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HEADER IMMUNE SYSTEM 11-DEC-03 1RUR TITLE CRYSTAL STRUCTURE (I) OF NATIVE DIELS-ALDER ANTIBODY 13G5 TITLE 2 FAB AT PH 8.0 WITH A DATA SET COLLECTED AT SSRL BEAMLINE 9- TITLE 3 1. COMPND MOL_ID: 1; COMPND 2 MOLECULE: IMMUNOGLOBULIN 13G5, LIGHT CHAIN; COMPND 3 CHAIN: L; COMPND 4 FRAGMENT: FAB; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: IMMUNOGLOBULIN 13G5, HEAVY 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: 13G5 MURINE HYBRIDIMA; SOURCE 5 MOL_ID: 2; SOURCE 6 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 7 ORGANISM_COMMON: MOUSE; SOURCE 8 STRAIN: 13G5 MURINE HYBRIDIMA 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 1RUR 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 A.HEINE,E.A.STURA,J.T.YLI-KAUHALUOMA,C.GAO,Q.DENG, REMARK 1 AUTH 2 B.R.BENO,K.N.HOUK,K.D.JANDA,I.A.WILSON REMARK 1 TITL AN ANTIBODY EXO DIELS-ALDERASE INHIBITOR COMPLEX REMARK 1 TITL 2 AT 1.95 ANGSTROM RESOLUTION REMARK 1 REF SCIENCE V. 279 1934 1998 REMARK 1 REFN ASTM SCIEAS US ISSN 0036-8075 REMARK 2 REMARK 2 RESOLUTION. 1.50 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) : 1.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 84.0 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) : 0.191 REMARK 3 FREE R VALUE (NO CUTOFF) : 0.256 REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 4021 REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 65588 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)) : 0.176 REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.240 REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 2966 REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 48682 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3308 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 2 REMARK 3 SOLVENT ATOMS : 372 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) : 0.008 REMARK 3 ANGLE DISTANCES (A) : 0.024 REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000 REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.026 REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.036 REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.046 REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.012 REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.003 REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.051 REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.066 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED: NULL REMARK 3 REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER REMARK 3 SPECIAL CASE: NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1RUR 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 RCSB021051. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 07-FEB-2002 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 : 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) : 0.99184 REMARK 200 MONOCHROMATOR : SINGLE CRYSTAL SI(111) BENT REMARK 200 OPTICS : FLAT MIRROR REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 71213 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500 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 (%) : 97.4 REMARK 200 DATA REDUNDANCY : 2.700 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.04700 REMARK 200 FOR THE DATA SET : 24.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.53 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.9 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.53600 REMARK 200 FOR SHELL : 1.600 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 1A3L REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 49.64 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M IMIDAZOLE, PH 8.0, 0.2 M ZINC REMARK 280 ACETATE, 5-7% (V/V) ISOPROPANOL, 20% (W/V) PEG 3000, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 295K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 1/2+X,1/2+Y,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 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 89.63750 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 20.15500 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 89.63750 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 20.15500 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: 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 LEU L 27C C ASN L 27D N -0.051 REMARK 500 THR H 134 CA THR H 134 C -0.060 REMARK 500 SER H 136 N SER H 136 CA 0.077 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 MET L 51 -38.76 68.56 REMARK 500 ALA H 129 88.12 143.03 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 293 DISTANCE = 5.61 ANGSTROMS REMARK 525 HOH 321 DISTANCE = 5.54 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1RUQ RELATED DB: PDB REMARK 900 U.V.-IRRADIATED PROTEIN REMARK 999 REMARK 999 SEQUENCE REMARK 999 NO SUITABLE SEQUENCE DATA BASE REFERENCE REMARK 999 WAS AVAILABLE AT THE TIME OF PROCESSING REMARK 999 THIS FILE. DBREF 1RUR H 114 227 UNP P01869 IGH1M_MOUSE 1 99 SEQRES 1 L 217 ASP ILE VAL LEU THR GLN ALA ALA PHE SER ASN PRO VAL SEQRES 2 L 217 THR LEU GLY ALA SER ALA SER ILE SER CYS ARG SER SER SEQRES 3 L 217 LYS SER LEU LEU ASN SER ASN GLY ILE ILE HIS MET TYR SEQRES 4 L 217 TRP TYR LEU GLN LYS PRO GLY GLN SER PRO GLN LEU LEU SEQRES 5 L 217 ILE TYR GLN MET SER LYS LEU ALA SER GLY ALA PRO ASP SEQRES 6 L 217 ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU SEQRES 7 L 217 ARG ILE SER ARG VAL GLU ALA GLU ASP VAL GLY VAL TYR SEQRES 8 L 217 TYR CYS ALA GLN ASN LEU GLU LEU PRO TYR THR PHE GLY SEQRES 9 L 217 GLY GLY THR LYS LEU GLU ILE LYS ARG ALA ASP ALA ALA SEQRES 10 L 217 PRO THR VAL SER ILE PHE PRO PRO SER SER GLU GLN LEU SEQRES 11 L 217 THR SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN ASN SEQRES 12 L 217 PHE TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE ASP SEQRES 13 L 217 GLY SER GLU ARG GLN ASN GLY VAL LEU ASN SER TRP THR SEQRES 14 L 217 ASP GLN ASP THR LYS ASP SER THR TYR SER MET SER SER SEQRES 15 L 217 THR LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS ASN SEQRES 16 L 217 SER TYR THR CYS GLU ALA THR HIS LYS THR SER THR SER SEQRES 17 L 217 PRO ILE VAL LYS SER PHE ASN ARG ASN SEQRES 1 H 218 GLU VAL GLN LEU GLU GLU SER GLY PRO GLU LEU VAL ARG SEQRES 2 H 218 PRO GLY THR SER VAL LYS ILE SER CYS LYS ALA SER GLY SEQRES 3 H 218 TYR THR PHE THR ASN TYR TRP LEU GLY TRP VAL LYS GLN SEQRES 4 H 218 ARG PRO GLY HIS GLY PHE GLU TRP ILE GLY ASP ILE TYR SEQRES 5 H 218 PRO GLY GLY VAL TYR THR THR ASN ASN GLU LYS PHE ARG SEQRES 6 H 218 GLY LYS ALA ILE LEU THR ALA ASP THR SER SER SER THR SEQRES 7 H 218 ALA TYR MET GLN LEU SER SER LEU THR SER GLU ASP SER SEQRES 8 H 218 ALA VAL TYR PHE CYS ALA ARG ALA GLY GLY TYR TYR THR SEQRES 9 H 218 GLY GLY ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL SEQRES 10 H 218 SER SER ALA LYS THR THR PRO PRO SER VAL TYR PRO LEU SEQRES 11 H 218 ALA PRO GLY SER ALA ALA GLN THR ASN SER MET VAL THR SEQRES 12 H 218 LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL SEQRES 13 H 218 THR VAL THR TRP ASN SER GLY SER LEU SER SER GLY VAL SEQRES 14 H 218 HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR SEQRES 15 H 218 LEU SER SER SER VAL THR VAL PRO SER SER THR TRP PRO SEQRES 16 H 218 SER GLU THR VAL THR CYS ASN VAL ALA HIS PRO ALA SER SEQRES 17 H 218 SER THR LYS VAL ASP LYS LYS ILE VAL PRO HET ZN 601 1 HET ZN 602 1 HETNAM ZN ZINC ION FORMUL 3 ZN 2(ZN 2+) FORMUL 5 HOH *372(H2 O) HELIX 1 1 GLU L 79 VAL 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 THR H 28 TYR H 32 5 5 HELIX 5 5 GLU H 61 ARG H 64 5 4 HELIX 6 6 THR H 83 SER H 87 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 LEU L 4 THR L 5 0 SHEET 2 A 4 ALA L 19 SER L 25 -1 O ARG L 24 N THR L 5 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 GLY L 66 -1 N SER L 63 O ARG L 74 SHEET 1 B 2 VAL L 13 THR L 14 0 SHEET 2 B 2 ILE L 106 LYS L 107 1 O LYS L 107 N VAL L 13 SHEET 1 C 5 LYS L 53 LEU L 54 0 SHEET 2 C 5 GLN L 45 TYR L 49 -1 N TYR L 49 O LYS L 53 SHEET 3 C 5 MET L 33 GLN L 38 -1 N TRP L 35 O LEU L 47 SHEET 4 C 5 GLY L 84 GLN L 90 -1 O VAL L 85 N GLN L 38 SHEET 5 C 5 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 D 5 LYS L 53 LEU L 54 0 SHEET 2 D 5 GLN L 45 TYR L 49 -1 N TYR L 49 O LYS L 53 SHEET 3 D 5 MET L 33 GLN L 38 -1 N TRP L 35 O LEU L 47 SHEET 4 D 5 GLY L 84 GLN L 90 -1 O VAL L 85 N GLN L 38 SHEET 5 D 5 THR L 102 LEU L 104 -1 O THR L 102 N TYR L 86 SHEET 1 E 4 THR L 114 PHE L 118 0 SHEET 2 E 4 GLY L 129 PHE L 139 -1 O ASN L 137 N THR L 114 SHEET 3 E 4 TYR L 173 THR L 182 -1 O SER L 177 N CYS L 134 SHEET 4 E 4 VAL L 159 TRP L 163 -1 N SER L 162 O SER L 176 SHEET 1 F 4 SER L 153 ARG L 155 0 SHEET 2 F 4 ASN L 145 ILE L 150 -1 N ILE L 150 O SER L 153 SHEET 3 F 4 SER L 191 THR L 197 -1 O THR L 197 N ASN L 145 SHEET 4 F 4 ILE L 205 ASN L 210 -1 O ILE L 205 N ALA L 196 SHEET 1 G 4 GLN H 3 GLU H 6 0 SHEET 2 G 4 VAL H 18 SER H 25 -1 O LYS H 23 N GLU H 5 SHEET 3 G 4 THR H 77 LEU H 82 -1 O ALA H 78 N CYS H 22 SHEET 4 G 4 ALA H 67 ASP H 72 -1 N ILE H 68 O GLN H 81 SHEET 1 H 6 GLU H 10 VAL H 12 0 SHEET 2 H 6 THR H 107 VAL H 111 1 O THR H 110 N GLU H 10 SHEET 3 H 6 ALA H 88 ALA H 95 -1 N TYR H 90 O THR H 107 SHEET 4 H 6 LEU H 34 GLN H 39 -1 N GLY H 35 O ALA H 93 SHEET 5 H 6 GLU H 46 TYR H 52 -1 O GLU H 46 N LYS H 38 SHEET 6 H 6 TYR H 56 ASN H 59 -1 O TYR H 56 N TYR H 52 SHEET 1 I 4 GLU H 10 VAL H 12 0 SHEET 2 I 4 THR H 107 VAL H 111 1 O THR H 110 N GLU H 10 SHEET 3 I 4 ALA H 88 ALA H 95 -1 N TYR H 90 O THR H 107 SHEET 4 I 4 GLY H 100B TRP H 103 -1 O TYR H 102 N ARG H 94 SHEET 1 J 4 SER H 120 LEU H 124 0 SHEET 2 J 4 MET H 137 TYR H 147 -1 O LYS H 145 N SER H 120 SHEET 3 J 4 LEU H 184 PRO H 194 -1 O TYR H 185 N TYR H 147 SHEET 4 J 4 VAL H 171 THR H 173 -1 N HIS H 172 O SER H 190 SHEET 1 K 4 SER H 120 LEU H 124 0 SHEET 2 K 4 MET H 137 TYR H 147 -1 O LYS H 145 N SER H 120 SHEET 3 K 4 LEU H 184 PRO H 194 -1 O TYR H 185 N TYR H 147 SHEET 4 K 4 VAL H 177 GLN H 179 -1 N VAL H 177 O THR H 186 SHEET 1 L 3 THR H 153 TRP H 157 0 SHEET 2 L 3 THR H 206 HIS H 212 -1 O ALA H 211 N THR H 153 SHEET 3 L 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 LEU L 94 PRO L 95 0 -8.01 CISPEP 2 TYR L 140 PRO L 141 0 -3.08 CISPEP 3 GLY H 54 VAL H 55 0 -1.05 CISPEP 4 PHE H 148 PRO H 149 0 -7.14 CISPEP 5 GLU H 150 PRO H 151 0 -5.80 CISPEP 6 TRP H 199 PRO H 200 0 -0.73 CRYST1 179.275 40.310 67.631 90.00 109.91 90.00 C 1 2 1 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 0.005578 0.000000 0.002020 0.00000 SCALE2 0.000000 0.024808 0.000000 0.00000 SCALE3 0.000000 0.000000 0.015726 0.00000