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HEADER IMMUNE SYSTEM 09-NOV-99 1C5C TITLE DECARBOXYLASE CATALYTIC ANTIBODY 21D8-HAPTEN COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: CHIMERIC DECARBOXYLASE ANTIBODY 21D8; COMPND 3 CHAIN: L; COMPND 4 FRAGMENT: FAB; COMPND 5 ENGINEERED: YES; COMPND 6 OTHER_DETAILS: THE CONSTANT DOMAIN (RESIDUES 103-214) IS COMPND 7 FROM HUMAN SOURCE, AND THE VARIABLE DOMAIN (RESIDUES 1- COMPND 8 102) IS FROM MURINE SOURCE; COMPND 9 MOL_ID: 2; COMPND 10 MOLECULE: CHIMERIC DECARBOXYLASE ANTIBODY 21D8; COMPND 11 CHAIN: H; COMPND 12 FRAGMENT: FAB; COMPND 13 ENGINEERED: YES; COMPND 14 OTHER_DETAILS: THE CONSTANT DOMAIN (RESIDUES 109-230) IS COMPND 15 FROM HUMAN SOURCE, AND THE VARIABLE DOMAIN (RESIDUES 1- COMPND 16 108) IS FROM MURINE SOURCE SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS + HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE + HUMAN; SOURCE 4 STRAIN: BALB/C; SOURCE 5 CELL_LINE: 21D8; SOURCE 6 ORGAN: SPLEEN; SOURCE 7 CELL: B-LYMPHOCYTE; SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 9 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 10 EXPRESSION_SYSTEM_STRAIN: TOPP2; SOURCE 11 EXPRESSION_SYSTEM_CELLULAR_LOCATION: PERIPLASM; SOURCE 12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 13 EXPRESSION_SYSTEM_PLASMID: P4XH-M13; SOURCE 14 MOL_ID: 2; SOURCE 15 ORGANISM_SCIENTIFIC: MUS MUSCULUS + HOMO SAPIENS; SOURCE 16 ORGANISM_COMMON: HOUSE MOUSE + HUMAN; SOURCE 17 STRAIN: BALB/C; SOURCE 18 CELL_LINE: 21D8; SOURCE 19 ORGAN: SPLEEN; SOURCE 20 CELL: B-LYMPHOCYTE; SOURCE 21 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 22 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 23 EXPRESSION_SYSTEM_STRAIN: TOPP2; SOURCE 24 EXPRESSION_SYSTEM_CELLULAR_LOCATION: PERIPLASM; SOURCE 25 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 26 EXPRESSION_SYSTEM_PLASMID: P4XH-M13 KEYWDS IMMUNOGLOBULIN, CATALYTIC ANTIBODY, CHIMERIC FAB, KEYWDS 2 DECARBOXYLASE, HAPTEN COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR K.HOTTA,I.A.WILSON REVDAT 2 01-APR-03 1C5C 1 JRNL REVDAT 1 11-OCT-00 1C5C 0 JRNL AUTH K.HOTTA,H.LANGE,D.J.TANTILLO,K.N.HOUK,D.HILVERT, JRNL AUTH 2 I.A.WILSON JRNL TITL CATALYSIS OF DECARBOXYLATION BY A PREORGANIZED JRNL TITL 2 HETEROGENEOUS MICROENVIRONMENT: CRYSTAL STRUCTURES JRNL TITL 3 OF ABZYME 21D8. JRNL REF J.MOL.BIOL. V. 302 1213 2000 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.61 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : SHELXL-97 REMARK 3 AUTHORS : G.M.SHELDRICK REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.61 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 84.1 REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF). REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.188 REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.193 REMARK 3 FREE R VALUE (NO CUTOFF) : 0.253 REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 11.300 REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 4790 REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 42517 REMARK 3 REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F). REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.181 REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.186 REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.243 REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 11.200 REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 4257 REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 37873 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3207 REMARK 3 NUCLEIC ACID ATOMS : NULL REMARK 3 HETEROGEN ATOMS : 34 REMARK 3 SOLVENT ATOMS : 311 REMARK 3 REMARK 3 MODEL REFINEMENT. REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 3615.00 REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 3229.00 REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 9 REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 14592 REMARK 3 NUMBER OF RESTRAINTS : 13877 REMARK 3 REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES. REMARK 3 BOND LENGTHS (A) : 0.012 REMARK 3 ANGLE DISTANCES (A) : 0.026 REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000 REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.028 REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.045 REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.047 REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.048 REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.000 REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.072 REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.000 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED: MOEWS & KRETSINGER, J.MOL.BIOL.91(1973)201-228 REMARK 3 REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER REMARK 3 SPECIAL CASE: NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: ANISOTROPIC SCALING APPLIED BY THE REMARK 3 METHOD OF PARKIN, MOEZZI & HOPE, J.APPL.CRYST.28 (1995)53-56 REMARK 4 REMARK 4 1C5C 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 RCSB001356. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-JUL-1997 REMARK 200 TEMPERATURE (KELVIN) : 74.0 REMARK 200 PH : 6.00 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRL REMARK 200 BEAMLINE : BL9-1 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 : IMAGE PLATE 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 : 49213 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.610 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.6 REMARK 200 DATA REDUNDANCY : 3.600 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.05400 REMARK 200 FOR THE DATA SET : 20.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.61 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.67 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8 REMARK 200 DATA REDUNDANCY IN SHELL : 3.50 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.42100 REMARK 200 FOR SHELL : 3.380 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MERLOT, AMORE REMARK 200 STARTING MODEL: PDB ENTRY 1FRG AND 1GAF REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 37.98 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.0 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 1/2-X,-Y,1/2+Z REMARK 290 3555 -X,1/2+Y,1/2-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 19.60850 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 110.60250 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 21.96600 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 110.60250 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 19.60850 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 21.96600 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 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: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI REMARK 500 O LYS H 129 O HOH 95 0.85 REMARK 500 C LYS H 129 O HOH 95 1.92 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH 162 O HOH 278 1565 2.17 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 -33.27 64.56 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 58 DISTANCE = 5.43 ANGSTROMS REMARK 525 HOH 196 DISTANCE = 10.62 ANGSTROMS REMARK 525 HOH 218 DISTANCE = 5.15 ANGSTROMS REMARK 525 HOH 250 DISTANCE = 5.52 ANGSTROMS REMARK 525 HOH 276 DISTANCE = 5.33 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1C5B RELATED DB: PDB REMARK 900 DECARBOXYLASE CATALYTIC ANTIBODY 21D8 UNLIGANDED SEQRES 1 L 214 GLU ILE GLN LEU THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 214 SER LEU GLY GLU ARG VAL SER LEU THR CYS ARG THR SER SEQRES 3 L 214 GLN GLU ILE SER GLY TYR LEU SER TRP LEU GLN GLN LYS SEQRES 4 L 214 PRO ASP GLY THR ILE LYS ARG LEU ILE TYR ASP ALA THR SEQRES 5 L 214 LYS LEU ASP SER GLY ALA PRO LYS ARG PHE SER GLY SER SEQRES 6 L 214 ARG SER GLY SER ASP TYR SER LEU THR ILE SER SER LEU SEQRES 7 L 214 GLU SER GLU ASP PHE ALA ASP TYR TYR CYS LEU GLN TYR SEQRES 8 L 214 ALA SER PHE PRO ARG THR PHE GLY GLY GLY THR LYS LEU 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 215 GLN VAL GLN LEU LEU GLU PRO GLY THR GLU LEU VAL LYS SEQRES 2 H 215 PRO GLY ALA SER VAL LYS LEU SER CYS ARG ALA SER GLY SEQRES 3 H 215 TYR SER PHE THR SER TYR TRP MET HIS TRP VAL LYS GLN SEQRES 4 H 215 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY LEU ILE ASP SEQRES 5 H 215 PRO SER ASN GLY ARG THR ASN PHE ASN ASP LYS PHE LYS SEQRES 6 H 215 SER ARG ALA THR LEU THR VAL ASP THR SER SER SER THR SEQRES 7 H 215 ALA TYR MET GLN LEU SER SER LEU THR SER GLU ASP SER SEQRES 8 H 215 ALA VAL TYR TYR CYS VAL ARG ILE ALA TYR TRP GLY GLN SEQRES 9 H 215 GLY THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY SEQRES 10 H 215 PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SEQRES 11 H 215 SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP SEQRES 12 H 215 TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SEQRES 13 H 215 ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 14 H 215 GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR SEQRES 15 H 215 VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS SEQRES 16 H 215 ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS SEQRES 17 H 215 LYS VAL GLU PRO LYS SER CYS HET TK4 1001 22 HET GOL 2001 6 HET GOL 2002 6 HETNAM TK4 2-ACETYLAMINO-NAPTHALENE-1,5-DISULFONIC ACID HETNAM GOL GLYCEROL FORMUL 3 TK4 C12 H11 N O7 S2 FORMUL 4 GOL 2(C3 H8 O3) FORMUL 6 HOH *311(H2 O) HELIX 1 H1 SER L 80 ASP L 82 5 3 HELIX 2 H2 ASP L 122 LYS L 126 1 5 HELIX 3 H3 LYS L 183 GLU L 187 1 5 HELIX 4 H4 ASP H 61 LYS H 64 1 4 HELIX 5 H5 SER H 84 ASP H 86 1 3 HELIX 6 H6 SER H 195 GLY H 199 5 5 SHEET 1 A 4 LEU L 4 SER L 7 0 SHEET 2 A 4 VAL L 19 THR L 25 -1 N THR L 22 O SER L 7 SHEET 3 A 4 ASP L 70 ILE L 75 -1 O TYR L 71 N CYS L 23 SHEET 4 A 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 B 5 LYS L 53 LEU L 54 0 SHEET 2 B 5 ILE L 44 TYR L 49 -1 N TYR L 49 O LYS L 53 SHEET 3 B 5 LEU L 33 GLN L 38 -1 O TRP L 35 N LEU L 47 SHEET 4 B 5 ASP L 85 GLN L 90 -1 O ASP L 85 N 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 LYS L 53 LEU L 54 0 SHEET 2 C 6 ILE L 44 TYR L 49 -1 N TYR L 49 O LYS L 53 SHEET 3 C 6 LEU L 33 GLN L 38 -1 O TRP L 35 N LEU L 47 SHEET 4 C 6 ASP L 85 GLN L 90 -1 O ASP L 85 N 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 ALA L 13 1 N LEU L 11 O LYS L 103 SHEET 1 D 4 SER L 114 PHE L 118 0 SHEET 2 D 4 THR L 129 PHE L 139 -1 O VAL L 133 N PHE L 118 SHEET 3 D 4 TYR L 173 SER L 182 -1 O TYR L 173 N PHE L 139 SHEET 4 D 4 SER L 159 VAL L 163 -1 O GLN L 160 N THR L 178 SHEET 1 E 4 ALA L 153 LEU L 154 0 SHEET 2 E 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 E 4 VAL L 191 THR L 197 -1 N ALA L 193 O LYS L 149 SHEET 4 E 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196 SHEET 1 F 4 GLN H 3 LEU H 5 0 SHEET 2 F 4 VAL H 18 SER H 25 -1 N ARG H 23 O LEU H 5 SHEET 3 F 4 THR H 77 LEU H 82 -1 N ALA H 78 O CYS H 22 SHEET 4 F 4 ALA H 67 ASP H 72 -1 O THR H 68 N GLN H 81 SHEET 1 G 5 THR H 57 PHE H 59 0 SHEET 2 G 5 LEU H 45 ILE H 51 -1 N LEU H 50 O ASN H 58 SHEET 3 G 5 MET H 34 GLN H 39 -1 N MET H 34 O ILE H 51 SHEET 4 G 5 ALA H 88 ARG H 94 -1 N VAL H 89 O GLN H 39 SHEET 5 G 5 TYR H 102 TRP H 103 -1 O TYR H 102 N ARG H 94 SHEET 1 H 6 THR H 57 PHE H 59 0 SHEET 2 H 6 LEU H 45 ILE H 51 -1 N LEU H 50 O ASN H 58 SHEET 3 H 6 MET H 34 GLN H 39 -1 N MET H 34 O ILE H 51 SHEET 4 H 6 ALA H 88 ARG H 94 -1 N VAL 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 THR H 9 VAL H 12 1 O GLU H 10 N THR H 110 SHEET 1 I 3 THR H 153 TRP H 157 0 SHEET 2 I 3 ILE H 207 HIS H 212 -1 N ASN H 209 O SER H 156 SHEET 3 I 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 SER L 7 PRO L 8 0 -1.78 CISPEP 2 PHE L 94 PRO L 95 0 0.36 CISPEP 3 TYR L 140 PRO L 141 0 1.81 CISPEP 4 PHE H 148 PRO H 149 0 -12.60 CISPEP 5 GLU H 150 PRO H 151 0 -4.60 CRYST1 39.217 43.932 221.205 90.00 90.00 90.00 P 21 21 21 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 0.025499 0.000000 0.000000 0.00000 SCALE2 0.000000 0.022762 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004521 0.00000