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HEADER IMMUNE SYSTEM 23-AUG-00 1FNS TITLE CRYSTAL STRUCTURE OF THE VON WILLEBRAND FACTOR (VWF) A1 TITLE 2 DOMAIN I546V MUTANT IN COMPLEX WITH THE FUNCTION BLOCKING TITLE 3 FAB NMC4 COMPND MOL_ID: 1; COMPND 2 MOLECULE: IMMUNOGLOBULIN NMC-4 IGG1; COMPND 3 CHAIN: L; COMPND 4 FRAGMENT: FAB FRAGMENT, LIGHT CHAIN; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: IMMUNOGLOBULIN NMC-4 IGG1; COMPND 7 CHAIN: H; COMPND 8 FRAGMENT: FAB FRAGMENT, HEAVY CHAIN; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: VON WILLEBRAND FACTOR; COMPND 11 CHAIN: A; COMPND 12 FRAGMENT: A1 DOMAIN RESIDUES 507 - 702, OR GLYCOPROTEIN COMPND 13 IBA (A\:ALPHA) BINDING DOMAIN; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 CELL: HYBRIDOMA CELLS, MOPC21 CELLS; SOURCE 5 MOL_ID: 2; SOURCE 6 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 7 ORGANISM_COMMON: MOUSE; SOURCE 8 CELL: HYBRIDOMA CELLS, MOPC21 CELLS; 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_VECTOR_TYPE: T7 PROMOTER; SOURCE 15 EXPRESSION_SYSTEM_PLASMID: PET8C KEYWDS VON WILLEBRAND FACTOR, GLYCOPROTEIN IBA (A:ALPHA) BINDING, KEYWDS 2 COMPLEX (WILLEBRAND/IMMUNOGLOBULIN), BLOOD COAGULATION TYPE KEYWDS 3 2B VON WILLEBRAND DISEASE EXPDTA X-RAY DIFFRACTION AUTHOR K.I.VARUGHESE REVDAT 3 22-MAY-07 1FNS 1 SOURCE DBREF SEQRES REMARK REVDAT 3 2 1 MASTER REVDAT 2 01-APR-03 1FNS 1 JRNL REVDAT 1 18-OCT-00 1FNS 0 JRNL AUTH R.CELIKEL,Z.M.RUGGERI,K.I.VARUGHESE JRNL TITL VON WILLEBRAND FACTOR CONFORMATION AND ADHESIVE JRNL TITL 2 FUNCTION IS MODULATED BY AN INTERNALIZED WATER JRNL TITL 3 MOLECULE. JRNL REF NAT.STRUCT.BIOL. V. 7 881 2000 JRNL REFN ASTM NSBIEW US ISSN 1072-8368 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH R.CELIKEL,K.I.VARUGHESE,MADHUSUDAN,A.YOSHIOKA, REMARK 1 AUTH 2 J.WARE,Z.M.RUGGERI REMARK 1 TITL CRYSTAL STRUCTURE OF THE VON WILLEBRAND FACTOR A1 REMARK 1 TITL 2 D DOMAIN IN COMPLEX WITH THE FUNCTION BLOCKING REMARK 1 TITL 3 NMC-4 DOMAIN IN COMPLEX WITH THE FUNCTION BLOCKING REMARK 1 TITL 4 NMC-4 FAB REMARK 1 REF NAT.STRUCT.BIOL. V. 5 189 1998 REMARK 1 REFN ASTM NSBIEW US ISSN 1072-8368 REMARK 2 REMARK 2 RESOLUTION. 2.00 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 : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 666370.390 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 80.0 REMARK 3 NUMBER OF REFLECTIONS : 49150 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) : 0.172 REMARK 3 FREE R VALUE : 0.207 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.300 REMARK 3 FREE R VALUE TEST SET COUNT : 1139 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) : 2.00 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.13 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 57.70 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5706 REMARK 3 BIN R VALUE (WORKING SET) : 0.2080 REMARK 3 BIN FREE R VALUE : 0.2530 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 2.30 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 136 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.017 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4900 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 636 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 23.50 REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -3.96000 REMARK 3 B22 (A**2) : 5.52000 REMARK 3 B33 (A**2) : -1.56000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.09000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.19 REMARK 3 ESD FROM SIGMAA (A) : 0.18 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) : 0.19 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.11 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.018 REMARK 3 BOND ANGLES (DEGREES) : 1.90 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 26.50 REMARK 3 IMPROPER ANGLES (DEGREES) : 1.22 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) : 1.340 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.020 ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 2.210 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.200 ; 2.500 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : FLAT MODEL REMARK 3 KSOL : 0.35 REMARK 3 BSOL : 52.94 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 : ION.PARAM REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM 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 1FNS 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 RCSB011748. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : 90.0 REMARK 200 PH : NULL 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) : NULL 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 : NULL REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL REMARK 200 RESOLUTION RANGE HIGH (A) : NULL REMARK 200 RESOLUTION RANGE LOW (A) : NULL REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : NULL REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL 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: NULL REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 62.27 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.26 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 1/2+X,1/2+Y,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 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 104.69800 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.33650 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 104.69800 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 31.33650 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: L, H, A 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 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH 1226 LIES ON A SPECIAL POSITION. 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 ALA H 352 REMARK 465 ALA H 353 REMARK 465 GLN H 354 REMARK 465 THR H 355 REMARK 465 ASN H 356 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 A 540 SD MET A 540 CE 0.115 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 L 33 CA - CB - CG ANGL. DEV. =-17.7 DEGREES REMARK 500 LEU L 136 N - CA - C ANGL. DEV. =-11.8 DEGREES REMARK 500 CYS L 214 N - CA - C ANGL. DEV. =-18.0 DEGREES REMARK 500 GLY H 439 N - CA - C ANGL. DEV. = 13.7 DEGREES REMARK 500 ASP A 560 N - CA - C ANGL. DEV. =-14.6 DEGREES REMARK 500 GLY A 561 N - CA - C ANGL. DEV. =-11.5 DEGREES REMARK 500 ALA A 592 N - CA - C ANGL. DEV. =-14.5 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 THR L 51 -44.86 63.94 REMARK 525 REMARK 525 SOLVENT REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH 1164 DISTANCE = 5.39 ANGSTROMS DBREF 1FNS A 508 702 UNP P04275 VWF_HUMAN 1271 1465 SEQADV 1FNS MET A 507 UNP P04275 CLONING ARTIFACT SEQADV 1FNS VAL A 546 UNP P04275 ILE 1309 CONFLICT SEQRES 1 L 214 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 214 SER LEU GLY ASP ARG VAL THR ILE SER CYS SER ALA SER SEQRES 3 L 214 GLN ASP ILE ASN LYS TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 L 214 PRO ASP GLY ALA VAL LYS LEU LEU ILE PHE TYR THR SER SEQRES 5 L 214 SER LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 214 GLY SER GLY THR ASP TYR SER LEU THR ILE SER ASN LEU SEQRES 7 L 214 GLU PRO GLU ASP ILE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 L 214 GLU LYS LEU PRO TRP THR PHE GLY GLY GLY THR LYS LEU SEQRES 9 L 214 GLU VAL LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE SEQRES 10 L 214 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SEQRES 11 L 214 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP SEQRES 12 L 214 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN SEQRES 13 L 214 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS SEQRES 14 L 214 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR SEQRES 15 L 214 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU SEQRES 16 L 214 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER SEQRES 17 L 214 PHE ASN ARG ASN GLU CYS SEQRES 1 H 225 GLN VAL GLN LEU LYS GLU SER GLY PRO GLY LEU VAL ALA SEQRES 2 H 225 PRO SER GLN SER LEU SER ILE THR CYS THR VAL SER GLY SEQRES 3 H 225 PHE SER LEU THR ASP TYR GLY VAL ASP TRP VAL ARG GLN SEQRES 4 H 225 PRO PRO GLY LYS GLY LEU GLU TRP LEU GLY MET ILE TRP SEQRES 5 H 225 GLY ASP GLY SER THR ASP TYR ASN SER ALA LEU LYS SER SEQRES 6 H 225 ARG LEU SER ILE THR LYS ASP ASN SER LYS SER GLN VAL SEQRES 7 H 225 PHE LEU LYS MET ASN SER LEU GLN THR ASP ASP THR ALA SEQRES 8 H 225 ARG TYR TYR CYS VAL ARG ASP PRO ALA ASP TYR GLY ASN SEQRES 9 H 225 TYR ASP TYR ALA LEU ASP TYR TRP GLY GLN GLY THR SER SEQRES 10 H 225 VAL THR VAL SER SER ALA LYS THR THR PRO PRO SER VAL SEQRES 11 H 225 TYR PRO LEU ALA PRO GLY SER ALA ALA GLN THR ASN SER SEQRES 12 H 225 MET VAL THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO SEQRES 13 H 225 GLU PRO VAL THR VAL THR TRP ASN SER GLY SER LEU SER SEQRES 14 H 225 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER ASP SEQRES 15 H 225 LEU TYR THR LEU SER SER SER VAL THR VAL PRO SER SER SEQRES 16 H 225 THR TRP PRO SER GLU THR VAL THR CYS ASN VAL ALA HIS SEQRES 17 H 225 PRO ALA SER SER THR LYS VAL ASP LYS LYS ILE VAL PRO SEQRES 18 H 225 ARG ASP CYS GLY SEQRES 1 A 196 MET TYR CYS SER ARG LEU LEU ASP LEU VAL PHE LEU LEU SEQRES 2 A 196 ASP GLY SER SER ARG LEU SER GLU ALA GLU PHE GLU VAL SEQRES 3 A 196 LEU LYS ALA PHE VAL VAL ASP MET MET GLU ARG LEU ARG SEQRES 4 A 196 VAL SER GLN LYS TRP VAL ARG VAL ALA VAL VAL GLU TYR SEQRES 5 A 196 HIS ASP GLY SER HIS ALA TYR ILE GLY LEU LYS ASP ARG SEQRES 6 A 196 LYS ARG PRO SER GLU LEU ARG ARG ILE ALA SER GLN VAL SEQRES 7 A 196 LYS TYR ALA GLY SER GLN VAL ALA SER THR SER GLU VAL SEQRES 8 A 196 LEU LYS TYR THR LEU PHE GLN ILE PHE SER LYS ILE ASP SEQRES 9 A 196 ARG PRO GLU ALA SER ARG ILE ALA LEU LEU LEU MET ALA SEQRES 10 A 196 SER GLN GLU PRO GLN ARG MET SER ARG ASN PHE VAL ARG SEQRES 11 A 196 TYR VAL GLN GLY LEU LYS LYS LYS LYS VAL ILE VAL ILE SEQRES 12 A 196 PRO VAL GLY ILE GLY PRO HIS ALA ASN LEU LYS GLN ILE SEQRES 13 A 196 ARG LEU ILE GLU LYS GLN ALA PRO GLU ASN LYS ALA PHE SEQRES 14 A 196 VAL LEU SER SER VAL ASP GLU LEU GLU GLN GLN ARG ASP SEQRES 15 A 196 GLU ILE VAL SER TYR LEU CYS ASP LEU ALA PRO GLU ALA SEQRES 16 A 196 PRO FORMUL 4 HOH *636(H2 O) HELIX 1 1 GLU L 79 ILE L 83 5 5 HELIX 2 2 SER L 121 THR L 126 1 6 HELIX 3 3 LYS L 183 GLU L 187 1 5 HELIX 4 4 SER H 275 LYS H 278 5 4 HELIX 5 5 ASN H 287 LYS H 289 5 3 HELIX 6 6 GLN H 300 THR H 304 5 5 HELIX 7 7 TYR H 316 TYR H 319 5 4 HELIX 8 8 SER H 379 SER H 381 5 3 HELIX 9 9 SER H 409 TRP H 411 5 3 HELIX 10 10 PRO H 423 SER H 426 5 4 HELIX 11 11 SER A 526 ARG A 543 1 18 HELIX 12 12 ARG A 573 GLN A 583 1 11 HELIX 13 13 SER A 593 GLN A 604 1 12 HELIX 14 14 PRO A 627 ARG A 632 5 6 HELIX 15 15 ASN A 633 LYS A 644 1 12 HELIX 16 16 ASN A 658 ALA A 669 1 12 HELIX 17 17 ASP A 681 LEU A 697 1 17 SHEET 1 A 4 MET L 4 THR L 5 0 SHEET 2 A 4 VAL L 19 ALA L 25 -1 O SER L 24 N THR L 5 SHEET 3 A 4 ASP L 70 ILE L 75 -1 N TYR L 71 O CYS L 23 SHEET 4 A 4 PHE L 62 SER L 67 -1 O SER L 63 N THR L 74 SHEET 1 B 5 SER L 53 LEU L 54 0 SHEET 2 B 5 VAL L 44 PHE L 49 -1 O PHE L 49 N SER L 53 SHEET 3 B 5 LEU L 33 GLN L 38 -1 O TRP L 35 N LEU L 47 SHEET 4 B 5 THR L 85 GLN L 90 -1 O THR L 85 N GLN L 38 SHEET 5 B 5 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 C 6 SER L 53 LEU L 54 0 SHEET 2 C 6 VAL L 44 PHE L 49 -1 O PHE L 49 N SER L 53 SHEET 3 C 6 LEU L 33 GLN L 38 -1 O TRP L 35 N LEU L 47 SHEET 4 C 6 THR L 85 GLN L 90 -1 O THR L 85 N GLN L 38 SHEET 5 C 6 THR L 102 VAL L 106 -1 O THR L 102 N TYR L 86 SHEET 6 C 6 SER L 10 ALA L 13 1 N LEU L 11 O LYS L 103 SHEET 1 D 4 THR L 114 PHE L 118 0 SHEET 2 D 4 GLY L 129 PHE L 139 -1 O VAL L 133 N PHE L 118 SHEET 3 D 4 TYR L 173 THR L 182 -1 O TYR L 173 N PHE L 139 SHEET 4 D 4 VAL L 159 TRP L 163 -1 N LEU L 160 O THR L 178 SHEET 1 E 4 SER L 153 ARG L 155 0 SHEET 2 E 4 ASN L 145 ILE L 150 -1 O TRP L 148 N ARG L 155 SHEET 3 E 4 SER L 191 THR L 197 -1 N THR L 193 O LYS L 149 SHEET 4 E 4 ILE L 205 ASN L 210 -1 O ILE L 205 N ALA L 196 SHEET 1 F 4 GLN H 217 SER H 221 0 SHEET 2 F 4 LEU H 232 SER H 239 -1 N THR H 235 O SER H 221 SHEET 3 F 4 GLN H 291 MET H 296 -1 O VAL H 292 N CYS H 236 SHEET 4 F 4 LEU H 281 ASP H 286 -1 N SER H 282 O LYS H 295 SHEET 1 G 5 THR H 271 TYR H 273 0 SHEET 2 G 5 GLU H 260 ILE H 265 -1 N MET H 264 O ASP H 272 SHEET 3 G 5 GLY H 247 GLN H 253 -1 N VAL H 248 O ILE H 265 SHEET 4 G 5 ALA H 305 ASP H 312 -1 O ARG H 306 N GLN H 253 SHEET 5 G 5 TYR H 325 TRP H 326 -1 O TYR H 325 N ARG H 311 SHEET 1 H 6 THR H 271 TYR H 273 0 SHEET 2 H 6 GLU H 260 ILE H 265 -1 N MET H 264 O ASP H 272 SHEET 3 H 6 GLY H 247 GLN H 253 -1 N VAL H 248 O ILE H 265 SHEET 4 H 6 ALA H 305 ASP H 312 -1 O ARG H 306 N GLN H 253 SHEET 5 H 6 THR H 330 VAL H 334 -1 O THR H 330 N TYR H 307 SHEET 6 H 6 LEU H 225 VAL H 226 1 N VAL H 226 O THR H 333 SHEET 1 I 4 SER H 343 LEU H 347 0 SHEET 2 I 4 MET H 358 TYR H 368 -1 O GLY H 362 N LEU H 347 SHEET 3 I 4 TYR H 398 PRO H 407 -1 N TYR H 398 O TYR H 368 SHEET 4 I 4 VAL H 386 THR H 388 -1 O HIS H 387 N SER H 403 SHEET 1 J 4 SER H 343 LEU H 347 0 SHEET 2 J 4 MET H 358 TYR H 368 -1 O GLY H 362 N LEU H 347 SHEET 3 J 4 TYR H 398 PRO H 407 -1 N TYR H 398 O TYR H 368 SHEET 4 J 4 VAL H 392 LEU H 393 -1 N VAL H 392 O THR H 399 SHEET 1 K 3 THR H 374 TRP H 377 0 SHEET 2 K 3 THR H 417 HIS H 422 -1 N ASN H 419 O THR H 376 SHEET 3 K 3 THR H 427 LYS H 432 -1 O THR H 427 N HIS H 422 SHEET 1 L 6 SER A 562 ILE A 566 0 SHEET 2 L 6 VAL A 551 TYR A 558 -1 O VAL A 555 N TYR A 565 SHEET 3 L 6 LEU A 513 ASP A 520 1 O LEU A 513 N ARG A 552 SHEET 4 L 6 SER A 615 MET A 622 1 O SER A 615 N ASP A 514 SHEET 5 L 6 VAL A 646 ILE A 653 1 O ILE A 647 N ALA A 618 SHEET 6 L 6 PHE A 675 LEU A 677 1 N PHE A 675 O PRO A 650 SSBOND 1 CYS L 23 CYS L 88 SSBOND 2 CYS L 134 CYS L 194 SSBOND 3 CYS L 214 CYS H 438 SSBOND 4 CYS H 236 CYS H 309 SSBOND 5 CYS H 363 CYS H 418 SSBOND 6 CYS A 509 CYS A 695 CISPEP 1 LEU L 94 PRO L 95 0 -0.62 CISPEP 2 TYR L 140 PRO L 141 0 0.44 CISPEP 3 PHE H 369 PRO H 370 0 0.09 CISPEP 4 GLU H 371 PRO H 372 0 -0.66 CISPEP 5 TRP H 411 PRO H 412 0 0.48 CRYST1 209.396 62.673 73.789 90.00 108.88 90.00 C 1 2 1 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 0.004776 0.000000 0.001633 0.00000 SCALE2 0.000000 0.015956 0.000000 0.00000 SCALE3 0.000000 0.000000 0.014323 0.00000