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HEADER BLOOD CLOTTING/TOXIN 26-APR-01 1IJK TITLE THE VON WILLEBRAND FACTOR MUTANT (I546V) A1 DOMAIN- TITLE 2 BOTROCETIN COMPLEX 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: BOTROCETIN; COMPND 9 CHAIN: B; COMPND 10 FRAGMENT: A-SUBUNIT; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: BOTROCETIN; COMPND 13 CHAIN: C; COMPND 14 FRAGMENT: B-SUBUNIT SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: BOTHROPS JARARACA; SOURCE 8 ORGANISM_COMMON: JARARACA; SOURCE 9 SECRETION: VENOM; SOURCE 10 MOL_ID: 3; SOURCE 11 ORGANISM_SCIENTIFIC: BOTHROPS JARARACA; SOURCE 12 ORGANISM_COMMON: JARARACA; SOURCE 13 SECRETION: VENOM KEYWDS DINUCLEOTIDE-BINDING FOLD, C-TYPE LECTIN FOLD EXPDTA X-RAY DIFFRACTION AUTHOR K.FUKUDA,T.A.DOGGETT,L.A.BANKSTON,M.A.CRUZ,T.G.DIACOVO, AUTHOR 2 R.C.LIDDINGTON REVDAT 3 01-APR-03 1IJK 1 JRNL REVDAT 2 17-JUL-02 1IJK 1 TITLE JRNL REVDAT 1 10-JUL-02 1IJK 0 JRNL AUTH K.FUKUDA,T.A.DOGGETT,L.A.BANKSTON,M.A.CRUZ, JRNL AUTH 2 T.G.DIACOVO,R.C.LIDDINGTON JRNL TITL STRUCTURAL BASIS OF VON WILLEBRAND FACTOR JRNL TITL 2 ACTIVATION BY THE SNAKE TOXIN BOTROCETIN. JRNL REF STRUCTURE V. 10 943 2002 JRNL REFN ASTM STRUE6 UK ISSN 0969-2126 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH J.EMSLEY,M.CRUZ,R.HANDIN,R.LIDDINGTON REMARK 1 TITL CRYSTAL STRUCTURE OF THE VON WILLEBRAND FACTOR A1 REMARK 1 TITL 2 DOMAIN AND IMPLICATIONS FOR THE BINDING OF REMARK 1 TITL 3 PLATELET GLYCOPROTEIN IB REMARK 1 REF J.BIOL.CHEM. V. 273 10396 1998 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 REMARK 2 REMARK 2 RESOLUTION. 2.60 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) : 2.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1281188.060 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 92.7 REMARK 3 NUMBER OF REFLECTIONS : 15258 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) : 0.219 REMARK 3 FREE R VALUE : 0.279 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900 REMARK 3 FREE R VALUE TEST SET COUNT : 746 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.010 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) : 2.60 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.66 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 62.50 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2215 REMARK 3 BIN R VALUE (WORKING SET) : 0.2540 REMARK 3 BIN FREE R VALUE : 0.2740 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.40 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 41 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 : 3666 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 94 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 38.90 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.90 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -10.73000 REMARK 3 B22 (A**2) : 15.41000 REMARK 3 B33 (A**2) : -4.68000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.16000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.33 REMARK 3 ESD FROM SIGMAA (A) : 0.37 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) : 0.45 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.53 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.007 REMARK 3 BOND ANGLES (DEGREES) : 1.30 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.40 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.78 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) : 1.500 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.400 ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 1.860 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.810 ; 2.500 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : FLAT MODEL REMARK 3 KSOL : 0.90 REMARK 3 BSOL : 94.79 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 1IJK 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 RCSB013336. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-FEB-2001 REMARK 200 TEMPERATURE (KELVIN) : 111.0 REMARK 200 PH : 5.60 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRL REMARK 200 BEAMLINE : BL11-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.989 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE 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 : 18178 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600 REMARK 200 RESOLUTION RANGE LOW (A) : 100.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 92.9 REMARK 200 DATA REDUNDANCY : 2.700 REMARK 200 R MERGE (I) : 0.04600 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 23.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64 REMARK 200 COMPLETENESS FOR SHELL (%) : 62.5 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.20700 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL 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 (%): 56.60 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, SODIUM CITRATE, PH 5.6, REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -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 33.33600 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 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 SER A 500 REMARK 465 GLU A 501 REMARK 465 ALA A 701 REMARK 465 THR C 255 REMARK 465 SER C 256 REMARK 465 GLU C 257 REMARK 465 MET C 258 REMARK 465 LEU C 259 REMARK 465 LYS C 260 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 ARG A 571 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 608 CG CD CE NZ REMARK 470 LYS B 35 CG CD CE NZ REMARK 470 LYS B 47 CG CD CE NZ REMARK 470 LYS C 218 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 502 CB PRO A 502 CG 0.043 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 ASP A 514 N - CA - C ANGL. DEV. = -8.6 DEGREES REMARK 500 GLU A 557 N - CA - C ANGL. DEV. = -8.0 DEGREES REMARK 500 ASP A 560 N - CA - C ANGL. DEV. = -9.3 DEGREES REMARK 500 GLY A 561 N - CA - C ANGL. DEV. = -8.0 DEGREES REMARK 500 ALA A 592 N - CA - C ANGL. DEV. =-10.0 DEGREES REMARK 500 LEU B 39 N - CA - C ANGL. DEV. =-10.5 DEGREES REMARK 500 SER B 41 N - CA - C ANGL. DEV. = -9.7 DEGREES REMARK 500 SER B 62 N - CA - C ANGL. DEV. = -8.5 DEGREES REMARK 500 GLY B 70 N - CA - C ANGL. DEV. = 8.6 DEGREES REMARK 500 CYS B 80 N - CA - C ANGL. DEV. = 8.1 DEGREES REMARK 500 GLY B 111 N - CA - C ANGL. DEV. = 8.0 DEGREES REMARK 500 PRO B 125 N - CA - C ANGL. DEV. = -8.6 DEGREES REMARK 500 LEU C 239 N - CA - C ANGL. DEV. = -9.0 DEGREES REMARK 500 GLY C 267 N - CA - C ANGL. DEV. = 10.7 DEGREES REMARK 500 VAL C 271 N - CA - C ANGL. DEV. = 8.2 DEGREES REMARK 500 ILE C 310 N - CA - C ANGL. DEV. = -9.5 DEGREES REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1AUQ RELATED DB: PDB REMARK 900 1AUQ IS THE WILD TYPE A1 DOMAIN OF VON WILLEBRAND FACTOR REMARK 900 RELATED ID: 1IJB RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE MUTANT (I546V) A1 DOMAIN OF THE REMARK 900 VON WILLEBRAND FACTOR DBREF 1IJK A 500 701 UNP P04275 VWF_HUMAN 1263 1464 DBREF 1IJK B 1 133 UNP P22029 BOTA_BOTJA 1 133 DBREF 1IJK C 1 125 UNP P22030 BOTB_BOTJA 1 125 SEQADV 1IJK VAL A 546 UNP P04275 ILE 1309 ENGINEERED SEQRES 1 A 202 SER GLU PRO PRO LEU HIS ASP PHE TYR CYS SER ARG LEU SEQRES 2 A 202 LEU ASP LEU VAL PHE LEU LEU ASP GLY SER SER ARG LEU SEQRES 3 A 202 SER GLU ALA GLU PHE GLU VAL LEU LYS ALA PHE VAL VAL SEQRES 4 A 202 ASP MET MET GLU ARG LEU ARG VAL SER GLN LYS TRP VAL SEQRES 5 A 202 ARG VAL ALA VAL VAL GLU TYR HIS ASP GLY SER HIS ALA SEQRES 6 A 202 TYR ILE GLY LEU LYS ASP ARG LYS ARG PRO SER GLU LEU SEQRES 7 A 202 ARG ARG ILE ALA SER GLN VAL LYS TYR ALA GLY SER GLN SEQRES 8 A 202 VAL ALA SER THR SER GLU VAL LEU LYS TYR THR LEU PHE SEQRES 9 A 202 GLN ILE PHE SER LYS ILE ASP ARG PRO GLU ALA SER ARG SEQRES 10 A 202 ILE ALA LEU LEU LEU MET ALA SER GLN GLU PRO GLN ARG SEQRES 11 A 202 MET SER ARG ASN PHE VAL ARG TYR VAL GLN GLY LEU LYS SEQRES 12 A 202 LYS LYS LYS VAL ILE VAL ILE PRO VAL GLY ILE GLY PRO SEQRES 13 A 202 HIS ALA ASN LEU LYS GLN ILE ARG LEU ILE GLU LYS GLN SEQRES 14 A 202 ALA PRO GLU ASN LYS ALA PHE VAL LEU SER SER VAL ASP SEQRES 15 A 202 GLU LEU GLU GLN GLN ARG ASP GLU ILE VAL SER TYR LEU SEQRES 16 A 202 CYS ASP LEU ALA PRO GLU ALA 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 FORMUL 4 HOH *94(H2 O) HELIX 1 1 ALA A 528 ARG A 543 1 16 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 PRO A 627 SER A 631 5 5 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 GLN A 686 ASP A 696 1 11 HELIX 8 8 ASN B 22 GLN B 33 1 12 HELIX 9 9 LYS B 47 LYS B 58 1 12 HELIX 10 10 VAL B 96 VAL B 100 5 5 HELIX 11 11 HIS C 222 GLU C 232 1 11 HELIX 12 12 SER C 244 LEU C 254 1 11 HELIX 13 13 ASP C 286 TYR C 290 5 5 SHEET 1 A 6 SER A 562 ILE A 566 0 SHEET 2 A 6 VAL A 551 TYR A 558 -1 O VAL A 555 N TYR A 565 SHEET 3 A 6 LEU A 513 ASP A 520 1 O LEU A 513 N ARG A 552 SHEET 4 A 6 SER A 615 MET A 622 1 O SER A 615 N ASP A 514 SHEET 5 A 6 VAL A 646 ILE A 653 1 N ILE A 647 O ARG A 616 SHEET 6 A 6 PHE A 675 LEU A 677 1 N PHE A 675 O PRO A 650 SHEET 1 B 4 SER B 7 TYR B 9 0 SHEET 2 B 4 ASN B 12 MET B 21 -1 N ASN B 12 O TYR B 9 SHEET 3 B 4 ASN B 124 SER B 130 -1 N ASN B 124 O MET B 21 SHEET 4 B 4 HIS B 38 LEU B 39 -1 N HIS B 38 O LYS B 129 SHEET 1 C 4 TRP B 115 LEU B 118 0 SHEET 2 C 4 CYS B 103 GLU B 107 -1 O CYS B 103 N LEU B 118 SHEET 3 C 4 TYR B 66 VAL B 73 -1 O ALA B 67 N LEU B 106 SHEET 4 C 4 PHE C 277 TRP C 279 -1 N GLU C 278 O ARG B 72 SHEET 1 D 4 SER C 207 TYR C 209 0 SHEET 2 D 4 HIS C 212 MET C 221 -1 N HIS C 212 O TYR C 209 SHEET 3 D 4 LYS C 317 GLN C 324 -1 N LYS C 317 O MET C 221 SHEET 4 D 4 HIS C 238 LEU C 239 -1 N HIS C 238 O GLU C 322 SHEET 1 E 6 SER C 207 TYR C 209 0 SHEET 2 E 6 HIS C 212 MET C 221 -1 N HIS C 212 O TYR C 209 SHEET 3 E 6 LYS C 317 GLN C 324 -1 N LYS C 317 O MET C 221 SHEET 4 E 6 VAL C 264 TRP C 265 1 N TRP C 265 O ASN C 318 SHEET 5 E 6 GLU C 297 SER C 301 -1 N SER C 301 O VAL C 264 SHEET 6 E 6 TRP C 309 PRO C 312 -1 N TRP C 309 O ALA C 300 SSBOND 1 CYS A 509 CYS A 695 SSBOND 2 CYS B 2 CYS B 13 SSBOND 3 CYS B 30 CYS B 128 SSBOND 4 CYS B 80 CYS C 275 SSBOND 5 CYS B 103 CYS B 120 SSBOND 6 CYS C 202 CYS C 213 SSBOND 7 CYS C 230 CYS C 321 SSBOND 8 CYS C 298 CYS C 313 CRYST1 65.664 66.672 69.402 90.00 105.41 90.00 P 1 21 1 2 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 0.015229 0.000000 0.004198 0.00000 SCALE2 0.000000 0.014999 0.000000 0.00000 SCALE3 0.000000 0.000000 0.014946 0.00000