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HEADER BLOOD CLOTTING 13-JUL-04 1U0N TITLE THE TERNARY VON WILLEBRAND FACTOR A1-GLYCOPROTEIN IBALPHA- TITLE 2 BOTROCETIN COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: VON WILLEBRAND FACTOR; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: VWFA 1; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: BOTROCETIN; COMPND 8 CHAIN: B; COMPND 9 FRAGMENT: ALPHA CHAIN; COMPND 10 SYNONYM: PLATELET COAGGLUTININ; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: BOTROCETIN; COMPND 13 CHAIN: C; COMPND 14 FRAGMENT: BETA CHAIN; COMPND 15 SYNONYM: PLATELET COAGGLUTININ; COMPND 16 MOL_ID: 4; COMPND 17 MOLECULE: PLATELET GLYCOPROTEIN IB; COMPND 18 CHAIN: D; COMPND 19 FRAGMENT: ALPHA CHAIN; COMPND 20 SYNONYM: GLYCOPROTEIN IBALPHA, GP-IB ALPHA, GPIBA, GPIB- COMPND 21 ALPHA, CD42B-ALPHA, CD42B; COMPND 22 ENGINEERED: YES; COMPND 23 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 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: BOTHROPS JARARACA; SOURCE 9 ORGANISM_COMMON: JARARACA; SOURCE 10 SECRETION: VENOM; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: BOTHROPS JARARACA; SOURCE 13 ORGANISM_COMMON: JARARACA; SOURCE 14 SECRETION: VENOM; SOURCE 15 MOL_ID: 4; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_COMMON: HUMAN; SOURCE 18 GENE: GP1BA; SOURCE 19 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 20 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 21 EXPRESSION_SYSTEM_CELL_LINE: SF9; SOURCE 22 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS; SOURCE 23 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1 KEYWDS ROSSMANN FOLD, LRR MOTIF, C-TYPE LECTIN FOLD, PROTEIN- KEYWDS 2 PROTEIN COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR K.FUKUDA,R.C.LIDDINGTON REVDAT 1 19-APR-05 1U0N 0 JRNL AUTH K.FUKUDA,T.DOGGETT,I.J.LAURENZI,R.C.LIDDINGTON, JRNL AUTH 2 T.G.DIACOVO JRNL TITL THE SNAKE VENOM PROTEIN BOTROCETIN ACTS AS A JRNL TITL 2 BIOLOGICAL BRACE TO PROMOTE DYSFUNCTIONAL PLATELET JRNL TITL 3 AGGREGATION JRNL REF NAT.STRUCT.MOL.BIOL. V. 12 152 2005 JRNL REFN US ISSN 1545-9993 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.95 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.0 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) : 2.95 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 171879.490 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.5 REMARK 3 NUMBER OF REFLECTIONS : 23643 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) : 0.213 REMARK 3 FREE R VALUE : 0.276 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1172 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008 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) : 2.95 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.11 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.40 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3505 REMARK 3 BIN R VALUE (WORKING SET) : 0.3600 REMARK 3 BIN FREE R VALUE : 0.3900 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.50 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 204 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.027 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 5864 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) : 48.80 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 3.95000 REMARK 3 B22 (A**2) : 3.95000 REMARK 3 B33 (A**2) : -7.89000 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) : 0.35 REMARK 3 ESD FROM SIGMAA (A) : 0.74 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) : 0.46 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.79 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) : 24.70 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) : 1.310 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.320 ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 1.620 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.660 ; 2.500 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : FLAT MODEL REMARK 3 KSOL : 0.81 REMARK 3 BSOL : 119.47 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 1U0N 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 RCSB023097. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 03-DEC-2003 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 7.50 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : ROTATING ANODE REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : RIGAKU REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : GRAPHITE REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27144 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.950 REMARK 200 RESOLUTION RANGE LOW (A) : 200.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.500 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.6 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : 0.09900 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 16.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.95 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00 REMARK 200 COMPLETENESS FOR SHELL (%) : 87.9 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.34700 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 3.100 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 (%): 68.44 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.90 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE, PH 7.5, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 277K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 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,1/4+Z REMARK 290 4555 1/2+Y,1/2-X,3/4+Z REMARK 290 5555 1/2-X,1/2+Y,1/4-Z REMARK 290 6555 1/2+X,1/2-Y,3/4-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 110.98350 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 54.15750 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 54.15750 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 55.49175 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 54.15750 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 54.15750 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 166.47525 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 54.15750 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 54.15750 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 55.49175 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 54.15750 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 54.15750 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 166.47525 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 110.98350 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, C, D 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 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 THR A 705 CA C O CB OG1 CG2 REMARK 470 LYS B1035 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 PRO A 503 CB PRO A 503 CG -0.049 REMARK 500 MET A 540 SD MET A 540 CE 0.057 REMARK 500 ILE A 647 CG1 ILE A 647 CD1 -0.047 REMARK 500 PRO A 704 C THR A 705 N -0.076 REMARK 500 MET D 239 SD MET D 239 CE -0.079 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 SER A 500 N - CA - C ANGL. DEV. = 8.4 DEGREES REMARK 500 TYR A 558 N - CA - C ANGL. DEV. = 10.1 DEGREES REMARK 500 PRO A 704 C - N - CA ANGL. DEV. = 15.6 DEGREES REMARK 500 PRO A 704 C - N - CD ANGL. DEV. =-12.7 DEGREES REMARK 500 GLY B1070 N - CA - C ANGL. DEV. = 8.5 DEGREES REMARK 500 GLY C2067 N - CA - C ANGL. DEV. = 13.8 DEGREES REMARK 500 LEU D 13 N - CA - C ANGL. DEV. = -8.7 DEGREES REMARK 500 ASN D 110 N - CA - C ANGL. DEV. =-12.3 DEGREES REMARK 500 LEU D 155 N - CA - C ANGL. DEV. = -8.9 DEGREES REMARK 500 MET D 239 N - CA - C ANGL. DEV. =-10.0 DEGREES REMARK 500 ASN D 250 N - CA - C ANGL. DEV. = 8.8 DEGREES REMARK 500 ASP D 252 N - CA - C ANGL. DEV. =-11.3 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 SER A 500 -104.06 31.66 REMARK 500 GLU A 501 125.73 78.12 REMARK 500 VAL D 234 -36.39 59.85 REMARK 500 ASN D 250 -139.78 -16.26 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1AUQ RELATED DB: PDB REMARK 900 THE UNCOMPLEXED A1 (WILD TYPE) REMARK 900 RELATED ID: 1IJB RELATED DB: PDB REMARK 900 THE MUTANT A1 (I546V) REMARK 900 RELATED ID: 1IJK RELATED DB: PDB REMARK 900 THE MUTANT A1:BOTROCETIN COMPLEX DBREF 1U0N A 498 705 UNP P04275 VWF_HUMAN 1261 1468 DBREF 1U0N B 1001 1133 UNP P22029 BOTA_BOTJA 1 133 DBREF 1U0N C 2001 2125 UNP P22030 BOTB_BOTJA 1 125 DBREF 1U0N D 1 265 UNP P07359 GP1BA_HUMAN 17 281 SEQADV 1U0N GLN D 21 UNP P07359 ASN 37 ENGINEERED SEQADV 1U0N GLN D 159 UNP P07359 ASN 175 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 ARG 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 133 ASP CYS PRO SER GLY TRP SER SER TYR GLU GLY ASN CYS SEQRES 2 B 133 TYR LYS PHE PHE GLN GLN LYS MET ASN TRP ALA ASP ALA SEQRES 3 B 133 GLU ARG PHE CYS SER GLU GLN ALA LYS GLY GLY HIS LEU SEQRES 4 B 133 VAL SER ILE LYS ILE TYR SER LYS GLU LYS ASP PHE VAL SEQRES 5 B 133 GLY ASP LEU VAL THR LYS ASN ILE GLN SER SER ASP LEU SEQRES 6 B 133 TYR ALA TRP ILE GLY LEU ARG VAL GLU ASN LYS GLU LYS SEQRES 7 B 133 GLN CYS SER SER GLU TRP SER ASP GLY SER SER VAL SER SEQRES 8 B 133 TYR GLU ASN VAL VAL GLU ARG THR VAL LYS LYS CYS PHE SEQRES 9 B 133 ALA LEU GLU LYS ASP LEU GLY PHE VAL LEU TRP ILE ASN SEQRES 10 B 133 LEU TYR CYS ALA GLN LYS ASN PRO PHE VAL CYS LYS SER SEQRES 11 B 133 PRO PRO PRO SEQRES 1 C 125 ASP CYS PRO PRO ASP TRP SER SER TYR GLU GLY HIS CYS SEQRES 2 C 125 TYR ARG PHE PHE LYS GLU TRP MET HIS TRP ASP ASP ALA SEQRES 3 C 125 GLU GLU PHE CYS THR GLU GLN GLN THR GLY ALA HIS LEU SEQRES 4 C 125 VAL SER PHE GLN SER LYS GLU GLU ALA ASP PHE VAL ARG SEQRES 5 C 125 SER LEU THR SER GLU MET LEU LYS GLY ASP VAL VAL TRP SEQRES 6 C 125 ILE GLY LEU SER ASP VAL TRP ASN LYS CYS ARG PHE GLU SEQRES 7 C 125 TRP THR ASP GLY MET GLU PHE ASP TYR ASP ASP TYR TYR SEQRES 8 C 125 LEU ILE ALA GLU TYR GLU CYS VAL ALA SER LYS PRO THR SEQRES 9 C 125 ASN ASN LYS TRP TRP ILE ILE PRO CYS THR ARG PHE LYS SEQRES 10 C 125 ASN PHE VAL CYS GLU PHE GLN ALA SEQRES 1 D 265 HIS PRO ILE CYS GLU VAL SER LYS VAL ALA SER HIS LEU SEQRES 2 D 265 GLU VAL ASN CYS ASP LYS ARG GLN LEU THR ALA LEU PRO SEQRES 3 D 265 PRO ASP LEU PRO LYS ASP THR THR ILE LEU HIS LEU SER SEQRES 4 D 265 GLU ASN LEU LEU TYR THR PHE SER LEU ALA THR LEU MET SEQRES 5 D 265 PRO TYR THR ARG LEU THR GLN LEU ASN LEU ASP ARG CYS SEQRES 6 D 265 GLU LEU THR LYS LEU GLN VAL ASP GLY THR LEU PRO VAL SEQRES 7 D 265 LEU GLY THR LEU ASP LEU SER HIS ASN GLN LEU GLN SER SEQRES 8 D 265 LEU PRO LEU LEU GLY GLN THR LEU PRO ALA LEU THR VAL SEQRES 9 D 265 LEU ASP VAL SER PHE ASN ARG LEU THR SER LEU PRO LEU SEQRES 10 D 265 GLY ALA LEU ARG GLY LEU GLY GLU LEU GLN GLU LEU TYR SEQRES 11 D 265 LEU LYS GLY ASN GLU LEU LYS THR LEU PRO PRO GLY LEU SEQRES 12 D 265 LEU THR PRO THR PRO LYS LEU GLU LYS LEU SER LEU ALA SEQRES 13 D 265 ASN ASN GLN LEU THR GLU LEU PRO ALA GLY LEU LEU ASN SEQRES 14 D 265 GLY LEU GLU ASN LEU ASP THR LEU LEU LEU GLN GLU ASN SEQRES 15 D 265 SER LEU TYR THR ILE PRO LYS GLY PHE PHE GLY SER HIS SEQRES 16 D 265 LEU LEU PRO PHE ALA PHE LEU HIS GLY ASN PRO TRP LEU SEQRES 17 D 265 CYS ASN CYS GLU ILE LEU TYR PHE ARG ARG TRP LEU GLN SEQRES 18 D 265 ASP ASN ALA GLU ASN VAL TYR VAL TRP LYS GLN GLY VAL SEQRES 19 D 265 ASP VAL LYS ALA MET THR SER ASN VAL ALA SER VAL GLN SEQRES 20 D 265 CYS ASP ASN SER ASP LYS PHE PRO VAL TYR LYS TYR PRO SEQRES 21 D 265 GLY LYS GLY CYS PRO HELIX 1 1 SER A 526 ARG A 543 1 18 HELIX 2 2 ARG A 573 GLN A 583 1 11 HELIX 3 3 SER A 593 GLN A 604 1 12 HELIX 4 4 MET A 630 ARG A 632 5 3 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 ASP A 681 ASP A 696 1 16 HELIX 8 8 ASN B 1022 ALA B 1034 1 13 HELIX 9 9 SER B 1046 LYS B 1058 1 13 HELIX 10 10 HIS C 2022 GLN C 2034 1 13 HELIX 11 11 SER C 2044 THR C 2055 1 12 HELIX 12 12 PRO C 2103 ASN C 2106 5 4 HELIX 13 13 ALA D 49 MET D 52 5 4 HELIX 14 14 LEU D 214 ASN D 223 1 10 HELIX 15 15 VAL D 243 VAL D 246 5 4 HELIX 16 16 PRO D 255 TYR D 259 5 5 SHEET 1 A 5 VAL A 551 ARG A 552 0 SHEET 2 A 5 LEU A 513 ASP A 520 1 N LEU A 513 O ARG A 552 SHEET 3 A 5 SER A 615 MET A 622 1 O ILE A 617 N VAL A 516 SHEET 4 A 5 VAL A 646 ILE A 653 1 O ILE A 653 N MET A 622 SHEET 5 A 5 PHE A 675 LEU A 677 1 O LEU A 677 N GLY A 652 SHEET 1 B 6 VAL A 551 ARG A 552 0 SHEET 2 B 6 LEU A 513 ASP A 520 1 N LEU A 513 O ARG A 552 SHEET 3 B 6 VAL A 555 TYR A 558 1 O VAL A 556 N LEU A 519 SHEET 4 B 6 SER A 562 ILE A 566 -1 O HIS A 563 N GLU A 557 SHEET 5 B 6 LYS D 237 SER D 241 -1 O LYS D 237 N ALA A 564 SHEET 6 B 6 TYR D 228 LYS D 231 -1 N LYS D 231 O ALA D 238 SHEET 1 C 4 SER B1007 SER B1008 0 SHEET 2 C 4 CYS B1013 MET B1021 -1 O TYR B1014 N SER B1007 SHEET 3 C 4 ASN B1124 SER B1130 -1 O SER B1130 N CYS B1013 SHEET 4 C 4 HIS B1038 LEU B1039 -1 N HIS B1038 O LYS B1129 SHEET 1 D 4 TRP B1115 LEU B1118 0 SHEET 2 D 4 CYS B1103 GLU B1107 -1 N CYS B1103 O LEU B1118 SHEET 3 D 4 TYR B1066 VAL B1073 -1 N ALA B1067 O LEU B1106 SHEET 4 D 4 PHE C2077 TRP C2079 -1 O GLU C2078 N ARG B1072 SHEET 1 E 3 ARG C2015 MET C2021 0 SHEET 2 E 3 LYS C2117 PHE C2123 -1 O CYS C2121 N ARG C2015 SHEET 3 E 3 ALA C2037 LEU C2039 -1 N HIS C2038 O GLU C2122 SHEET 1 F 5 ARG C2015 MET C2021 0 SHEET 2 F 5 LYS C2117 PHE C2123 -1 O CYS C2121 N ARG C2015 SHEET 3 F 5 VAL C2064 TRP C2065 1 N TRP C2065 O ASN C2118 SHEET 4 F 5 GLU C2097 SER C2101 -1 O SER C2101 N VAL C2064 SHEET 5 F 5 TRP C2108 PRO C2112 -1 O ILE C2111 N CYS C2098 SHEET 1 G10 GLU D 5 VAL D 9 0 SHEET 2 G10 HIS D 12 ASN D 16 -1 O ASN D 16 N GLU D 5 SHEET 3 G10 ILE D 35 HIS D 37 1 O HIS D 37 N VAL D 15 SHEET 4 G10 GLN D 59 ASN D 61 1 O ASN D 61 N LEU D 36 SHEET 5 G10 THR D 81 ASP D 83 1 O THR D 81 N LEU D 60 SHEET 6 G10 VAL D 104 ASP D 106 1 O ASP D 106 N LEU D 82 SHEET 7 G10 GLU D 128 TYR D 130 1 O GLU D 128 N LEU D 105 SHEET 8 G10 LYS D 152 SER D 154 1 O LYS D 152 N LEU D 129 SHEET 9 G10 THR D 176 LEU D 178 1 O LEU D 178 N LEU D 153 SHEET 10 G10 PHE D 199 PHE D 201 1 O PHE D 201 N LEU D 177 SHEET 1 H 2 THR D 45 SER D 47 0 SHEET 2 H 2 LYS D 69 GLN D 71 1 O GLN D 71 N PHE D 46 SSBOND 1 CYS A 509 CYS A 695 SSBOND 2 CYS B 1002 CYS B 1013 SSBOND 3 CYS B 1030 CYS B 1128 SSBOND 4 CYS B 1080 CYS C 2075 SSBOND 5 CYS B 1103 CYS B 1120 SSBOND 6 CYS C 2002 CYS C 2013 SSBOND 7 CYS C 2030 CYS C 2121 SSBOND 8 CYS C 2098 CYS C 2113 SSBOND 9 CYS D 4 CYS D 17 SSBOND 10 CYS D 209 CYS D 248 SSBOND 11 CYS D 211 CYS D 264 CISPEP 1 PRO A 703 PRO A 704 0 0.16 CRYST1 108.315 108.315 221.967 90.00 90.00 90.00 P 41 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 0.009232 0.000000 0.000000 0.00000 SCALE2 0.000000 0.009232 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004505 0.00000