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HEADER IMMUNE SYSTEM 15-NOV-02 1N7M TITLE GERMLINE 7G12 WITH N-METHYLMESOPORPHYRIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: GERMLINE METAL CHELATASE CATALYTIC ANTIBODY, COMPND 3 CHAIN H; COMPND 4 CHAIN: H; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: GERMLINE METAL CHELATASE CATALYTIC ANTIBODY, COMPND 8 CHAIN L; COMPND 9 CHAIN: L; COMPND 10 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS, HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: MOUSE, HUMAN; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MUS MUSCULUS, HOMO SAPIENS; SOURCE 8 ORGANISM_COMMON: MOUSE, HUMAN; SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 10 EXPRESSION_SYSTEM_COMMON: BACTERIA KEYWDS IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR J.YIN,S.E.ANDRYSKI,A.E.BEUSCHER IV,R.C.STEVENS,P.G.SCHULTZ REVDAT 2 18-MAR-03 1N7M 1 JRNL REVDAT 1 04-FEB-03 1N7M 0 JRNL AUTH J.YIN,S.E.ANDRYSKI,A.E.BEUSCHER IV,R.C.STEVENS, JRNL AUTH 2 P.G.SCHULTZ JRNL TITL STRUCTURAL EVIDENCE FOR SUBSTRATE STRAIN IN JRNL TITL 2 ANTIBODY CATALYSIS JRNL REF PROC.NATL.ACAD.SCI.USA V. 100 856 2003 JRNL REFN ASTM PNASA6 US ISSN 0027-8424 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.0 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) : 19.79 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) (%) : 95.1 REMARK 3 NUMBER OF REFLECTIONS : 44164 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) : 0.220 REMARK 3 FREE R VALUE : 0.253 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1341 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 8 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.80 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.88 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 69.90 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3904 REMARK 3 BIN R VALUE (WORKING SET) : 0.3150 REMARK 3 BIN FREE R VALUE : 0.3040 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 2.50 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 145 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.025 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3261 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 43 REMARK 3 SOLVENT ATOMS : 505 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 23.80 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.79 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.43000 REMARK 3 B22 (A**2) : 3.94000 REMARK 3 B33 (A**2) : -5.37000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 4.95000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.22 REMARK 3 ESD FROM SIGMAA (A) : 0.13 REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00 REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.26 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.18 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.005 REMARK 3 BOND ANGLES (DEGREES) : 1.30 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 : CNS BULK SOLVENT MODEL USED REMARK 3 KSOL : 0.33 REMARK 3 BSOL : 47.20 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 : PROTEIN_REP.PARAM REMARK 3 PARAMETER FILE 2 : CARBOHYDRATE.PARAM.PAR REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM REMARK 3 PARAMETER FILE 4 : MMP.PAR REMARK 3 PARAMETER FILE 5 : NULL REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : CARBOHYDRATE.TOP REMARK 3 TOPOLOGY FILE 3 : WATER.TOP REMARK 3 TOPOLOGY FILE 4 : MMP.TOP REMARK 3 TOPOLOGY FILE 5 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1N7M 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 RCSB017619. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : NULL REMARK 200 PH : 4.20 REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRL REMARK 200 BEAMLINE : BL11-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : NULL 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 : 44580 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800 REMARK 200 RESOLUTION RANGE LOW (A) : 19.790 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : NULL REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL 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) : 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: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: EPMR REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 48.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 22% PEG2000MME, 0.2M AMMONIUM REMARK 280 SULFATE, 10MM CD SULFATE, 1MM NMP, 0.1M SODIUM ACETATE, PH REMARK 280 4.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K 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 38.11800 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 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: H, L 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 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 ILE H 48 CG1 ILE H 48 CD1 -0.032 REMARK 500 MET L 34 SD MET L 34 CE 0.035 REMARK 500 PRO L 150 CG PRO L 150 CD 0.033 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 H 73 N - CA - C ANGL. DEV. = -8.8 DEGREES REMARK 500 SER H 114 N - CA - C ANGL. DEV. =-10.7 DEGREES REMARK 500 LEU H 136 N - CA - C ANGL. DEV. = -9.7 DEGREES REMARK 500 SER H 174 N - CA - C ANGL. DEV. = -8.6 DEGREES REMARK 500 ASN L 61 N - CA - C ANGL. DEV. =-11.3 DEGREES REMARK 500 VAL L 93 N - CA - C ANGL. DEV. = -8.2 DEGREES REMARK 500 CYS L 96 N - CA - C ANGL. DEV. =-12.4 DEGREES REMARK 500 GLY L 105 N - CA - C ANGL. DEV. = -9.1 DEGREES REMARK 500 SER L 121 N - CA - C ANGL. DEV. =-11.0 DEGREES REMARK 500 LEU L 125 N - CA - C ANGL. DEV. =-13.9 DEGREES REMARK 500 LYS L 144 N - CA - C ANGL. DEV. = 8.5 DEGREES REMARK 500 ASP L 209 N - CA - C 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 H 51 -38.91 67.68 REMARK 500 SER H 121 130.11 72.93 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3FCT RELATED DB: PDB REMARK 900 AFFINITY-MATURED 7G12 WITH N-METHYLMESOPORPHYRIN REMARK 999 REMARK 999 SEQUENCE REMARK 999 THE GENE SEQUENCES ARE DERIVED FROM A MOUSE HYBRIDOMA. REMARK 999 THE SEQUENCES OF THE PROTEIN CHAINS ARE NOT FOUND IN ANY REMARK 999 SEQUENCE DATABASE. DBREF 1N7M L 115 216 UNP P01857 IGHG1_HUMAN 1 102 SEQRES 1 H 213 GLU LEU VAL MET THR GLN THR PRO LYS PHE MET SER THR SEQRES 2 H 213 SER VAL GLY ASP ARG VAL SER ILE THR CYS LYS ALA SER SEQRES 3 H 213 GLN ASN VAL GLY THR ALA VAL ALA TRP TYR GLN GLN LYS SEQRES 4 H 213 PRO GLY GLN SER PRO LYS LEU LEU ILE TYR SER ALA SER SEQRES 5 H 213 ASN ARG TYR THR GLY VAL PRO ASP ARG PHE THR GLY SER SEQRES 6 H 213 GLY SER GLY THR ASP PHE THR LEU THR ILE SER ASN MET SEQRES 7 H 213 GLN SER GLU ASP LEU ALA ASP TYR PHE CYS GLN GLN TYR SEQRES 8 H 213 SER SER TYR PRO LEU THR PHE GLY GLY GLY THR LYS VAL SEQRES 9 H 213 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 H 213 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 H 213 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 H 213 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 H 213 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 H 213 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 H 213 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 H 213 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 H 213 PHE ASN ARG GLY GLU SEQRES 1 L 216 GLN VAL GLN LEU LEU GLU SER GLY ALA GLU LEU VAL LYS SEQRES 2 L 216 PRO GLY ALA SER VAL LYS LEU SER CYS LYS ALA SER GLY SEQRES 3 L 216 TYR THR PHE THR SER TYR TRP MET HIS TRP VAL LYS GLN SEQRES 4 L 216 ARG PRO GLY ARG GLY LEU GLU TRP ILE GLY ARG ILE ASP SEQRES 5 L 216 PRO ASN SER GLY GLY THR LYS TYR ASN GLU LYS PHE LYS SEQRES 6 L 216 SER LYS ALA THR LEU THR VAL ASP LYS PRO SER SER THR SEQRES 7 L 216 ALA TYR MET GLN LEU SER SER LEU THR SER GLU ASP SER SEQRES 8 L 216 ALA VAL TYR TYR CYS THR ARG ARG ASP SER ASP TYR TRP SEQRES 9 L 216 GLY ALA GLY THR THR VAL THR VAL SER SER ALA SER THR SEQRES 10 L 216 LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SEQRES 11 L 216 SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL SEQRES 12 L 216 LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SEQRES 13 L 216 SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA SEQRES 14 L 216 VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL SEQRES 15 L 216 VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR SEQRES 16 L 216 ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL SEQRES 17 L 216 ASP LYS LYS VAL GLU PRO LYS SER HET MMP 600 43 HETNAM MMP N-METHYLMESOPORPHYRIN FORMUL 3 MMP C35 H40 N4 O4 FORMUL 4 HOH *505(H2 O) HELIX 1 1 GLN H 79 LEU H 83 5 5 HELIX 2 2 PRO H 120 LYS H 126 1 7 HELIX 3 3 LYS H 183 HIS H 189 1 7 HELIX 4 4 THR L 28 TYR L 32 5 5 HELIX 5 5 GLU L 62 LYS L 65 5 4 HELIX 6 6 THR L 87 SER L 91 5 5 HELIX 7 7 SER L 157 ALA L 159 5 3 HELIX 8 8 LYS L 202 ASN L 205 5 4 SHEET 1 A 4 MET H 4 THR H 7 0 SHEET 2 A 4 VAL H 19 ALA H 25 -1 O LYS H 24 N THR H 5 SHEET 3 A 4 ASP H 70 ILE H 75 -1 O ILE H 75 N VAL H 19 SHEET 4 A 4 PHE H 62 SER H 67 -1 N THR H 63 O THR H 74 SHEET 1 B 5 ASN H 53 ARG H 54 0 SHEET 2 B 5 LYS H 45 TYR H 49 -1 N TYR H 49 O ASN H 53 SHEET 3 B 5 VAL H 33 GLN H 38 -1 N TRP H 35 O LEU H 47 SHEET 4 B 5 ASP H 85 GLN H 90 -1 O ASP H 85 N GLN H 38 SHEET 5 B 5 THR H 97 PHE H 98 -1 O THR H 97 N GLN H 90 SHEET 1 C 6 ASN H 53 ARG H 54 0 SHEET 2 C 6 LYS H 45 TYR H 49 -1 N TYR H 49 O ASN H 53 SHEET 3 C 6 VAL H 33 GLN H 38 -1 N TRP H 35 O LEU H 47 SHEET 4 C 6 ASP H 85 GLN H 90 -1 O ASP H 85 N GLN H 38 SHEET 5 C 6 THR H 102 ILE H 106 -1 O THR H 102 N TYR H 86 SHEET 6 C 6 PHE H 10 THR H 13 1 N THR H 13 O GLU H 105 SHEET 1 D 4 SER H 114 PHE H 118 0 SHEET 2 D 4 THR H 129 PHE H 139 -1 O LEU H 135 N PHE H 116 SHEET 3 D 4 TYR H 173 SER H 182 -1 O LEU H 181 N ALA H 130 SHEET 4 D 4 SER H 159 VAL H 163 -1 N GLN H 160 O THR H 178 SHEET 1 E 4 ALA H 153 LEU H 154 0 SHEET 2 E 4 LYS H 145 VAL H 150 -1 N VAL H 150 O ALA H 153 SHEET 3 E 4 VAL H 191 THR H 197 -1 O GLU H 195 N GLN H 147 SHEET 4 E 4 VAL H 205 ASN H 210 -1 O VAL H 205 N VAL H 196 SHEET 1 F 4 GLN L 3 GLU L 6 0 SHEET 2 F 4 VAL L 18 SER L 25 -1 O LYS L 23 N LEU L 5 SHEET 3 F 4 THR L 78 LEU L 83 -1 O LEU L 83 N VAL L 18 SHEET 4 F 4 ALA L 68 ASP L 73 -1 N THR L 71 O TYR L 80 SHEET 1 G 6 ALA L 9 VAL L 12 0 SHEET 2 G 6 THR L 108 VAL L 112 1 O THR L 111 N VAL L 12 SHEET 3 G 6 ALA L 92 ARG L 98 -1 N ALA L 92 O VAL L 110 SHEET 4 G 6 MET L 34 ARG L 40 -1 N HIS L 35 O THR L 97 SHEET 5 G 6 GLY L 44 ILE L 51 -1 O GLU L 46 N LYS L 38 SHEET 6 G 6 THR L 58 TYR L 60 -1 O LYS L 59 N ARG L 50 SHEET 1 H 4 SER L 121 LEU L 125 0 SHEET 2 H 4 THR L 136 TYR L 146 -1 O LEU L 142 N PHE L 123 SHEET 3 H 4 TYR L 177 PRO L 186 -1 O LEU L 179 N VAL L 143 SHEET 4 H 4 VAL L 164 THR L 166 -1 N HIS L 165 O VAL L 182 SHEET 1 I 4 SER L 121 LEU L 125 0 SHEET 2 I 4 THR L 136 TYR L 146 -1 O LEU L 142 N PHE L 123 SHEET 3 I 4 TYR L 177 PRO L 186 -1 O LEU L 179 N VAL L 143 SHEET 4 I 4 VAL L 170 LEU L 171 -1 N VAL L 170 O SER L 178 SHEET 1 J 3 THR L 152 TRP L 155 0 SHEET 2 J 3 ILE L 196 HIS L 201 -1 O ASN L 198 N SER L 154 SHEET 3 J 3 THR L 206 LYS L 211 -1 O THR L 206 N HIS L 201 SSBOND 1 CYS H 23 CYS H 88 SSBOND 2 CYS H 134 CYS H 194 SSBOND 3 CYS L 22 CYS L 96 SSBOND 4 CYS L 141 CYS L 197 CISPEP 1 THR H 7 PRO H 8 0 -0.39 CISPEP 2 TYR H 94 PRO H 95 0 -0.04 CISPEP 3 TYR H 140 PRO H 141 0 0.05 CISPEP 4 PHE L 147 PRO L 148 0 -0.30 CISPEP 5 GLU L 149 PRO L 150 0 -0.05 CRYST1 55.274 76.236 60.435 90.00 93.33 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 0.018092 0.000000 0.001054 0.00000 SCALE2 0.000000 0.013117 0.000000 0.00000 SCALE3 0.000000 0.000000 0.016575 0.00000