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HEADER BLOOD CLOTTING 16-JUN-02 1M0Z TITLE CRYSTAL STRUCTURE OF THE VON WILLEBRAND FACTOR BINDING TITLE 2 DOMAIN OF GLYCOPROTEIN IB ALPHA COMPND MOL_ID: 1; COMPND 2 MOLECULE: GLYCOPROTEIN IB ALPHA; COMPND 3 CHAIN: A, B; COMPND 4 FRAGMENT: VON WILLEBRAND FACTOR BINDING DOMAIN; COMPND 5 SYNONYM: PLATELET GLYCOPROTEIN IB ALPHA CHAIN; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 GENE: GP1BA; SOURCE 5 EXPRESSION_SYSTEM: MESOCRICETUS AURATUS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: SYRIAN HAMSTER; SOURCE 7 EXPRESSION_SYSTEM_TISSUE: KIDNEY; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1 KEYWDS LEUCINE-RICH REPEAT, HEMOSTASIS EXPDTA X-RAY DIFFRACTION AUTHOR E.G.HUIZINGA,S.TSUJI,R.A.P.ROMIJN,M.E.SCHIPHORST,P.G.DE AUTHOR 2 GROOT,J.J.SIXMA,P.GROS REVDAT 2 01-APR-03 1M0Z 1 JRNL REVDAT 1 28-AUG-02 1M0Z 0 JRNL AUTH E.G.HUIZINGA,S.TSUJI,R.A.ROMIJN,M.E.SCHIPHORST, JRNL AUTH 2 P.G.DE GROOT,J.J.SIXMA,P.GROS JRNL TITL STRUCTURES OF GLYCOPROTEIN IBALPHA AND ITS COMPLEX JRNL TITL 2 WITH VON WILLEBRAND FACTOR A1 DOMAIN. JRNL REF SCIENCE V. 297 1176 2002 JRNL REFN ASTM SCIEAS US ISSN 0036-8075 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.85 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 : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.85 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2161360.310 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.0 REMARK 3 NUMBER OF REFLECTIONS : 53895 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) : 0.186 REMARK 3 FREE R VALUE : 0.216 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 2766 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004 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) : 1.85 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.97 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.30 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 7197 REMARK 3 BIN R VALUE (WORKING SET) : 0.2300 REMARK 3 BIN FREE R VALUE : 0.2530 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.50 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 420 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.012 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4113 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 687 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 10.80 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.70 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 3.16000 REMARK 3 B22 (A**2) : 0.48000 REMARK 3 B33 (A**2) : -3.64000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -1.26000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.19 REMARK 3 ESD FROM SIGMAA (A) : 0.14 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) : 0.23 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.16 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.005 REMARK 3 BOND ANGLES (DEGREES) : 1.30 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 26.00 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.91 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED ISOTROPIC REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 1.330 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.090 ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 2.070 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.160 ; 2.500 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : FLAT MODEL REMARK 3 KSOL : 0.36 REMARK 3 BSOL : 49.09 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 : NULL REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : WATER.TOP REMARK 3 TOPOLOGY FILE 3 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1M0Z 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 PDBJ . REMARK 100 THE RCSB ID CODE IS RCSB016462. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 02-SEP-2001 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 8.20 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID14-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.933 REMARK 200 MONOCHROMATOR : DIAMOND (111) REMARK 200 OPTICS : TOROIDAL MIRROR REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53895 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850 REMARK 200 RESOLUTION RANGE LOW (A) : 36.850 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.700 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8 REMARK 200 DATA REDUNDANCY : 3.600 REMARK 200 R MERGE (I) : 0.07300 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 16.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.89 REMARK 200 COMPLETENESS FOR SHELL (%) : 80.8 REMARK 200 DATA REDUNDANCY IN SHELL : 2.40 REMARK 200 R MERGE FOR SHELL (I) : 0.33700 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.900 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 (%): 51.34 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, LITHIUM SULFATE, REMARK 280 CAPS, PH 8.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 301K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 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 60.75000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.25000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 60.75000 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 27.25000 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 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 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 BIOMOLECULE: 2 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 VAL A 9 REMARK 465 ALA A 10 REMARK 465 SER A 11 REMARK 465 ASP A 235 REMARK 465 VAL A 236 REMARK 465 LYS A 237 REMARK 465 ALA A 238 REMARK 465 LEU A 267 REMARK 465 GLY A 268 REMARK 465 ASP A 269 REMARK 465 GLU A 270 REMARK 465 GLY A 271 REMARK 465 ASP A 272 REMARK 465 THR A 273 REMARK 465 ASP A 274 REMARK 465 LEU A 275 REMARK 465 TYR A 276 REMARK 465 ASP A 277 REMARK 465 TYR A 278 REMARK 465 TYR A 279 REMARK 465 PRO A 280 REMARK 465 GLU A 281 REMARK 465 GLU A 282 REMARK 465 ASP A 283 REMARK 465 THR A 284 REMARK 465 GLU A 285 REMARK 465 GLY A 286 REMARK 465 ASP A 287 REMARK 465 LYS A 288 REMARK 465 VAL A 289 REMARK 465 ARG A 290 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 465 VAL B 289 REMARK 465 ARG B 290 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 76 N - CA - C ANGL. DEV. =-12.4 DEGREES REMARK 500 PRO A 77 N - CA - C ANGL. DEV. = 9.2 DEGREES REMARK 500 GLY A 96 N - CA - C ANGL. DEV. = 8.7 DEGREES REMARK 500 ASN A 110 N - CA - C ANGL. DEV. = -9.0 DEGREES REMARK 500 LEU A 115 N - CA - C ANGL. DEV. = -8.1 DEGREES REMARK 500 ASN A 158 N - CA - C ANGL. DEV. =-10.5 DEGREES REMARK 500 LEU A 196 N - CA - C ANGL. DEV. = -8.7 DEGREES REMARK 500 LEU B 13 N - CA - C ANGL. DEV. =-10.6 DEGREES REMARK 500 LEU B 76 N - CA - C ANGL. DEV. =-12.1 DEGREES REMARK 500 LEU B 95 N - CA - C ANGL. DEV. = 8.1 DEGREES REMARK 500 GLY B 96 N - CA - C ANGL. DEV. = 8.3 DEGREES REMARK 500 ASN B 158 N - CA - C ANGL. DEV. = -8.1 DEGREES REMARK 500 SER B 251 N - CA - C ANGL. DEV. = 8.6 DEGREES REMARK 500 ASP B 252 N - CA - C ANGL. DEV. = 11.2 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 TYR A 44 -49.20 71.40 REMARK 500 TYR B 44 -45.76 71.40 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1M10 RELATED DB: PDB REMARK 900 1M10 CONTAINS THE COMPLEX OF GLYCOPROTEIN IB ALPHA AND THE REMARK 900 VON WILLEBRAND FACTOR A1 DOMAIN DBREF 1M0Z A 1 290 UNP P07359 GP1BA_HUMAN 17 306 DBREF 1M0Z B 1 290 UNP P07359 GP1BA_HUMAN 17 306 SEQADV 1M0Z GLN A 21 UNP P07359 ASN 37 ENGINEERED SEQADV 1M0Z GLN A 159 UNP P07359 ASN 175 ENGINEERED SEQADV 1M0Z GLN B 21 UNP P07359 ASN 37 ENGINEERED SEQADV 1M0Z GLN B 159 UNP P07359 ASN 175 ENGINEERED SEQRES 1 A 290 HIS PRO ILE CYS GLU VAL SER LYS VAL ALA SER HIS LEU SEQRES 2 A 290 GLU VAL ASN CYS ASP LYS ARG GLN LEU THR ALA LEU PRO SEQRES 3 A 290 PRO ASP LEU PRO LYS ASP THR THR ILE LEU HIS LEU SER SEQRES 4 A 290 GLU ASN LEU LEU TYR THR PHE SER LEU ALA THR LEU MET SEQRES 5 A 290 PRO TYR THR ARG LEU THR GLN LEU ASN LEU ASP ARG CYS SEQRES 6 A 290 GLU LEU THR LYS LEU GLN VAL ASP GLY THR LEU PRO VAL SEQRES 7 A 290 LEU GLY THR LEU ASP LEU SER HIS ASN GLN LEU GLN SER SEQRES 8 A 290 LEU PRO LEU LEU GLY GLN THR LEU PRO ALA LEU THR VAL SEQRES 9 A 290 LEU ASP VAL SER PHE ASN ARG LEU THR SER LEU PRO LEU SEQRES 10 A 290 GLY ALA LEU ARG GLY LEU GLY GLU LEU GLN GLU LEU TYR SEQRES 11 A 290 LEU LYS GLY ASN GLU LEU LYS THR LEU PRO PRO GLY LEU SEQRES 12 A 290 LEU THR PRO THR PRO LYS LEU GLU LYS LEU SER LEU ALA SEQRES 13 A 290 ASN ASN GLN LEU THR GLU LEU PRO ALA GLY LEU LEU ASN SEQRES 14 A 290 GLY LEU GLU ASN LEU ASP THR LEU LEU LEU GLN GLU ASN SEQRES 15 A 290 SER LEU TYR THR ILE PRO LYS GLY PHE PHE GLY SER HIS SEQRES 16 A 290 LEU LEU PRO PHE ALA PHE LEU HIS GLY ASN PRO TRP LEU SEQRES 17 A 290 CYS ASN CYS GLU ILE LEU TYR PHE ARG ARG TRP LEU GLN SEQRES 18 A 290 ASP ASN ALA GLU ASN VAL TYR VAL TRP LYS GLN GLY VAL SEQRES 19 A 290 ASP VAL LYS ALA MET THR SER ASN VAL ALA SER VAL GLN SEQRES 20 A 290 CYS ASP ASN SER ASP LYS PHE PRO VAL TYR LYS TYR PRO SEQRES 21 A 290 GLY LYS GLY CYS PRO THR LEU GLY ASP GLU GLY ASP THR SEQRES 22 A 290 ASP LEU TYR ASP TYR TYR PRO GLU GLU ASP THR GLU GLY SEQRES 23 A 290 ASP LYS VAL ARG SEQRES 1 B 290 HIS PRO ILE CYS GLU VAL SER LYS VAL ALA SER HIS LEU SEQRES 2 B 290 GLU VAL ASN CYS ASP LYS ARG GLN LEU THR ALA LEU PRO SEQRES 3 B 290 PRO ASP LEU PRO LYS ASP THR THR ILE LEU HIS LEU SER SEQRES 4 B 290 GLU ASN LEU LEU TYR THR PHE SER LEU ALA THR LEU MET SEQRES 5 B 290 PRO TYR THR ARG LEU THR GLN LEU ASN LEU ASP ARG CYS SEQRES 6 B 290 GLU LEU THR LYS LEU GLN VAL ASP GLY THR LEU PRO VAL SEQRES 7 B 290 LEU GLY THR LEU ASP LEU SER HIS ASN GLN LEU GLN SER SEQRES 8 B 290 LEU PRO LEU LEU GLY GLN THR LEU PRO ALA LEU THR VAL SEQRES 9 B 290 LEU ASP VAL SER PHE ASN ARG LEU THR SER LEU PRO LEU SEQRES 10 B 290 GLY ALA LEU ARG GLY LEU GLY GLU LEU GLN GLU LEU TYR SEQRES 11 B 290 LEU LYS GLY ASN GLU LEU LYS THR LEU PRO PRO GLY LEU SEQRES 12 B 290 LEU THR PRO THR PRO LYS LEU GLU LYS LEU SER LEU ALA SEQRES 13 B 290 ASN ASN GLN LEU THR GLU LEU PRO ALA GLY LEU LEU ASN SEQRES 14 B 290 GLY LEU GLU ASN LEU ASP THR LEU LEU LEU GLN GLU ASN SEQRES 15 B 290 SER LEU TYR THR ILE PRO LYS GLY PHE PHE GLY SER HIS SEQRES 16 B 290 LEU LEU PRO PHE ALA PHE LEU HIS GLY ASN PRO TRP LEU SEQRES 17 B 290 CYS ASN CYS GLU ILE LEU TYR PHE ARG ARG TRP LEU GLN SEQRES 18 B 290 ASP ASN ALA GLU ASN VAL TYR VAL TRP LYS GLN GLY VAL SEQRES 19 B 290 ASP VAL LYS ALA MET THR SER ASN VAL ALA SER VAL GLN SEQRES 20 B 290 CYS ASP ASN SER ASP LYS PHE PRO VAL TYR LYS TYR PRO SEQRES 21 B 290 GLY LYS GLY CYS PRO THR LEU GLY ASP GLU GLY ASP THR SEQRES 22 B 290 ASP LEU TYR ASP TYR TYR PRO GLU GLU ASP THR GLU GLY SEQRES 23 B 290 ASP LYS VAL ARG FORMUL 3 HOH *687(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 ASN A 242 VAL A 246 5 5 HELIX 5 5 PRO A 255 TYR A 259 5 5 HELIX 6 6 ALA B 49 MET B 52 5 4 HELIX 7 7 ASN B 210 GLU B 212 5 3 HELIX 8 8 ILE B 213 ASN B 223 1 11 HELIX 9 9 ALA B 224 VAL B 227 5 4 HELIX 10 10 ASN B 242 VAL B 246 5 5 HELIX 11 11 ASN B 250 PHE B 254 5 5 HELIX 12 12 PRO B 255 TYR B 259 5 5 SHEET 1 A11 GLU A 5 SER A 7 0 SHEET 2 A11 GLU A 14 ASN A 16 -1 O ASN A 16 N GLU A 5 SHEET 3 A11 ILE A 35 HIS A 37 1 O ILE A 35 N VAL A 15 SHEET 4 A11 GLN A 59 ASN A 61 1 O GLN A 59 N LEU A 36 SHEET 5 A11 THR A 81 ASP A 83 1 O ASP A 83 N LEU A 60 SHEET 6 A11 VAL A 104 ASP A 106 1 O VAL A 104 N LEU A 82 SHEET 7 A11 GLU A 128 TYR A 130 1 O TYR A 130 N LEU A 105 SHEET 8 A11 LYS A 152 SER A 154 1 O SER A 154 N LEU A 129 SHEET 9 A11 THR A 176 LEU A 178 1 O THR A 176 N LEU A 153 SHEET 10 A11 PHE A 199 PHE A 201 1 O PHE A 199 N LEU A 177 SHEET 11 A11 VAL A 227 TYR A 228 1 O TYR A 228 N ALA A 200 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 C10 GLU B 5 VAL B 9 0 SHEET 2 C10 HIS B 12 ASN B 16 -1 O GLU B 14 N SER B 7 SHEET 3 C10 ILE B 35 HIS B 37 1 O ILE B 35 N VAL B 15 SHEET 4 C10 GLN B 59 ASN B 61 1 O GLN B 59 N LEU B 36 SHEET 5 C10 THR B 81 ASP B 83 1 O THR B 81 N LEU B 60 SHEET 6 C10 VAL B 104 ASP B 106 1 O ASP B 106 N LEU B 82 SHEET 7 C10 GLU B 128 TYR B 130 1 O TYR B 130 N LEU B 105 SHEET 8 C10 LYS B 152 SER B 154 1 O SER B 154 N LEU B 129 SHEET 9 C10 THR B 176 LEU B 178 1 O LEU B 178 N LEU B 153 SHEET 10 C10 PHE B 199 PHE B 201 1 O PHE B 199 N LEU B 177 SHEET 1 D 2 THR B 45 SER B 47 0 SHEET 2 D 2 LYS B 69 GLN B 71 1 O GLN B 71 N PHE B 46 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 B 17 SSBOND 5 CYS B 209 CYS B 248 SSBOND 6 CYS B 211 CYS B 264 CRYST1 121.500 54.500 101.800 90.00 103.70 90.00 C 1 2 1 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 0.008234 0.000000 0.002003 0.00000 SCALE2 0.000000 0.018352 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010111 0.00000