[Scop | Full Entry | Seq (local cached copy) | More Options ]
HEADER TOXIN/BLOOD CLOTTING 22-MAY-03 1UEX TITLE CRYSTAL STRUCTURE OF VON WILLEBRAND FACTOR A1 DOMAIN TITLE 2 COMPLEXED WITH SNAKE VENOM BITISCETIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: BITISCETIN ALPHA CHAIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: ALPHA-SUBUNIT; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: BITISCETIN BETA CHAIN; COMPND 7 CHAIN: B; COMPND 8 SYNONYM: BETA-SUBUNIT; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: VON WILLEBRAND FACTOR; COMPND 11 CHAIN: C; COMPND 12 FRAGMENT: A1 DOMAIN; COMPND 13 SYNONYM: VWF; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BITIS ARIETANS; SOURCE 3 ORGANISM_COMMON: PUFF ADDER; SOURCE 4 SECRETION: VENOM; SOURCE 5 MOL_ID: 2; SOURCE 6 ORGANISM_SCIENTIFIC: BITIS ARIETANS; SOURCE 7 ORGANISM_COMMON: PUFF ADDER; SOURCE 8 SECRETION: VENOM; SOURCE 9 MOL_ID: 3; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_COMMON: HUMAN; SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 13 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 14 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PET11B KEYWDS C-TYPE LECTIN HETERODIMER EXPDTA X-RAY DIFFRACTION AUTHOR N.MAITA,K.NISHIO,E.NISHIMOTO,T.MATSUI,Y.SHIKAMOTO,T.MORITA, AUTHOR 2 J.E.SADLER,H.MIZUNO REVDAT 1 30-SEP-03 1UEX 0 JRNL AUTH N.MAITA,K.NISHIO,E.NISHIMOTO,T.MATSUI,Y.SHIKAMOTO, JRNL AUTH 2 T.MORITA,J.E.SADLER,H.MIZUNO JRNL TITL CRYSTAL STRUCTURE OF VON WILLEBRAND FACTOR A1 JRNL TITL 2 DOMAIN COMPLEXED WITH SNAKE VENOM, BITISCETIN. JRNL TITL 3 INSIGHT INTO GLYCOPROTEIN IBALPHA BINDING JRNL TITL 4 MECHANISM INDUCED BY SNAKE VENOM PROTEINS. JRNL REF J.BIOL.CHEM. V. 278 37777 2003 JRNL REFN ASTM JBCHA3 US ISSN 0021-9258 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.85 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) : 2.85 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00 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) (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 9163 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) : 0.194 REMARK 3 FREE R VALUE : 0.276 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 1110 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 : 3651 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 40 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL 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) : NULL REMARK 3 ESD FROM SIGMAA (A) : NULL REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL 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) : 0.005 REMARK 3 BOND ANGLES (DEGREES) : 1.21 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.85 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.68 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 1UEX 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 3.102 (2007-05-29) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ . REMARK 100 THE RCSB ID CODE IS RCSB005748. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 13-OCT-2002 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 7.80 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : PHOTON FACTORY REMARK 200 BEAMLINE : BL-6B 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 : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA) REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9672 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.850 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 91.6 REMARK 200 DATA REDUNDANCY : 5.600 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.10700 REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.85 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.99 REMARK 200 COMPLETENESS FOR SHELL (%) : 91.6 REMARK 200 DATA REDUNDANCY IN SHELL : 5.70 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.31000 REMARK 200 FOR SHELL : 2.300 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: PDB ENTRY 1JWI AND 1AUQ REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 39.80 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 6000, 2% PEG-MME 550, 5% REMARK 280 MPD, PH 7.8, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 283K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 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 -Y,X,3/4+Z REMARK 290 4555 Y,-X,1/4+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 26.69700 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 40.04550 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 13.34850 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 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 1 REMARK 465 PRO A 2 REMARK 465 ARG A 128 REMARK 465 LEU A 129 REMARK 465 PRO A 130 REMARK 465 HIS A 131 REMARK 465 ASP B 1 REMARK 465 GLU B 2 REMARK 465 GLU C 497 REMARK 465 ASP C 498 REMARK 465 ILE C 499 REMARK 465 SER C 500 REMARK 465 PRO C 703 REMARK 465 PRO C 704 REMARK 465 THR C 705 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 GLY A 3 N GLY A 3 CA 0.039 REMARK 500 GLY B 3 N GLY B 3 CA 0.037 REMARK 500 MET C 541 SD MET C 541 CE -0.032 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 CYS A 79 N - CA - C ANGL. DEV. = 10.2 DEGREES REMARK 500 ASP A 114 N - CA - C ANGL. DEV. = -8.5 DEGREES REMARK 500 CYS A 117 N - CA - C ANGL. DEV. =-10.5 DEGREES REMARK 500 GLU A 119 N - CA - C ANGL. DEV. = -9.3 DEGREES REMARK 500 PRO A 122 N - CA - C ANGL. DEV. = -7.8 DEGREES REMARK 500 LEU B 41 N - CA - C ANGL. DEV. = 8.4 DEGREES REMARK 500 ARG B 115 N - CA - C ANGL. DEV. = -7.8 DEGREES REMARK 500 ARG C 545 N - CA - C ANGL. DEV. = -8.0 DEGREES REMARK 500 GLY C 561 N - CA - C ANGL. DEV. = -7.7 DEGREES REMARK 500 LEU C 621 CA - CB - CG ANGL. DEV. = -7.3 DEGREES REMARK 500 ARG C 629 N - CA - C ANGL. DEV. = -7.5 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 MET B 42 121.94 65.78 REMARK 500 HIS C 559 -102.29 -150.14 REMARK 500 LEU C 659 -45.11 66.69 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1JWI RELATED DB: PDB REMARK 900 FREE-FORM OF BITISCETIN REMARK 900 RELATED ID: 1AUQ RELATED DB: PDB REMARK 900 FREE-FORM OF VON WILLEBRAND FACTOR A1 DOMAIN DBREF 1UEX A 1 131 GB 2134244 JC5058 1 131 DBREF 1UEX B 1 125 GB 2134245 JC5059 1 125 DBREF 1UEX C 497 705 UNP P04275 VWF_HUMAN 1260 1468 SEQRES 1 A 131 ASP PRO GLY CYS LEU PRO ASP TRP SER SER TYR LYS GLY SEQRES 2 A 131 HIS CYS TYR LYS VAL PHE LYS LYS VAL GLY THR TRP GLU SEQRES 3 A 131 ASP ALA GLU LYS PHE CYS VAL GLU ASN SER GLY HIS LEU SEQRES 4 A 131 ALA SER ILE ASP SER LYS GLU GLU ALA ASP PHE VAL THR SEQRES 5 A 131 LYS LEU ALA SER GLN THR LEU THR LYS PHE VAL TYR ASP SEQRES 6 A 131 ALA TRP ILE GLY LEU ARG ASP GLU SER LYS THR GLN GLN SEQRES 7 A 131 CYS SER PRO GLN TRP THR ASP GLY SER SER VAL VAL TYR SEQRES 8 A 131 GLU ASN VAL ASP GLU PRO THR LYS CYS PHE GLY LEU ASP SEQRES 9 A 131 VAL HIS THR GLU TYR ARG THR TRP THR ASP LEU PRO CYS SEQRES 10 A 131 GLY GLU LYS ASN PRO PHE ILE CYS LYS SER ARG LEU PRO SEQRES 11 A 131 HIS SEQRES 1 B 125 ASP GLU GLY CYS LEU PRO ASP TRP SER SER TYR LYS GLY SEQRES 2 B 125 HIS CYS TYR LYS VAL PHE LYS VAL GLU LYS THR TRP ALA SEQRES 3 B 125 ASP ALA GLU LYS PHE CYS LYS GLU LEU VAL ASN GLY GLY SEQRES 4 B 125 HIS LEU MET SER VAL ASN SER ARG GLU GLU GLY GLU PHE SEQRES 5 B 125 ILE SER LYS LEU ALA LEU GLU LYS MET ARG ILE VAL LEU SEQRES 6 B 125 VAL TRP ILE GLY LEU SER HIS PHE TRP ARG ILE CYS PRO SEQRES 7 B 125 LEU ARG TRP THR ASP GLY ALA ARG LEU ASP TYR ARG ALA SEQRES 8 B 125 LEU SER ASP GLU PRO ILE CYS PHE VAL ALA GLU SER PHE SEQRES 9 B 125 HIS ASN LYS TRP ILE GLN TRP THR CYS ASN ARG LYS LYS SEQRES 10 B 125 SER PHE VAL CYS LYS TYR ARG VAL SEQRES 1 C 209 GLU ASP ILE SER GLU PRO PRO LEU HIS ASP PHE TYR CYS SEQRES 2 C 209 SER ARG LEU LEU ASP LEU VAL PHE LEU LEU ASP GLY SER SEQRES 3 C 209 SER ARG LEU SER GLU ALA GLU PHE GLU VAL LEU LYS ALA SEQRES 4 C 209 PHE VAL VAL ASP MET MET GLU ARG LEU ARG ILE SER GLN SEQRES 5 C 209 LYS TRP VAL ARG VAL ALA VAL VAL GLU TYR HIS ASP GLY SEQRES 6 C 209 SER HIS ALA TYR ILE GLY LEU LYS ASP ARG LYS ARG PRO SEQRES 7 C 209 SER GLU LEU ARG ARG ILE ALA SER GLN VAL LYS TYR ALA SEQRES 8 C 209 GLY SER GLN VAL ALA SER THR SER GLU VAL LEU LYS TYR SEQRES 9 C 209 THR LEU PHE GLN ILE PHE SER LYS ILE ASP ARG PRO GLU SEQRES 10 C 209 ALA SER ARG ILE ALA LEU LEU LEU MET ALA SER GLN GLU SEQRES 11 C 209 PRO GLN ARG MET SER ARG ASN PHE VAL ARG TYR VAL GLN SEQRES 12 C 209 GLY LEU LYS LYS LYS LYS VAL ILE VAL ILE PRO VAL GLY SEQRES 13 C 209 ILE GLY PRO HIS ALA ASN LEU LYS GLN ILE ARG LEU ILE SEQRES 14 C 209 GLU LYS GLN ALA PRO GLU ASN LYS ALA PHE VAL LEU SER SEQRES 15 C 209 SER VAL ASP GLU LEU GLU GLN GLN ARG ASP GLU ILE VAL SEQRES 16 C 209 SER TYR LEU CYS ASP LEU ALA PRO GLU ALA PRO PRO PRO SEQRES 17 C 209 THR FORMUL 4 HOH *40(H2 O) HELIX 1 1 THR A 24 GLU A 34 1 11 HELIX 2 2 SER A 44 LEU A 59 1 16 HELIX 3 3 VAL A 105 GLU A 108 5 4 HELIX 4 4 THR B 24 GLU B 34 1 11 HELIX 5 5 SER B 46 LYS B 60 1 15 HELIX 6 6 PHE B 73 CYS B 77 5 5 HELIX 7 7 SER C 526 GLU C 542 1 17 HELIX 8 8 ARG C 573 GLN C 583 1 11 HELIX 9 9 SER C 593 GLN C 604 1 12 HELIX 10 10 ASN C 633 LYS C 644 1 12 HELIX 11 11 LEU C 659 ALA C 669 1 11 HELIX 12 12 VAL C 680 ASP C 696 1 17 SHEET 1 A 4 SER A 9 TYR A 11 0 SHEET 2 A 4 HIS A 14 GLY A 23 -1 O TYR A 16 N SER A 9 SHEET 3 A 4 ASN A 121 SER A 127 -1 O PHE A 123 N PHE A 19 SHEET 4 A 4 HIS A 38 LEU A 39 -1 N HIS A 38 O LYS A 126 SHEET 1 B 4 TRP A 112 LEU A 115 0 SHEET 2 B 4 CYS A 100 LEU A 103 -1 N GLY A 102 O THR A 113 SHEET 3 B 4 ALA A 66 ASP A 72 -1 N ALA A 66 O LEU A 103 SHEET 4 B 4 LEU B 79 TRP B 81 -1 O ARG B 80 N ARG A 71 SHEET 1 C 4 SER B 9 TYR B 11 0 SHEET 2 C 4 HIS B 14 LYS B 23 -1 O HIS B 14 N TYR B 11 SHEET 3 C 4 LYS B 117 ARG B 124 -1 O LYS B 117 N LYS B 23 SHEET 4 C 4 GLY B 39 HIS B 40 -1 N HIS B 40 O LYS B 122 SHEET 1 D 3 LEU B 65 HIS B 72 0 SHEET 2 D 3 ILE B 97 GLU B 102 -1 O ILE B 97 N HIS B 72 SHEET 3 D 3 TRP B 108 THR B 112 -1 O ILE B 109 N VAL B 100 SHEET 1 E 6 SER C 562 ILE C 566 0 SHEET 2 E 6 VAL C 551 TYR C 558 -1 N VAL C 555 O TYR C 565 SHEET 3 E 6 LEU C 513 ASP C 520 1 N PHE C 517 O ALA C 554 SHEET 4 E 6 SER C 615 MET C 622 1 O ILE C 617 N ASP C 514 SHEET 5 E 6 VAL C 646 ILE C 653 1 O ILE C 647 N ARG C 616 SHEET 6 E 6 PHE C 675 LEU C 677 1 O PHE C 675 N GLY C 652 SSBOND 1 CYS A 4 CYS A 15 SSBOND 2 CYS A 32 CYS A 125 SSBOND 3 CYS A 79 CYS B 77 SSBOND 4 CYS A 100 CYS A 117 SSBOND 5 CYS B 4 CYS B 15 SSBOND 6 CYS B 32 CYS B 121 SSBOND 7 CYS B 98 CYS B 113 SSBOND 8 CYS C 509 CYS C 695 CRYST1 89.282 89.282 53.394 90.00 90.00 90.00 P 43 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 0.011200 0.000000 0.000000 0.00000 SCALE2 0.000000 0.011200 0.000000 0.00000 SCALE3 0.000000 0.000000 0.018729 0.00000