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HEADER BLOOD CLOTTING/HYDROLASE INHIBITOR 09-JAN-03 1NM6 TITLE THROMBIN IN COMPLEX WITH SELECTIVE MACROCYCLIC INHIBITOR AT TITLE 2 1.8A COMPND MOL_ID: 1; COMPND 2 MOLECULE: THROMBIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: COAGULATION FACTOR II; COMPND 5 EC: 3.4.21.5; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: HIRUGEN; COMPND 8 CHAIN: B; COMPND 9 ENGINEERED: YES; COMPND 10 OTHER_DETAILS: 10 AA HIRUDIN ANALOGUE SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGAN: PLASMA FROM BLOOD; SOURCE 5 MOL_ID: 2; SOURCE 6 SYNTHETIC: YES KEYWDS THROMBIN INHIBITOR COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR P.G.NANTERMET,J.C.BARROW,C.L.NEWTON,J.M.PELLICORE,M.YOUNG, AUTHOR 2 S.D.LEWIS,B.J.LUCAS,J.A.KRUEGER,D.R.MCMASTERS,Y.YAN,L.C.KUO, AUTHOR 3 J.P.VACCA,H.G.SELNICK REVDAT 1 02-SEP-03 1NM6 0 JRNL AUTH P.G.NANTERMET,J.C.BARROW,C.L.NEWTON,J.M.PELLICORE, JRNL AUTH 2 M.YOUNG,S.D.LEWIS,B.J.LUCAS,J.A.KRUEGER, JRNL AUTH 3 D.R.MCMASTERS,Y.YAN,L.C.KUO,J.P.VACCA,H.G.SELNICK JRNL TITL DESIGN AND SYNTHESIS OF POTENT AND SELECTIVE JRNL TITL 2 MACROCYCLIC THROMBIN INHIBITORS JRNL REF BIOORG.MED.CHEM.LETT. V. 13 2781 2003 JRNL REFN ASTM BMCLE8 UK ISSN 0960-894X REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 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) : 1.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 500.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 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 : 32157 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) : 0.216 REMARK 3 FREE R VALUE : 0.238 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900 REMARK 3 FREE R VALUE TEST SET COUNT : 3181 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 : 2337 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 36 REMARK 3 SOLVENT ATOMS : 189 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL 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) : 0.009 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 BULK SOLVENT MODELING. REMARK 3 METHOD USED : NULL REMARK 3 KSOL : NULL REMARK 3 BSOL : 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 1NM6 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 RCSB017998. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 7.30 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : ROTATING ANODE REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200 REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS II REMARK 200 INTENSITY-INTEGRATION SOFTWARE : R-AXIS REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32157 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800 REMARK 200 RESOLUTION RANGE LOW (A) : 500.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0 REMARK 200 DATA REDUNDANCY : 5.000 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.04500 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: FOURIER SYNTHESIS REMARK 200 SOFTWARE USED: CNS REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 51.98 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, SODIUM PHOSPHATE, PH 7.3, REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K 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 34.85000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.70000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 34.85000 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 35.70000 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 2 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 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 A 14L REMARK 465 GLY A 14M REMARK 465 ARG A 15 REMARK 465 THR A 146A REMARK 465 TRP A 146B REMARK 465 THR A 146C REMARK 465 ALA A 146D REMARK 465 ASN A 146E REMARK 465 VAL A 146F REMARK 465 GLY A 146G REMARK 465 LYS A 146H 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 ILE A 14K CG1 CG2 CD1 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 HIS A 57 CA HIS A 57 CB 0.062 REMARK 500 PHE A 181 CA PHE A 181 CB 0.085 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 LYS A 14A N - CA - C ANGL. DEV. = 8.7 DEGREES REMARK 500 LEU A 33 N - CA - C ANGL. DEV. = -8.6 DEGREES REMARK 500 GLY A 43 N - CA - C ANGL. DEV. = -9.0 DEGREES REMARK 500 THR A 74 N - CA - C ANGL. DEV. = 9.0 DEGREES REMARK 500 GLU A 97A N - CA - C ANGL. DEV. = 9.0 DEGREES REMARK 500 ASP A 125 N - CA - C ANGL. DEV. = -8.3 DEGREES REMARK 500 ALA A 190 N - CA - C ANGL. DEV. = -9.0 DEGREES REMARK 500 PHE A 199 N - CA - C ANGL. DEV. =-13.5 DEGREES REMARK 500 GLU A 217 N - CA - C ANGL. DEV. = -8.8 DEGREES REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1NT1 RELATED DB: PDB DBREF 1NM6 A 1A 246 UNP P00734 THRB_HUMAN 335 621 SEQRES 1 A 287 ASP CYS GLY LEU ARG PRO LEU PHE GLU LYS LYS SER LEU SEQRES 2 A 287 GLU ASP LYS THR GLU ARG GLU LEU LEU GLU SER TYR ILE SEQRES 3 A 287 ASP GLY ARG ILE VAL GLU GLY SER ASP ALA GLU ILE GLY SEQRES 4 A 287 MET SER PRO TRP GLN VAL MET LEU PHE ARG LYS SER PRO SEQRES 5 A 287 GLN GLU LEU LEU CYS GLY ALA SER LEU ILE SER ASP ARG SEQRES 6 A 287 TRP VAL LEU THR ALA ALA HIS CYS LEU LEU TYR PRO PRO SEQRES 7 A 287 TRP ASP LYS ASN PHE THR GLU ASN ASP LEU LEU VAL ARG SEQRES 8 A 287 ILE GLY LYS HIS SER ARG THR ARG TYR GLU ARG ASN ILE SEQRES 9 A 287 GLU LYS ILE SER MET LEU GLU LYS ILE TYR ILE HIS PRO SEQRES 10 A 287 ARG TYR ASN TRP ARG GLU ASN LEU ASP ARG ASP ILE ALA SEQRES 11 A 287 LEU MET LYS LEU LYS LYS PRO VAL ALA PHE SER ASP TYR SEQRES 12 A 287 ILE HIS PRO VAL CYS LEU PRO ASP ARG GLU THR ALA ALA SEQRES 13 A 287 SER LEU LEU GLN ALA GLY TYR LYS GLY ARG VAL THR GLY SEQRES 14 A 287 TRP GLY ASN LEU LYS GLU THR TRP THR ALA ASN VAL GLY SEQRES 15 A 287 LYS GLY GLN PRO SER VAL LEU GLN VAL VAL ASN LEU PRO SEQRES 16 A 287 ILE VAL GLU ARG PRO VAL CYS LYS ASP SER THR ARG ILE SEQRES 17 A 287 ARG ILE THR ASP ASN MET PHE CYS ALA GLY TYR LYS PRO SEQRES 18 A 287 ASP GLU GLY LYS ARG GLY ASP ALA CYS GLU GLY ASP SER SEQRES 19 A 287 GLY GLY PRO PHE VAL MET LYS SER PRO PHE ASN ASN ARG SEQRES 20 A 287 TRP TYR GLN MET GLY ILE VAL SER TRP GLY GLU GLY CYS SEQRES 21 A 287 ASP ARG ASP GLY LYS TYR GLY PHE TYR THR HIS VAL PHE SEQRES 22 A 287 ARG LEU LYS LYS TRP ILE GLN LYS VAL ILE ASP GLN PHE SEQRES 23 A 287 GLY SEQRES 1 B 11 ASP PHE GLU GLU ILE PRO GLU GLU TYS LEU ALA MODRES 1NM6 TYS B 363 TYR SULFONATED TYROSINE HET TYS B 363 16 HET L86 1 36 HETNAM TYS SULFONATED TYROSINE HETNAM L86 (11S)-11-BENZYL-6-CHLORO-1,2,10,11,12,13,14,15,16,17, HETNAM 2 L86 18,19-DODECAHYDRO-5,9-METHANO-2,5,8,10,13,17- HETNAM 3 L86 BENZOHEXAAZACYCLOHENICOSINE-3,24-DIONE HETSYN L86 COMPOUND 31 FORMUL 2 TYS C9 H11 N O6 S FORMUL 3 L86 C27 H33 CL N6 O2 FORMUL 4 HOH *189(H2 O) HELIX 1 1 PHE A 7 SER A 11 5 5 HELIX 2 2 THR A 14B TYR A 14J 1 9 HELIX 3 3 ALA A 55 CYS A 58 5 4 HELIX 4 4 PRO A 60B ASP A 60E 5 4 HELIX 5 5 THR A 60I ASN A 62 5 3 HELIX 6 6 ASP A 125 LEU A 130 1 9 HELIX 7 7 GLU A 164 SER A 171 1 8 HELIX 8 8 LYS A 185 GLY A 186C 5 5 HELIX 9 9 LEU A 234 PHE A 245 1 12 HELIX 10 10 PRO B 360 ALA B 365 1 6 SHEET 1 A 7 SER A 20 ASP A 21 0 SHEET 2 A 7 GLN A 156 PRO A 161 -1 O VAL A 157 N SER A 20 SHEET 3 A 7 LYS A 135 GLY A 140 -1 N GLY A 136 O LEU A 160 SHEET 4 A 7 PRO A 198 LYS A 202 -1 O VAL A 200 N ARG A 137 SHEET 5 A 7 TRP A 207 TRP A 215 -1 O TYR A 208 N MET A 201 SHEET 6 A 7 GLY A 226 HIS A 230 -1 O PHE A 227 N TRP A 215 SHEET 7 A 7 MET A 180 ALA A 183 -1 N PHE A 181 O TYR A 228 SHEET 1 B 7 GLN A 30 ARG A 35 0 SHEET 2 B 7 GLU A 39 LEU A 46 -1 O CYS A 42 N LEU A 33 SHEET 3 B 7 TRP A 51 THR A 54 -1 O LEU A 53 N SER A 45 SHEET 4 B 7 ALA A 104 LEU A 108 -1 O ALA A 104 N THR A 54 SHEET 5 B 7 LYS A 81 ILE A 90 -1 N TYR A 89 O LEU A 105 SHEET 6 B 7 LEU A 64 ILE A 68 -1 N ILE A 68 O LYS A 81 SHEET 7 B 7 GLN A 30 ARG A 35 -1 N PHE A 34 O LEU A 65 SSBOND 1 CYS A 1 CYS A 122 SSBOND 2 CYS A 42 CYS A 58 SSBOND 3 CYS A 168 CYS A 182 SSBOND 4 CYS A 191 CYS A 220 CISPEP 1 SER A 36A PRO A 37 0 -0.17 CRYST1 69.700 71.400 72.300 90.00 100.50 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 0.014347 0.000000 0.002659 0.00000 SCALE2 0.000000 0.014006 0.000000 0.00000 SCALE3 0.000000 0.000000 0.014067 0.00000