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HEADER IMMUNE SYSTEM 22-JUL-99 1C1E TITLE CRYSTAL STRUCTURE OF A DIELS-ALDERASE CATALYTIC ANTIBODY TITLE 2 1E9 IN COMPLEX WITH ITS HAPTEN COMPND MOL_ID: 1; COMPND 2 MOLECULE: CATALYTIC ANTIBODY 1E9 (LIGHT CHAIN); COMPND 3 CHAIN: L; COMPND 4 FRAGMENT: FAB FRAGMENT; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: CATALYTIC ANTIBODY 1E9 (HEAVY CHAIN); COMPND 7 CHAIN: H; COMPND 8 FRAGMENT: FAB FRAGMENT SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 MOL_ID: 2; SOURCE 5 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 6 ORGANISM_COMMON: MOUSE KEYWDS CATALYTIC ANTIBODY, DIELS-ALDER, IMMUNOGLOBULIN EXPDTA X-RAY DIFFRACTION AUTHOR J.XU,I.A.WILSON REVDAT 2 25-OCT-00 1C1E 3 ATOM SHEET HELIX REMARK REVDAT 2 2 3 SEQRES REVDAT 1 01-MAR-00 1C1E 0 JRNL AUTH J.XU,Q.DENG,J.CHEN,K.N.HOUK,J.BARTEK,D.HILVERT, JRNL AUTH 2 I.A.WILSON JRNL TITL EVOLUTION OF SHAPE COMPLEMENTARITY AND CATALYTIC JRNL TITL 2 EFFICIENCY FROM A PRIMORDIAL ANTIBODY TEMPLATE. JRNL REF SCIENCE V. 286 2345 1999 JRNL REFN ASTM SCIEAS US ISSN 0036-8075 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 98.0 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90 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) (%) : 86.2 REMARK 3 NUMBER OF REFLECTIONS : 30764 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : 5% RANDOM REMARK 3 R VALUE (WORKING SET) : 0.239 REMARK 3 FREE R VALUE : 0.294 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 1521 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 : 3338 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 28 REMARK 3 SOLVENT ATOMS : 195 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 15.17 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) : 0.012 REMARK 3 BOND ANGLES (DEGREES) : 1.70 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 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: MAXIMUM LIKELIHOOD TARGET USED REMARK 4 REMARK 4 1C1E 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 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB . REMARK 100 THE RCSB ID CODE IS RCSB009372. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 14-JUL-1997 REMARK 200 TEMPERATURE (KELVIN) : 97.2 REMARK 200 PH : 5.50 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRL REMARK 200 BEAMLINE : BL7-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.98 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : AREA DETECTOR 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 : 39213 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900 REMARK 200 RESOLUTION RANGE LOW (A) : 19.960 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5 REMARK 200 DATA REDUNDANCY : 3.200 REMARK 200 R MERGE (I) : 0.07000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 14.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4 REMARK 200 DATA REDUNDANCY IN SHELL : 3.00 REMARK 200 R MERGE FOR SHELL (I) : 0.83600 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.200 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL REMARK 200 SOFTWARE USED: AMORE REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 52.88 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 10K, IMIDAZOLIUM MALATE, PH REMARK 280 5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 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 -X,Y,1/2-Z REMARK 290 4555 X,-Y,-Z REMARK 290 5555 1/2+X,1/2+Y,Z REMARK 290 6555 1/2-X,1/2-Y,1/2+Z REMARK 290 7555 1/2-X,1/2+Y,1/2-Z REMARK 290 8555 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 83.75000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 83.75000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 22.36500 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 66.22000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 22.36500 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 66.22000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 83.75000 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 22.36500 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 66.22000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 83.75000 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 22.36500 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 66.22000 REMARK 290 SMTRY3 8 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: L, H 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 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH 3 LIES ON A SPECIAL POSITION. REMARK 375 HOH 263 LIES ON A SPECIAL POSITION. REMARK 375 HOH 289 LIES ON A SPECIAL POSITION. REMARK 375 HOH 294 LIES ON A SPECIAL POSITION. REMARK 375 HOH 332 LIES ON A SPECIAL POSITION. 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 H 100B SD MET H 100B CE -0.087 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 2 CA - CB - CG ANGL. DEV. =-15.2 DEGREES REMARK 500 VAL L 51 N - CA - C ANGL. DEV. = 11.4 DEGREES REMARK 500 PHE L 95 N - CA - CB ANGL. DEV. = 12.7 DEGREES REMARK 500 PHE L 94 CA - C - N ANGL. DEV. =-12.5 DEGREES REMARK 500 PHE L 95 C - N - CA ANGL. DEV. = 15.6 DEGREES REMARK 500 LEU L 136 N - CA - C ANGL. DEV. =-11.6 DEGREES REMARK 500 GLN H 133 N - CA - C ANGL. DEV. = 11.0 DEGREES REMARK 500 ASN H 135 N - CA - C ANGL. DEV. =-10.6 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 VAL L 51 -46.98 70.94 REMARK 500 GLN H 133 -104.14 139.43 SEQRES 1 L 216 GLU LEU VAL MET THR GLN THR PRO LEU SER LEU PRO VAL SEQRES 2 L 216 SER LEU GLY ASP GLN ALA SER ILE SER CYS ARG SER SER SEQRES 3 L 216 GLN SER LEU VAL HIS SER ASN GLY ASN THR TYR LEU HIS SEQRES 4 L 216 TRP TYR LEU GLN LYS PRO GLY GLN SER PRO LYS PHE LEU SEQRES 5 L 216 ILE TYR LYS VAL SER ASN ARG PHE SER GLY VAL PRO ASP SEQRES 6 L 216 ARG PHE GLY GLY SER GLY SER GLY THR ASP PHE ILE LEU SEQRES 7 L 216 LYS ILE SER ARG VAL GLU ALA GLU ASP LEU GLY VAL TYR SEQRES 8 L 216 PHE CYS PHE GLN SER THR HIS PHE PHE PRO THR PHE GLY SEQRES 9 L 216 GLY GLY THR LYS LEU GLU ILE LYS SER ALA ASP ALA ALA SEQRES 10 L 216 PRO THR VAL SER ILE PHE PRO PRO SER SER GLU GLN LEU SEQRES 11 L 216 THR SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN ASN SEQRES 12 L 216 PHE TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE ASP SEQRES 13 L 216 GLY SER GLU ARG GLN ASN GLY VAL LEU ASN SER TRP THR SEQRES 14 L 216 ASP GLN ASP SER LYS ASP SER THR TYR SER MET SER SER SEQRES 15 L 216 THR LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS ASN SEQRES 16 L 216 SER TYR THR CYS GLU ALA THR HIS LYS THR SER THR SER SEQRES 17 L 216 PRO ILE VAL LYS SER PHE ASN ARG SEQRES 1 H 219 GLN ILE GLN LEU VAL GLN SER GLY PRO GLU LEU LYS LYS SEQRES 2 H 219 PRO GLY GLU THR VAL LYS ILE SER CYS LYS ALA SER GLY SEQRES 3 H 219 TYR MET PHE THR ASN TYR GLY MET ASN TRP VAL LYS GLN SEQRES 4 H 219 ALA PRO GLY LYS ALA LEU LYS LEU MET GLY TRP ILE ASN SEQRES 5 H 219 PRO TYR THR GLY GLU SER THR PHE ALA ASP ASP PHE LYS SEQRES 6 H 219 GLY ARG PHE ALA PHE PHE LEU GLU THR SER ALA THR THR SEQRES 7 H 219 ALA TYR LEU GLN ILE ASN ASN LEU LYS ASN GLU ASP MET SEQRES 8 H 219 ALA THR TYR PHE CYS ALA ARG GLY THR THR ILE VAL ARG SEQRES 9 H 219 ALA MET ASP TYR TRP GLY GLN GLY THR SER LEU THR VAL SEQRES 10 H 219 SER SER ALA LYS THR THR PRO PRO SER VAL TYR PRO LEU SEQRES 11 H 219 ALA PRO GLY SER ALA ALA GLN THR ASN SER MET VAL THR SEQRES 12 H 219 LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL SEQRES 13 H 219 THR VAL THR TRP ASN SER GLY SER LEU SER SER GLY VAL SEQRES 14 H 219 HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR SEQRES 15 H 219 LEU SER SER SER VAL THR VAL PRO SER SER PRO ARG PRO SEQRES 16 H 219 SER GLU THR VAL THR CYS ASN VAL ALA HIS PRO ALA SER SEQRES 17 H 219 SER THR LYS VAL ASP LYS LYS ILE VAL PRO ARG HET ENH 703 19 HET DMR 702 9 HETNAM ENH 1,7,8,9,10,10-HEXACHLORO-4-METHYL-4-AZA- HETNAM 2 ENH TRICYCLO[5.2.1.0(2,6)]DEC-8-ENE-3,5-DIONE HETNAM DMR 2-HYDROXY-SUCCINIC ACID FORMUL 3 ENH C10 H5 CL6 N O2 FORMUL 4 DMR C4 H6 O5 FORMUL 5 HOH *195(H2 O) HELIX 1 1 GLU L 79 LEU L 83 5 5 HELIX 2 2 SER L 121 SER L 127 1 7 HELIX 3 3 LYS L 183 GLU L 187 1 5 HELIX 4 4 MET H 28 TYR 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 LYS H 83 MET H 87 5 5 HELIX 8 8 SER H 163 SER H 165 5 3 HELIX 9 9 PRO H 213 SER H 216 5 4 SHEET 1 A 4 MET L 4 THR L 7 0 SHEET 2 A 4 ALA L 19 SER L 25 -1 N SER L 22 O THR L 7 SHEET 3 A 4 ASP L 70 ILE L 75 -1 N PHE L 71 O CYS L 23 SHEET 4 A 4 PHE L 62 SER L 67 -1 O GLY L 63 N LYS L 74 SHEET 1 B 5 ASN L 53 ARG L 54 0 SHEET 2 B 5 LYS L 45 TYR L 49 -1 N TYR L 49 O ASN L 53 SHEET 3 B 5 LEU L 33 GLN L 38 -1 N TRP L 35 O ILE L 48 SHEET 4 B 5 GLY L 84 GLN L 90 -1 N VAL L 85 O GLN L 38 SHEET 5 B 5 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 C 6 ASN L 53 ARG L 54 0 SHEET 2 C 6 LYS L 45 TYR L 49 -1 N TYR L 49 O ASN L 53 SHEET 3 C 6 LEU L 33 GLN L 38 -1 N TRP L 35 O ILE L 48 SHEET 4 C 6 GLY L 84 GLN L 90 -1 N VAL L 85 O GLN L 38 SHEET 5 C 6 THR L 102 ILE L 106 -1 O THR L 102 N TYR L 86 SHEET 6 C 6 SER L 10 VAL L 13 1 N LEU L 11 O LYS L 103 SHEET 1 D 4 THR L 114 PHE L 118 0 SHEET 2 D 4 GLY L 129 PHE L 139 -1 O VAL L 133 N PHE L 118 SHEET 3 D 4 TYR L 173 THR L 182 -1 O TYR L 173 N PHE L 139 SHEET 4 D 4 VAL L 159 TRP L 163 -1 O LEU L 160 N THR L 178 SHEET 1 E 4 GLU L 154 ARG L 155 0 SHEET 2 E 4 ASN L 145 ILE L 150 -1 O TRP L 148 N ARG L 155 SHEET 3 E 4 SER L 191 THR L 197 -1 N THR L 193 O LYS L 149 SHEET 4 E 4 ILE L 205 ASN L 210 -1 N ILE L 205 O ALA L 196 SHEET 1 F 4 GLN H 3 GLN H 6 0 SHEET 2 F 4 VAL H 18 SER H 25 -1 O LYS H 23 N VAL H 5 SHEET 3 F 4 THR H 77 ILE H 82 -1 N ALA H 78 O CYS H 22 SHEET 4 F 4 PHE H 67 GLU H 72 -1 O ALA H 68 N GLN H 81 SHEET 1 G 5 SER H 57 PHE H 59 0 SHEET 2 G 5 LEU H 45 ILE H 51 -1 O TRP H 50 N THR H 58 SHEET 3 G 5 GLY H 33 GLN H 39 -1 O MET H 34 N ILE H 51 SHEET 4 G 5 ALA H 88 GLY H 95 -1 N THR H 89 O GLN H 39 SHEET 1 H 6 SER H 57 PHE H 59 0 SHEET 2 H 6 LEU H 45 ILE H 51 -1 O TRP H 50 N THR H 58 SHEET 3 H 6 GLY H 33 GLN H 39 -1 O MET H 34 N ILE H 51 SHEET 4 H 6 ALA H 88 GLY H 95 -1 N THR H 89 O GLN H 39 SHEET 5 H 6 THR H 107 VAL H 111 -1 O THR H 107 N TYR H 90 SHEET 6 H 6 GLU H 10 LYS H 12 1 N GLU H 10 O SER H 108 SHEET 1 I 4 SER H 120 LEU H 124 0 SHEET 2 I 4 MET H 137 TYR H 147 -1 O GLY H 141 N LEU H 124 SHEET 3 I 4 TYR H 185 PRO H 194 -1 N TYR H 185 O TYR H 147 SHEET 4 I 4 VAL H 171 THR H 173 -1 O HIS H 172 N SER H 190 SHEET 1 J 4 SER H 120 LEU H 124 0 SHEET 2 J 4 MET H 137 TYR H 147 -1 O GLY H 141 N LEU H 124 SHEET 3 J 4 TYR H 185 PRO H 194 -1 N TYR H 185 O TYR H 147 SHEET 4 J 4 VAL H 177 LEU H 178 -1 N VAL H 177 O THR H 186 SHEET 1 K 3 THR H 153 TRP H 157 0 SHEET 2 K 3 THR H 207 HIS H 212 -1 N ASN H 209 O THR H 156 SHEET 3 K 3 THR H 217 LYS H 222 -1 O THR H 217 N HIS H 212 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 142 CYS H 208 CISPEP 1 THR L 7 PRO L 8 0 0.04 CISPEP 2 TYR L 140 PRO L 141 0 0.03 CISPEP 3 PHE H 148 PRO H 149 0 0.16 CISPEP 4 GLU H 150 PRO H 151 0 -0.24 CISPEP 5 ARG H 200 PRO H 202 0 0.21 CRYST1 44.730 132.440 167.500 90.00 90.00 90.00 C 2 2 21 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 0.022356 0.000000 0.000000 0.00000 SCALE2 0.000000 0.007551 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005970 0.00000