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HEADER COMPLEX (WILLEBRAND/IMMUNOGLOBULIN) 18-DEC-97 1OAK TITLE CRYSTAL STRUCTURE OF THE VON WILLEBRAND FACTOR (VWF) A1 TITLE 2 DOMAIN IN COMPLEX WITH THE FUNCTION BLOCKING NMC-4 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: NMC-4 IGG1; COMPND 3 CHAIN: L; COMPND 4 FRAGMENT: FAB FRAGMENT, AN ANTI VON WILLEBRAND FACTOR COMPND 5 (VWF) A1 DOMAIN; COMPND 6 ENGINEERED: YES; COMPND 7 OTHER_DETAILS: THE ANTIBODY HEAVY CHAIN CONSISTS OF TWO COMPND 8 SEGMENTS, H1 AND H2, BOTH LABELED CHAIN H IN THIS ENTRY; COMPND 9 MOL_ID: 2; COMPND 10 MOLECULE: NMC-4 IGG1; COMPND 11 CHAIN: H; COMPND 12 FRAGMENT: FAB FRAGMENT, AN ANTI VON WILLEBRAND FACTOR COMPND 13 (VWF) A1 DOMAIN; COMPND 14 ENGINEERED: YES; COMPND 15 OTHER_DETAILS: THE ANTIBODY HEAVY CHAIN CONSISTS OF TWO COMPND 16 SEGMENTS, H1 AND H2, BOTH LABELED CHAIN H IN THIS ENTRY; COMPND 17 MOL_ID: 3; COMPND 18 MOLECULE: VON WILLEBRAND FACTOR; COMPND 19 CHAIN: A; COMPND 20 FRAGMENT: A1 DOMAIN RESIDUES 507 - 702, OR GLYCOPROTEIN COMPND 21 IBA (A\:ALPHA) BINDING DOMAIN; COMPND 22 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 CELL_LINE: HYBRIDOMA; SOURCE 5 ORGAN: BLOOD; SOURCE 6 EXPRESSION_SYSTEM: MUS MUSCULUS; SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: MOPC21; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 10 ORGANISM_COMMON: MOUSE; SOURCE 11 CELL_LINE: HYBRIDOMA; SOURCE 12 ORGAN: BLOOD; SOURCE 13 EXPRESSION_SYSTEM: MUS MUSCULUS; SOURCE 14 EXPRESSION_SYSTEM_CELL_LINE: MOPC21; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_COMMON: HUMAN; SOURCE 18 ORGAN: BLOOD; SOURCE 19 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 20 EXPRESSION_SYSTEM_VECTOR_TYPE: T7 PROMOTER; SOURCE 21 EXPRESSION_SYSTEM_PLASMID: PET8C KEYWDS VON WILLEBRAND FACTOR, GLYCOPROTEIN IBA (A:ALPHA) BINDING, KEYWDS 2 COMPLEX (WILLEBRAND/IMMUNOGLOBULIN), BLOOD COAGULATION EXPDTA X-RAY DIFFRACTION AUTHOR R.CELIKEL,K.I.VARUGHESE REVDAT 2 01-APR-03 1OAK 1 JRNL REVDAT 1 21-OCT-98 1OAK 0 JRNL AUTH R.CELIKEL,K.I.VARUGHESE,MADHUSUDAN,A.YOSHIOKA, JRNL AUTH 2 J.WARE,Z.M.RUGGERI JRNL TITL CRYSTAL STRUCTURE OF THE VON WILLEBRAND FACTOR A1 JRNL TITL 2 DOMAIN IN COMPLEX WITH THE FUNCTION BLOCKING NMC-4 JRNL TITL 3 FAB. JRNL REF NAT.STRUCT.BIOL. V. 5 189 1998 JRNL REFN ASTM NSBIEW US ISSN 1072-8368 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH R.CELIKEL,MADHUSUDAN,K.I.VARUGHESE,M.SHIMA, REMARK 1 AUTH 2 A.YOSHIOKA,J.WARE,Z.M.RUGGERI REMARK 1 TITL CRYSTAL STRUCTURE OF NMC-4 FAB ANTI-VON WILLEBRAND REMARK 1 TITL 2 FACTOR A1 DOMAIN REMARK 1 REF BLOOD CELLS MOL.DIS. V. 23 123 1997 REMARK 1 REFN ASTM BCMDFX US ISSN 1079-9796 REMARK 2 REMARK 2 RESOLUTION. 2.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.0 REMARK 3 NUMBER OF REFLECTIONS : 44346 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING SET) : 0.201 REMARK 3 FREE R VALUE : 0.274 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1610 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 : 5241 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 366 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.00 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 11.90000 REMARK 3 B22 (A**2) : -17.30000 REMARK 3 B33 (A**2) : 5.30000 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) : 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) : 0.007 REMARK 3 BOND ANGLES (DEGREES) : 1.40 REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : NULL 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 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 1OAK 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 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : JUN-1995 REMARK 200 TEMPERATURE (KELVIN) : 90.0 REMARK 200 PH : 8.00 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 : BENT CYLINDRICAL GE(111) REMARK 200 OPTICS : PT COATED SI FLAT MIRROR BENT REMARK 200 FOR VERTICAL FOCUS REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE AREA DETECTOR 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 : 44346 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0 REMARK 200 DATA REDUNDANCY : 3.400 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.04800 REMARK 200 FOR THE DATA SET : 18.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.30 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.5 REMARK 200 DATA REDUNDANCY IN SHELL : 3.40 REMARK 200 R MERGE FOR SHELL (I) : 0.18400 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 6.400 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: NULL REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 AND MULTIPLE ISOMORPHOUS REPLACEMENT REMARK 200 SOFTWARE USED: PHASES, X-PLOR REMARK 200 STARTING MODEL: NMC4 (FAB) REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 64.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8 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 104.10000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.95000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 104.10000 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 30.95000 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 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 H 351 REMARK 465 ALA H 352 REMARK 465 ALA H 353 REMARK 465 GLN H 354 REMARK 465 THR H 355 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI REMARK 500 O HOH 744 O HOH 1016 2.13 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH 916 O HOH 916 2657 2.07 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 H 370 CB PRO H 370 CG 0.054 REMARK 500 PRO H 372 CB PRO H 372 CG 0.058 REMARK 500 LYS A 644 N LYS A 644 CA 0.078 REMARK 500 PRO A 702 CB PRO A 702 CG 0.058 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 PRO L 8 C - N - CD ANGL. DEV. = 8.6 DEGREES REMARK 500 ARG L 18 N - CA - C ANGL. DEV. =-10.2 DEGREES REMARK 500 SER L 52 N - CA - C ANGL. DEV. = 9.2 DEGREES REMARK 500 ILE L 75 N - CA - C ANGL. DEV. = -9.4 DEGREES REMARK 500 LEU L 136 N - CA - C ANGL. DEV. = -9.5 DEGREES REMARK 500 ASN L 137 N - CA - C ANGL. DEV. = 9.2 DEGREES REMARK 500 ASP H 272 N - CA - C ANGL. DEV. = -9.4 DEGREES REMARK 500 ARG H 306 N - CA - C ANGL. DEV. = -9.5 DEGREES REMARK 500 CYS H 309 N - CA - C ANGL. DEV. =-10.7 DEGREES REMARK 500 ASP H 324 N - CA - C ANGL. DEV. = 9.6 DEGREES REMARK 500 GLY H 367 N - CA - C ANGL. DEV. = 9.7 DEGREES REMARK 500 LEU H 397 N - CA - C ANGL. DEV. = -9.1 DEGREES REMARK 500 ALA A 592 N - CA - C ANGL. DEV. = -9.0 DEGREES REMARK 500 SER A 615 N - CA - C ANGL. DEV. = -8.7 DEGREES REMARK 500 VAL A 646 N - CA - C ANGL. DEV. = -9.5 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 -48.25 69.93 REMARK 500 ASP L 170 -7.80 128.53 DBREF 1OAK L 9 208 GB 1890296 AAB49725 1 200 DBREF 1OAK H 223 432 GB 1890294 AAB49724 1 210 DBREF 1OAK A 508 702 UNP P04275 VWF_HUMAN 1271 1465 SEQRES 1 L 212 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 212 SER LEU GLY ASP ARG VAL THR ILE SER CYS SER ALA SER SEQRES 3 L 212 GLN ASP ILE ASN LYS TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 L 212 PRO ASP GLY ALA VAL LYS LEU LEU ILE PHE TYR THR SER SEQRES 5 L 212 SER LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 212 GLY SER GLY THR ASP TYR SER LEU THR ILE SER ASN LEU SEQRES 7 L 212 GLU PRO GLU ASP ILE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 L 212 GLU LYS LEU PRO TRP THR PHE GLY GLY GLY THR LYS LEU SEQRES 9 L 212 GLU VAL LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE SEQRES 10 L 212 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SEQRES 11 L 212 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP SEQRES 12 L 212 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN SEQRES 13 L 212 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS SEQRES 14 L 212 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR SEQRES 15 L 212 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU SEQRES 16 L 212 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER SEQRES 17 L 212 PHE ASN ARG ASN SEQRES 1 H 223 GLN VAL GLN LEU ALA GLU SER GLY PRO GLY LEU VAL ALA SEQRES 2 H 223 PRO SER GLN SER LEU SER ILE THR CYS THR VAL SER GLY SEQRES 3 H 223 PHE SER LEU THR ASP TYR GLY VAL ASP TRP VAL ARG GLN SEQRES 4 H 223 PRO PRO GLY LYS GLY LEU GLU TRP LEU GLY MET ILE TRP SEQRES 5 H 223 GLY ASP GLY SER THR ASP TYR ASN SER ALA LEU LYS SER SEQRES 6 H 223 ARG LEU SER ILE THR LYS ASP ASN SER LYS SER GLN VAL SEQRES 7 H 223 PHE LEU LYS MET ASN SER LEU GLN THR ASP ASP THR ALA SEQRES 8 H 223 ARG TYR TYR CYS VAL ARG ASP PRO ALA ASP TYR GLY ASN SEQRES 9 H 223 TYR ASP TYR ALA LEU ASP TYR TRP GLY GLN GLY THR SER SEQRES 10 H 223 VAL THR VAL SER SER ALA LYS THR THR PRO PRO SER VAL SEQRES 11 H 223 TYR PRO LEU ALA PRO GLY SER ALA ALA GLN THR ASN SER SEQRES 12 H 223 MET VAL THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO SEQRES 13 H 223 GLU PRO VAL THR VAL THR TRP ASN SER GLY SER LEU SER SEQRES 14 H 223 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER ASP SEQRES 15 H 223 LEU TYR THR LEU SER SER SER VAL THR VAL PRO SER SER SEQRES 16 H 223 THR TRP PRO SER GLU THR VAL THR CYS ASN VAL ALA HIS SEQRES 17 H 223 PRO ALA SER SER THR LYS VAL ASP LYS LYS ILE VAL PRO SEQRES 18 H 223 ARG ASP 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 ILE 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 *366(H2 O) HELIX 1 1 PRO L 80 ASP L 82 5 3 HELIX 2 2 SER L 122 SER L 127 1 6 HELIX 3 3 LYS L 183 ARG L 188 1 6 HELIX 4 4 SER H 275 LEU H 277 5 3 HELIX 5 5 ASN H 287 LYS H 289 5 3 HELIX 6 6 THR H 301 ASP H 303 5 3 HELIX 7 7 ASN H 378 GLY H 380 5 3 HELIX 8 8 SER H 408 THR H 410 5 3 HELIX 9 9 PRO H 423 SER H 425 5 3 HELIX 10 10 GLU A 527 ARG A 543 1 17 HELIX 11 11 PRO A 574 GLN A 583 1 10 HELIX 12 12 THR A 594 PHE A 603 1 10 HELIX 13 13 GLN A 628 SER A 631 1 4 HELIX 14 14 PHE A 634 LYS A 644 1 11 HELIX 15 15 LEU A 659 GLN A 668 1 10 HELIX 16 16 VAL A 680 LEU A 697 1 18 SHEET 1 A 2 SER L 10 ALA L 13 0 SHEET 2 A 2 LYS L 103 VAL L 106 1 N LYS L 103 O LEU L 11 SHEET 1 B 3 VAL L 19 SER L 24 0 SHEET 2 B 3 ASP L 70 ILE L 75 -1 N ILE L 75 O VAL L 19 SHEET 3 B 3 PHE L 62 SER L 67 -1 N SER L 67 O ASP L 70 SHEET 1 C 3 ALA L 84 GLN L 90 0 SHEET 2 C 3 LEU L 33 LYS L 39 -1 N GLN L 38 O THR L 85 SHEET 3 C 3 VAL L 44 ILE L 48 -1 N ILE L 48 O TRP L 35 SHEET 1 D 4 THR L 114 PHE L 118 0 SHEET 2 D 4 GLY L 129 ASN L 137 -1 N ASN L 137 O THR L 114 SHEET 3 D 4 MET L 175 THR L 182 -1 N LEU L 181 O ALA L 130 SHEET 4 D 4 VAL L 159 TRP L 163 -1 N SER L 162 O SER L 176 SHEET 1 E 4 SER L 153 ARG L 155 0 SHEET 2 E 4 ILE L 144 ILE L 150 -1 N ILE L 150 O SER L 153 SHEET 3 E 4 SER L 191 HIS L 198 -1 N THR L 197 O ASN L 145 SHEET 4 E 4 ILE L 205 ASN L 210 -1 N PHE L 209 O TYR L 192 SHEET 1 F 4 GLN H 217 SER H 221 0 SHEET 2 F 4 LEU H 232 SER H 239 -1 N SER H 239 O GLN H 217 SHEET 3 F 4 GLN H 291 MET H 296 -1 N MET H 296 O LEU H 232 SHEET 4 F 4 LEU H 281 ASP H 286 -1 N ASP H 286 O GLN H 291 SHEET 1 G 5 THR H 330 VAL H 332 0 SHEET 2 G 5 ALA H 305 ASP H 312 -1 N TYR H 307 O THR H 330 SHEET 3 G 5 GLY H 247 GLN H 253 -1 N GLN H 253 O ARG H 306 SHEET 4 G 5 GLU H 260 ILE H 265 -1 N ILE H 265 O VAL H 248 SHEET 5 G 5 THR H 271 TYR H 273 -1 N ASP H 272 O MET H 264 SHEET 1 H 3 MET H 358 VAL H 365 0 SHEET 2 H 3 LEU H 400 PRO H 407 -1 N VAL H 406 O VAL H 359 SHEET 3 H 3 VAL H 386 THR H 388 -1 N HIS H 387 O SER H 403 SHEET 1 I 3 THR H 374 TRP H 377 0 SHEET 2 I 3 THR H 417 HIS H 422 -1 N ALA H 421 O THR H 374 SHEET 3 I 3 THR H 427 LYS H 432 -1 N LYS H 431 O CYS H 418 SHEET 1 J 6 PHE A 675 LEU A 677 0 SHEET 2 J 6 VAL A 646 ILE A 653 1 N GLY A 652 O PHE A 675 SHEET 3 J 6 SER A 615 MET A 622 1 N ARG A 616 O ILE A 647 SHEET 4 J 6 LEU A 513 ASP A 520 1 N ASP A 514 O SER A 615 SHEET 5 J 6 VAL A 551 TYR A 558 1 N ARG A 552 O LEU A 513 SHEET 6 J 6 SER A 562 ILE A 566 -1 N ILE A 566 O VAL A 555 SSBOND 1 CYS L 23 CYS L 88 SSBOND 2 CYS L 134 CYS L 194 SSBOND 3 CYS H 236 CYS H 309 SSBOND 4 CYS H 363 CYS H 418 SSBOND 5 CYS A 509 CYS A 695 CISPEP 1 LEU L 94 PRO L 95 0 -1.07 CISPEP 2 TYR L 140 PRO L 141 0 -0.44 CISPEP 3 PHE H 369 PRO H 370 0 0.13 CISPEP 4 GLU H 371 PRO H 372 0 0.04 CISPEP 5 TRP H 411 PRO H 412 0 0.68 CRYST1 208.200 61.900 72.900 90.00 108.60 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 0.004803 0.000000 0.001616 0.00000 SCALE2 0.000000 0.016155 0.000000 0.00000 SCALE3 0.000000 0.000000 0.014473 0.00000