[Scop | Full Entry | Seq (local cached copy) | More Options ]
HEADER BLOOD CLOTTING 14-JUL-04 1U0O TITLE THE MOUSE VON WILLEBRAND FACTOR A1-BOTROCETIN COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: BOTROCETIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: ALPHA CHAIN; COMPND 5 SYNONYM: PLATELET COAGGLUTININ; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: BOTROCETIN; COMPND 8 CHAIN: B; COMPND 9 FRAGMENT: BETA CHAIN; COMPND 10 SYNONYM: PLATELET COAGGLUTININ; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: VON WILLEBRAND FACTOR; COMPND 13 CHAIN: C; COMPND 14 FRAGMENT: VWF A1; COMPND 15 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BOTHROPS JARARACA; SOURCE 3 ORGANISM_COMMON: JARARACA; SOURCE 4 SECRETION: VENOM; SOURCE 5 MOL_ID: 2; SOURCE 6 ORGANISM_SCIENTIFIC: BOTHROPS JARARACA; SOURCE 7 ORGANISM_COMMON: JARARACA; SOURCE 8 SECRETION: VENOM; SOURCE 9 MOL_ID: 3; SOURCE 10 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 11 ORGANISM_COMMON: MOUSE; SOURCE 12 GENE: VWF; SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 14 EXPRESSION_SYSTEM_COMMON: BACTERIA KEYWDS ROSSMANN FOLD, C-TYPE LECTIN FOLD, PROTEIN-PROTEIN COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR K.FUKUDA,R.C.LIDDINGTON REVDAT 1 19-APR-05 1U0O 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. 2.70 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) : 2.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 290750.720 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 92.0 REMARK 3 NUMBER OF REFLECTIONS : 11310 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) : 0.218 REMARK 3 FREE R VALUE : 0.288 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 574 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.012 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) : 2.70 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.85 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 81.00 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1552 REMARK 3 BIN R VALUE (WORKING SET) : 0.3200 REMARK 3 BIN FREE R VALUE : 0.3330 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 84 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.036 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3689 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 39 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 23.70 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.00 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -14.24000 REMARK 3 B22 (A**2) : 2.08000 REMARK 3 B33 (A**2) : 12.15000 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) : 0.33 REMARK 3 ESD FROM SIGMAA (A) : 0.48 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) : 0.54 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.008 REMARK 3 BOND ANGLES (DEGREES) : 1.40 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.10 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.83 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) : 1.250 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.150 ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 1.710 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.620 ; 2.500 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : FLAT MODEL REMARK 3 KSOL : 0.84 REMARK 3 BSOL : 104.42 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 : WATER_REP.PARAM REMARK 3 PARAMETER FILE 3 : NULL REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : WATER.TOP REMARK 3 TOPOLOGY FILE 3 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1U0O 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 RCSB023098. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 07-JAN-2003 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 6.50 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRL REMARK 200 BEAMLINE : BL7-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.08 REMARK 200 MONOCHROMATOR : SI(111) 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 : 12759 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700 REMARK 200 RESOLUTION RANGE LOW (A) : 200.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 92.4 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : 0.08900 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 16.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.75 REMARK 200 COMPLETENESS FOR SHELL (%) : 79.6 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.28400 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.500 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 (%): 44.21 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 5000 MME, PH 6.5, VAPOR REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K 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 28.16900 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 57.21200 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.83000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 57.21200 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.16900 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.83000 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 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 C 498 REMARK 465 THR C 499 REMARK 465 PRO C 500 REMARK 465 GLU C 501 REMARK 465 PRO C 502 REMARK 465 PRO C 503 REMARK 465 LEU C 504 REMARK 465 HIS C 505 REMARK 465 ASN C 506 REMARK 465 ALA C 703 REMARK 465 PRO C 704 REMARK 465 THR C 705 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 PRO C 702 CA C O CB CG CD 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 MET C 630 SD MET C 630 CE 0.083 REMARK 500 GLU C 700 C ALA C 701 N 0.151 REMARK 500 ALA C 701 C PRO C 702 N -0.090 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 GLU A 77 N - CA - C ANGL. DEV. = -8.5 DEGREES REMARK 500 CYS A 80 N - CA - C ANGL. DEV. = 9.1 DEGREES REMARK 500 GLU A 97 N - CA - C ANGL. DEV. = 9.7 DEGREES REMARK 500 LEU B 239 N - CA - C ANGL. DEV. = -9.3 DEGREES REMARK 500 GLY B 267 N - CA - C ANGL. DEV. = 11.0 DEGREES REMARK 500 ARG B 276 N - CA - C ANGL. DEV. = -9.8 DEGREES REMARK 500 ASN B 318 N - CA - C ANGL. DEV. =-10.9 DEGREES REMARK 500 ASP C 514 N - CA - C ANGL. DEV. =-11.8 DEGREES REMARK 500 ALA C 554 N - CA - C ANGL. DEV. = -8.7 DEGREES REMARK 500 HIS C 559 N - CA - C ANGL. DEV. = -9.2 DEGREES REMARK 500 ASP C 560 N - CA - C ANGL. DEV. = -9.4 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 ALA C 701 -80.66 52.78 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1AUQ RELATED DB: PDB REMARK 900 THE HUMAN A1 WILD TYPE REMARK 900 RELATED ID: 1IJB RELATED DB: PDB REMARK 900 THE MUTANT (I546V) A1 REMARK 900 RELATED ID: 1IJK RELATED DB: PDB REMARK 900 THE MUTANT (I546V):BOTROCETIN COMPLEX REMARK 900 RELATED ID: 1U0N RELATED DB: PDB DBREF 1U0O A 1 133 UNP P22029 BOTA_BOTJA 1 133 DBREF 1U0O B 201 325 UNP P22030 BOTB_BOTJA 1 125 DBREF 1U0O C 498 705 UNP Q8CIZ8 VWF_MOUSE 1261 1468 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 208 ASP THR PRO GLU PRO PRO LEU HIS ASN PHE TYR CYS SER SEQRES 2 C 208 LYS LEU LEU ASP LEU VAL PHE LEU LEU ASP GLY SER SER SEQRES 3 C 208 MET LEU SER GLU ALA GLU PHE GLU VAL LEU LYS ALA PHE SEQRES 4 C 208 VAL VAL GLY MET MET GLU ARG LEU HIS ILE SER GLN LYS SEQRES 5 C 208 ARG ILE ARG VAL ALA VAL VAL GLU TYR HIS ASP GLY SER SEQRES 6 C 208 ARG ALA TYR LEU GLU LEU LYS ALA ARG LYS ARG PRO SER SEQRES 7 C 208 GLU LEU ARG ARG ILE THR SER GLN ILE LYS TYR THR GLY SEQRES 8 C 208 SER GLN VAL ALA SER THR SER GLU VAL LEU LYS TYR THR SEQRES 9 C 208 LEU PHE GLN ILE PHE GLY LYS ILE ASP ARG PRO GLU ALA SEQRES 10 C 208 SER HIS ILE THR LEU LEU LEU THR ALA SER GLN GLU PRO SEQRES 11 C 208 PRO ARG MET ALA ARG ASN LEU VAL ARG TYR VAL GLN GLY SEQRES 12 C 208 LEU LYS LYS LYS LYS VAL ILE VAL ILE PRO VAL GLY ILE SEQRES 13 C 208 GLY PRO HIS ALA SER LEU LYS GLN ILE ARG LEU ILE GLU SEQRES 14 C 208 LYS GLN ALA PRO GLU ASN LYS ALA PHE LEU LEU SER GLY SEQRES 15 C 208 VAL ASP GLU LEU GLU GLN ARG ARG ASP GLU ILE VAL SER SEQRES 16 C 208 TYR LEU CYS ASP LEU ALA PRO GLU ALA PRO ALA PRO THR FORMUL 4 HOH *39(H2 O) HELIX 1 1 ASN A 22 SER A 31 1 10 HELIX 2 2 SER A 46 ILE A 60 1 15 HELIX 3 3 LYS A 108 VAL A 113 1 6 HELIX 4 4 HIS B 222 GLU B 232 1 11 HELIX 5 5 SER B 244 THR B 255 1 12 HELIX 6 6 ASP B 286 TYR B 291 5 6 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 PRO C 627 ARG C 632 1 6 HELIX 11 11 ASN C 633 LYS C 644 1 12 HELIX 12 12 SER C 658 GLN C 668 1 11 HELIX 13 13 GLY C 679 ASP C 696 1 18 SHEET 1 A 4 SER A 7 SER A 8 0 SHEET 2 A 4 CYS A 13 MET A 21 -1 O TYR A 14 N SER A 7 SHEET 3 A 4 ASN A 124 SER A 130 -1 O PHE A 126 N PHE A 17 SHEET 4 A 4 HIS A 38 LEU A 39 -1 N HIS A 38 O LYS A 129 SHEET 1 B 4 LEU A 114 LEU A 118 0 SHEET 2 B 4 CYS A 103 GLU A 107 -1 N CYS A 103 O LEU A 118 SHEET 3 B 4 TYR A 66 VAL A 73 -1 N ALA A 67 O LEU A 106 SHEET 4 B 4 PHE B 277 TRP B 279 -1 O GLU B 278 N ARG A 72 SHEET 1 C 4 SER B 207 TYR B 209 0 SHEET 2 C 4 HIS B 212 MET B 221 -1 O HIS B 212 N TYR B 209 SHEET 3 C 4 LYS B 317 PHE B 323 -1 O PHE B 319 N PHE B 217 SHEET 4 C 4 HIS B 238 LEU B 239 -1 N HIS B 238 O GLU B 322 SHEET 1 D 6 SER B 207 TYR B 209 0 SHEET 2 D 6 HIS B 212 MET B 221 -1 O HIS B 212 N TYR B 209 SHEET 3 D 6 LYS B 317 PHE B 323 -1 O PHE B 319 N PHE B 217 SHEET 4 D 6 VAL B 264 TRP B 265 1 N TRP B 265 O ASN B 318 SHEET 5 D 6 GLU B 297 LYS B 302 -1 O SER B 301 N VAL B 264 SHEET 6 D 6 LYS B 307 PRO B 312 -1 O TRP B 309 N ALA B 300 SHEET 1 E 6 SER C 562 LEU C 566 0 SHEET 2 E 6 ILE C 551 TYR C 558 -1 N GLU C 557 O ARG C 563 SHEET 3 E 6 LEU C 513 ASP C 520 1 N LEU C 519 O VAL C 556 SHEET 4 E 6 SER C 615 THR C 622 1 O ILE C 617 N VAL C 516 SHEET 5 E 6 VAL C 646 ILE C 653 1 O VAL C 651 N LEU C 620 SHEET 6 E 6 PHE C 675 LEU C 677 1 O LEU C 677 N GLY C 652 SSBOND 1 CYS A 2 CYS A 13 SSBOND 2 CYS A 30 CYS A 128 SSBOND 3 CYS A 80 CYS B 275 SSBOND 4 CYS A 103 CYS A 120 SSBOND 5 CYS B 202 CYS B 213 SSBOND 6 CYS B 230 CYS B 321 SSBOND 7 CYS B 298 CYS B 313 SSBOND 8 CYS C 509 CYS C 695 CRYST1 56.338 73.660 114.424 90.00 90.00 90.00 P 21 21 21 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 0.017750 0.000000 0.000000 0.00000 SCALE2 0.000000 0.013576 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008739 0.00000