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HEADER IMMUNE SYSTEM/HYDROLASE 13-DEC-02 1J1P TITLE CRYSTAL STRUCTURE OF HYHEL-10 FV MUTANT LS91A COMPLEXED TITLE 2 WITH HEN EGG WHITE LYSOZYME COMPND MOL_ID: 1; COMPND 2 MOLECULE: LYSOZYME BINDING IG KAPPA CHAIN V23-J2 REGION; COMPND 3 CHAIN: L; COMPND 4 SYNONYM: LYSOZYME ANTIBODY, HYHEL-10; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: IG VH,ANTI-LYSOZYME; COMPND 9 CHAIN: H; COMPND 10 SYNONYM: LYSOZYME ANTIBODY, HYHEL-10; COMPND 11 ENGINEERED: YES; COMPND 12 MOL_ID: 3; COMPND 13 MOLECULE: LYSOZYME C; COMPND 14 CHAIN: Y; COMPND 15 EC: 3.2.1.17 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PKTN2; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 11 ORGANISM_COMMON: MOUSE; SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 13 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 14 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PKTN2; SOURCE 17 MOL_ID: 3; SOURCE 18 ORGANISM_SCIENTIFIC: GALLUS GALLUS; SOURCE 19 ORGANISM_COMMON: CHICKEN; SOURCE 20 TISSUE: EGG WHITE KEYWDS ANTIGEN-ANTIBODY COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR A.YOKOTA,K.TSUMOTO,M.SHIROISHI,H.KONDO,I.KUMAGAI REVDAT 2 18-FEB-03 1J1P 1 JRNL REVDAT 1 14-JAN-03 1J1P 0 JRNL AUTH A.YOKOTA,K.TSUMOTO,M.SHIROISHI,H.KONDO,I.KUMAGAI JRNL TITL THE ROLE OF HYDROGEN BONDING VIA INTERFACIAL WATER JRNL TITL 2 MOLECULES IN ANTIGEN-ANTIBODY COMPLEXATION. THE JRNL TITL 3 HYHEL-10-HEL INTERACTION JRNL REF J.BIOL.CHEM. V. 278 5410 2003 JRNL REFN ASTM JBCHA3 US ISSN 0021-9258 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 : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00 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) (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 36100 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING SET) : 0.191 REMARK 3 FREE R VALUE : 0.212 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1794 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) : 1.80 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.82 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.2413 REMARK 3 BIN FREE R VALUE : 0.2452 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : 47 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 : 2720 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 364 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) : 0.004 REMARK 3 BOND ANGLES (DEGREES) : 1.28 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 1J1P 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 3.102 (2007-05-29) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ . REMARK 100 THE RCSB ID CODE IS RCSB005519. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 25-OCT-2000 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 7.60 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : PHOTON FACTORY REMARK 200 BEAMLINE : BL-6A REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.00 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA) REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36699 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800 REMARK 200 RESOLUTION RANGE LOW (A) : 28.800 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 14.000 REMARK 200 R MERGE (I) : 0.06000 REMARK 200 R SYM (I) : 0.05800 REMARK 200 FOR THE DATA SET : 6.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 13.90 REMARK 200 R MERGE FOR SHELL (I) : 0.15600 REMARK 200 R SYM FOR SHELL (I) : 0.15000 REMARK 200 FOR SHELL : 4.700 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT 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 (%): 42.98 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, HEPES, GLYCEROL, METHYL- REMARK 280 PENTANEDIOL, PH 7.6, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 293.0K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,1/2+Z REMARK 290 3555 1/2-Y,1/2+X,1/4+Z REMARK 290 4555 1/2+Y,1/2-X,3/4+Z REMARK 290 5555 1/2-X,1/2+Y,1/4-Z REMARK 290 6555 1/2+X,1/2-Y,3/4-Z REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,1/2-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 117.37550 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 28.28000 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 28.28000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 58.68775 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 28.28000 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 28.28000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 176.06325 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 28.28000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 28.28000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 58.68775 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 28.28000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 28.28000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 176.06325 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 117.37550 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, Y 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: 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 ALA L 51 N - CA - C ANGL. DEV. = 7.8 DEGREES REMARK 500 LEU L 73 N - CA - C ANGL. DEV. = -8.1 DEGREES REMARK 500 TYR H 33 N - CA - C ANGL. DEV. = -9.2 DEGREES REMARK 500 GLY Y 4 N - CA - C ANGL. DEV. =-11.7 DEGREES REMARK 500 GLY Y 16 N - CA - C ANGL. DEV. = 9.0 DEGREES REMARK 500 GLY Y 54 N - CA - C ANGL. DEV. = 10.4 DEGREES REMARK 500 TRP Y 63 N - CA - C ANGL. DEV. = 12.1 DEGREES REMARK 500 ARG Y 128 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 L 51 -43.02 67.77 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1C08 RELATED DB: PDB REMARK 900 HYHEL-10 FV WILD TYPE COMPLEXED WITH HEN EGG WHITE LYSOZYME REMARK 900 RELATED ID: 1J1O RELATED DB: PDB REMARK 900 HYHEL-10 FV MUTANT LY50F COMPLEXED WITH HEN EGG WHITE REMARK 900 LYSOZYME REMARK 900 RELATED ID: 1J1X RELATED DB: PDB REMARK 900 HYHEL-10 FV MUTANT LS93A COMPLEXED WITH HEN EGG WHITE REMARK 900 LYSOZYME DBREF 1J1P L 1 107 UNP P01642 KV5I_MOUSE 1 107 DBREF 1J1P H 1 113 UNP P01823 HV47_MOUSE 1 113 DBREF 1J1P Y 1 129 UNP P00698 LYSC_CHICK 19 147 SEQADV 1J1P ALA L 91 UNP P01642 SER 91 ENGINEERED SEQADV 1J1P ALA H 114 UNP P01823 SEE REMARK 999 SEQRES 1 L 107 ASP ILE VAL LEU THR GLN SER PRO ALA THR LEU SER VAL SEQRES 2 L 107 THR PRO GLY ASN SER VAL SER LEU SER CYS ARG ALA SER SEQRES 3 L 107 GLN SER ILE GLY ASN ASN LEU HIS TRP TYR GLN GLN LYS SEQRES 4 L 107 SER HIS GLU SER PRO ARG LEU LEU ILE LYS TYR ALA SER SEQRES 5 L 107 GLN SER ILE SER GLY ILE PRO SER ARG PHE SER GLY SER SEQRES 6 L 107 GLY SER GLY THR ASP PHE THR LEU SER ILE ASN SER VAL SEQRES 7 L 107 GLU THR GLU ASP PHE GLY MET TYR PHE CYS GLN GLN ALA SEQRES 8 L 107 ASN SER TRP PRO TYR THR PHE GLY GLY GLY THR LYS LEU SEQRES 9 L 107 GLU ILE LYS SEQRES 1 H 114 ASP VAL GLN LEU GLN GLU SER GLY PRO SER LEU VAL LYS SEQRES 2 H 114 PRO SER GLN THR LEU SER LEU THR CYS SER VAL THR GLY SEQRES 3 H 114 ASP SER ILE THR SER ASP TYR TRP SER TRP ILE ARG LYS SEQRES 4 H 114 PHE PRO GLY ASN ARG LEU GLU TYR MET GLY TYR VAL SER SEQRES 5 H 114 TYR SER GLY SER THR TYR TYR ASN PRO SER LEU LYS SER SEQRES 6 H 114 ARG ILE SER ILE THR ARG ASP THR SER LYS ASN GLN TYR SEQRES 7 H 114 TYR LEU ASP LEU ASN SER VAL THR THR GLU ASP THR ALA SEQRES 8 H 114 THR TYR TYR CYS ALA ASN TRP ASP GLY ASP TYR TRP GLY SEQRES 9 H 114 GLN GLY THR LEU VAL THR VAL SER ALA ALA SEQRES 1 Y 129 LYS VAL PHE GLY ARG CYS GLU LEU ALA ALA ALA MET LYS SEQRES 2 Y 129 ARG HIS GLY LEU ASP ASN TYR ARG GLY TYR SER LEU GLY SEQRES 3 Y 129 ASN TRP VAL CYS ALA ALA LYS PHE GLU SER ASN PHE ASN SEQRES 4 Y 129 THR GLN ALA THR ASN ARG ASN THR ASP GLY SER THR ASP SEQRES 5 Y 129 TYR GLY ILE LEU GLN ILE ASN SER ARG TRP TRP CYS ASN SEQRES 6 Y 129 ASP GLY ARG THR PRO GLY SER ARG ASN LEU CYS ASN ILE SEQRES 7 Y 129 PRO CYS SER ALA LEU LEU SER SER ASP ILE THR ALA SER SEQRES 8 Y 129 VAL ASN CYS ALA LYS LYS ILE VAL SER ASP GLY ASN GLY SEQRES 9 Y 129 MET ASN ALA TRP VAL ALA TRP ARG ASN ARG CYS LYS GLY SEQRES 10 Y 129 THR ASP VAL GLN ALA TRP ILE ARG GLY CYS ARG LEU FORMUL 4 HOH *364(H2 O) HELIX 1 1 GLU L 79 PHE L 83 5 5 HELIX 2 2 SER H 28 ASP H 32 5 5 HELIX 3 3 PRO H 61 LYS H 64 5 4 HELIX 4 4 THR H 86 THR H 90 5 5 HELIX 5 5 GLY Y 4 HIS Y 15 1 12 HELIX 6 6 ASN Y 19 TYR Y 23 5 5 HELIX 7 7 SER Y 24 ASN Y 37 1 14 HELIX 8 8 PRO Y 79 SER Y 85 5 7 HELIX 9 9 ILE Y 88 SER Y 100 1 13 HELIX 10 10 ASN Y 103 ALA Y 107 5 5 HELIX 11 11 TRP Y 108 CYS Y 115 1 8 HELIX 12 12 ASP Y 119 ILE Y 124 5 6 SHEET 1 A 4 LEU L 4 SER L 7 0 SHEET 2 A 4 VAL L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 A 4 ASP L 70 ILE L 75 -1 O LEU L 73 N LEU L 21 SHEET 4 A 4 PHE L 62 SER L 67 -1 N SER L 63 O SER L 74 SHEET 1 B 5 GLN L 53 SER L 54 0 SHEET 2 B 5 ARG L 45 LYS L 49 -1 N LYS L 49 O GLN L 53 SHEET 3 B 5 LEU L 33 GLN L 38 -1 N TRP L 35 O LEU L 47 SHEET 4 B 5 GLY L 84 GLN L 90 -1 O GLN L 89 N HIS L 34 SHEET 5 B 5 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 C 6 GLN L 53 SER L 54 0 SHEET 2 C 6 ARG L 45 LYS L 49 -1 N LYS L 49 O GLN L 53 SHEET 3 C 6 LEU L 33 GLN L 38 -1 N TRP L 35 O LEU L 47 SHEET 4 C 6 GLY L 84 GLN L 90 -1 O GLN L 89 N HIS L 34 SHEET 5 C 6 THR L 102 ILE L 106 -1 O LEU L 104 N GLY L 84 SHEET 6 C 6 THR L 10 VAL L 13 1 N LEU L 11 O LYS L 103 SHEET 1 D 4 GLN H 3 SER H 7 0 SHEET 2 D 4 LEU H 18 THR H 25 -1 O THR H 21 N SER H 7 SHEET 3 D 4 GLN H 77 LEU H 82 -1 O LEU H 82 N LEU H 18 SHEET 4 D 4 ILE H 67 ASP H 72 -1 N THR H 70 O TYR H 79 SHEET 1 E 6 LEU H 11 VAL H 12 0 SHEET 2 E 6 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 E 6 ALA H 91 ASN H 97 -1 N TYR H 93 O THR H 107 SHEET 4 E 6 TRP H 34 PHE H 40 -1 N ILE H 37 O TYR H 94 SHEET 5 E 6 ARG H 44 VAL H 51 -1 O ARG H 44 N PHE H 40 SHEET 6 E 6 THR H 57 TYR H 59 -1 O TYR H 58 N TYR H 50 SHEET 1 F 3 THR Y 43 ARG Y 45 0 SHEET 2 F 3 THR Y 51 TYR Y 53 -1 O ASP Y 52 N ASN Y 44 SHEET 3 F 3 ILE Y 58 ASN Y 59 -1 O ILE Y 58 N TYR Y 53 SSBOND 1 CYS L 23 CYS L 88 SSBOND 2 CYS H 22 CYS H 95 SSBOND 3 CYS Y 6 CYS Y 127 SSBOND 4 CYS Y 30 CYS Y 115 SSBOND 5 CYS Y 64 CYS Y 80 SSBOND 6 CYS Y 76 CYS Y 94 CISPEP 1 SER L 7 PRO L 8 0 -0.32 CISPEP 2 TRP L 94 PRO L 95 0 0.32 CRYST1 56.560 56.560 234.751 90.00 90.00 90.00 P 41 21 2 8 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 0.017680 0.000000 0.000000 0.00000 SCALE2 0.000000 0.017680 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004260 0.00000