HEADER IMMUNE SYSTEM 01-NOV-02 1J05 TITLE THE CRYSTAL STRUCTURE OF ANTI-CARCINOEMBRYONIC ANTIGEN TITLE 2 MONOCLONAL ANTIBODY T84.66 FV FRAGMENT COMPND MOL_ID: 1; COMPND 2 MOLECULE: ANTI-CEA MAB T84.66, LIGHT CHAIN; COMPND 3 CHAIN: L, A; COMPND 4 FRAGMENT: FV FRAGMENT; COMPND 5 SYNONYM: T84.66 ANTIBODY; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: ANTI-CEA MAB T84.66, HEAVY CHAIN; COMPND 9 CHAIN: H, B; COMPND 10 FRAGMENT: FV FRAGMENT; COMPND 11 SYNONYM: T84.66 ANTIBODY; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 10 ORGANISM_COMMON: MOUSE; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 13 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 14 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID KEYWDS IMMUNOGLOBULIN EXPDTA X-RAY DIFFRACTION AUTHOR H.KONDO,Y.NISHIMURA,M.SHIROISHI,R.ASANO,N.NORO,K.TSUMOTO, AUTHOR 2 I.KUMAGAI REVDAT 1 16-DEC-03 1J05 0 JRNL AUTH H.KONDO,Y.NISHIMURA,M.SHIROISHI,R.ASANO,N.NORO, JRNL AUTH 2 K.TSUMOTO,I.KUMAGAI JRNL TITL THE CRYSTAL STRUCTURE OF ANTI-CARCINOEMBRYONIC JRNL TITL 2 ANTIGEN MONOCLONAL ANTIBODY T84.66 FV FRAGMENT JRNL REF TO BE PUBLISHED JRNL REFN REMARK 1 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) : 5.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000 REMARK 3 COMPLETENESS FOR RANGE (%) : NULL REMARK 3 CROSS-VALIDATION METHOD : NULL 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) : 0.190 REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.185 REMARK 3 FREE R VALUE (NO CUTOFF) : 0.217 REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 8909 REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 91647 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)) : NULL REMARK 3 FREE R VALUE (F>4SIG(F)) : NULL REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : NULL REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3581 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 10 REMARK 3 SOLVENT ATOMS : 268 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) : NULL REMARK 3 ANGLE DISTANCES (A) : NULL REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : NULL REMARK 3 ZERO CHIRAL VOLUMES (A**3) : NULL REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : NULL REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : NULL REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : NULL REMARK 3 SIMILAR ADP COMPONENTS (A**2) : NULL REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : NULL 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 1J05 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 3.102 (2007-05-29) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ . REMARK 100 THE RCSB ID CODE IS RCSB005463. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 23-APR-2002 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 7.00 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : PHOTON FACTORY REMARK 200 BEAMLINE : BL-6A REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.000 REMARK 200 MONOCHROMATOR : NULL 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 : 91647 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500 REMARK 200 RESOLUTION RANGE LOW (A) : 23.250 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 200 DATA REDUNDANCY : 3.600 REMARK 200 R MERGE (I) : 0.06900 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.7000 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) : 1.58 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8 REMARK 200 DATA REDUNDANCY IN SHELL : 3.50 REMARK 200 R MERGE FOR SHELL (I) : 0.32500 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.200 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: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.04 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NA, K PHOSPHATE, NA HEPES, REMARK 280 GLYCEROL, PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE REMARK 280 293K 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 37.51650 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 4 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 350 BIOMOLECULE: 2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS L 107 O REMARK 470 SER H 113 O REMARK 470 LYS A 107 O REMARK 470 SER B 113 O 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 SER L 7 CB SER L 7 OG -0.094 REMARK 500 LEU L 54 CG LEU L 54 CD1 -0.147 REMARK 500 LEU L 54 CG LEU L 54 CD2 0.099 REMARK 500 SER H 25 CB SER H 25 OG -0.062 REMARK 500 VAL A 13 CB VAL A 13 CG1 0.115 REMARK 500 VAL A 13 CB VAL A 13 CG2 -0.091 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 ARG B 40 CD - NE - CZ ANGL. DEV. = 33.2 DEGREES REMARK 500 ARG B 50 CD - NE - CZ ANGL. DEV. = 13.6 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 ALA L 51 -40.96 74.64 REMARK 500 ARG L 68 -93.96 47.48 REMARK 500 ALA A 51 -41.59 72.67 DBREF 1J05 L 1 107 UNP P01660 KV3H_MOUSE 1 111 DBREF 1J05 H 1 113 UNP Q9JL85 Q9JL85_MOUSE 1 103 DBREF 1J05 A 1 107 UNP P01660 KV3H_MOUSE 1 111 DBREF 1J05 B 1 113 UNP Q9JL85 Q9JL85_MOUSE 1 103 SEQRES 1 L 111 ASP ILE VAL LEU THR GLN SER PRO ALA SER LEU ALA VAL SEQRES 2 L 111 SER LEU GLY GLN ARG ALA THR MET SER CYS ARG ALA GLY SEQRES 3 L 111 GLU SER VAL ASP ILE PHE GLY VAL GLY PHE LEU HIS TRP SEQRES 4 L 111 TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE SEQRES 5 L 111 TYR ARG ALA SER ASN LEU GLU SER GLY ILE PRO VAL ARG SEQRES 6 L 111 PHE SER GLY THR GLY SER ARG THR ASP PHE THR LEU ILE SEQRES 7 L 111 ILE ASP PRO VAL GLU ALA ASP ASP VAL ALA THR TYR TYR SEQRES 8 L 111 CYS GLN GLN THR ASN GLU ASP PRO TYR THR PHE GLY GLY SEQRES 9 L 111 GLY THR LYS LEU GLU ILE LYS SEQRES 1 H 121 GLU VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL GLU SEQRES 2 H 121 PRO GLY ALA SER VAL LYS LEU SER CYS THR ALA SER GLY SEQRES 3 H 121 PHE ASN ILE LYS ASP THR TYR MET HIS TRP VAL LYS GLN SEQRES 4 H 121 ARG PRO GLU GLN GLY LEU GLU TRP ILE GLY ARG ILE ASP SEQRES 5 H 121 PRO ALA ASN GLY ASN SER LYS TYR VAL PRO LYS PHE GLN SEQRES 6 H 121 GLY LYS ALA THR ILE THR ALA ASP THR SER SER ASN THR SEQRES 7 H 121 ALA TYR LEU GLN LEU THR SER LEU THR SER GLU ASP THR SEQRES 8 H 121 ALA VAL TYR TYR CYS ALA PRO PHE GLY TYR TYR VAL SER SEQRES 9 H 121 ASP TYR ALA MET ALA TYR TRP GLY GLN GLY THR SER VAL SEQRES 10 H 121 THR VAL SER SER SEQRES 1 A 111 ASP ILE VAL LEU THR GLN SER PRO ALA SER LEU ALA VAL SEQRES 2 A 111 SER LEU GLY GLN ARG ALA THR MET SER CYS ARG ALA GLY SEQRES 3 A 111 GLU SER VAL ASP ILE PHE GLY VAL GLY PHE LEU HIS TRP SEQRES 4 A 111 TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE SEQRES 5 A 111 TYR ARG ALA SER ASN LEU GLU SER GLY ILE PRO VAL ARG SEQRES 6 A 111 PHE SER GLY THR GLY SER ARG THR ASP PHE THR LEU ILE SEQRES 7 A 111 ILE ASP PRO VAL GLU ALA ASP ASP VAL ALA THR TYR TYR SEQRES 8 A 111 CYS GLN GLN THR ASN GLU ASP PRO TYR THR PHE GLY GLY SEQRES 9 A 111 GLY THR LYS LEU GLU ILE LYS SEQRES 1 B 121 GLU VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL GLU SEQRES 2 B 121 PRO GLY ALA SER VAL LYS LEU SER CYS THR ALA SER GLY SEQRES 3 B 121 PHE ASN ILE LYS ASP THR TYR MET HIS TRP VAL LYS GLN SEQRES 4 B 121 ARG PRO GLU GLN GLY LEU GLU TRP ILE GLY ARG ILE ASP SEQRES 5 B 121 PRO ALA ASN GLY ASN SER LYS TYR VAL PRO LYS PHE GLN SEQRES 6 B 121 GLY LYS ALA THR ILE THR ALA ASP THR SER SER ASN THR SEQRES 7 B 121 ALA TYR LEU GLN LEU THR SER LEU THR SER GLU ASP THR SEQRES 8 B 121 ALA VAL TYR TYR CYS ALA PRO PHE GLY TYR TYR VAL SER SEQRES 9 B 121 ASP TYR ALA MET ALA TYR TRP GLY GLN GLY THR SER VAL SEQRES 10 B 121 THR VAL SER SER HET PO4 501 5 HET PO4 502 5 HET GOL 1201 6 HET GOL 1202 6 HETNAM PO4 PHOSPHATE ION HETNAM GOL GLYCEROL FORMUL 5 PO4 2(O4 P 3-) FORMUL 7 GOL 2(C3 H8 O3) FORMUL 9 HOH *256(H2 O) HELIX 1 1 GLU L 79 VAL L 83 5 5 HELIX 2 2 ASN H 28 THR H 32 5 5 HELIX 3 3 PRO H 61 GLN H 64 5 4 HELIX 4 4 THR H 73 SER H 75 5 3 HELIX 5 5 THR H 83 THR H 87 5 5 HELIX 6 6 GLU A 79 VAL A 83 5 5 HELIX 7 7 ASN B 28 THR B 32 5 5 HELIX 8 8 PRO B 61 GLN B 64 5 4 HELIX 9 9 THR B 73 SER B 75 5 3 HELIX 10 10 THR B 83 THR B 87 5 5 SHEET 1 A 4 LEU L 4 SER L 7 0 SHEET 2 A 4 ALA L 19 ALA 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 SER L 67 -1 N SER L 63 O ILE L 74 SHEET 1 B 5 ASN L 53 LEU L 54 0 SHEET 2 B 5 PRO L 44 TYR L 49 -1 N TYR L 49 O ASN L 53 SHEET 3 B 5 LEU L 33 GLN L 38 -1 N GLN L 37 O LYS L 45 SHEET 4 B 5 ALA L 84 GLN L 90 -1 O THR 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 ASN L 53 LEU L 54 0 SHEET 2 C 6 PRO L 44 TYR L 49 -1 N TYR L 49 O ASN L 53 SHEET 3 C 6 LEU L 33 GLN L 38 -1 N GLN L 37 O LYS L 45 SHEET 4 C 6 ALA L 84 GLN L 90 -1 O THR L 85 N GLN L 38 SHEET 5 C 6 THR L 102 ILE L 106 -1 O LEU L 104 N ALA L 84 SHEET 6 C 6 SER L 10 VAL L 13 1 N LEU L 11 O LYS L 103 SHEET 1 D 2 VAL L 30 GLY L 31 0 SHEET 1 E 4 GLN H 3 GLN H 6 0 SHEET 2 E 4 VAL H 18 SER H 25 -1 O THR H 23 N GLN H 5 SHEET 3 E 4 THR H 77 LEU H 82 -1 O LEU H 80 N LEU H 20 SHEET 4 E 4 ALA H 67 ASP H 72 -1 N THR H 70 O TYR H 79 SHEET 1 F 6 GLU H 10 VAL H 12 0 SHEET 2 F 6 THR H 107 VAL H 111 1 O SER H 108 N GLU H 10 SHEET 3 F 6 ALA H 88 PHE H 95 -1 N ALA H 88 O VAL H 109 SHEET 4 F 6 TYR H 33 GLN H 39 -1 N VAL H 37 O TYR H 91 SHEET 5 F 6 LEU H 45 ILE H 51 -1 O ILE H 51 N MET H 34 SHEET 6 F 6 SER H 57 TYR H 59 -1 O LYS H 58 N ARG H 50 SHEET 1 G 4 LEU A 4 SER A 7 0 SHEET 2 G 4 ALA A 19 ALA A 25 -1 O ARG A 24 N THR A 5 SHEET 3 G 4 ASP A 70 ILE A 75 -1 O LEU A 73 N MET A 21 SHEET 4 G 4 PHE A 62 THR A 65 -1 N SER A 63 O ILE A 74 SHEET 1 H 5 ASN A 53 LEU A 54 0 SHEET 2 H 5 LYS A 45 TYR A 49 -1 N TYR A 49 O ASN A 53 SHEET 3 H 5 LEU A 33 GLN A 38 -1 N TRP A 35 O LEU A 47 SHEET 4 H 5 ALA A 84 GLN A 90 -1 O GLN A 89 N HIS A 34 SHEET 5 H 5 THR A 97 PHE A 98 -1 O THR A 97 N GLN A 90 SHEET 1 I 6 ASN A 53 LEU A 54 0 SHEET 2 I 6 LYS A 45 TYR A 49 -1 N TYR A 49 O ASN A 53 SHEET 3 I 6 LEU A 33 GLN A 38 -1 N TRP A 35 O LEU A 47 SHEET 4 I 6 ALA A 84 GLN A 90 -1 O GLN A 89 N HIS A 34 SHEET 5 I 6 THR A 102 ILE A 106 -1 O LEU A 104 N ALA A 84 SHEET 6 I 6 SER A 10 VAL A 13 1 N LEU A 11 O GLU A 105 SHEET 1 J 4 GLN B 3 GLN B 6 0 SHEET 2 J 4 VAL B 18 SER B 25 -1 O THR B 23 N GLN B 5 SHEET 3 J 4 THR B 77 LEU B 82 -1 O LEU B 80 N LEU B 20 SHEET 4 J 4 ALA B 67 ASP B 72 -1 N ASP B 72 O THR B 77 SHEET 1 K 6 GLU B 10 VAL B 12 0 SHEET 2 K 6 THR B 107 VAL B 111 1 O THR B 110 N GLU B 10 SHEET 3 K 6 ALA B 88 PHE B 95 -1 N ALA B 88 O VAL B 109 SHEET 4 K 6 TYR B 33 GLN B 39 -1 N TYR B 33 O PHE B 95 SHEET 5 K 6 GLU B 46 ILE B 51 -1 O GLU B 46 N LYS B 38 SHEET 6 K 6 SER B 57 TYR B 59 -1 O LYS B 58 N ARG B 50 SSBOND 1 CYS L 23 CYS L 88 SSBOND 2 CYS H 22 CYS H 92 SSBOND 3 CYS A 23 CYS A 88 SSBOND 4 CYS B 22 CYS B 92 CISPEP 1 SER L 7 PRO L 8 0 -0.36 CISPEP 2 ASP L 76 PRO L 77 0 1.06 CISPEP 3 ASP L 94 PRO L 95 0 -1.65 CISPEP 4 SER A 7 PRO A 8 0 -9.58 CISPEP 5 ASP A 76 PRO A 77 0 6.46 CISPEP 6 ASP A 94 PRO A 95 0 -8.81 CRYST1 61.774 75.033 63.105 90.00 94.82 90.00 P 1 21 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 0.016188 0.000000 0.001365 0.00000 SCALE2 0.000000 0.013327 0.000000 0.00000 SCALE3 0.000000 0.000000 0.015903 0.00000