HEADER IMMUNE SYSTEM 15-MAR-02 1L7I TITLE CRYSTAL STRUCTURE OF THE ANTI-ERBB2 FAB2C4 COMPND MOL_ID: 1; COMPND 2 MOLECULE: CHIMERA OF FAB2C4: "HUMANIZED" MURINE MONOCLONAL COMPND 3 ANTIBODY; COMPND 4 CHAIN: L; COMPND 5 FRAGMENT: LIGHT CHAIN (RESIDUES 1-214); COMPND 6 ENGINEERED: YES; COMPND 7 OTHER_DETAILS: THE CHIMERA CONSISTS OF THE HUMAN IG AND COMPND 8 THE ORIGINAL MURINE SEQUENCE; COMPND 9 MOL_ID: 2; COMPND 10 MOLECULE: CHIMERA OF FAB2C4: "HUMANIZED" MURINE MONOCLONAL COMPND 11 ANTIBODY; COMPND 12 CHAIN: H; COMPND 13 FRAGMENT: HEAVY CHAIN (RESIDUES 1-216); COMPND 14 ENGINEERED: YES; COMPND 15 OTHER_DETAILS: THE CHIMERA CONSISTS OF THE HUMAN IG AND COMPND 16 THE ORIGINAL MURINE SEQUENCE SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_COMMON: HUMAN; SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 10 EXPRESSION_SYSTEM_COMMON: BACTERIA KEYWDS IG DOMAIN, FAB FRAGMENT EXPDTA X-RAY DIFFRACTION AUTHOR F.F.VAJDOS,C.W.ADAMS,T.N.BREECE,L.G.PRESTA,A.M.DE VOS, AUTHOR 2 S.S.SIDHU REVDAT 1 10-JUL-02 1L7I 0 JRNL AUTH F.F.VAJDOS,C.W.ADAMS,T.N.BREECE,L.G.PRESTA, JRNL AUTH 2 A.M.DE VOS,S.S.SIDHU JRNL TITL COMPREHENSIVE FUNCTIONAL MAPS OF THE JRNL TITL 2 ANTIGEN-BINDING SITE OF AN ANTI-ERBB2 ANTIBODY JRNL TITL 3 OBTAINED WITH SHOTGUN SCANNING MUTAGENESIS. JRNL REF J.MOL.BIOL. V. 320 415 2002 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNX 2000.1 REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU, REMARK 3 : READ,RICE,SIMONSON,WARREN,MOLECULAR REMARK 3 : SIMULATIONS (BADGER,BERARD,KUMAR,SZALMA, REMARK 3 : YIP,DZAKULA) REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 14.39 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1429863.380 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.4 REMARK 3 NUMBER OF REFLECTIONS : 36864 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 + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.197 REMARK 3 FREE R VALUE : 0.230 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1833 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005 REMARK 3 REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA. REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL REMARK 3 FREE R VALUE (NO CUTOFF) : NULL REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 36884 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 6 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.80 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.90 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5809 REMARK 3 BIN R VALUE (WORKING SET) : 0.2700 REMARK 3 BIN FREE R VALUE : 0.3380 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.50 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 271 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.021 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3323 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 10 REMARK 3 SOLVENT ATOMS : 392 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 14.90 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.00 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 3.76000 REMARK 3 B22 (A**2) : -2.30000 REMARK 3 B33 (A**2) : -1.46000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -2.36000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.20 REMARK 3 ESD FROM SIGMAA (A) : 0.18 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) : 0.25 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.24 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.005 REMARK 3 BOND ANGLES (DEGREES) : 1.40 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 27.40 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.83 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 1.370 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.140 ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 2.110 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.090 ; 2.500 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 PARAMETER FILE 1 : PROTEIN_REP.PARAM REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM REMARK 3 PARAMETER FILE 3 : ION.PARAM REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : WATER.TOP REMARK 3 TOPOLOGY FILE 3 : ION.TOP REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1L7I 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 RCSB015712. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 30-OCT-2000 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 8.00 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ALS REMARK 200 BEAMLINE : 5.0.2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.100 REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL 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 : 36884 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800 REMARK 200 RESOLUTION RANGE LOW (A) : 15.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6 REMARK 200 DATA REDUNDANCY : 2.300 REMARK 200 R MERGE (I) : 0.06500 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 5.2000 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 (%) : 97.6 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.32800 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.400 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: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 43.71 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 35%-45% SATURATED (NH4)2SO4, 0.1 M REMARK 280 TRIS-HCL, PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE REMARK 280 292K 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 32.12450 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: 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 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 PRO L 113 CG PRO L 113 CD 0.035 REMARK 500 PRO H 119 CG PRO H 119 CD 0.035 REMARK 500 PRO H 147 CG PRO H 147 CD 0.033 REMARK 500 PRO H 149 CG PRO H 149 CD 0.034 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 ILE L 75 N - CA - C ANGL. DEV. =-10.8 DEGREES REMARK 500 GLN L 90 N - CA - C ANGL. DEV. = -9.5 DEGREES REMARK 500 TYR L 91 N - CA - C ANGL. DEV. = 9.2 DEGREES REMARK 500 THR L 97 N - CA - C ANGL. DEV. = 9.5 DEGREES REMARK 500 SER L 114 N - CA - C ANGL. DEV. =-12.4 DEGREES REMARK 500 LEU L 136 N - CA - C ANGL. DEV. = -9.3 DEGREES REMARK 500 CYS H 92 N - CA - C ANGL. DEV. =-10.9 DEGREES REMARK 500 SER H 120 N - CA - C ANGL. DEV. =-12.4 DEGREES REMARK 500 LEU H 124 N - CA - C ANGL. DEV. =-14.5 DEGREES REMARK 500 SER H 180 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 SER L 30 -114.13 43.65 REMARK 500 ALA L 51 -42.25 66.01 REMARK 999 REMARK 999 SEQUENCE REMARK 999 AN APPROPRIATE SEQUENCE DATABASE REFERENCE REMARK 999 WAS NOT AVAILABLE AT THE TIME OF PROCESSING. REMARK 999 REMARK 999 FAB2C4 IS A "HUMANIZED" MURINE MONOCLONAL ANTIBODY, REMARK 999 WITH THE FOLLOWING RESIDUES CORRESPONDING TO THE HUMAN REMARK 999 IG SEQUENCE: L1-L23, L35-L49, L57-L88, L98-L214, REMARK 999 H1-H25, H36-H49, H66-H68, H70, H72, H74-H94, H102-223. REMARK 999 REMARK 999 RESIDUES L24-L34, L50-L56, L89-L97, H26-H35, H50-H65, REMARK 999 H69, H71, H73, H95-H102 CORRESPOND TO THE ORIGINAL REMARK 999 MURINE SEQUENCE. DBREF 1L7I L 1 214 UNP Q7Z3Y4 Q7Z3Y4_HUMAN 23 236 DBREF 1L7I H 1 216 UNP Q7Z5W1 Q7Z5W1_HUMAN 20 243 SEQRES 1 L 214 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS LYS ALA SER SEQRES 3 L 214 GLN ASP VAL SER ILE GLY VAL ALA TRP TYR GLN GLN LYS SEQRES 4 L 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SER SEQRES 5 L 214 TYR ARG TYR THR GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 214 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 214 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 L 214 TYR ILE TYR PRO TYR THR PHE GLY GLN GLY THR LYS VAL SEQRES 9 L 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 L 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 L 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 L 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 L 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 L 214 PHE ASN ARG GLY GLU CYS SEQRES 1 H 222 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 222 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 222 PHE THR PHE THR ASP TYR THR MET ASP TRP VAL ARG GLN SEQRES 4 H 222 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ASP VAL ASN SEQRES 5 H 222 PRO ASN SER GLY GLY SER ILE TYR ASN GLN ARG PHE LYS SEQRES 6 H 222 GLY ARG PHE THR LEU SER VAL ASP ARG SER LYS ASN THR SEQRES 7 H 222 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 H 222 ALA VAL TYR TYR CYS ALA ARG ASN LEU GLY PRO SER PHE SEQRES 9 H 222 TYR PHE ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL SEQRES 10 H 222 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU SEQRES 11 H 222 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA SEQRES 12 H 222 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL SEQRES 13 H 222 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL SEQRES 14 H 222 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SEQRES 15 H 222 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU SEQRES 16 H 222 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SEQRES 17 H 222 SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER SEQRES 18 H 222 CYS HET SO4 401 5 HET SO4 402 5 HETNAM SO4 SULFATE ION FORMUL 3 SO4 2(O4 S 2-) FORMUL 5 HOH *392(H2 O) HELIX 1 1 GLN L 79 PHE L 83 5 5 HELIX 2 2 SER L 121 LYS L 126 1 6 HELIX 3 3 LYS L 183 GLU L 187 1 5 HELIX 4 4 GLY L 212 CYS L 214 5 3 HELIX 5 5 THR H 28 TYR H 32 5 5 HELIX 6 6 GLN H 61 LYS H 64 5 4 HELIX 7 7 ARG H 83 THR H 87 5 5 HELIX 8 8 SER H 127 LYS H 129 5 3 HELIX 9 9 SER H 156 ALA H 158 5 3 HELIX 10 10 SER H 187 LEU H 189 5 3 HELIX 11 11 LYS H 201 ASN H 204 5 4 SHEET 1 A 4 MET L 4 SER L 7 0 SHEET 2 A 4 VAL L 19 ALA L 25 -1 N THR L 22 O SER 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 SER L 63 N 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 LYS L 103 N LEU L 11 SHEET 3 B 6 ALA L 84 GLN L 90 -1 O ALA L 84 N VAL L 104 SHEET 4 B 6 VAL L 33 GLN L 38 -1 N ALA L 34 O GLN L 89 SHEET 5 B 6 LYS L 45 TYR L 49 -1 O LYS L 45 N GLN L 37 SHEET 6 B 6 TYR L 53 ARG L 54 -1 N TYR L 53 O TYR L 49 SHEET 1 C 4 SER L 114 PHE L 118 0 SHEET 2 C 4 THR L 129 PHE L 139 -1 O VAL L 133 N PHE L 118 SHEET 3 C 4 TYR L 173 SER L 182 -1 O TYR L 173 N PHE L 139 SHEET 4 C 4 SER L 159 VAL L 163 -1 O GLN L 160 N THR L 178 SHEET 1 D 4 ALA L 153 LEU L 154 0 SHEET 2 D 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 D 4 VAL L 191 THR L 197 -1 O ALA L 193 N LYS L 149 SHEET 4 D 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196 SHEET 1 E 4 GLN H 3 SER H 7 0 SHEET 2 E 4 LEU H 18 SER H 25 -1 N SER H 21 O SER H 7 SHEET 3 E 4 THR H 77 MET H 82 -1 O LEU H 78 N CYS H 22 SHEET 4 E 4 PHE H 67 ASP H 72 -1 O THR H 68 N GLN H 81 SHEET 1 F 8 LEU H 11 VAL H 12 0 SHEET 2 F 8 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 F 8 ALA H 88 ASN H 95 -1 O ALA H 88 N VAL H 109 SHEET 4 F 8 TYR H 102 TRP H 103 -1 O TYR H 102 N ARG H 94 SHEET 5 F 8 ALA H 88 ASN H 95 -1 N ARG H 94 O TYR H 102 SHEET 6 F 8 THR H 33 GLN H 39 -1 O THR H 33 N ASN H 95 SHEET 7 F 8 GLU H 46 VAL H 51 -1 O GLU H 46 N ARG H 38 SHEET 8 F 8 SER H 57 TYR H 59 -1 O ILE H 58 N ASP H 50 SHEET 1 G 8 SER H 120 LEU H 124 0 SHEET 2 G 8 THR H 135 TYR H 145 -1 O GLY H 139 N LEU H 124 SHEET 3 G 8 THR H 131 SER H 132 -1 N SER H 132 O THR H 135 SHEET 4 G 8 THR H 135 TYR H 145 -1 O THR H 135 N SER H 132 SHEET 5 G 8 TYR H 176 PRO H 185 -1 N TYR H 176 O TYR H 145 SHEET 6 G 8 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 7 G 8 TYR H 176 PRO H 185 -1 O SER H 177 N VAL H 169 SHEET 8 G 8 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 H 3 THR H 151 TRP H 154 0 SHEET 2 H 3 ILE H 195 HIS H 200 -1 N ASN H 197 O SER H 153 SHEET 3 H 3 THR H 205 LYS H 210 -1 O THR H 205 N HIS H 200 SSBOND 1 CYS L 23 CYS L 88 SSBOND 2 CYS L 134 CYS L 194 SSBOND 3 CYS L 214 CYS H 216 SSBOND 4 CYS H 22 CYS H 92 SSBOND 5 CYS H 140 CYS H 196 CISPEP 1 SER L 7 PRO L 8 0 -0.20 CISPEP 2 TYR L 94 PRO L 95 0 0.67 CISPEP 3 TYR L 140 PRO L 141 0 0.02 CISPEP 4 PHE H 146 PRO H 147 0 -0.34 CISPEP 5 GLU H 148 PRO H 149 0 -0.29 CRYST1 41.966 64.249 79.445 90.00 105.44 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 0.023829 0.000000 0.006581 0.00000 SCALE2 0.000000 0.015564 0.000000 0.00000 SCALE3 0.000000 0.000000 0.013059 0.00000