB-ALPHA, GP-IB ALPHA, GPIBA, GPIB- COMPND 22 ALPHA, CD42B, [PART OF: GLYCOCALICIN]; COMPND 23 ENGINEERED: YES; COMPND 24 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 OTHER_DETAILS: PURIFIED FROM PLASMA; SOURCE 5 MOL_ID: 2; SOURCE 6 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 7 ORGANISM_COMMON: HUMAN; SOURCE 8 OTHER_DETAILS: PURIFIED FROM PLASMA; SOURCE 9 MOL_ID: 3; SOURCE 10 SYNTHETIC: YES; SOURCE 11 OTHER_DETAILS: CHEMICALLY SYNTHESIZED; SOURCE 12 MOL_ID: 4; SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 14 ORGANISM_COMMON: HUMAN; SOURCE 15 GENE: GP1BA; SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 17 EXPRESSION_SYSTEM_COMMON: BACTERIA KEYWDS LEUCINE RICH REPEATS EXPDTA X-RAY DIFFRACTION AUTHOR K.I.VARUGHESE,R.CELIKEL,Z.M.RUGGERI REVDAT 1 22-JUL-03 1OOK 0 JRNL AUTH R.CELIKEL,R.A.MCCLINTOCK,J.R.ROBERTS, JRNL AUTH 2 G.L.MENDOLICCHIO,J.WARE,K.I.VARUGHESE,Z.M.RUGGERI JRNL TITL MODULATION OF ALPHA-THROMBIN FUNCTION BY DISTINCT JRNL TITL 2 INTERACTIONS WITH PLATELET GLYCOPROTEIN IBALPHA JRNL REF SCIENCE V. 301 218 2003 JRNL REFN ASTM SCIEAS US ISSN 0036-8075 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.30 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 : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00 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) (%) : 98.2 REMARK 3 NUMBER OF REFLECTIONS : 34514 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING SET) : 0.212 REMARK 3 FREE R VALUE : 0.260 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 1716 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) : NULL REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : NULL REMARK 3 BIN FREE R VALUE : NULL REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL 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 : 4643 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 76 REMARK 3 SOLVENT ATOMS : 392 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 31.90 REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.28 REMARK 3 ESD FROM SIGMAA (A) : 0.24 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) : 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) : NULL REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : NULL REMARK 3 KSOL : NULL REMARK 3 BSOL : NULL REMARK 3 REMARK 3 NCS MODEL : NULL REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : NULL REMARK 3 TOPOLOGY FILE 1 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1OOK 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 3.100 (2007-03-17) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE RCSB ID CODE IS RCSB018507. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 02-DEC-2002 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 7.00 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRL REMARK 200 BEAMLINE : BL9-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.033167 REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35360 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 200 DATA REDUNDANCY : 17.200 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.06600 REMARK 200 FOR THE DATA SET : 38.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.5 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.29200 REMARK 200 FOR SHELL : 5.200 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: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 52.81 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, AMMONIUM PHOSPHATE, PH REMARK 280 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277.0K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,1/2+Z REMARK 290 3555 1/2-Y,1/2+X,3/4+Z REMARK 290 4555 1/2+Y,1/2-X,1/4+Z REMARK 290 5555 1/2-X,1/2+Y,3/4-Z REMARK 290 6555 1/2+X,1/2-Y,1/4-Z REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,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 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 164.28900 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 33.82450 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 33.82450 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 246.43350 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 33.82450 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 33.82450 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 82.14450 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 33.82450 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 33.82450 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 246.43350 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 33.82450 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 33.82450 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 82.14450 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 164.28900 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 4 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, P, G, S 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 GLU G 285 REMARK 465 GLY G 286 REMARK 465 ASP G 287 REMARK 465 LYS G 288 REMARK 465 VAL G 289 REMARK 465 ARG G 290 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 NE2 HIS B 57 OXT ARG P 3 2.09 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 B 106 SD MET B 106 CE -0.116 REMARK 500 MET B 180 SD MET B 180 CE -0.059 REMARK 500 VAL B 241 CA VAL B 241 CB 0.053 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 LYS A 14A N - CA - C ANGL. DEV. = 8.5 DEGREES REMARK 500 LEU B 40 N - CA - C ANGL. DEV. = -7.9 DEGREES REMARK 500 LEU B 65 N - CA - C ANGL. DEV. = -9.5 DEGREES REMARK 500 GLU B 97A N - CA - C ANGL. DEV. = 9.2 DEGREES REMARK 500 GLU B 146 N - CA - C ANGL. DEV. = -8.1 DEGREES REMARK 500 ALA B 190 N - CA - C ANGL. DEV. =-10.2 DEGREES REMARK 500 PHE B 199 N - CA - C ANGL. DEV. =-12.6 DEGREES REMARK 500 GLY B 219 N - CA - C ANGL. DEV. = -9.2 DEGREES 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 M RES CSSEQI PSI PHI REMARK 500 ARG B 77A -110.51 -0.17 REMARK 500 LYS G 262 -103.09 22.95 DBREF 1OOK A 1 15 UNP P00734 THRB_HUMAN 328 363 DBREF 1OOK B 16 247 UNP P00734 THRB_HUMAN 364 622 DBREF 1OOK G 1 290 UNP P07359 GPBA_HUMAN 17 306 SEQADV 1OOK ALA G 65 UNP P07359 CYS 81 ENGINEERED SEQADV 1OOK TYS G 276 UNP P07359 TYR 292 MODIFIED RESIDUE SEQADV 1OOK TYS G 279 UNP P07359 TYR 295 MODIFIED RESIDUE SEQRES 1 A 36 THR PHE GLY SER GLY GLU ALA ASP CYS GLY LEU ARG PRO SEQRES 2 A 36 LEU PHE GLU LYS LYS SER LEU GLU ASP LYS THR GLU ARG SEQRES 3 A 36 GLU LEU LEU GLU SER TYR ILE ASP GLY ARG SEQRES 1 B 259 ILE VAL GLU GLY SER ASP ALA GLU ILE GLY MET SER PRO SEQRES 2 B 259 TRP GLN VAL MET LEU PHE ARG LYS SER PRO GLN GLU LEU SEQRES 3 B 259 LEU CYS GLY ALA SER LEU ILE SER ASP ARG TRP VAL LEU SEQRES 4 B 259 THR ALA ALA HIS CYS LEU LEU TYR PRO PRO TRP ASP LYS SEQRES 5 B 259 ASN PHE THR GLU ASN ASP LEU LEU VAL ARG ILE GLY LYS SEQRES 6 B 259 HIS SER ARG THR ARG TYR GLU ARG ASN ILE GLU LYS ILE SEQRES 7 B 259 SER MET LEU GLU LYS ILE TYR ILE HIS PRO ARG TYR ASN SEQRES 8 B 259 TRP ARG GLU ASN LEU ASP ARG ASP ILE ALA LEU MET LYS SEQRES 9 B 259 LEU LYS LYS PRO VAL ALA PHE SER ASP TYR ILE HIS PRO SEQRES 10 B 259 VAL CYS LEU PRO ASP ARG GLU THR ALA ALA SER LEU LEU SEQRES 11 B 259 GLN ALA GLY TYR LYS GLY ARG VAL THR GLY TRP GLY ASN SEQRES 12 B 259 LEU LYS GLU THR TRP THR ALA ASN VAL GLY LYS GLY GLN SEQRES 13 B 259 PRO SER VAL LEU GLN VAL VAL ASN LEU PRO ILE VAL GLU SEQRES 14 B 259 ARG PRO VAL CYS LYS ASP SER THR ARG ILE ARG ILE THR SEQRES 15 B 259 ASP ASN MET PHE CYS ALA GLY TYR LYS PRO ASP GLU GLY SEQRES 16 B 259 LYS ARG GLY ASP ALA CYS GLU GLY ASP SER GLY GLY PRO SEQRES 17 B 259 PHE VAL MET LYS SER PRO PHE ASN ASN ARG TRP TYR GLN SEQRES 18 B 259 MET GLY ILE VAL SER TRP GLY GLU GLY CYS ASP ARG ASP SEQRES 19 B 259 GLY LYS TYR GLY PHE TYR THR HIS VAL PHE ARG LEU LYS SEQRES 20 B 259 LYS TRP ILE GLN LYS VAL ILE ASP GLN PHE GLY GLU SEQRES 1 P 3 PHE PRO ARG SEQRES 1 G 290 HIS PRO ILE CYS GLU VAL SER LYS VAL ALA SER HIS LEU SEQRES 2 G 290 GLU VAL ASN CYS ASP LYS ARG ASN LEU THR ALA LEU PRO SEQRES 3 G 290 PRO ASP LEU PRO LYS ASP THR THR ILE LEU HIS LEU SER SEQRES 4 G 290 GLU ASN LEU LEU TYR THR PHE SER LEU ALA THR LEU MET SEQRES 5 G 290 PRO TYR THR ARG LEU THR GLN LEU ASN LEU ASP ARG ALA SEQRES 6 G 290 GLU LEU THR LYS LEU GLN VAL ASP GLY THR LEU PRO VAL SEQRES 7 G 290 LEU GLY THR LEU ASP LEU SER HIS ASN GLN LEU GLN SER SEQRES 8 G 290 LEU PRO LEU LEU GLY GLN THR LEU PRO ALA LEU THR VAL SEQRES 9 G 290 LEU ASP VAL SER PHE ASN ARG LEU THR SER LEU PRO LEU SEQRES 10 G 290 GLY ALA LEU ARG GLY LEU GLY GLU LEU GLN GLU LEU TYR SEQRES 11 G 290 LEU LYS GLY ASN GLU LEU LYS THR LEU PRO PRO GLY LEU SEQRES 12 G 290 LEU THR PRO THR PRO LYS LEU GLU LYS LEU SER LEU ALA SEQRES 13 G 290 ASN ASN ASN LEU THR GLU LEU PRO ALA GLY LEU LEU ASN SEQRES 14 G 290 GLY LEU GLU ASN LEU ASP THR LEU LEU LEU GLN GLU ASN SEQRES 15 G 290 SER LEU TYR THR ILE PRO LYS GLY PHE PHE GLY SER HIS SEQRES 16 G 290 LEU LEU PRO PHE ALA PHE LEU HIS GLY ASN PRO TRP LEU SEQRES 17 G 290 CYS ASN CYS GLU ILE LEU TYR PHE ARG ARG TRP LEU GLN SEQRES 18 G 290 ASP ASN ALA GLU ASN VAL TYR VAL TRP LYS GLN GLY VAL SEQRES 19 G 290 ASP VAL LYS ALA MET THR SER ASN VAL ALA SER VAL GLN SEQRES 20 G 290 CYS ASP ASN SER ASP LYS PHE PRO VAL TYR LYS TYR PRO SEQRES 21 G 290 GLY LYS GLY CYS PRO THR LEU GLY ASP GLU GLY ASP THR SEQRES 22 G 290 ASP LEU TYS ASP TYR TYS PRO GLU GLU ASP THR GLU GLY SEQRES 23 G 290 ASP LYS VAL ARG MODRES 1OOK TYS G 276 TYR SULFONATED TYROSINE MODRES 1OOK TYS G 279 TYR SULFONATED TYROSINE MODRES 1OOK ASN B 60G ASN GLYCOSYLATION SITE MODRES 1OOK ASN G 159 ASN GLYCOSYLATION SITE HET TYS G 276 16 HET TYS G 279 16 HET NAG S 501 14 HET NAG S 502 14 HET MAN S 503 11 HET MAN S 504 11 HET MAN S 508 11 HET NAG G 601 14 HET CL 400 1 HETNAM TYS SULFONATED TYROSINE HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM MAN ALPHA-D-MANNOSE HETNAM CL CHLORIDE ION HETSYN NAG NAG FORMUL 4 TYS 2(C9 H11 N O6 S) FORMUL 5 NAG 3(C8 H15 N O6) FORMUL 5 MAN 3(C6 H12 O6) FORMUL 7 CL CL 1- FORMUL 8 HOH *392(H2 O) HELIX 1 1 PHE A 7 SER A 11 5 5 HELIX 2 2 THR A 14B SER A 14I 1 8 HELIX 3 3 ALA B 55 CYS B 58 5 4 HELIX 4 4 PRO B 60B ASP B 60E 5 4 HELIX 5 5 THR B 60I ASN B 62 5 3 HELIX 6 6 ASP B 125 LEU B 130 1 9 HELIX 7 7 GLU B 164 ASP B 170 1 7 HELIX 8 8 LEU B 234 ASP B 243 1 10 HELIX 9 9 ALA G 49 MET G 52 5 4 HELIX 10 10 ILE G 213 ASN G 223 1 11 HELIX 11 11 ALA G 224 VAL G 227 5 4 HELIX 12 12 ASN G 242 VAL G 246 5 5 HELIX 13 13 GLN G 247 SER G 251 5 5 HELIX 14 14 PRO G 255 TYR G 259 5 5 SHEET 1 A 7 SER B 20 ASP B 21 0 SHEET 2 A 7 GLN B 156 VAL B 163 -1 O VAL B 157 N SER B 20 SHEET 3 A 7 LYS B 135 GLY B 140 -1 N GLY B 136 O LEU B 160 SHEET 4 A 7 PRO B 198 LYS B 202 -1 O PRO B 198 N THR B 139 SHEET 5 A 7 TRP B 207 TRP B 215 -1 N TYR B 208 O MET B 201 SHEET 6 A 7 GLY B 226 HIS B 230 -1 N PHE B 227 O TRP B 215 SHEET 7 A 7 MET B 180 ALA B 183 -1 O PHE B 181 N TYR B 228 SHEET 1 B 6 GLN B 30 ARG B 35 0 SHEET 2 B 6 GLU B 39 LEU B 46 -1 O GLU B 39 N ARG B 35 SHEET 3 B 6 TRP B 51 THR B 54 -1 N LEU B 53 O SER B 45 SHEET 4 B 6 ALA B 104 LEU B 108 -1 O ALA B 104 N THR B 54 SHEET 5 B 6 LYS B 81 ILE B 90 -1 N GLU B 86 O LYS B 107 SHEET 6 B 6 LEU B 64 ILE B 68 -1 O LEU B 64 N LEU B 85 SHEET 1 C 2 LEU B 60 TYR B 60A 0 SHEET 2 C 2 LYS B 60F ASN B 60G-1 O LYS B 60F N TYR B 60A SHEET 1 D10 GLU G 5 VAL G 9 0 SHEET 2 D10 HIS G 12 ASN G 16 -1 N HIS G 12 O VAL G 9 SHEET 3 D10 THR G 33 HIS G 37 1 N THR G 34 O LEU G 13 SHEET 4 D10 GLN G 59 ASN G 61 1 O GLN G 59 N LEU G 36 SHEET 5 D10 THR G 81 ASP G 83 1 O THR G 81 N LEU G 60 SHEET 6 D10 VAL G 104 ASP G 106 1 O VAL G 104 N LEU G 82 SHEET 7 D10 GLU G 128 TYR G 130 1 O GLU G 128 N LEU G 105 SHEET 8 D10 LYS G 152 SER G 154 1 O LYS G 152 N LEU G 129 SHEET 9 D10 THR G 176 LEU G 178 1 O THR G 176 N LEU G 153 SHEET 10 D10 PHE G 199 PHE G 201 1 O PHE G 199 N LEU G 177 SHEET 1 E 2 THR G 45 SER G 47 0 SHEET 2 E 2 LYS G 69 GLN G 71 1 O LYS G 69 N PHE G 46 SSBOND 1 CYS A 1 CYS B 122 SSBOND 2 CYS B 42 CYS B 58 SSBOND 3 CYS B 168 CYS B 182 SSBOND 4 CYS B 191 CYS B 220 SSBOND 5 CYS G 4 CYS G 17 SSBOND 6 CYS G 209 CYS G 248 SSBOND 7 CYS G 211 CYS G 264 LINK ND2 ASN B 60G C1 NAG S 501 LINK ND2 ASN G 159 C1 NAG G 601 LINK O4 NAG S 501 C1 NAG S 502 LINK O4 NAG S 502 C1 MAN S 503 LINK O3 MAN S 503 C1 MAN S 508 LINK O6 MAN S 503 C1 MAN S 504 CISPEP 1 SER B 36A PRO B 37 0 -0.49 CRYST1 67.649 67.649 328.578 90.00 90.00 90.00 P 43 21 2 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 0.014782 0.000000 0.000000 0.00000 SCALE2 0.000000 0.014782 0.000000 0.00000 SCALE3 0.000000 0.000000 0.003043 0.00000