HEADER DNA BINDING PROTEIN 02-DEC-25 9TGO TITLE CRYO-EM STRUCTURE OF Z22 MAB IN COMPLEX WITH LEFT-HANDED Z-DNA (DIMER TITLE 2 OF TRIMER) COMPND MOL_ID: 1; COMPND 2 MOLECULE: Z22-VH; COMPND 3 CHAIN: A, C, D, I, K, L; COMPND 4 ENGINEERED: YES; COMPND 5 OTHER_DETAILS: HEAVY CHAIN OF Z22; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: Z22-VL; COMPND 8 CHAIN: B, E, F, J, M, N; COMPND 9 ENGINEERED: YES; COMPND 10 OTHER_DETAILS: LIGHT CHAIN OF Z22; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: DNA (5'-D(P*CP*GP*CP*GP*CP*GP*CP*GP*CP*GP*CP*G)-3'); COMPND 13 CHAIN: O, P, S, T; COMPND 14 ENGINEERED: YES; COMPND 15 OTHER_DETAILS: DNA CHEMICALLY SYNTHESISED FROM IDT SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 EXPRESSION_SYSTEM_CELL_LINE: HYBRIDOMA Z22; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 9 ORGANISM_TAXID: 10090; SOURCE 10 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM_CELL_LINE: HYBRIDOMA Z22; SOURCE 13 MOL_ID: 3; SOURCE 14 SYNTHETIC: YES; SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 16 ORGANISM_TAXID: 9606 KEYWDS Z-DNA, MONOCLONAL ANTIBODY, ANTIBODY AVIDITY, LEFT-HANDED GEOMETRY, KEYWDS 2 DNA BINDING PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR D.H.R.CHIN,Y.B.LUO,D.LUO REVDAT 1 14-JAN-26 9TGO 0 JRNL AUTH D.CHIN,Y.LUO,Y.LAU,N.DUTTA,Z.HE,C.YIN,R.M.WILLIAMS, JRNL AUTH 2 S.BALACHANDRAN,Q.VICENS,P.DROGE,D.LUO JRNL TITL CRYO-EM STRUCTURES OF ANTI Z-DNA ANTIBODIES IN COMPLEX WITH JRNL TITL 2 ANTIGEN REVEAL DISTINCT RECOGNITION MODES OF A LEFT-HANDED JRNL TITL 3 GEOMETRY. JRNL REF BIORXIV 2025 JRNL REFN ISSN 2692-8205 JRNL PMID 41415447 JRNL DOI 10.64898/2025.12.12.693871 REMARK 2 REMARK 2 RESOLUTION. 2.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, PHENIX, SERIALEM, CRYOSPARC, REMARK 3 CRYOSPARC REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 2.800 REMARK 3 NUMBER OF PARTICLES : 59879 REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE REMARK 3 CORRECTION REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 9TGO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-DEC-25. REMARK 100 THE DEPOSITION ID IS D_1292152686. REMARK 245 REMARK 245 EXPERIMENTAL DETAILS REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE REMARK 245 SPECIMEN TYPE : NULL REMARK 245 REMARK 245 ELECTRON MICROSCOPE SAMPLE REMARK 245 SAMPLE TYPE : PARTICLE REMARK 245 PARTICLE TYPE : POINT REMARK 245 NAME OF SAMPLE : DIMER OF TRIMER COMPLEX OF Z22 REMARK 245 ANTIBODY WITH LEFT-HANDED Z-DNA REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 1.10 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.20 REMARK 245 SAMPLE DETAILS : FULL LENGTH ANTIBODY ARRANGED REMARK 245 AS A DIMER OF TRIMER AROUND THE Z-DNA REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 4660 REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS KRIOS REMARK 245 DETECTOR TYPE : FEI FALCON IV (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 500.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2230.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : 2.70 REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5000.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : 165000 REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 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 AUTHOR DETERMINED BIOLOGICAL UNIT: 16-MERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 16-MERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, E, O, P, D, F, I, J, REMARK 350 AND CHAINS: K, M, S, T, L, N 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 DC S 11 C5 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 PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 DC S 11 C6 - N1 - C2 ANGL. DEV. = 3.7 DEGREES REMARK 500 DC S 11 N1 - C2 - N3 ANGL. DEV. = 4.6 DEGREES REMARK 500 DC S 11 C2 - N3 - C4 ANGL. DEV. = 5.0 DEGREES REMARK 500 REMARK 500 REMARK: NULL 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 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 MET A 66 56.38 -90.99 REMARK 500 THR B 51 -8.96 67.29 REMARK 500 SER B 52 -37.10 -132.83 REMARK 500 THR E 51 -10.08 69.96 REMARK 500 SER E 67 146.47 -171.43 REMARK 500 ALA D 94 -169.11 -161.50 REMARK 500 THR F 51 -9.92 70.41 REMARK 500 SER F 52 -36.34 -132.57 REMARK 500 VAL I 48 -64.19 -91.12 REMARK 500 THR J 7 -91.85 46.98 REMARK 500 THR J 51 -78.92 52.08 REMARK 500 GLN J 89 139.71 -170.20 REMARK 500 SER M 26 -61.18 -92.80 REMARK 500 THR M 51 -8.30 67.73 REMARK 500 SER M 52 30.56 -145.05 REMARK 500 THR N 51 -7.04 67.06 REMARK 500 SER N 52 -31.03 -134.03 REMARK 500 PRO N 80 0.47 -69.66 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-55906 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF Z22 MAB IN COMPLEX WITH LEFT-HANDED Z-DNA REMARK 900 (DIMER OF TRIMER) DBREF 9TGO A 1 121 PDB 9TGO 9TGO 1 121 DBREF 9TGO B 1 106 PDB 9TGO 9TGO 1 106 DBREF 9TGO C 1 121 PDB 9TGO 9TGO 1 121 DBREF 9TGO E 1 106 PDB 9TGO 9TGO 1 106 DBREF 9TGO O 1 12 PDB 9TGO 9TGO 1 12 DBREF 9TGO P 1 12 PDB 9TGO 9TGO 1 12 DBREF 9TGO D 1 121 PDB 9TGO 9TGO 1 121 DBREF 9TGO F 1 106 PDB 9TGO 9TGO 1 106 DBREF 9TGO I 1 121 PDB 9TGO 9TGO 1 121 DBREF 9TGO J 1 106 PDB 9TGO 9TGO 1 106 DBREF 9TGO K 1 121 PDB 9TGO 9TGO 1 121 DBREF 9TGO M 1 106 PDB 9TGO 9TGO 1 106 DBREF 9TGO S 1 12 PDB 9TGO 9TGO 1 12 DBREF 9TGO T 1 12 PDB 9TGO 9TGO 1 12 DBREF 9TGO L 1 121 PDB 9TGO 9TGO 1 121 DBREF 9TGO N 1 106 PDB 9TGO 9TGO 1 106 SEQRES 1 A 121 LYS VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 A 121 PRO LYS GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 A 121 PHE ASN PHE ASN THR TYR ALA MET ASN TRP VAL ARG GLN SEQRES 4 A 121 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ARG ILE ARG SEQRES 5 A 121 SER LYS SER ASN ASN TYR ALA THR TYR TYR ALA ASP SER SEQRES 6 A 121 MET LYS ASP ARG PHE THR ILE SER ARG ASP ASP SER GLU SEQRES 7 A 121 ASN MET LEU TYR LEU GLN MET ILE ASN LEU LYS ALA GLU SEQRES 8 A 121 ASP THR ALA MET TYR TYR CYS VAL ARG GLN ALA TYR SER SEQRES 9 A 121 ASN TYR GLY ALA MET ASP TYR TRP GLY GLN GLY ILE SER SEQRES 10 A 121 VAL THR VAL SER SEQRES 1 B 106 ASP ILE GLN MET THR GLN THR ILE SER SER LEU SER ALA SEQRES 2 B 106 SER LEU GLY ASP ARG VAL THR ILE SER CYS SER ALA SER SEQRES 3 B 106 GLN GLY ILE SER ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 B 106 PRO ASP GLY THR VAL LYS LEU LEU ILE TYR TYR THR SER SEQRES 5 B 106 ARG LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 B 106 GLY SER GLY THR ASP TYR SER LEU THR ILE SER ASN LEU SEQRES 7 B 106 GLU PRO GLU ASP ILE ALA THR TYR PHE CYS GLN GLN TYR SEQRES 8 B 106 SER LYS PHE PRO PHE THR PHE GLY SER GLY THR LYS LEU SEQRES 9 B 106 GLU ILE SEQRES 1 C 121 LYS VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 C 121 PRO LYS GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 C 121 PHE ASN PHE ASN THR TYR ALA MET ASN TRP VAL ARG GLN SEQRES 4 C 121 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ARG ILE ARG SEQRES 5 C 121 SER LYS SER ASN ASN TYR ALA THR TYR TYR ALA ASP SER SEQRES 6 C 121 MET LYS ASP ARG PHE THR ILE SER ARG ASP ASP SER GLU SEQRES 7 C 121 ASN MET LEU TYR LEU GLN MET ILE ASN LEU LYS ALA GLU SEQRES 8 C 121 ASP THR ALA MET TYR TYR CYS VAL ARG GLN ALA TYR SER SEQRES 9 C 121 ASN TYR GLY ALA MET ASP TYR TRP GLY GLN GLY ILE SER SEQRES 10 C 121 VAL THR VAL SER SEQRES 1 E 106 ASP ILE GLN MET THR GLN THR ILE SER SER LEU SER ALA SEQRES 2 E 106 SER LEU GLY ASP ARG VAL THR ILE SER CYS SER ALA SER SEQRES 3 E 106 GLN GLY ILE SER ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 E 106 PRO ASP GLY THR VAL LYS LEU LEU ILE TYR TYR THR SER SEQRES 5 E 106 ARG LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 E 106 GLY SER GLY THR ASP TYR SER LEU THR ILE SER ASN LEU SEQRES 7 E 106 GLU PRO GLU ASP ILE ALA THR TYR PHE CYS GLN GLN TYR SEQRES 8 E 106 SER LYS PHE PRO PHE THR PHE GLY SER GLY THR LYS LEU SEQRES 9 E 106 GLU ILE SEQRES 1 O 12 DC DG DC DG DC DG DC DG DC DG DC DG SEQRES 1 P 12 DC DG DC DG DC DG DC DG DC DG DC DG SEQRES 1 D 121 LYS VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 D 121 PRO LYS GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 D 121 PHE ASN PHE ASN THR TYR ALA MET ASN TRP VAL ARG GLN SEQRES 4 D 121 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ARG ILE ARG SEQRES 5 D 121 SER LYS SER ASN ASN TYR ALA THR TYR TYR ALA ASP SER SEQRES 6 D 121 MET LYS ASP ARG PHE THR ILE SER ARG ASP ASP SER GLU SEQRES 7 D 121 ASN MET LEU TYR LEU GLN MET ILE ASN LEU LYS ALA GLU SEQRES 8 D 121 ASP THR ALA MET TYR TYR CYS VAL ARG GLN ALA TYR SER SEQRES 9 D 121 ASN TYR GLY ALA MET ASP TYR TRP GLY GLN GLY ILE SER SEQRES 10 D 121 VAL THR VAL SER SEQRES 1 F 106 ASP ILE GLN MET THR GLN THR ILE SER SER LEU SER ALA SEQRES 2 F 106 SER LEU GLY ASP ARG VAL THR ILE SER CYS SER ALA SER SEQRES 3 F 106 GLN GLY ILE SER ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 F 106 PRO ASP GLY THR VAL LYS LEU LEU ILE TYR TYR THR SER SEQRES 5 F 106 ARG LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 F 106 GLY SER GLY THR ASP TYR SER LEU THR ILE SER ASN LEU SEQRES 7 F 106 GLU PRO GLU ASP ILE ALA THR TYR PHE CYS GLN GLN TYR SEQRES 8 F 106 SER LYS PHE PRO PHE THR PHE GLY SER GLY THR LYS LEU SEQRES 9 F 106 GLU ILE SEQRES 1 I 121 LYS VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 I 121 PRO LYS GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 I 121 PHE ASN PHE ASN THR TYR ALA MET ASN TRP VAL ARG GLN SEQRES 4 I 121 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ARG ILE ARG SEQRES 5 I 121 SER LYS SER ASN ASN TYR ALA THR TYR TYR ALA ASP SER SEQRES 6 I 121 MET LYS ASP ARG PHE THR ILE SER ARG ASP ASP SER GLU SEQRES 7 I 121 ASN MET LEU TYR LEU GLN MET ILE ASN LEU LYS ALA GLU SEQRES 8 I 121 ASP THR ALA MET TYR TYR CYS VAL ARG GLN ALA TYR SER SEQRES 9 I 121 ASN TYR GLY ALA MET ASP TYR TRP GLY GLN GLY ILE SER SEQRES 10 I 121 VAL THR VAL SER SEQRES 1 J 106 ASP ILE GLN MET THR GLN THR ILE SER SER LEU SER ALA SEQRES 2 J 106 SER LEU GLY ASP ARG VAL THR ILE SER CYS SER ALA SER SEQRES 3 J 106 GLN GLY ILE SER ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 J 106 PRO ASP GLY THR VAL LYS LEU LEU ILE TYR TYR THR SER SEQRES 5 J 106 ARG LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 J 106 GLY SER GLY THR ASP TYR SER LEU THR ILE SER ASN LEU SEQRES 7 J 106 GLU PRO GLU ASP ILE ALA THR TYR PHE CYS GLN GLN TYR SEQRES 8 J 106 SER LYS PHE PRO PHE THR PHE GLY SER GLY THR LYS LEU SEQRES 9 J 106 GLU ILE SEQRES 1 K 121 LYS VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 K 121 PRO LYS GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 K 121 PHE ASN PHE ASN THR TYR ALA MET ASN TRP VAL ARG GLN SEQRES 4 K 121 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ARG ILE ARG SEQRES 5 K 121 SER LYS SER ASN ASN TYR ALA THR TYR TYR ALA ASP SER SEQRES 6 K 121 MET LYS ASP ARG PHE THR ILE SER ARG ASP ASP SER GLU SEQRES 7 K 121 ASN MET LEU TYR LEU GLN MET ILE ASN LEU LYS ALA GLU SEQRES 8 K 121 ASP THR ALA MET TYR TYR CYS VAL ARG GLN ALA TYR SER SEQRES 9 K 121 ASN TYR GLY ALA MET ASP TYR TRP GLY GLN GLY ILE SER SEQRES 10 K 121 VAL THR VAL SER SEQRES 1 M 106 ASP ILE GLN MET THR GLN THR ILE SER SER LEU SER ALA SEQRES 2 M 106 SER LEU GLY ASP ARG VAL THR ILE SER CYS SER ALA SER SEQRES 3 M 106 GLN GLY ILE SER ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 M 106 PRO ASP GLY THR VAL LYS LEU LEU ILE TYR TYR THR SER SEQRES 5 M 106 ARG LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 M 106 GLY SER GLY THR ASP TYR SER LEU THR ILE SER ASN LEU SEQRES 7 M 106 GLU PRO GLU ASP ILE ALA THR TYR PHE CYS GLN GLN TYR SEQRES 8 M 106 SER LYS PHE PRO PHE THR PHE GLY SER GLY THR LYS LEU SEQRES 9 M 106 GLU ILE SEQRES 1 S 12 DC DG DC DG DC DG DC DG DC DG DC DG SEQRES 1 T 12 DC DG DC DG DC DG DC DG DC DG DC DG SEQRES 1 L 121 LYS VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 L 121 PRO LYS GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 L 121 PHE ASN PHE ASN THR TYR ALA MET ASN TRP VAL ARG GLN SEQRES 4 L 121 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ARG ILE ARG SEQRES 5 L 121 SER LYS SER ASN ASN TYR ALA THR TYR TYR ALA ASP SER SEQRES 6 L 121 MET LYS ASP ARG PHE THR ILE SER ARG ASP ASP SER GLU SEQRES 7 L 121 ASN MET LEU TYR LEU GLN MET ILE ASN LEU LYS ALA GLU SEQRES 8 L 121 ASP THR ALA MET TYR TYR CYS VAL ARG GLN ALA TYR SER SEQRES 9 L 121 ASN TYR GLY ALA MET ASP TYR TRP GLY GLN GLY ILE SER SEQRES 10 L 121 VAL THR VAL SER SEQRES 1 N 106 ASP ILE GLN MET THR GLN THR ILE SER SER LEU SER ALA SEQRES 2 N 106 SER LEU GLY ASP ARG VAL THR ILE SER CYS SER ALA SER SEQRES 3 N 106 GLN GLY ILE SER ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 N 106 PRO ASP GLY THR VAL LYS LEU LEU ILE TYR TYR THR SER SEQRES 5 N 106 ARG LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 N 106 GLY SER GLY THR ASP TYR SER LEU THR ILE SER ASN LEU SEQRES 7 N 106 GLU PRO GLU ASP ILE ALA THR TYR PHE CYS GLN GLN TYR SEQRES 8 N 106 SER LYS PHE PRO PHE THR PHE GLY SER GLY THR LYS LEU SEQRES 9 N 106 GLU ILE HET MG O 101 1 HET MG O 102 1 HET MG O 103 1 HET MG O 104 1 HET MG O 105 1 HET MG O 106 1 HET MG P 101 1 HET MG P 102 1 HET MG S 101 1 HET MG S 102 1 HET MG S 103 1 HET MG S 104 1 HET MG S 105 1 HET MG T 101 1 HET MG T 102 1 HETNAM MG MAGNESIUM ION FORMUL 17 MG 15(MG 2+) FORMUL 32 HOH *32(H2 O) HELIX 1 AA1 ASN A 28 TYR A 32 5 5 HELIX 2 AA2 SER A 53 ASN A 57 5 5 HELIX 3 AA3 GLU B 79 ILE B 83 5 5 HELIX 4 AA4 ASN C 28 TYR C 32 5 5 HELIX 5 AA5 SER C 53 ASN C 57 5 5 HELIX 6 AA6 LYS C 89 THR C 93 5 5 HELIX 7 AA7 GLU E 79 ILE E 83 5 5 HELIX 8 AA8 ASN D 28 TYR D 32 5 5 HELIX 9 AA9 LYS D 89 THR D 93 5 5 HELIX 10 AB1 ASN I 28 TYR I 32 5 5 HELIX 11 AB2 SER I 53 ASN I 57 5 5 HELIX 12 AB3 LYS I 89 THR I 93 5 5 HELIX 13 AB4 GLU J 79 ILE J 83 5 5 HELIX 14 AB5 ASN K 28 TYR K 32 5 5 HELIX 15 AB6 SER K 53 ASN K 57 5 5 HELIX 16 AB7 GLU M 79 ILE M 83 5 5 HELIX 17 AB8 ASN L 28 TYR L 32 5 5 HELIX 18 AB9 SER L 53 ASN L 57 5 5 HELIX 19 AC1 LYS L 89 THR L 93 5 5 SHEET 1 AA1 4 GLN A 3 SER A 7 0 SHEET 2 AA1 4 SER A 17 SER A 25 -1 O SER A 21 N SER A 7 SHEET 3 AA1 4 MET A 80 ILE A 86 -1 O MET A 85 N LEU A 18 SHEET 4 AA1 4 PHE A 70 ASP A 75 -1 N SER A 73 O TYR A 82 SHEET 1 AA2 6 GLY A 10 VAL A 12 0 SHEET 2 AA2 6 ILE A 116 VAL A 120 1 O THR A 119 N GLY A 10 SHEET 3 AA2 6 ALA A 94 GLN A 101 -1 N TYR A 96 O ILE A 116 SHEET 4 AA2 6 MET A 34 GLN A 39 -1 N VAL A 37 O TYR A 97 SHEET 5 AA2 6 LEU A 45 ILE A 51 -1 O VAL A 48 N TRP A 36 SHEET 6 AA2 6 THR A 60 TYR A 62 -1 O TYR A 61 N ARG A 50 SHEET 1 AA3 4 GLY A 10 VAL A 12 0 SHEET 2 AA3 4 ILE A 116 VAL A 120 1 O THR A 119 N GLY A 10 SHEET 3 AA3 4 ALA A 94 GLN A 101 -1 N TYR A 96 O ILE A 116 SHEET 4 AA3 4 MET A 109 TRP A 112 -1 O TYR A 111 N ARG A 100 SHEET 1 AA4 6 SER B 10 SER B 12 0 SHEET 2 AA4 6 THR B 102 GLU B 105 1 O LYS B 103 N LEU B 11 SHEET 3 AA4 6 THR B 85 GLN B 90 -1 N TYR B 86 O THR B 102 SHEET 4 AA4 6 LEU B 33 GLN B 38 -1 N GLN B 38 O THR B 85 SHEET 5 AA4 6 VAL B 44 TYR B 49 -1 O ILE B 48 N TRP B 35 SHEET 6 AA4 6 ARG B 53 LEU B 54 -1 O ARG B 53 N TYR B 49 SHEET 1 AA5 4 SER B 10 SER B 12 0 SHEET 2 AA5 4 THR B 102 GLU B 105 1 O LYS B 103 N LEU B 11 SHEET 3 AA5 4 THR B 85 GLN B 90 -1 N TYR B 86 O THR B 102 SHEET 4 AA5 4 THR B 97 PHE B 98 -1 O THR B 97 N GLN B 90 SHEET 1 AA6 3 VAL B 19 SER B 24 0 SHEET 2 AA6 3 ASP B 70 ILE B 75 -1 O LEU B 73 N ILE B 21 SHEET 3 AA6 3 PHE B 62 SER B 67 -1 N SER B 63 O THR B 74 SHEET 1 AA7 4 GLN C 3 SER C 7 0 SHEET 2 AA7 4 SER C 17 SER C 25 -1 O ALA C 23 N VAL C 5 SHEET 3 AA7 4 MET C 80 ILE C 86 -1 O LEU C 83 N LEU C 20 SHEET 4 AA7 4 PHE C 70 ASP C 75 -1 N SER C 73 O TYR C 82 SHEET 1 AA8 6 LEU C 11 VAL C 12 0 SHEET 2 AA8 6 ILE C 116 VAL C 120 1 O THR C 119 N VAL C 12 SHEET 3 AA8 6 ALA C 94 ARG C 100 -1 N TYR C 96 O ILE C 116 SHEET 4 AA8 6 MET C 34 GLN C 39 -1 N VAL C 37 O TYR C 97 SHEET 5 AA8 6 LEU C 45 ILE C 51 -1 O VAL C 48 N TRP C 36 SHEET 6 AA8 6 THR C 60 TYR C 62 -1 O TYR C 61 N ARG C 50 SHEET 1 AA9 4 MET E 4 THR E 5 0 SHEET 2 AA9 4 VAL E 19 ALA E 25 -1 O SER E 24 N THR E 5 SHEET 3 AA9 4 ASP E 70 ILE E 75 -1 O LEU E 73 N ILE E 21 SHEET 4 AA9 4 PHE E 62 SER E 67 -1 N SER E 63 O THR E 74 SHEET 1 AB1 6 SER E 10 SER E 12 0 SHEET 2 AB1 6 THR E 102 GLU E 105 1 O GLU E 105 N LEU E 11 SHEET 3 AB1 6 THR E 85 GLN E 90 -1 N TYR E 86 O THR E 102 SHEET 4 AB1 6 LEU E 33 GLN E 38 -1 N GLN E 38 O THR E 85 SHEET 5 AB1 6 VAL E 44 TYR E 49 -1 O LEU E 47 N TRP E 35 SHEET 6 AB1 6 ARG E 53 LEU E 54 -1 O ARG E 53 N TYR E 49 SHEET 1 AB2 4 SER E 10 SER E 12 0 SHEET 2 AB2 4 THR E 102 GLU E 105 1 O GLU E 105 N LEU E 11 SHEET 3 AB2 4 THR E 85 GLN E 90 -1 N TYR E 86 O THR E 102 SHEET 4 AB2 4 THR E 97 PHE E 98 -1 O THR E 97 N GLN E 90 SHEET 1 AB3 4 GLN D 3 SER D 7 0 SHEET 2 AB3 4 SER D 17 SER D 25 -1 O ALA D 23 N VAL D 5 SHEET 3 AB3 4 MET D 80 ILE D 86 -1 O MET D 85 N LEU D 18 SHEET 4 AB3 4 PHE D 70 ASP D 75 -1 N SER D 73 O TYR D 82 SHEET 1 AB4 6 GLY D 10 VAL D 12 0 SHEET 2 AB4 6 ILE D 116 VAL D 120 1 O THR D 119 N GLY D 10 SHEET 3 AB4 6 ALA D 94 GLN D 101 -1 N TYR D 96 O ILE D 116 SHEET 4 AB4 6 MET D 34 GLN D 39 -1 N VAL D 37 O TYR D 97 SHEET 5 AB4 6 LEU D 45 ILE D 51 -1 O GLU D 46 N ARG D 38 SHEET 6 AB4 6 THR D 60 TYR D 62 -1 O TYR D 61 N ARG D 50 SHEET 1 AB5 4 GLY D 10 VAL D 12 0 SHEET 2 AB5 4 ILE D 116 VAL D 120 1 O THR D 119 N GLY D 10 SHEET 3 AB5 4 ALA D 94 GLN D 101 -1 N TYR D 96 O ILE D 116 SHEET 4 AB5 4 MET D 109 TRP D 112 -1 O TYR D 111 N ARG D 100 SHEET 1 AB6 4 MET F 4 THR F 5 0 SHEET 2 AB6 4 VAL F 19 ALA F 25 -1 O SER F 24 N THR F 5 SHEET 3 AB6 4 ASP F 70 ILE F 75 -1 O LEU F 73 N ILE F 21 SHEET 4 AB6 4 PHE F 62 SER F 67 -1 N SER F 65 O SER F 72 SHEET 1 AB7 6 SER F 10 SER F 12 0 SHEET 2 AB7 6 THR F 102 GLU F 105 1 O GLU F 105 N LEU F 11 SHEET 3 AB7 6 THR F 85 GLN F 90 -1 N TYR F 86 O THR F 102 SHEET 4 AB7 6 LEU F 33 GLN F 38 -1 N GLN F 38 O THR F 85 SHEET 5 AB7 6 VAL F 44 TYR F 49 -1 O ILE F 48 N TRP F 35 SHEET 6 AB7 6 ARG F 53 LEU F 54 -1 O ARG F 53 N TYR F 49 SHEET 1 AB8 4 SER F 10 SER F 12 0 SHEET 2 AB8 4 THR F 102 GLU F 105 1 O GLU F 105 N LEU F 11 SHEET 3 AB8 4 THR F 85 GLN F 90 -1 N TYR F 86 O THR F 102 SHEET 4 AB8 4 THR F 97 PHE F 98 -1 O THR F 97 N GLN F 90 SHEET 1 AB9 4 GLN I 3 SER I 7 0 SHEET 2 AB9 4 SER I 21 SER I 25 -1 O ALA I 23 N VAL I 5 SHEET 3 AB9 4 MET I 80 ILE I 86 -1 O LEU I 81 N CYS I 22 SHEET 4 AB9 4 SER I 17 LYS I 19 -1 N LEU I 18 O MET I 85 SHEET 1 AC1 4 GLN I 3 SER I 7 0 SHEET 2 AC1 4 SER I 21 SER I 25 -1 O ALA I 23 N VAL I 5 SHEET 3 AC1 4 MET I 80 ILE I 86 -1 O LEU I 81 N CYS I 22 SHEET 4 AC1 4 PHE I 70 ASP I 75 -1 N SER I 73 O TYR I 82 SHEET 1 AC2 6 LEU I 11 VAL I 12 0 SHEET 2 AC2 6 ILE I 116 VAL I 120 1 O THR I 119 N VAL I 12 SHEET 3 AC2 6 ALA I 94 ARG I 100 -1 N TYR I 96 O ILE I 116 SHEET 4 AC2 6 MET I 34 GLN I 39 -1 N VAL I 37 O TYR I 97 SHEET 5 AC2 6 TRP I 47 ILE I 51 -1 O VAL I 48 N TRP I 36 SHEET 6 AC2 6 THR I 60 TYR I 62 -1 O TYR I 61 N ARG I 50 SHEET 1 AC3 4 MET J 4 THR J 5 0 SHEET 2 AC3 4 VAL J 19 ALA J 25 -1 O SER J 24 N THR J 5 SHEET 3 AC3 4 ASP J 70 ILE J 75 -1 O LEU J 73 N ILE J 21 SHEET 4 AC3 4 PHE J 62 SER J 67 -1 N SER J 65 O SER J 72 SHEET 1 AC4 2 SER J 10 SER J 12 0 SHEET 2 AC4 2 LYS J 103 GLU J 105 1 O LYS J 103 N LEU J 11 SHEET 1 AC5 3 VAL J 44 TYR J 49 0 SHEET 2 AC5 3 ASN J 34 GLN J 38 -1 N TRP J 35 O ILE J 48 SHEET 3 AC5 3 THR J 85 PHE J 87 -1 O THR J 85 N GLN J 38 SHEET 1 AC6 4 GLN K 3 SER K 7 0 SHEET 2 AC6 4 SER K 17 SER K 25 -1 O SER K 25 N GLN K 3 SHEET 3 AC6 4 MET K 80 ILE K 86 -1 O MET K 85 N LEU K 18 SHEET 4 AC6 4 PHE K 70 ASP K 75 -1 N THR K 71 O GLN K 84 SHEET 1 AC7 6 GLY K 10 VAL K 12 0 SHEET 2 AC7 6 ILE K 116 VAL K 120 1 O THR K 119 N GLY K 10 SHEET 3 AC7 6 ALA K 94 GLN K 101 -1 N TYR K 96 O ILE K 116 SHEET 4 AC7 6 MET K 34 GLN K 39 -1 N VAL K 37 O TYR K 97 SHEET 5 AC7 6 LEU K 45 ILE K 51 -1 O VAL K 48 N TRP K 36 SHEET 6 AC7 6 THR K 60 TYR K 62 -1 O TYR K 61 N ARG K 50 SHEET 1 AC8 4 GLY K 10 VAL K 12 0 SHEET 2 AC8 4 ILE K 116 VAL K 120 1 O THR K 119 N GLY K 10 SHEET 3 AC8 4 ALA K 94 GLN K 101 -1 N TYR K 96 O ILE K 116 SHEET 4 AC8 4 MET K 109 TYR K 111 -1 O TYR K 111 N ARG K 100 SHEET 1 AC9 5 SER M 10 SER M 12 0 SHEET 2 AC9 5 THR M 102 GLU M 105 1 O GLU M 105 N LEU M 11 SHEET 3 AC9 5 THR M 85 PHE M 87 -1 N TYR M 86 O THR M 102 SHEET 4 AC9 5 ASN M 34 GLN M 38 -1 N GLN M 38 O THR M 85 SHEET 5 AC9 5 VAL M 44 TYR M 49 -1 O LEU M 47 N TRP M 35 SHEET 1 AD1 3 VAL M 19 CYS M 23 0 SHEET 2 AD1 3 TYR M 71 ILE M 75 -1 O ILE M 75 N VAL M 19 SHEET 3 AD1 3 PHE M 62 SER M 65 -1 N SER M 63 O THR M 74 SHEET 1 AD2 2 GLN M 89 GLN M 90 0 SHEET 2 AD2 2 THR M 97 PHE M 98 -1 O THR M 97 N GLN M 90 SHEET 1 AD3 4 GLN L 3 SER L 7 0 SHEET 2 AD3 4 SER L 17 SER L 25 -1 O SER L 25 N GLN L 3 SHEET 3 AD3 4 MET L 80 ILE L 86 -1 O LEU L 83 N LEU L 20 SHEET 4 AD3 4 PHE L 70 ASP L 75 -1 N SER L 73 O TYR L 82 SHEET 1 AD4 6 GLY L 10 VAL L 12 0 SHEET 2 AD4 6 ILE L 116 VAL L 120 1 O SER L 117 N GLY L 10 SHEET 3 AD4 6 ALA L 94 GLN L 101 -1 N ALA L 94 O VAL L 118 SHEET 4 AD4 6 MET L 34 GLN L 39 -1 N VAL L 37 O TYR L 97 SHEET 5 AD4 6 LEU L 45 ILE L 51 -1 O VAL L 48 N TRP L 36 SHEET 6 AD4 6 THR L 60 TYR L 62 -1 O TYR L 61 N ARG L 50 SHEET 1 AD5 4 GLY L 10 VAL L 12 0 SHEET 2 AD5 4 ILE L 116 VAL L 120 1 O SER L 117 N GLY L 10 SHEET 3 AD5 4 ALA L 94 GLN L 101 -1 N ALA L 94 O VAL L 118 SHEET 4 AD5 4 MET L 109 TYR L 111 -1 O TYR L 111 N ARG L 100 SHEET 1 AD6 4 MET N 4 THR N 5 0 SHEET 2 AD6 4 VAL N 19 ALA N 25 -1 O SER N 24 N THR N 5 SHEET 3 AD6 4 ASP N 70 ILE N 75 -1 O TYR N 71 N CYS N 23 SHEET 4 AD6 4 PHE N 62 SER N 67 -1 N SER N 63 O THR N 74 SHEET 1 AD7 6 SER N 10 SER N 12 0 SHEET 2 AD7 6 THR N 102 GLU N 105 1 O GLU N 105 N LEU N 11 SHEET 3 AD7 6 THR N 85 GLN N 90 -1 N TYR N 86 O THR N 102 SHEET 4 AD7 6 LEU N 33 GLN N 38 -1 N GLN N 38 O THR N 85 SHEET 5 AD7 6 VAL N 44 TYR N 49 -1 O LEU N 47 N TRP N 35 SHEET 6 AD7 6 ARG N 53 LEU N 54 -1 O ARG N 53 N TYR N 49 SHEET 1 AD8 4 SER N 10 SER N 12 0 SHEET 2 AD8 4 THR N 102 GLU N 105 1 O GLU N 105 N LEU N 11 SHEET 3 AD8 4 THR N 85 GLN N 90 -1 N TYR N 86 O THR N 102 SHEET 4 AD8 4 THR N 97 PHE N 98 -1 O THR N 97 N GLN N 90 SSBOND 1 CYS A 22 CYS A 98 1555 1555 2.04 SSBOND 2 CYS B 23 CYS B 88 1555 1555 2.04 SSBOND 3 CYS C 22 CYS C 98 1555 1555 2.04 SSBOND 4 CYS E 23 CYS E 88 1555 1555 2.03 SSBOND 5 CYS D 22 CYS D 98 1555 1555 2.04 SSBOND 6 CYS F 23 CYS F 88 1555 1555 2.04 SSBOND 7 CYS I 22 CYS I 98 1555 1555 2.04 SSBOND 8 CYS J 23 CYS J 88 1555 1555 2.03 SSBOND 9 CYS K 22 CYS K 98 1555 1555 2.03 SSBOND 10 CYS M 23 CYS M 88 1555 1555 2.03 SSBOND 11 CYS L 22 CYS L 98 1555 1555 2.04 SSBOND 12 CYS N 23 CYS N 88 1555 1555 2.03 LINK N2 DG O 6 MG MG O 102 1555 1555 2.69 LINK N2 DG O 10 MG MG O 104 1555 1555 2.90 LINK N2 DG O 12 MG MG O 106 1555 1555 2.15 LINK N2 DG S 6 MG MG S 105 1555 1555 2.42 LINK N2 DG S 10 MG MG S 102 1555 1555 2.55 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 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 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000