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HEADER TOXIN 20-SEP-00 1FVU TITLE CRYSTAL STRUCTURE OF BOTROCETIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: BOTROCETIN ALPHA CHAIN; COMPND 3 CHAIN: A, C; COMPND 4 SYNONYM: PLATELET COAGGLUTININ ALPHA; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: BOTROCETIN BETA CHAIN; COMPND 7 CHAIN: B, D; COMPND 8 SYNONYM: PLATELET COAGGLUTININ BETA SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BOTHROPS JARARACA; SOURCE 3 ORGANISM_COMMON: SNAKE; SOURCE 4 SECRETION: VENOM; SOURCE 5 MOL_ID: 2; SOURCE 6 ORGANISM_SCIENTIFIC: BOTHROPS JARARACA; SOURCE 7 ORGANISM_COMMON: SNAKE; SOURCE 8 SECRETION: VENOM KEYWDS VON WILLBRAND FACTOR MODULATOR, C-TYPE LECTIN, METAL- KEYWDS 2 BINDING, LOOP EXCHANGED DIMER EXPDTA X-RAY DIFFRACTION AUTHOR U.SEN,S.VASUDEVAN,G.SUBBARAO,R.A.MCCLINTOC,R.CELIKEL, AUTHOR 2 Z.M.RUGGERI,K.I.VARUGHESE REVDAT 2 01-APR-03 1FVU 1 JRNL REVDAT 1 14-FEB-01 1FVU 0 JRNL AUTH U.SEN,S.VASUDEVAN,G.SUBBARAO,R.A.MCCLINTOCK, JRNL AUTH 2 R.CELIKEL,Z.M.RUGGERI,K.I.VARUGHESE JRNL TITL CRYSTAL STRUCTURE OF THE VON WILLEBRAND FACTOR JRNL TITL 2 MODULATOR BOTROCETIN. JRNL REF BIOCHEMISTRY V. 40 345 2001 JRNL REFN ASTM BICHAW US ISSN 0006-2960 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 0.4 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) : 1.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 381569.620 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 87.7 REMARK 3 NUMBER OF REFLECTIONS : 38784 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) : 0.199 REMARK 3 FREE R VALUE : 0.218 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1953 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005 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) : 1.80 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 60.70 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4151 REMARK 3 BIN R VALUE (WORKING SET) : 0.2350 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 : 241 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.016 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4160 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 2 REMARK 3 SOLVENT ATOMS : 603 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 16.00 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.40 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.24000 REMARK 3 B22 (A**2) : 0.09000 REMARK 3 B33 (A**2) : 0.16000 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) : 0.21 REMARK 3 ESD FROM SIGMAA (A) : 0.17 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) : 0.24 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.19 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.005 REMARK 3 BOND ANGLES (DEGREES) : 1.40 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.50 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.72 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) : 3.030 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 4.600 ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 4.250 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 6.380 ; 2.500 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : FLAT MODEL REMARK 3 KSOL : 0.33 REMARK 3 BSOL : 43.77 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.PA REMARK 3 PARAMETER FILE 2 : ION.PARAM REMARK 3 PARAMETER FILE 3 : WATER_REP.PARA REMARK 3 PARAMETER FILE 4 : NULL REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : ION.TOP REMARK 3 TOPOLOGY FILE 3 : WATER_REP.TOP REMARK 3 TOPOLOGY FILE 4 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1FVU 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 RCSB . REMARK 100 THE RCSB ID CODE IS RCSB011944. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 24-NOV-1999 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 8.50 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRL REMARK 200 BEAMLINE : BL9-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.980 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL 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 : 43228 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8 REMARK 200 DATA REDUNDANCY : 4.400 REMARK 200 R MERGE (I) : 0.04500 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 33.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83 REMARK 200 COMPLETENESS FOR SHELL (%) : 85.4 REMARK 200 DATA REDUNDANCY IN SHELL : 3.00 REMARK 200 R MERGE FOR SHELL (I) : 0.36000 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: NULL 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 (%): 36.24 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.93 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, PEG 400 AND MGCL2, PH REMARK 280 8.5. VAPOR DIFFUSION, HANGING DROP AT 295 K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 1/2-X,-Y,1/2+Z REMARK 290 3555 -X,1/2+Y,1/2-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 32.41450 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 51.75450 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.83300 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 51.75450 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.41450 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.83300 REMARK 290 SMTRY3 4 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 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 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 B 488 REMARK 465 ASP B 489 REMARK 465 TYR B 490 REMARK 465 TYR B 491 REMARK 465 ASP D 688 REMARK 465 ASP D 689 REMARK 465 TYR D 690 REMARK 465 TYR D 691 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 LYS A 35 CG CD CE NZ REMARK 470 TYR A 45 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 TYR C 245 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 THR D 635 OG1 CG2 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 GLU C 232 CD GLU C 232 OE2 0.076 REMARK 500 GLU D 678 C GLU D 678 O 0.035 REMARK 500 TRP D 679 CA TRP D 679 CB -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 LEU A 39 N - CA - C ANGL. DEV. =-12.5 DEGREES REMARK 500 SER A 41 N - CA - C ANGL. DEV. =-10.4 DEGREES REMARK 500 GLY A 70 N - CA - C ANGL. DEV. = 9.8 DEGREES REMARK 500 CYS A 80 N - CA - C ANGL. DEV. = 12.0 DEGREES REMARK 500 GLY A 111 N - CA - C ANGL. DEV. = 9.3 DEGREES REMARK 500 THR B 455 N - CA - C ANGL. DEV. = 9.9 DEGREES REMARK 500 GLY B 467 N - CA - C ANGL. DEV. = 14.4 DEGREES REMARK 500 ARG B 476 N - CA - C ANGL. DEV. = -9.9 DEGREES REMARK 500 LYS B 502 N - CA - C ANGL. DEV. = -8.7 DEGREES REMARK 500 ASN B 518 N - CA - C ANGL. DEV. = -9.9 DEGREES REMARK 500 LEU C 239 N - CA - C ANGL. DEV. = -9.6 DEGREES REMARK 500 SER C 241 N - CA - C ANGL. DEV. = -8.8 DEGREES REMARK 500 CYS C 280 N - CA - C ANGL. DEV. = 12.9 DEGREES REMARK 500 GLY C 311 N - CA - C ANGL. DEV. = 9.5 DEGREES REMARK 500 LEU D 659 N - CA - C ANGL. DEV. = -8.6 DEGREES REMARK 500 GLY D 667 N - CA - C ANGL. DEV. = 13.2 DEGREES REMARK 500 ARG D 676 N - CA - C ANGL. DEV. =-10.9 DEGREES REMARK 500 ASN D 718 N - CA - C ANGL. DEV. = -9.3 DEGREES DBREF 1FVU A 1 133 UNP P22029 BOTA_BOTJA 1 133 DBREF 1FVU B 401 525 UNP P22030 BOTB_BOTJA 1 125 DBREF 1FVU C 201 333 UNP P22029 BOTA_BOTJA 1 133 DBREF 1FVU D 601 725 UNP P22030 BOTB_BOTJA 1 125 SEQRES 1 A 133 ASP CYS PRO SER GLY TRP SER SER TYR GLU GLY ASN CYS SEQRES 2 A 133 TYR LYS PHE PHE GLN GLN LYS MET ASN TRP ALA ASP ALA SEQRES 3 A 133 GLU ARG PHE CYS SER GLU GLN ALA LYS GLY GLY HIS LEU SEQRES 4 A 133 VAL SER ILE LYS ILE TYR SER LYS GLU LYS ASP PHE VAL SEQRES 5 A 133 GLY ASP LEU VAL THR LYS ASN ILE GLN SER SER ASP LEU SEQRES 6 A 133 TYR ALA TRP ILE GLY LEU ARG VAL GLU ASN LYS GLU LYS SEQRES 7 A 133 GLN CYS SER SER GLU TRP SER ASP GLY SER SER VAL SER SEQRES 8 A 133 TYR GLU ASN VAL VAL GLU ARG THR VAL LYS LYS CYS PHE SEQRES 9 A 133 ALA LEU GLU LYS ASP LEU GLY PHE VAL LEU TRP ILE ASN SEQRES 10 A 133 LEU TYR CYS ALA GLN LYS ASN PRO PHE VAL CYS LYS SER SEQRES 11 A 133 PRO PRO PRO SEQRES 1 B 125 ASP CYS PRO PRO ASP TRP SER SER TYR GLU GLY HIS CYS SEQRES 2 B 125 TYR ARG PHE PHE LYS GLU TRP MET HIS TRP ASP ASP ALA SEQRES 3 B 125 GLU GLU PHE CYS THR GLU GLN GLN THR GLY ALA HIS LEU SEQRES 4 B 125 VAL SER PHE GLN SER LYS GLU GLU ALA ASP PHE VAL ARG SEQRES 5 B 125 SER LEU THR SER GLU MET LEU LYS GLY ASP VAL VAL TRP SEQRES 6 B 125 ILE GLY LEU SER ASP VAL TRP ASN LYS CYS ARG PHE GLU SEQRES 7 B 125 TRP THR ASP GLY MET GLU PHE ASP TYR ASP ASP TYR TYR SEQRES 8 B 125 LEU ILE ALA GLU TYR GLU CYS VAL ALA SER LYS PRO THR SEQRES 9 B 125 ASN ASN LYS TRP TRP ILE ILE PRO CYS THR ARG PHE LYS SEQRES 10 B 125 ASN PHE VAL CYS GLU PHE GLN ALA SEQRES 1 C 133 ASP CYS PRO SER GLY TRP SER SER TYR GLU GLY ASN CYS SEQRES 2 C 133 TYR LYS PHE PHE GLN GLN LYS MET ASN TRP ALA ASP ALA SEQRES 3 C 133 GLU ARG PHE CYS SER GLU GLN ALA LYS GLY GLY HIS LEU SEQRES 4 C 133 VAL SER ILE LYS ILE TYR SER LYS GLU LYS ASP PHE VAL SEQRES 5 C 133 GLY ASP LEU VAL THR LYS ASN ILE GLN SER SER ASP LEU SEQRES 6 C 133 TYR ALA TRP ILE GLY LEU ARG VAL GLU ASN LYS GLU LYS SEQRES 7 C 133 GLN CYS SER SER GLU TRP SER ASP GLY SER SER VAL SER SEQRES 8 C 133 TYR GLU ASN VAL VAL GLU ARG THR VAL LYS LYS CYS PHE SEQRES 9 C 133 ALA LEU GLU LYS ASP LEU GLY PHE VAL LEU TRP ILE ASN SEQRES 10 C 133 LEU TYR CYS ALA GLN LYS ASN PRO PHE VAL CYS LYS SER SEQRES 11 C 133 PRO PRO PRO SEQRES 1 D 125 ASP CYS PRO PRO ASP TRP SER SER TYR GLU GLY HIS CYS SEQRES 2 D 125 TYR ARG PHE PHE LYS GLU TRP MET HIS TRP ASP ASP ALA SEQRES 3 D 125 GLU GLU PHE CYS THR GLU GLN GLN THR GLY ALA HIS LEU SEQRES 4 D 125 VAL SER PHE GLN SER LYS GLU GLU ALA ASP PHE VAL ARG SEQRES 5 D 125 SER LEU THR SER GLU MET LEU LYS GLY ASP VAL VAL TRP SEQRES 6 D 125 ILE GLY LEU SER ASP VAL TRP ASN LYS CYS ARG PHE GLU SEQRES 7 D 125 TRP THR ASP GLY MET GLU PHE ASP TYR ASP ASP TYR TYR SEQRES 8 D 125 LEU ILE ALA GLU TYR GLU CYS VAL ALA SER LYS PRO THR SEQRES 9 D 125 ASN ASN LYS TRP TRP ILE ILE PRO CYS THR ARG PHE LYS SEQRES 10 D 125 ASN PHE VAL CYS GLU PHE GLN ALA HET MG 1001 1 HET MG 1002 1 HETNAM MG MAGNESIUM ION FORMUL 5 MG 2(MG 2+) FORMUL 7 HOH *603(H2 O) HELIX 1 1 ASN A 22 ALA A 34 1 13 HELIX 2 2 LYS A 47 ILE A 60 1 14 HELIX 3 3 VAL A 96 VAL A 100 5 5 HELIX 4 4 HIS B 422 GLN B 434 1 13 HELIX 5 5 SER B 444 SER B 453 1 10 HELIX 6 6 ASN C 222 ALA C 234 1 13 HELIX 7 7 LYS C 247 LYS C 258 1 12 HELIX 8 8 VAL C 296 VAL C 300 5 5 HELIX 9 9 HIS D 622 GLU D 632 1 11 HELIX 10 10 SER D 644 SER D 653 1 10 SHEET 1 A 4 SER A 7 TYR A 9 0 SHEET 2 A 4 ASN A 12 MET A 21 -1 O ASN A 12 N TYR A 9 SHEET 3 A 4 ASN A 124 SER A 130 -1 N ASN A 124 O MET A 21 SHEET 4 A 4 HIS A 38 LEU A 39 -1 O HIS A 38 N LYS A 129 SHEET 1 B 4 TRP A 115 LEU A 118 0 SHEET 2 B 4 CYS A 103 GLU A 107 -1 O CYS A 103 N LEU A 118 SHEET 3 B 4 TYR A 66 VAL A 73 -1 O ALA A 67 N LEU A 106 SHEET 4 B 4 PHE B 477 TRP B 479 -1 N GLU B 478 O ARG A 72 SHEET 1 C 4 SER B 407 TYR B 409 0 SHEET 2 C 4 HIS B 412 MET B 421 -1 O HIS B 412 N TYR B 409 SHEET 3 C 4 LYS B 517 PHE B 523 -1 N LYS B 517 O MET B 421 SHEET 4 C 4 HIS B 438 LEU B 439 -1 O HIS B 438 N GLU B 522 SHEET 1 D 6 SER B 407 TYR B 409 0 SHEET 2 D 6 HIS B 412 MET B 421 -1 O HIS B 412 N TYR B 409 SHEET 3 D 6 LYS B 517 PHE B 523 -1 N LYS B 517 O MET B 421 SHEET 4 D 6 VAL B 464 TRP B 465 1 N TRP B 465 O ASN B 518 SHEET 5 D 6 GLU B 497 LYS B 502 -1 N SER B 501 O VAL B 464 SHEET 6 D 6 LYS B 507 PRO B 512 -1 O LYS B 507 N LYS B 502 SHEET 1 E 4 SER C 207 TYR C 209 0 SHEET 2 E 4 ASN C 212 MET C 221 -1 N ASN C 212 O TYR C 209 SHEET 3 E 4 ASN C 324 SER C 330 -1 N ASN C 324 O MET C 221 SHEET 4 E 4 HIS C 238 LEU C 239 -1 O HIS C 238 N LYS C 329 SHEET 1 F 4 TRP C 315 LEU C 318 0 SHEET 2 F 4 CYS C 303 GLU C 307 -1 O CYS C 303 N LEU C 318 SHEET 3 F 4 TYR C 266 VAL C 273 -1 O ALA C 267 N LEU C 306 SHEET 4 F 4 PHE D 677 TRP D 679 -1 O GLU D 678 N ARG C 272 SHEET 1 G 4 SER D 607 TYR D 609 0 SHEET 2 G 4 HIS D 612 MET D 621 -1 O HIS D 612 N TYR D 609 SHEET 3 G 4 LYS D 717 GLN D 724 -1 N LYS D 717 O MET D 621 SHEET 4 G 4 HIS D 638 LEU D 639 -1 O HIS D 638 N GLU D 722 SHEET 1 H 6 SER D 607 TYR D 609 0 SHEET 2 H 6 HIS D 612 MET D 621 -1 O HIS D 612 N TYR D 609 SHEET 3 H 6 LYS D 717 GLN D 724 -1 N LYS D 717 O MET D 621 SHEET 4 H 6 VAL D 664 SER D 669 1 N TRP D 665 O ASN D 718 SHEET 5 H 6 GLU D 697 LYS D 702 -1 N VAL D 699 O LEU D 668 SHEET 6 H 6 LYS D 707 PRO D 712 -1 O LYS D 707 N LYS D 702 SSBOND 1 CYS A 2 CYS A 13 SSBOND 2 CYS A 30 CYS A 128 SSBOND 3 CYS A 80 CYS B 475 SSBOND 4 CYS A 103 CYS A 120 SSBOND 5 CYS B 402 CYS B 413 SSBOND 6 CYS B 430 CYS B 521 SSBOND 7 CYS B 498 CYS B 513 SSBOND 8 CYS C 202 CYS C 213 SSBOND 9 CYS C 230 CYS C 328 SSBOND 10 CYS C 280 CYS D 675 SSBOND 11 CYS C 303 CYS C 320 SSBOND 12 CYS D 602 CYS D 613 SSBOND 13 CYS D 630 CYS D 721 SSBOND 14 CYS D 698 CYS D 713 CRYST1 64.829 69.666 103.509 90.00 90.00 90.00 P 21 21 21 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 0.015425 0.000000 0.000000 0.00000 SCALE2 0.000000 0.014354 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009661 0.00000