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HEADER COMPLEX (IMMUNOGLOBULIN/HYDROLASE) 13-JAN-98 1A2Y TITLE HEN EGG WHITE LYSOZYME, D18A MUTANT, IN COMPLEX WITH MOUSE TITLE 2 MONOCLONAL ANTIBODY D1.3 COMPND MOL_ID: 1; COMPND 2 MOLECULE: IGG1-KAPPA D1.3 FV (LIGHT CHAIN); COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: IGG1-KAPPA D1.3 FV (HEAVY CHAIN); COMPND 7 CHAIN: B; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: LYSOZYME; COMPND 11 CHAIN: C; COMPND 12 EC: 3.2.1.17; COMPND 13 ENGINEERED: YES; COMPND 14 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 ORGAN: EGG; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 8 ORGANISM_COMMON: MOUSE; SOURCE 9 ORGAN: EGG; SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: GALLUS GALLUS; SOURCE 13 ORGANISM_COMMON: CHICKEN; SOURCE 14 ORGAN: EGG; SOURCE 15 CELL: EGG; SOURCE 16 CELLULAR_LOCATION: CYTOPLASM (WHITE); SOURCE 17 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE KEYWDS COMPLEX (IMMUNOGLOBULIN/HYDROLASE), IMMUNOGLOBULIN V REGION, KEYWDS 2 SIGNAL, HYDROLASE, GLYCOSIDASE, BACTERIOLYTIC ENZYME, EGG KEYWDS 3 WHITE EXPDTA X-RAY DIFFRACTION AUTHOR D.TSUCHIYA,R.A.MARIUZZA REVDAT 2 01-APR-03 1A2Y 1 JRNL REVDAT 1 29-APR-98 1A2Y 0 JRNL AUTH W.DALL'ACQUA,E.R.GOLDMAN,W.LIN,C.TENG,D.TSUCHIYA, JRNL AUTH 2 H.LI,X.YSERN,B.C.BRADEN,Y.LI,S.J.SMITH-GILL, JRNL AUTH 3 R.A.MARIUZZA JRNL TITL A MUTATIONAL ANALYSIS OF BINDING INTERACTIONS IN JRNL TITL 2 AN ANTIGEN-ANTIBODY PROTEIN-PROTEIN COMPLEX. JRNL REF BIOCHEMISTRY V. 37 7981 1998 JRNL REFN ASTM BICHAW US ISSN 0006-2960 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH B.A.FIELDS,F.A.GOLDBAUM,W.DALL'ACQUA,E.L.MALCHIODI, REMARK 1 AUTH 2 A.CAUERHFF,F.P.SCHWARZ,X.YSERN,R.J.POLJAK, REMARK 1 AUTH 3 R.A.MARIUZZA REMARK 1 TITL HYDROGEN BONDING AND SOLVENT STRUCTURE IN AN REMARK 1 TITL 2 ANTIGEN-ANTIBODY INTERFACE. CRYSTAL STRUCTURES AND REMARK 1 TITL 3 THERMODYNAMIC CHARACTERIZATION OF THREE FV MUTANTS REMARK 1 TITL 4 COMPLEXED WITH LYSOZYME REMARK 1 REF BIOCHEMISTRY V. 35 15494 1996 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 REMARK 1 REFERENCE 2 REMARK 1 AUTH T.N.BHAT,G.A.BENTLEY,G.BOULOT,M.I.GREENE,D.TELLO, REMARK 1 AUTH 2 W.DALL'ACQUA,H.SOUCHON,F.P.SCHWARZ,R.A.MARIUZZA, REMARK 1 AUTH 3 R.J.POLJAK REMARK 1 TITL BOUND WATER MOLECULES AND CONFORMATIONAL REMARK 1 TITL 2 STABILIZATION HELP MEDIATE AN ANTIGEN-ANTIBODY REMARK 1 TITL 3 ASSOCIATION REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 91 1089 1994 REMARK 1 REFN ASTM PNASA6 US ISSN 0027-8424 REMARK 1 REFERENCE 3 REMARK 1 AUTH X.YSERN,B.A.FIELDS,T.N.BHAT,F.A.GOLDBAUM, REMARK 1 AUTH 2 W.DALL'ACQUA,F.P.SCHWARZ,R.J.POLJAK,R.A.MARIUZZA REMARK 1 TITL SOLVENT REARRANGEMENT IN AN ANTIGEN-ANTIBODY REMARK 1 TITL 2 INTERFACE INTRODUCED BY SITE-DIRECTED MUTAGENESIS REMARK 1 TITL 3 OF THE ANTIBODY COMBINING SITE REMARK 1 REF J.MOL.BIOL. V. 238 496 1994 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 2 REMARK 2 RESOLUTION. 1.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 7.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 3.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 100000.000 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.1000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 90.4 REMARK 3 NUMBER OF REFLECTIONS : 56703 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) : 0.203 REMARK 3 FREE R VALUE : 0.251 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.000 REMARK 3 FREE R VALUE TEST SET COUNT : 3416 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 : 10 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.50 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.55 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 50.50 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2939 REMARK 3 BIN R VALUE (WORKING SET) : 0.3020 REMARK 3 BIN FREE R VALUE : 0.3080 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 3.30 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 208 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 : 2754 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 5 REMARK 3 SOLVENT ATOMS : 485 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) : 0.20 REMARK 3 ESD FROM SIGMAA (A) : 0.20 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) : 0.012 REMARK 3 BOND ANGLES (DEGREES) : 1.49 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.90 REMARK 3 IMPROPER ANGLES (DEGREES) : 1.35 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 : PARHCSDX.PRO REMARK 3 PARAMETER FILE 2 : NULL REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO REMARK 3 TOPOLOGY FILE 2 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1A2Y 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 (2007-03-16) REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : JUL-1997 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 6.50 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : CHESS REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.928 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD AREA DETECTOR REMARK 200 DETECTOR MANUFACTURER : NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59595 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500 REMARK 200 RESOLUTION RANGE LOW (A) : NULL REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 90.4 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : 0.06900 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) : 1.50 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.55 REMARK 200 COMPLETENESS FOR SHELL (%) : 30.1 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.30100 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: NULL REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL REMARK 200 SOFTWARE USED: X-PLOR 3.1 REMARK 200 STARTING MODEL: PDB ENTRY 1VFB REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 52.35 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.5 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 65.33350 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.60600 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 65.33350 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 30.60600 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: A, B, C 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 LEU A 47 CA - CB - CG ANGL. DEV. = 10.9 DEGREES REMARK 500 TYR B 101 N - CA - C ANGL. DEV. = 9.7 DEGREES REMARK 500 ASP B 104 N - CA - C ANGL. DEV. = 10.3 DEGREES REMARK 500 GLY C 4 N - CA - C ANGL. DEV. =-12.3 DEGREES REMARK 500 TYR C 53 N - CA - C ANGL. DEV. = 10.6 DEGREES REMARK 500 GLY C 54 N - CA - C ANGL. DEV. = 9.2 DEGREES REMARK 500 TRP C 63 N - CA - C ANGL. DEV. = 10.4 DEGREES REMARK 500 GLY C 104 N - CA - C ANGL. DEV. = 11.1 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 A 51 -48.13 69.28 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 394 DISTANCE = 6.07 ANGSTROMS REMARK 525 HOH 458 DISTANCE = 6.31 ANGSTROMS REMARK 525 HOH 472 DISTANCE = 5.64 ANGSTROMS REMARK 525 HOH 476 DISTANCE = 5.18 ANGSTROMS DBREF 1A2Y A 1 107 UNP P01635 KV5C_MOUSE 1 108 DBREF 1A2Y B 1 116 UNP P01820 HV44_MOUSE 133 248 DBREF 1A2Y C 1 129 UNP P00698 LYSC_CHICK 19 147 SEQADV 1A2Y VAL A 3 UNP P01635 GLU 3 CONFLICT SEQADV 1A2Y TYR A 50 UNP P01635 LYS 50 CONFLICT SEQADV 1A2Y THR A 51 UNP P01635 ALA 51 CONFLICT SEQADV 1A2Y THR A 52 UNP P01635 GLN 52 CONFLICT SEQADV 1A2Y A UNP P01635 PRO 95 DELETION SEQADV 1A2Y ARG A 96 UNP P01635 TRP 97 CONFLICT SEQADV 1A2Y LEU B 112 UNP P01820 VAL 244 CONFLICT SEQADV 1A2Y ALA C 18 UNP P00698 ASP 36 ENGINEERED SEQRES 1 A 107 ASP ILE VAL LEU THR GLN SER PRO ALA SER LEU SER ALA SEQRES 2 A 107 SER VAL GLY GLU THR VAL THR ILE THR CYS ARG ALA SER SEQRES 3 A 107 GLY ASN ILE HIS ASN TYR LEU ALA TRP TYR GLN GLN LYS SEQRES 4 A 107 GLN GLY LYS SER PRO GLN LEU LEU VAL TYR TYR THR THR SEQRES 5 A 107 THR LEU ALA ASP GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 A 107 GLY SER GLY THR GLN TYR SER LEU LYS ILE ASN SER LEU SEQRES 7 A 107 GLN PRO GLU ASP PHE GLY SER TYR TYR CYS GLN HIS PHE SEQRES 8 A 107 TRP SER THR PRO ARG THR PHE GLY GLY GLY THR LYS LEU SEQRES 9 A 107 GLU ILE LYS SEQRES 1 B 116 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL ALA SEQRES 2 B 116 PRO SER GLN SER LEU SER ILE THR CYS THR VAL SER GLY SEQRES 3 B 116 PHE SER LEU THR GLY TYR GLY VAL ASN TRP VAL ARG GLN SEQRES 4 B 116 PRO PRO GLY LYS GLY LEU GLU TRP LEU GLY MET ILE TRP SEQRES 5 B 116 GLY ASP GLY ASN THR ASP TYR ASN SER ALA LEU LYS SER SEQRES 6 B 116 ARG LEU SER ILE SER LYS ASP ASN SER LYS SER GLN VAL SEQRES 7 B 116 PHE LEU LYS MET ASN SER LEU HIS THR ASP ASP THR ALA SEQRES 8 B 116 ARG TYR TYR CYS ALA ARG GLU ARG ASP TYR ARG LEU ASP SEQRES 9 B 116 TYR TRP GLY GLN GLY THR THR LEU THR VAL SER SER SEQRES 1 C 129 LYS VAL PHE GLY ARG CYS GLU LEU ALA ALA ALA MET LYS SEQRES 2 C 129 ARG HIS GLY LEU ALA ASN TYR ARG GLY TYR SER LEU GLY SEQRES 3 C 129 ASN TRP VAL CYS ALA ALA LYS PHE GLU SER ASN PHE ASN SEQRES 4 C 129 THR GLN ALA THR ASN ARG ASN THR ASP GLY SER THR ASP SEQRES 5 C 129 TYR GLY ILE LEU GLN ILE ASN SER ARG TRP TRP CYS ASN SEQRES 6 C 129 ASP GLY ARG THR PRO GLY SER ARG ASN LEU CYS ASN ILE SEQRES 7 C 129 PRO CYS SER ALA LEU LEU SER SER ASP ILE THR ALA SER SEQRES 8 C 129 VAL ASN CYS ALA LYS LYS ILE VAL SER ASP GLY ASN GLY SEQRES 9 C 129 MET ASN ALA TRP VAL ALA TRP ARG ASN ARG CYS LYS GLY SEQRES 10 C 129 THR ASP VAL GLN ALA TRP ILE ARG GLY CYS ARG LEU HET PO4 1 5 HETNAM PO4 PHOSPHATE ION FORMUL 4 PO4 O4 P 3- FORMUL 5 HOH *485(H2 O) HELIX 1 1 PRO A 80 ASP A 82 5 3 HELIX 2 2 LYS B 64 ARG B 66 5 3 HELIX 3 3 THR B 87 ASP B 89 5 3 HELIX 4 4 ARG C 5 ARG C 14 1 10 HELIX 5 5 TYR C 20 GLY C 22 5 3 HELIX 6 6 LEU C 25 SER C 36 1 12 HELIX 7 7 THR C 89 ILE C 98 1 10 HELIX 8 8 GLY C 104 ALA C 107 5 4 HELIX 9 9 VAL C 109 ARG C 114 1 6 HELIX 10 10 VAL C 120 TRP C 123 5 4 SHEET 1 A 4 LEU A 4 SER A 7 0 SHEET 2 A 4 VAL A 19 ALA A 25 -1 N ARG A 24 O THR A 5 SHEET 3 A 4 GLN A 70 ILE A 75 -1 N ILE A 75 O VAL A 19 SHEET 4 A 4 PHE A 62 SER A 67 -1 N SER A 67 O GLN A 70 SHEET 1 B 5 SER A 10 ALA A 13 0 SHEET 2 B 5 THR A 102 ILE A 106 1 N LYS A 103 O LEU A 11 SHEET 3 B 5 GLY A 84 HIS A 90 -1 N TYR A 86 O THR A 102 SHEET 4 B 5 LEU A 33 GLN A 38 -1 N GLN A 38 O SER A 85 SHEET 5 B 5 GLN A 45 VAL A 48 -1 N VAL A 48 O TRP A 35 SHEET 1 C 4 GLN B 3 SER B 7 0 SHEET 2 C 4 LEU B 18 SER B 25 -1 N SER B 25 O GLN B 3 SHEET 3 C 4 GLN B 77 MET B 82 -1 N MET B 82 O LEU B 18 SHEET 4 C 4 LEU B 67 ASP B 72 -1 N ASP B 72 O GLN B 77 SHEET 1 D 5 THR B 110 LEU B 112 0 SHEET 2 D 5 ALA B 91 GLU B 98 -1 N TYR B 93 O THR B 110 SHEET 3 D 5 GLY B 33 GLN B 39 -1 N GLN B 39 O ARG B 92 SHEET 4 D 5 LEU B 45 ILE B 51 -1 N ILE B 51 O VAL B 34 SHEET 5 D 5 THR B 57 TYR B 59 -1 N ASP B 58 O MET B 50 SHEET 1 E 2 THR C 43 ARG C 45 0 SHEET 2 E 2 THR C 51 TYR C 53 -1 N ASP C 52 O ASN C 44 SHEET 1 F 2 ALA B 96 GLU B 98 0 SHEET 2 F 2 LEU B 103 TRP B 106 -1 N TYR B 105 O ARG B 97 SSBOND 1 CYS A 23 CYS A 88 SSBOND 2 CYS B 22 CYS B 95 SSBOND 3 CYS C 6 CYS C 127 SSBOND 4 CYS C 30 CYS C 115 SSBOND 5 CYS C 64 CYS C 80 SSBOND 6 CYS C 76 CYS C 94 CISPEP 1 SER A 7 PRO A 8 0 0.26 CISPEP 2 THR A 94 PRO A 95 0 -0.83 CRYST1 130.667 61.212 57.425 90.00 119.14 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 0.007653 0.000000 0.004267 0.00000 SCALE2 0.000000 0.016337 0.000000 0.00000 SCALE3 0.000000 0.000000 0.019937 0.00000