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HEADER IMMUNE SYSTEM 11-DEC-03 1RUP TITLE CRYSTAL STRUCTURE (G) OF NATIVE CATIONIC CYCLIZATION TITLE 2 ANTIBODY 4C6 FAB AT PH 8.5 WITH A DATA SET COLLECTED AT TITLE 3 APS BEAMLINE 19-ID COMPND MOL_ID: 1; COMPND 2 MOLECULE: IMMUNOGLOBULIN IGG2A, HEAVY CHAIN; COMPND 3 CHAIN: L; COMPND 4 FRAGMENT: FAB; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: IMMUNOGLOBULIN IGG2A, LIGHT CHAIN; COMPND 7 CHAIN: H; COMPND 8 FRAGMENT: FAB SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 STRAIN: 129G1X+; SOURCE 5 MOL_ID: 2; SOURCE 6 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 7 ORGANISM_COMMON: MOUSE; SOURCE 8 STRAIN: 129G1X+ KEYWDS IMMUNOGLOBULIN, CATALYTIC ANTIBODY, WATER OXIDATION, AMINO KEYWDS 2 ACID MODIFICATION EXPDTA X-RAY DIFFRACTION AUTHOR X.ZHU,P.WENTWORTH JR.,A.D.WENTWORTH,A.ESCHENMOSER, AUTHOR 2 R.A.LERNER,I.A.WILSON REVDAT 1 02-MAR-04 1RUP 0 JRNL AUTH X.ZHU,P.WENTWORTH JR.,A.D.WENTWORTH,A.ESCHENMOSER, JRNL AUTH 2 R.A.LERNER,I.A.WILSON JRNL TITL PROBING THE ANTIBODY-CATALYZED WATER-OXIDATION JRNL TITL 2 PATHWAY AT ATOMIC RESOLUTION. JRNL REF PROC.NATL.ACAD.SCI.USA V. 110 2247 2004 JRNL REFN ASTM PNASA6 US ISSN 0027-8424 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH X.ZHU,A.HEINE,F.MONNAT,K.N.HOUK,K.D.JANDA, REMARK 1 AUTH 2 I.A.WILSON REMARK 1 TITL STRUCTURAL BASIS FOR ANTIBODY CATALYSIS OF A REMARK 1 TITL 2 CATIONIC CYCLIZATION REACTION REMARK 1 REF J.MOL.BIOL. V. 329 69 2003 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 2 REMARK 2 RESOLUTION. 1.40 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) : 1.40 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 86.3 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) : NULL REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.161 REMARK 3 FREE R VALUE (NO CUTOFF) : 0.212 REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 5069 REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 100805 REMARK 3 REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F). REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : NULL REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.155 REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.206 REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 4363 REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 86423 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3398 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 9 REMARK 3 SOLVENT ATOMS : 495 REMARK 3 REMARK 3 MODEL REFINEMENT. REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : NULL REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : NULL REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : NULL REMARK 3 NUMBER OF RESTRAINTS : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES. REMARK 3 BOND LENGTHS (A) : 0.013 REMARK 3 ANGLE DISTANCES (A) : 0.030 REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000 REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.032 REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.058 REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.073 REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.023 REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.004 REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.054 REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.082 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 & 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 1RUP 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 RCSB021049. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 06-JUN-2001 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 8.50 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 19-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0332 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : SBC2 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 104925 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 93.4 REMARK 200 DATA REDUNDANCY : 7.200 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.07900 REMARK 200 FOR THE DATA SET : 31.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.43 REMARK 200 COMPLETENESS FOR SHELL (%) : 90.7 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.61600 REMARK 200 FOR SHELL : 2.400 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: CNS REMARK 200 STARTING MODEL: PDB ENTRY 1NCW REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 56.60 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS HYDROCHLORIDE, 0.2 M REMARK 280 SODIUM ACETATE, 15% (W/V) PEG 4000 , PH 8.5, VAPOR DIFFUSION, REMARK 280 SITTING DROP, TEMPERATURE 295K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2 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 1/2-Y,1/2+X,1/4+Z REMARK 290 4555 1/2+Y,1/2-X,3/4+Z REMARK 290 5555 1/2-X,1/2+Y,1/4-Z REMARK 290 6555 1/2+X,1/2-Y,3/4-Z REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,1/2-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 133.23750 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 32.09850 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 32.09850 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 66.61875 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 32.09850 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 32.09850 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 199.85625 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 32.09850 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 32.09850 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 66.61875 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 32.09850 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 32.09850 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 199.85625 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 133.23750 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 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 18 CA - CB - CG ANGL. DEV. = 22.4 DEGREES REMARK 500 SER H 65 C - N - CA ANGL. DEV. = 15.6 DEGREES REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1NCW RELATED DB: PDB REMARK 900 SAME NATIVE PROTEIN REMARK 900 RELATED ID: 1ND0 RELATED DB: PDB REMARK 900 SAME NATIVE PROTEIN COMPLEX WITH TRANSITION STATE ANALOG REMARK 900 RELATED ID: 1RU9 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF U.V.-IRRADIATED CATIONIC CYCLIZATION REMARK 900 ANTIBODY 4C6 FAB AT PH 4.6 WITH A DATA SET COLLECTED IN- REMARK 900 HOUSE. REMARK 900 RELATED ID: 1RUA RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF U.V.-IRRADIATED CATIONIC CYCLIZATION REMARK 900 ANTIBODY 4C6 FAB AT PH 4.6 WITH A DATA SET COLLECTED AT REMARK 900 SSRL BEAMLINE 11-1. REMARK 900 RELATED ID: 1RUK RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF NATIVE CATIONIC CYCLIZATION ANTIBODY REMARK 900 4C6 FAB AT PH 4.6 WITH A DATA SET COLLECTED AT SSRL REMARK 900 BEAMLINE 9-1 REMARK 900 RELATED ID: 1RUL RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF U.V.-IRRADIATED CATIONIC CYCLIZATION REMARK 900 ANTIBODY 4C6 FAB AT PH 5.6 WITH A DATA SET COLLECTED AT REMARK 900 SSRL BEAMLINE 11-1. REMARK 900 RELATED ID: 1RUM RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF H2O2-SOAKED CATIONIC CYCLIZATION REMARK 900 ANTIBODY 4C6 FAB AT PH 8.5 WITH A DATA SET COLLECTED AT REMARK 900 SSRL BEAMLINE 9-1. DBREF 1RUP H 115 231 UNP P01865 GCAM_MOUSE 1 102 SEQRES 1 L 219 ASP VAL VAL MET THR GLN SER PRO LYS THR ILE SER VAL SEQRES 2 L 219 THR ILE GLY GLN PRO ALA SER ILE SER CYS LYS SER SER SEQRES 3 L 219 GLN ARG LEU LEU ASN SER ASN GLY LYS THR PHE LEU ASN SEQRES 4 L 219 TRP LEU LEU GLN ARG PRO GLY GLN SER PRO LYS ARG LEU SEQRES 5 L 219 ILE TYR LEU GLY THR LYS LEU ASP SER GLY VAL PRO ASP SEQRES 6 L 219 ARG PHE THR GLY SER GLY SER GLY THR ASP PHE THR LEU SEQRES 7 L 219 LYS ILE SER ARG VAL GLU ALA GLU ASP LEU GLY VAL TYR SEQRES 8 L 219 TYR CYS TRP GLN GLY THR HIS PHE PRO TYR THR PHE GLY SEQRES 9 L 219 GLY GLY THR LYS LEU GLU ILE LYS ARG ALA ASP ALA ALA SEQRES 10 L 219 PRO THR VAL SER ILE PHE PRO PRO SER SER GLU GLN LEU SEQRES 11 L 219 THR SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN ASN SEQRES 12 L 219 PHE TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE ASP SEQRES 13 L 219 GLY SER GLU ARG GLN ASN GLY VAL LEU ASN SER TRP THR SEQRES 14 L 219 ASP GLN ASP SER LYS ASP SER THR TYR SER MET SER SER SEQRES 15 L 219 THR LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS ASN SEQRES 16 L 219 SER TYR THR CYS GLU ALA THR HIS LYS THR SER THR SER SEQRES 17 L 219 PRO ILE VAL LYS SER PHE ASN ARG ASN GLU CYS SEQRES 1 H 222 ARG VAL GLN LEU GLN GLN SER GLY PRO GLY LEU VAL LYS SEQRES 2 H 222 PRO SER GLN SER LEU SER LEU THR CYS THR VAL THR GLY SEQRES 3 H 222 TYR SER ILE THR SER ASP PHE ALA TRP ASN TRP ILE ARG SEQRES 4 H 222 GLN PHE PRO GLY ASN LYS LEU GLU TRP MET GLY TYR ILE SEQRES 5 H 222 ASN TYR SER GLY PHE THR SER HIS ASN PRO SER LEU LYS SEQRES 6 H 222 SER ARG ILE SER ILE THR ARG ASP THR SER LYS ASN GLN SEQRES 7 H 222 PHE PHE LEU GLN LEU ASN SER VAL THR THR GLU ASP THR SEQRES 8 H 222 ALA THR TYR TYR CYS ALA GLY LEU LEU TRP TYR ASP GLY SEQRES 9 H 222 GLY ALA GLY SER TRP GLY GLN GLY THR LEU VAL THR VAL SEQRES 10 H 222 SER ALA ALA LYS THR THR ALA PRO SER VAL TYR PRO LEU SEQRES 11 H 222 ALA PRO VAL CYS GLY ASP THR THR GLY SER SER VAL THR SEQRES 12 H 222 LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL SEQRES 13 H 222 THR LEU THR TRP ASN SER GLY SER LEU SER SER GLY VAL SEQRES 14 H 222 HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR SEQRES 15 H 222 LEU SER SER SER VAL THR VAL THR SER SER THR TRP PRO SEQRES 16 H 222 SER GLN SER ILE THR CYS ASN VAL ALA HIS PRO ALA SER SEQRES 17 H 222 SER THR LYS VAL ASP LYS LYS ILE GLU PRO ARG GLY PRO SEQRES 18 H 222 THR HET BEZ 601 9 HET GOL 611 6 HET GOL 612 6 HET GOL 613 6 HET GOL 614 6 HETNAM BEZ BENZOIC ACID HETNAM GOL GLYCEROL FORMUL 3 BEZ C7 H6 O2 FORMUL 4 GOL 4(C3 H8 O3) FORMUL 8 HOH *471(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 HIS L 189 1 7 HELIX 4 4 PRO H 61 LYS H 64 5 4 HELIX 5 5 THR H 83 THR H 87 5 5 HELIX 6 6 VAL H 127 THR H 133 5 5 HELIX 7 7 SER H 163 SER H 165 5 3 HELIX 8 8 SER H 196 TRP H 199 5 3 HELIX 9 9 PRO H 213 SER H 216 5 4 SHEET 1 A 4 MET L 4 SER L 7 0 SHEET 2 A 4 ALA L 19 SER L 25 -1 O SER L 22 N SER L 7 SHEET 3 A 4 ASP L 70 ILE L 75 -1 O PHE L 71 N CYS L 23 SHEET 4 A 4 PHE L 62 SER L 67 -1 N THR L 63 O LYS L 74 SHEET 1 B 6 THR L 10 THR L 14 0 SHEET 2 B 6 THR L 102 LYS L 107 1 O GLU L 105 N ILE L 11 SHEET 3 B 6 GLY L 84 GLN L 90 -1 N GLY L 84 O LEU L 104 SHEET 4 B 6 LEU L 33 GLN L 38 -1 N GLN L 38 O VAL L 85 SHEET 5 B 6 PRO L 44 TYR L 49 -1 O LYS L 45 N LEU L 37 SHEET 6 B 6 LYS L 53 LEU L 54 -1 O LYS L 53 N TYR L 49 SHEET 1 C 4 THR L 10 THR L 14 0 SHEET 2 C 4 THR L 102 LYS L 107 1 O GLU L 105 N ILE L 11 SHEET 3 C 4 GLY L 84 GLN L 90 -1 N GLY L 84 O LEU L 104 SHEET 4 C 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 D 4 THR L 114 PHE L 118 0 SHEET 2 D 4 GLY L 129 PHE L 139 -1 O ASN L 137 N THR L 114 SHEET 3 D 4 TYR L 173 THR L 182 -1 O SER L 177 N CYS L 134 SHEET 4 D 4 VAL L 159 TRP L 163 -1 N SER L 162 O SER L 176 SHEET 1 E 4 SER L 153 GLU L 154 0 SHEET 2 E 4 ASN L 145 ILE L 150 -1 N ILE L 150 O SER L 153 SHEET 3 E 4 SER L 191 HIS L 198 -1 O THR L 197 N ASN L 145 SHEET 4 E 4 SER L 201 ASN L 210 -1 O ILE L 205 N ALA L 196 SHEET 1 F 4 GLN H 3 SER H 7 0 SHEET 2 F 4 LEU H 18 THR H 25 -1 O THR H 21 N SER H 7 SHEET 3 F 4 GLN H 77 LEU H 82 -1 O PHE H 78 N CYS H 22 SHEET 4 F 4 ILE H 67 ASP H 72 -1 N THR H 70 O PHE H 79 SHEET 1 G 6 LEU H 11 VAL H 12 0 SHEET 2 G 6 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 G 6 ALA H 88 LEU H 96 -1 N TYR H 90 O THR H 107 SHEET 4 G 6 PHE H 33 PHE H 40 -1 N ILE H 37 O TYR H 91 SHEET 5 G 6 LYS H 44 ASN H 52 -1 O MET H 48 N TRP H 36 SHEET 6 G 6 THR H 57 HIS H 59 -1 O SER H 58 N TYR H 50 SHEET 1 H 4 LEU H 11 VAL H 12 0 SHEET 2 H 4 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 H 4 ALA H 88 LEU H 96 -1 N TYR H 90 O THR H 107 SHEET 4 H 4 SER H 102 TRP H 103 -1 O SER H 102 N GLY H 94 SHEET 1 I 4 SER H 120 LEU H 124 0 SHEET 2 I 4 SER H 137 TYR H 147 -1 O LEU H 143 N TYR H 122 SHEET 3 I 4 LEU H 184 THR H 194 -1 O LEU H 187 N VAL H 144 SHEET 4 I 4 VAL H 171 THR H 173 -1 N HIS H 172 O SER H 190 SHEET 1 J 4 SER H 120 LEU H 124 0 SHEET 2 J 4 SER H 137 TYR H 147 -1 O LEU H 143 N TYR H 122 SHEET 3 J 4 LEU H 184 THR H 194 -1 O LEU H 187 N VAL H 144 SHEET 4 J 4 VAL H 177 GLN H 179 -1 N GLN H 179 O LEU H 184 SHEET 1 K 3 THR H 153 TRP H 157 0 SHEET 2 K 3 THR H 206 HIS H 212 -1 O ASN H 209 N THR H 156 SHEET 3 K 3 THR H 217 LYS H 222 -1 O VAL H 219 N VAL H 210 SSBOND 1 CYS L 23 CYS L 88 SSBOND 2 CYS L 134 CYS L 194 SSBOND 3 CYS L 214 CYS H 128 SSBOND 4 CYS H 22 CYS H 92 SSBOND 5 CYS H 142 CYS H 208 CISPEP 1 SER L 7 PRO L 8 0 -3.07 CISPEP 2 PHE L 94 PRO L 95 0 -8.42 CISPEP 3 TYR L 140 PRO L 141 0 -2.36 CISPEP 4 PHE H 148 PRO H 149 0 -6.23 CISPEP 5 GLU H 150 PRO H 151 0 -4.19 CISPEP 6 TRP H 199 PRO H 200 0 9.67 CRYST1 64.197 64.197 266.475 90.00 90.00 90.00 P 41 21 2 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 0.015577 0.000000 0.000000 0.00000 SCALE2 0.000000 0.015577 0.000000 0.00000 SCALE3 0.000000 0.000000 0.003753 0.00000