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HEADER IMMUNE SYSTEM 08-NOV-02 1N64 TITLE CRYSTAL STRUCTURE ANALYSIS OF THE IMMUNODOMINANT ANTIGENIC TITLE 2 SITE ON HEPATITIS C VIRUS PROTEIN BOUND TO MAB 19D9D6 COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB 19D9D6 LIGHT CHAIN; COMPND 3 CHAIN: L; COMPND 4 MOL_ID: 2; COMPND 5 MOLECULE: FAB 19D9D6 HEAVY CHAIN; COMPND 6 CHAIN: H; COMPND 7 ENGINEERED: YES; COMPND 8 MOL_ID: 3; COMPND 9 MOLECULE: GENOME POLYPROTEIN CAPSID PROTEIN C; COMPND 10 CHAIN: P; COMPND 11 SYNONYM: HCV CORE 13-40 PEPTIDE, CORE PROTEIN, P22; COMPND 12 EC: 3.4.22.-, 3.4.21.98, 2.7.7.48; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 STRAIN: ASCITES; SOURCE 5 MOL_ID: 2; SOURCE 6 MOL_ID: 3; SOURCE 7 SYNTHETIC: YES; SOURCE 8 OTHER_DETAILS: SEQUENCE FROM HEPATITIS C VIRUS CORE PROTEIN KEYWDS ANTIBODY PEPTIDE COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR R.MENEZ,M.BOSSUS,B.MULLER,G.SIBAI,P.DALBON,F.DUCANCEL, AUTHOR 2 C.JOLIVET-REYNAUD,E.STURA REVDAT 1 25-FEB-03 1N64 0 JRNL AUTH R.MENEZ,M.BOSSUS,B.H.MULLER,G.SIBAI,P.DALBON, JRNL AUTH 2 F.DUCANCEL,C.JOLIVET-REYNAUD,E.A.STURA JRNL TITL CRYSTAL STRUCTURE OF A HYDROPHOBIC IMMUNODOMINANT JRNL TITL 2 ANTIGENIC SITE ON HEPATITIS C VIRUS CORE PROTEIN JRNL TITL 3 COMPLEXED TO MONOCLONAL ANTIBODY 19D9D6. JRNL REF J.IMMUNOL. V. 170 1917 2003 JRNL REFN ASTM JOIMA3 US ISSN 0022-1767 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.34 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 : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.34 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00 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) (%) : 92.2 REMARK 3 NUMBER OF REFLECTIONS : 14779 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) : 0.190 REMARK 3 FREE R VALUE : 0.245 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 724 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 : 3484 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 202 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.44 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) : 0.006 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 : ISOTROPIC 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 1N64 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 RCSB017565. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 30-MAR-2001 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 9.00 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : BM30A REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.009112 REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI (111) REMARK 200 OPTICS : MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : CCD 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 : 19303 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.340 REMARK 200 RESOLUTION RANGE LOW (A) : 20.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9 REMARK 200 DATA REDUNDANCY : 3.000 REMARK 200 R MERGE (I) : 0.07100 REMARK 200 R SYM (I) : 0.06700 REMARK 200 FOR THE DATA SET : 9.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.34 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.39 REMARK 200 COMPLETENESS FOR SHELL (%) : 91.3 REMARK 200 DATA REDUNDANCY IN SHELL : 1.70 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.23300 REMARK 200 FOR SHELL : 1.500 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: PDB ENTRIES 1UCB; 1DBA; 1HIL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 47.89 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 10% MPEG 5000, 250MM NACL, 50MM REMARK 280 TRIS-HCL, PH 9.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE REMARK 280 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -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 50.85000 REMARK 290 SMTRY3 2 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, P 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 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 THR H 89 O THR H 107 2.15 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 L 4 SD MET L 4 CE -0.046 REMARK 500 VAL H 109 CA VAL H 109 CB 0.040 REMARK 500 VAL H 197 CA VAL H 197 CB 0.042 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 N - CA - C ANGL. DEV. = -9.7 DEGREES REMARK 500 ILE L 75 N - CA - C ANGL. DEV. = -9.1 DEGREES REMARK 500 THR L 114 N - CA - C ANGL. DEV. = -9.8 DEGREES REMARK 500 VAL L 132 N - CA - C ANGL. DEV. = -9.0 DEGREES REMARK 500 ASN L 137 N - CA - C ANGL. DEV. = 9.5 DEGREES REMARK 500 ILE L 205 N - CA - C ANGL. DEV. = -8.6 DEGREES REMARK 500 CYS H 92 N - CA - C ANGL. DEV. = -9.0 DEGREES REMARK 500 GLY H 104 N - CA - C ANGL. DEV. =-12.1 DEGREES REMARK 500 SER H 120 N - CA - C ANGL. DEV. = -9.0 DEGREES REMARK 500 GLY H 144 N - CA - C ANGL. DEV. = 9.2 DEGREES REMARK 500 PRO H 147 C - N - CA ANGL. DEV. = -8.7 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 L 51 -36.49 75.02 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 68 DISTANCE = 5.18 ANGSTROMS DBREF 1N64 P 25 40 UNP P29846 POLG_HCVTW 25 40 SEQRES 1 L 220 ASP ILE VAL MET SER GLN SER PRO SER SER LEU ALA VAL SEQRES 2 L 220 SER ALA GLY GLU LYS VAL THR MET SER CYS LYS SER SER SEQRES 3 L 220 GLN SER LEU LEU ASN SER ARG THR ARG LYS ASN TYR LEU SEQRES 4 L 220 ALA TRP TYR GLN GLN LYS PRO GLY GLN SER PRO LYS VAL SEQRES 5 L 220 LEU ILE TYR TRP ALA SER THR ARG GLU SER GLY VAL PRO SEQRES 6 L 220 ASP ARG PHE THR GLY ARG GLY SER GLY THR ASP PHE THR SEQRES 7 L 220 LEU THR ILE SER SER VAL GLN ALA GLU ASP GLN ALA VAL SEQRES 8 L 220 TYR TYR CYS LYS GLN ALA TYR ILE PRO PRO LEU THR PHE SEQRES 9 L 220 GLY ALA GLY THR LYS LEU GLU LEU LYS ARG ALA ASP ALA SEQRES 10 L 220 ALA PRO THR VAL SER ILE PHE PRO PRO SER SER GLU GLN SEQRES 11 L 220 LEU THR SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN SEQRES 12 L 220 ASN PHE TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE SEQRES 13 L 220 ASP GLY SER GLU ARG GLN ASN GLY VAL LEU ASN SER TRP SEQRES 14 L 220 THR ASP GLN ASP SER LYS ASP SER THR TYR SER MET SER SEQRES 15 L 220 SER THR LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS SEQRES 16 L 220 ASN SER TYR THR CYS GLU ALA THR HIS LYS THR SER THR SEQRES 17 L 220 SER PRO ILE VAL LYS SER PHE ASN ARG ASN GLU CYS SEQRES 1 H 218 GLN ILE GLN LEU VAL GLN SER GLY PRO GLU LEU LYS LYS SEQRES 2 H 218 PRO GLY GLU THR VAL LYS ILE SER CYS LYS ALA SER GLY SEQRES 3 H 218 TYR THR PHE THR ASP PHE SER MET HIS TRP VAL ASN GLN SEQRES 4 H 218 ALA PRO GLY LYS GLY LEU ASN TRP MET GLY TRP VAL ASN SEQRES 5 H 218 THR GLU THR GLY GLU PRO THR TYR ALA ASP ASP PHE LYS SEQRES 6 H 218 GLY ARG PHE ALA PHE SER LEU GLU THR SER ALA SER THR SEQRES 7 H 218 ALA TYR LEU GLN ILE ASN SER LEU LYS ASN GLU ASP THR SEQRES 8 H 218 ALA THR TYR PHE CYS ALA ARG PHE LEU LEU ARG GLN TYR SEQRES 9 H 218 PHE ASP VAL TRP GLY ALA GLY THR THR VAL THR VAL SER SEQRES 10 H 218 SER ALA LYS THR THR PRO PRO SER VAL TYR PRO LEU ALA SEQRES 11 H 218 PRO GLY SER ALA ALA GLN THR ASN SER MET VAL THR LEU SEQRES 12 H 218 GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR SEQRES 13 H 218 VAL THR TRP ASN SER GLY SER LEU SER SER GLY VAL HIS SEQRES 14 H 218 THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU SEQRES 15 H 218 SER SER SER VAL THR VAL PRO SER SER THR TRP PRO SER SEQRES 16 H 218 GLU THR VAL THR CYS ASN VAL ALA HIS PRO ALA SER SER SEQRES 17 H 218 THR LYS VAL ASP LYS LYS ILE VAL PRO ARG SEQRES 1 P 16 PRO GLY GLY GLY GLN ILE VAL GLY GLY VAL TYR LEU LEU SEQRES 2 P 16 PRO ARG ARG FORMUL 4 HOH *202(H2 O) HELIX 1 1 GLN L 79 GLN L 83 5 5 HELIX 2 2 SER L 121 SER L 127 1 7 HELIX 3 3 LYS L 183 ARG L 188 1 6 HELIX 4 4 THR H 28 PHE H 32 5 5 HELIX 5 5 ASP H 61 LYS H 64 5 4 HELIX 6 6 THR H 73 ALA H 75 5 3 HELIX 7 7 SER H 156 SER H 158 5 3 HELIX 8 8 SER H 186 TRP H 188 5 3 HELIX 9 9 PRO H 200 SER H 203 5 4 HELIX 10 10 GLY P 32 LEU P 36 5 5 SHEET 1 A 4 MET L 4 SER L 7 0 SHEET 2 A 4 VAL L 19 SER L 25 -1 O LYS L 24 N SER L 5 SHEET 3 A 4 ASP L 70 ILE L 75 -1 O ILE L 75 N VAL L 19 SHEET 4 A 4 PHE L 62 SER L 67 -1 N THR L 63 O THR L 74 SHEET 1 B 6 SER L 10 SER L 14 0 SHEET 2 B 6 THR L 102 LYS L 107 1 O GLU L 105 N LEU L 11 SHEET 3 B 6 ALA L 84 GLN L 90 -1 N ALA L 84 O LEU L 104 SHEET 4 B 6 LEU L 33 GLN L 38 -1 N TYR L 36 O TYR L 87 SHEET 5 B 6 LYS L 45 TYR L 49 -1 O LYS L 45 N GLN L 37 SHEET 6 B 6 THR L 53 ARG L 54 -1 O THR L 53 N TYR L 49 SHEET 1 C 4 SER L 10 SER L 14 0 SHEET 2 C 4 THR L 102 LYS L 107 1 O GLU L 105 N LEU L 11 SHEET 3 C 4 ALA L 84 GLN L 90 -1 N ALA L 84 O LEU L 104 SHEET 4 C 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 D 2 LYS L 30 ASN L 31 0 SHEET 1 E 4 THR L 114 PHE L 118 0 SHEET 2 E 4 GLY L 129 PHE L 139 -1 O VAL L 133 N PHE L 118 SHEET 3 E 4 TYR L 173 THR L 182 -1 O LEU L 179 N VAL L 132 SHEET 4 E 4 VAL L 159 TRP L 163 -1 N LEU L 160 O THR L 178 SHEET 1 F 4 SER L 153 ARG L 155 0 SHEET 2 F 4 ASN L 145 ILE L 150 -1 N ILE L 150 O SER L 153 SHEET 3 F 4 SER L 191 THR L 197 -1 O GLU L 195 N LYS L 147 SHEET 4 F 4 ILE L 205 ASN L 210 -1 O ILE L 205 N ALA L 196 SHEET 1 G 4 GLN H 3 GLN H 6 0 SHEET 2 G 4 VAL H 18 SER H 25 -1 O SER H 25 N GLN H 3 SHEET 3 G 4 THR H 77 ILE H 82 -1 O LEU H 80 N ILE H 20 SHEET 4 G 4 PHE H 67 GLU H 72 -1 N SER H 70 O TYR H 79 SHEET 1 H 2 GLU H 10 LYS H 12 0 SHEET 2 H 2 VAL H 109 VAL H 111 1 O THR H 110 N GLU H 10 SHEET 1 I 5 PRO H 57 TYR H 59 0 SHEET 2 I 5 LEU H 45 VAL H 51 -1 N TRP H 50 O THR H 58 SHEET 3 I 5 MET H 34 GLN H 39 -1 N TRP H 36 O MET H 48 SHEET 4 I 5 PHE H 91 PHE H 95 -1 O PHE H 91 N VAL H 37 SHEET 1 J 4 SER H 120 LEU H 124 0 SHEET 2 J 4 MET H 135 TYR H 145 -1 O GLY H 139 N LEU H 124 SHEET 3 J 4 LEU H 174 PRO H 184 -1 O LEU H 177 N VAL H 142 SHEET 4 J 4 VAL H 163 THR H 165 -1 N HIS H 164 O SER H 180 SHEET 1 K 4 SER H 120 LEU H 124 0 SHEET 2 K 4 MET H 135 TYR H 145 -1 O GLY H 139 N LEU H 124 SHEET 3 K 4 LEU H 174 PRO H 184 -1 O LEU H 177 N VAL H 142 SHEET 4 K 4 VAL H 169 GLN H 171 -1 N VAL H 169 O THR H 176 SHEET 1 L 3 THR H 151 TRP H 154 0 SHEET 2 L 3 THR H 194 HIS H 199 -1 O ASN H 196 N THR H 153 SHEET 3 L 3 THR H 204 LYS H 209 -1 O LYS H 208 N CYS H 195 SSBOND 1 CYS L 23 CYS L 88 SSBOND 2 CYS L 134 CYS L 194 SSBOND 3 CYS H 22 CYS H 92 SSBOND 4 CYS H 140 CYS H 195 CISPEP 1 SER L 7 PRO L 8 0 -0.30 CISPEP 2 PRO L 94 PRO L 95 0 0.05 CISPEP 3 TYR L 140 PRO L 141 0 0.42 CISPEP 4 TRP H 188 PRO H 189 0 0.42 CRYST1 42.180 101.700 55.180 90.00 98.70 90.00 P 1 21 1 2 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 0.023708 0.000000 0.003628 0.00000 SCALE2 0.000000 0.009833 0.000000 0.00000 SCALE3 0.000000 0.000000 0.018333 0.00000