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HEADER BLOOD CLOTTING 16-JUN-02 1M10 TITLE CRYSTAL STRUCTURE OF THE COMPLEX OF GLYCOPROTEIN IB ALPHA TITLE 2 AND THE VON WILLEBRAND FACTOR A1 DOMAIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: VON WILLEBRAND FACTOR; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: A1 DOMAIN; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: GLYCOPROTEIN IB ALPHA; COMPND 9 CHAIN: B; COMPND 10 FRAGMENT: VON WILLEBRAND FACTOR BINDING DOMAIN; COMPND 11 SYNONYM: PLATELET GLYCOPROTEIN IB ALPHA CHAIN; COMPND 12 ENGINEERED: YES; COMPND 13 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 GENE: VWF; SOURCE 5 EXPRESSION_SYSTEM: PICHIA PASTORIS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: FUNGI; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: GS115; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PPIC9; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 12 ORGANISM_COMMON: HUMAN; SOURCE 13 GENE: GP1BA; SOURCE 14 EXPRESSION_SYSTEM: MESOCRICETUS AURATUS; SOURCE 15 EXPRESSION_SYSTEM_COMMON: SYRIAN HAMSTER; SOURCE 16 EXPRESSION_SYSTEM_TISSUE: KIDNEY; SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1 KEYWDS LEUCINE-RICH REPEAT, HEMOSTASIS, DINUCLEOTIDE BINDING FOLD 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 1M10 1 JRNL REVDAT 1 28-AUG-02 1M10 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. 3.10 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) : 3.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.50 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1123736.970 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 10391 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) : 0.234 REMARK 3 FREE R VALUE : 0.296 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 529 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.013 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) : 3.10 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.29 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.90 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1622 REMARK 3 BIN R VALUE (WORKING SET) : 0.3260 REMARK 3 BIN FREE R VALUE : 0.3700 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 85 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.040 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3688 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.20 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 10.10000 REMARK 3 B22 (A**2) : 10.10000 REMARK 3 B33 (A**2) : -20.20000 REMARK 3 B12 (A**2) : 17.03000 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) : 0.40 REMARK 3 ESD FROM SIGMAA (A) : 0.47 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) : 0.52 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.50 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.009 REMARK 3 BOND ANGLES (DEGREES) : 1.60 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.00 REMARK 3 IMPROPER ANGLES (DEGREES) : 1.08 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC RESTRAINED REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 1.220 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.160 ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 1.510 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.510 ; 2.500 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : FLAT MODEL REMARK 3 KSOL : 0.30 REMARK 3 BSOL : 20.28 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 : NULL REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1M10 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 PDBJ . REMARK 100 THE RCSB ID CODE IS RCSB016463. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 12-DEC-2001 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 5.50 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG REMARK 200 BEAMLINE : X11 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.8075 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10454 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.090 REMARK 200 RESOLUTION RANGE LOW (A) : 30.500 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.700 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 5.800 REMARK 200 R MERGE (I) : 0.08700 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 19.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.09 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.20 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9 REMARK 200 DATA REDUNDANCY IN SHELL : 5.40 REMARK 200 R MERGE FOR SHELL (I) : 0.48000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 3.600 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 ENTRIES 1AUQ AND 1M0Z REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 52.47 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3000, SODIUM CHLORIDE, MES, PH REMARK 280 5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,1/3+Z REMARK 290 3555 -X+Y,-X,2/3+Z REMARK 290 4555 -X,-Y,1/2+Z REMARK 290 5555 Y,-X+Y,5/6+Z REMARK 290 6555 X-Y,X,1/6+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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 41.54333 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 83.08667 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 62.31500 REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 103.85833 REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 20.77167 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 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 PRO A 704 REMARK 465 THR A 705 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 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 ARG A 616 CG ARG A 616 CD -0.058 REMARK 500 PRO A 702 CB PRO A 702 CG 0.119 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 PRO B 2 N - CA - C ANGL. DEV. = 9.9 DEGREES REMARK 500 GLN B 21 N - CA - C ANGL. DEV. = 10.5 DEGREES REMARK 500 VAL B 78 N - CA - C ANGL. DEV. = 9.5 DEGREES REMARK 500 HIS B 195 N - CA - C ANGL. DEV. =-12.0 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 HIS A 559 -99.03 171.04 REMARK 500 ASP B 252 64.17 -3.86 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1M0Z RELATED DB: PDB REMARK 900 1M0Z CONTAINS THE VON WILLEBRAND FACTOR BINDING DOMAIN OF REMARK 900 GLYCOPROTEIN IB ALPHA DBREF 1M10 A 498 705 UNP P04275 VWF_HUMAN 1261 1468 DBREF 1M10 B 1 290 UNP P07359 GP1BA_HUMAN 17 306 SEQADV 1M10 GLN A 543 UNP P04275 ARG 1306 ENGINEERED SEQADV 1M10 GLN B 21 UNP P07359 ASN 37 ENGINEERED SEQADV 1M10 GLN B 159 UNP P07359 ASN 175 ENGINEERED SEQADV 1M10 VAL B 239 UNP P07359 MET 255 ENGINEERED SEQRES 1 A 208 ASP ILE SER GLU PRO PRO LEU HIS ASP PHE TYR CYS SER SEQRES 2 A 208 ARG LEU LEU ASP LEU VAL PHE LEU LEU ASP GLY SER SER SEQRES 3 A 208 ARG LEU SER GLU ALA GLU PHE GLU VAL LEU LYS ALA PHE SEQRES 4 A 208 VAL VAL ASP MET MET GLU GLN LEU ARG ILE SER GLN LYS SEQRES 5 A 208 TRP VAL ARG VAL ALA VAL VAL GLU TYR HIS ASP GLY SER SEQRES 6 A 208 HIS ALA TYR ILE GLY LEU LYS ASP ARG LYS ARG PRO SER SEQRES 7 A 208 GLU LEU ARG ARG ILE ALA SER GLN VAL LYS TYR ALA GLY SEQRES 8 A 208 SER GLN VAL ALA SER THR SER GLU VAL LEU LYS TYR THR SEQRES 9 A 208 LEU PHE GLN ILE PHE SER LYS ILE ASP ARG PRO GLU ALA SEQRES 10 A 208 SER ARG ILE ALA LEU LEU LEU MET ALA SER GLN GLU PRO SEQRES 11 A 208 GLN ARG MET SER ARG ASN PHE VAL ARG TYR VAL GLN GLY SEQRES 12 A 208 LEU LYS LYS LYS LYS VAL ILE VAL ILE PRO VAL GLY ILE SEQRES 13 A 208 GLY PRO HIS ALA ASN LEU LYS GLN ILE ARG LEU ILE GLU SEQRES 14 A 208 LYS GLN ALA PRO GLU ASN LYS ALA PHE VAL LEU SER SER SEQRES 15 A 208 VAL ASP GLU LEU GLU GLN GLN ARG ASP GLU ILE VAL SER SEQRES 16 A 208 TYR LEU CYS ASP LEU ALA PRO GLU ALA PRO PRO PRO THR 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 VAL 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 HELIX 1 1 SER A 526 GLN A 543 1 18 HELIX 2 2 ARG A 573 GLN A 583 1 11 HELIX 3 3 SER A 593 ILE A 605 1 13 HELIX 4 4 PRO A 627 ARG A 632 5 6 HELIX 5 5 ASN A 633 LYS A 643 1 11 HELIX 6 6 ASN A 658 LYS A 667 1 10 HELIX 7 7 SER A 679 ASP A 681 5 3 HELIX 8 8 GLU A 682 ASP A 696 1 15 HELIX 9 9 ALA B 49 MET B 52 5 4 HELIX 10 10 ILE B 213 ASP B 222 1 10 HELIX 11 11 ASN B 223 ASN B 226 5 4 HELIX 12 12 VAL B 243 VAL B 246 5 4 HELIX 13 13 PRO B 255 TYR B 259 5 5 SHEET 1 A 8 PHE A 675 LEU A 677 0 SHEET 2 A 8 VAL A 646 ILE A 653 1 N GLY A 652 O LEU A 677 SHEET 3 A 8 SER A 615 LEU A 621 1 N ALA A 618 O ILE A 647 SHEET 4 A 8 LEU A 513 ASP A 520 1 N VAL A 516 O ILE A 617 SHEET 5 A 8 VAL A 551 TYR A 558 1 O ALA A 554 N PHE A 517 SHEET 6 A 8 SER A 562 ALA A 564 -1 O HIS A 563 N GLU A 557 SHEET 7 A 8 LYS B 237 SER B 241 -1 O LYS B 237 N ALA A 564 SHEET 8 A 8 TYR B 228 GLN B 232 -1 N VAL B 229 O THR B 240 SHEET 1 B10 GLU B 5 VAL B 9 0 SHEET 2 B10 HIS B 12 ASN B 16 -1 O HIS B 12 N VAL B 9 SHEET 3 B10 ILE B 35 HIS B 37 1 O HIS B 37 N VAL B 15 SHEET 4 B10 GLN B 59 ASN B 61 1 O ASN B 61 N LEU B 36 SHEET 5 B10 THR B 81 ASP B 83 1 O THR B 81 N LEU B 60 SHEET 6 B10 VAL B 104 ASP B 106 1 O VAL B 104 N LEU B 82 SHEET 7 B10 GLU B 128 TYR B 130 1 O GLU B 128 N LEU B 105 SHEET 8 B10 LYS B 152 SER B 154 1 O LYS B 152 N LEU B 129 SHEET 9 B10 THR B 176 LEU B 178 1 O LEU B 178 N LEU B 153 SHEET 10 B10 PHE B 199 PHE B 201 1 O PHE B 199 N LEU B 177 SHEET 1 C 2 THR B 45 SER B 47 0 SHEET 2 C 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 89.840 89.840 124.630 90.00 90.00 120.00 P 61 6 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 0.011131 0.006426 0.000000 0.00000 SCALE2 0.000000 0.012853 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008024 0.00000