HEADER DNA BINDING PROTEIN 02-DEC-25 9TGN TITLE CRYO-EM STRUCTURE OF Z-DNA BINDING ANTIBODY Z-D11 IN COMPLEX WITH TITLE 2 LEFT-HANDED Z-DNA COMPND MOL_ID: 1; COMPND 2 MOLECULE: ZD11-VL; COMPND 3 CHAIN: A, C, E, G, I, K; COMPND 4 ENGINEERED: YES; COMPND 5 OTHER_DETAILS: LIGHT CHAIN OF ANTIBODY Z-D11; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: ZD11-VH; COMPND 8 CHAIN: B, D, F, H, J, L; COMPND 9 ENGINEERED: YES; COMPND 10 OTHER_DETAILS: HEAVY CHAIN OF ANTIBODY Z-D11; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: DNA (5'-D(*CP*GP*CP*GP*CP*GP*CP*GP*CP*GP*CP*G)-3'); COMPND 13 CHAIN: M, N, O, P; COMPND 14 ENGINEERED: YES; COMPND 15 OTHER_DETAILS: DNA 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: EXPI293; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PCDNA3.1; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 10 ORGANISM_TAXID: 10090; SOURCE 11 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 13 EXPRESSION_SYSTEM_CELL_LINE: EXPI293; SOURCE 14 EXPRESSION_SYSTEM_VECTOR_TYPE: PCDNA3.1; SOURCE 15 MOL_ID: 3; SOURCE 16 SYNTHETIC: YES; SOURCE 17 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 18 ORGANISM_TAXID: 9606 KEYWDS Z-DNA, MONOCLONAL ANTIBODY, LEFT-HANDED GEOMETRY, ANTIBODY AVIDITY, KEYWDS 2 DNA BINDING PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR D.H.R.CHIN,Y.B.LUO,D.LUO REVDAT 1 14-JAN-26 9TGN 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. 2.55 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) : 2.550 REMARK 3 NUMBER OF PARTICLES : 146988 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 9TGN 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_1292152677. 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 : Z-DNA BINDING ANTIBODY Z-D11 IN REMARK 245 COMPLEX WITH LEFT-HANDED Z-DNA REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.30 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 USED FOR REMARK 245 COMPLEX PREPARATION WITH 12-MER DNA: COMPLEX FORMS A DIMER OF REMARK 245 TRIMER ALONG THE Z-DNA AXIS REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 4000 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) : 1500.00 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, D, E, F, G, H, I, J, REMARK 350 AND CHAINS: K, L, M, N, O, P 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 DISTANCE REMARK 500 OG SER I 14 OD1 ASP I 17 2.19 REMARK 500 REMARK 500 REMARK: NULL 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),1X,F6.3) 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 RES CSSEQI ATM2 DEVIATION REMARK 500 PRO D 41 CG PRO D 41 CD -0.302 REMARK 500 REMARK 500 REMARK: NULL 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 PRO D 41 CA - CB - CG ANGL. DEV. = -23.7 DEGREES REMARK 500 PRO D 41 N - CD - CG ANGL. DEV. = -20.9 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 LEU A 11 115.42 -161.89 REMARK 500 SER A 30 -114.86 55.31 REMARK 500 LEU A 47 -60.02 -100.23 REMARK 500 THR A 51 -6.11 59.89 REMARK 500 SER A 52 -23.50 -140.30 REMARK 500 SER A 67 147.71 -172.19 REMARK 500 ASN B 30 -2.99 -144.40 REMARK 500 SER C 30 -117.10 62.72 REMARK 500 THR C 51 -19.96 74.46 REMARK 500 ALA C 84 -168.41 -161.42 REMARK 500 SER E 30 -118.60 58.88 REMARK 500 THR E 51 -15.58 73.96 REMARK 500 SER E 52 -3.54 -144.43 REMARK 500 ASP F 68 -2.83 72.67 REMARK 500 SER G 30 -117.47 61.65 REMARK 500 THR G 51 -17.01 73.56 REMARK 500 ALA G 84 -169.42 -160.44 REMARK 500 ASP H 92 49.82 -88.72 REMARK 500 SER I 30 -111.68 55.34 REMARK 500 THR I 51 -16.74 74.53 REMARK 500 SER I 67 149.29 -174.04 REMARK 500 ALA I 84 -168.50 -161.08 REMARK 500 ASP J 68 -3.04 70.97 REMARK 500 ASP J 92 47.56 -86.95 REMARK 500 SER K 30 -112.79 52.75 REMARK 500 THR K 51 -13.07 72.46 REMARK 500 GLU K 81 44.79 -81.56 REMARK 500 LYS L 89 -74.36 -97.11 REMARK 500 THR L 90 -26.63 -146.35 REMARK 500 SER L 121 141.39 -172.90 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-55905 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF Z-DNA BINDING ANTIBODY Z-D11 IN COMPLEX WITH REMARK 900 LEFT-HANDED Z-DNA DBREF 9TGN A 1 109 PDB 9TGN 9TGN 1 109 DBREF 9TGN B 1 123 PDB 9TGN 9TGN 1 123 DBREF 9TGN C 1 109 PDB 9TGN 9TGN 1 109 DBREF 9TGN D 1 123 PDB 9TGN 9TGN 1 123 DBREF 9TGN E 1 109 PDB 9TGN 9TGN 1 109 DBREF 9TGN F 1 123 PDB 9TGN 9TGN 1 123 DBREF 9TGN G 1 109 PDB 9TGN 9TGN 1 109 DBREF 9TGN H 1 123 PDB 9TGN 9TGN 1 123 DBREF 9TGN I 1 109 PDB 9TGN 9TGN 1 109 DBREF 9TGN J 1 123 PDB 9TGN 9TGN 1 123 DBREF 9TGN K 1 109 PDB 9TGN 9TGN 1 109 DBREF 9TGN L 1 123 PDB 9TGN 9TGN 1 123 DBREF 9TGN M 1 12 PDB 9TGN 9TGN 1 12 DBREF 9TGN N 1 12 PDB 9TGN 9TGN 1 12 DBREF 9TGN O 1 12 PDB 9TGN 9TGN 1 12 DBREF 9TGN P 1 12 PDB 9TGN 9TGN 1 12 SEQRES 1 A 109 ASP ILE GLN MET THR GLN THR THR SER SER LEU SER ALA SEQRES 2 A 109 SER LEU GLY ASP ARG VAL THR ILE ASN CYS ARG ALA SER SEQRES 3 A 109 GLN ASP ILE SER ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 A 109 PRO ASP GLY THR VAL LYS LEU LEU ILE TYR TYR THR SER SEQRES 5 A 109 ARG LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 A 109 GLY SER GLY THR ASP PHE SER LEU THR ILE SER TYR LEU SEQRES 7 A 109 GLU GLN GLU ASP ILE ALA THR TYR PHE CYS GLN GLN GLY SEQRES 8 A 109 LYS THR LEU PRO PHE THR PHE GLY ALA GLY THR LYS LEU SEQRES 9 A 109 GLU LEU LYS ARG ALA SEQRES 1 B 123 GLU VAL GLN LEU VAL GLU THR GLY GLY GLY LEU VAL GLN SEQRES 2 B 123 PRO LYS GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 B 123 PHE THR PHE ASN THR ASN ALA MET ASN TRP VAL ARG GLN SEQRES 4 B 123 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ARG ILE ARG SEQRES 5 B 123 SER LYS SER ASN ASN TYR ALA THR TYR TYR ALA ASP SER SEQRES 6 B 123 VAL LYS ASP ARG PHE THR ILE SER ARG ASP ASP SER GLN SEQRES 7 B 123 SER MET LEU TYR LEU GLN MET ASN ASN LEU LYS THR GLU SEQRES 8 B 123 ASP THR ALA MET TYR TYR CYS VAL ARG GLY TYR VAL ASN SEQRES 9 B 123 TYR TYR TYR VAL MET ASP TYR TRP GLY GLN GLY THR SER SEQRES 10 B 123 VAL THR VAL SER SER ALA SEQRES 1 C 109 ASP ILE GLN MET THR GLN THR THR SER SER LEU SER ALA SEQRES 2 C 109 SER LEU GLY ASP ARG VAL THR ILE ASN CYS ARG ALA SER SEQRES 3 C 109 GLN ASP ILE SER ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 C 109 PRO ASP GLY THR VAL LYS LEU LEU ILE TYR TYR THR SER SEQRES 5 C 109 ARG LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 C 109 GLY SER GLY THR ASP PHE SER LEU THR ILE SER TYR LEU SEQRES 7 C 109 GLU GLN GLU ASP ILE ALA THR TYR PHE CYS GLN GLN GLY SEQRES 8 C 109 LYS THR LEU PRO PHE THR PHE GLY ALA GLY THR LYS LEU SEQRES 9 C 109 GLU LEU LYS ARG ALA SEQRES 1 D 123 GLU VAL GLN LEU VAL GLU THR GLY GLY GLY LEU VAL GLN SEQRES 2 D 123 PRO LYS GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 D 123 PHE THR PHE ASN THR ASN ALA MET ASN TRP VAL ARG GLN SEQRES 4 D 123 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ARG ILE ARG SEQRES 5 D 123 SER LYS SER ASN ASN TYR ALA THR TYR TYR ALA ASP SER SEQRES 6 D 123 VAL LYS ASP ARG PHE THR ILE SER ARG ASP ASP SER GLN SEQRES 7 D 123 SER MET LEU TYR LEU GLN MET ASN ASN LEU LYS THR GLU SEQRES 8 D 123 ASP THR ALA MET TYR TYR CYS VAL ARG GLY TYR VAL ASN SEQRES 9 D 123 TYR TYR TYR VAL MET ASP TYR TRP GLY GLN GLY THR SER SEQRES 10 D 123 VAL THR VAL SER SER ALA SEQRES 1 E 109 ASP ILE GLN MET THR GLN THR THR SER SER LEU SER ALA SEQRES 2 E 109 SER LEU GLY ASP ARG VAL THR ILE ASN CYS ARG ALA SER SEQRES 3 E 109 GLN ASP ILE SER ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 E 109 PRO ASP GLY THR VAL LYS LEU LEU ILE TYR TYR THR SER SEQRES 5 E 109 ARG LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 E 109 GLY SER GLY THR ASP PHE SER LEU THR ILE SER TYR LEU SEQRES 7 E 109 GLU GLN GLU ASP ILE ALA THR TYR PHE CYS GLN GLN GLY SEQRES 8 E 109 LYS THR LEU PRO PHE THR PHE GLY ALA GLY THR LYS LEU SEQRES 9 E 109 GLU LEU LYS ARG ALA SEQRES 1 F 123 GLU VAL GLN LEU VAL GLU THR GLY GLY GLY LEU VAL GLN SEQRES 2 F 123 PRO LYS GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 F 123 PHE THR PHE ASN THR ASN ALA MET ASN TRP VAL ARG GLN SEQRES 4 F 123 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ARG ILE ARG SEQRES 5 F 123 SER LYS SER ASN ASN TYR ALA THR TYR TYR ALA ASP SER SEQRES 6 F 123 VAL LYS ASP ARG PHE THR ILE SER ARG ASP ASP SER GLN SEQRES 7 F 123 SER MET LEU TYR LEU GLN MET ASN ASN LEU LYS THR GLU SEQRES 8 F 123 ASP THR ALA MET TYR TYR CYS VAL ARG GLY TYR VAL ASN SEQRES 9 F 123 TYR TYR TYR VAL MET ASP TYR TRP GLY GLN GLY THR SER SEQRES 10 F 123 VAL THR VAL SER SER ALA SEQRES 1 G 109 ASP ILE GLN MET THR GLN THR THR SER SER LEU SER ALA SEQRES 2 G 109 SER LEU GLY ASP ARG VAL THR ILE ASN CYS ARG ALA SER SEQRES 3 G 109 GLN ASP ILE SER ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 G 109 PRO ASP GLY THR VAL LYS LEU LEU ILE TYR TYR THR SER SEQRES 5 G 109 ARG LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 G 109 GLY SER GLY THR ASP PHE SER LEU THR ILE SER TYR LEU SEQRES 7 G 109 GLU GLN GLU ASP ILE ALA THR TYR PHE CYS GLN GLN GLY SEQRES 8 G 109 LYS THR LEU PRO PHE THR PHE GLY ALA GLY THR LYS LEU SEQRES 9 G 109 GLU LEU LYS ARG ALA SEQRES 1 H 123 GLU VAL GLN LEU VAL GLU THR GLY GLY GLY LEU VAL GLN SEQRES 2 H 123 PRO LYS GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 H 123 PHE THR PHE ASN THR ASN ALA MET ASN TRP VAL ARG GLN SEQRES 4 H 123 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ARG ILE ARG SEQRES 5 H 123 SER LYS SER ASN ASN TYR ALA THR TYR TYR ALA ASP SER SEQRES 6 H 123 VAL LYS ASP ARG PHE THR ILE SER ARG ASP ASP SER GLN SEQRES 7 H 123 SER MET LEU TYR LEU GLN MET ASN ASN LEU LYS THR GLU SEQRES 8 H 123 ASP THR ALA MET TYR TYR CYS VAL ARG GLY TYR VAL ASN SEQRES 9 H 123 TYR TYR TYR VAL MET ASP TYR TRP GLY GLN GLY THR SER SEQRES 10 H 123 VAL THR VAL SER SER ALA SEQRES 1 I 109 ASP ILE GLN MET THR GLN THR THR SER SER LEU SER ALA SEQRES 2 I 109 SER LEU GLY ASP ARG VAL THR ILE ASN CYS ARG ALA SER SEQRES 3 I 109 GLN ASP ILE SER ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 I 109 PRO ASP GLY THR VAL LYS LEU LEU ILE TYR TYR THR SER SEQRES 5 I 109 ARG LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 I 109 GLY SER GLY THR ASP PHE SER LEU THR ILE SER TYR LEU SEQRES 7 I 109 GLU GLN GLU ASP ILE ALA THR TYR PHE CYS GLN GLN GLY SEQRES 8 I 109 LYS THR LEU PRO PHE THR PHE GLY ALA GLY THR LYS LEU SEQRES 9 I 109 GLU LEU LYS ARG ALA SEQRES 1 J 123 GLU VAL GLN LEU VAL GLU THR GLY GLY GLY LEU VAL GLN SEQRES 2 J 123 PRO LYS GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 J 123 PHE THR PHE ASN THR ASN ALA MET ASN TRP VAL ARG GLN SEQRES 4 J 123 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ARG ILE ARG SEQRES 5 J 123 SER LYS SER ASN ASN TYR ALA THR TYR TYR ALA ASP SER SEQRES 6 J 123 VAL LYS ASP ARG PHE THR ILE SER ARG ASP ASP SER GLN SEQRES 7 J 123 SER MET LEU TYR LEU GLN MET ASN ASN LEU LYS THR GLU SEQRES 8 J 123 ASP THR ALA MET TYR TYR CYS VAL ARG GLY TYR VAL ASN SEQRES 9 J 123 TYR TYR TYR VAL MET ASP TYR TRP GLY GLN GLY THR SER SEQRES 10 J 123 VAL THR VAL SER SER ALA SEQRES 1 K 109 ASP ILE GLN MET THR GLN THR THR SER SER LEU SER ALA SEQRES 2 K 109 SER LEU GLY ASP ARG VAL THR ILE ASN CYS ARG ALA SER SEQRES 3 K 109 GLN ASP ILE SER ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 K 109 PRO ASP GLY THR VAL LYS LEU LEU ILE TYR TYR THR SER SEQRES 5 K 109 ARG LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 K 109 GLY SER GLY THR ASP PHE SER LEU THR ILE SER TYR LEU SEQRES 7 K 109 GLU GLN GLU ASP ILE ALA THR TYR PHE CYS GLN GLN GLY SEQRES 8 K 109 LYS THR LEU PRO PHE THR PHE GLY ALA GLY THR LYS LEU SEQRES 9 K 109 GLU LEU LYS ARG ALA SEQRES 1 L 123 GLU VAL GLN LEU VAL GLU THR GLY GLY GLY LEU VAL GLN SEQRES 2 L 123 PRO LYS GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 L 123 PHE THR PHE ASN THR ASN ALA MET ASN TRP VAL ARG GLN SEQRES 4 L 123 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ARG ILE ARG SEQRES 5 L 123 SER LYS SER ASN ASN TYR ALA THR TYR TYR ALA ASP SER SEQRES 6 L 123 VAL LYS ASP ARG PHE THR ILE SER ARG ASP ASP SER GLN SEQRES 7 L 123 SER MET LEU TYR LEU GLN MET ASN ASN LEU LYS THR GLU SEQRES 8 L 123 ASP THR ALA MET TYR TYR CYS VAL ARG GLY TYR VAL ASN SEQRES 9 L 123 TYR TYR TYR VAL MET ASP TYR TRP GLY GLN GLY THR SER SEQRES 10 L 123 VAL THR VAL SER SER ALA SEQRES 1 M 12 DC DG DC DG DC DG DC DG DC DG DC DG SEQRES 1 N 12 DC DG DC DG DC DG DC DG DC DG DC DG 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 HET MG M 101 1 HET MG M 102 1 HET MG M 103 1 HET MG N 101 1 HET MG O 101 1 HET MG O 102 1 HET MG P 101 1 HET MG P 102 1 HETNAM MG MAGNESIUM ION FORMUL 17 MG 8(MG 2+) FORMUL 25 HOH *22(H2 O) HELIX 1 AA1 GLU A 79 ILE A 83 5 5 HELIX 2 AA2 SER B 53 ASN B 57 5 5 HELIX 3 AA3 LYS B 89 THR B 93 5 5 HELIX 4 AA4 GLU C 79 ILE C 83 5 5 HELIX 5 AA5 THR D 28 ASN D 32 5 5 HELIX 6 AA6 SER D 53 ASN D 57 5 5 HELIX 7 AA7 LYS D 89 THR D 93 5 5 HELIX 8 AA8 GLU E 79 ILE E 83 5 5 HELIX 9 AA9 THR F 28 ASN F 32 5 5 HELIX 10 AB1 LYS F 89 THR F 93 5 5 HELIX 11 AB2 GLU G 79 ILE G 83 5 5 HELIX 12 AB3 THR H 28 ASN H 32 5 5 HELIX 13 AB4 SER H 53 ASN H 57 5 5 HELIX 14 AB5 GLU I 79 ILE I 83 5 5 HELIX 15 AB6 THR J 28 ASN J 32 5 5 HELIX 16 AB7 SER J 53 ASN J 57 5 5 HELIX 17 AB8 GLU K 79 ILE K 83 5 5 HELIX 18 AB9 THR L 28 ASN L 32 5 5 HELIX 19 AC1 SER L 53 ASN L 57 5 5 SHEET 1 AA1 4 MET A 4 THR A 5 0 SHEET 2 AA1 4 VAL A 19 ALA A 25 -1 O ARG A 24 N THR A 5 SHEET 3 AA1 4 ASP A 70 ILE A 75 -1 O LEU A 73 N ILE A 21 SHEET 4 AA1 4 PHE A 62 SER A 67 -1 N SER A 65 O SER A 72 SHEET 1 AA2 6 SER A 10 ALA A 13 0 SHEET 2 AA2 6 THR A 102 LEU A 106 1 O GLU A 105 N ALA A 13 SHEET 3 AA2 6 THR A 85 GLN A 90 -1 N TYR A 86 O THR A 102 SHEET 4 AA2 6 LEU A 33 GLN A 38 -1 N GLN A 38 O THR A 85 SHEET 5 AA2 6 VAL A 44 TYR A 49 -1 O ILE A 48 N TRP A 35 SHEET 6 AA2 6 ARG A 53 LEU A 54 -1 O ARG A 53 N TYR A 49 SHEET 1 AA3 4 SER A 10 ALA A 13 0 SHEET 2 AA3 4 THR A 102 LEU A 106 1 O GLU A 105 N ALA A 13 SHEET 3 AA3 4 THR A 85 GLN A 90 -1 N TYR A 86 O THR A 102 SHEET 4 AA3 4 THR A 97 PHE A 98 -1 O THR A 97 N GLN A 90 SHEET 1 AA4 4 GLN B 3 THR B 7 0 SHEET 2 AA4 4 SER B 17 SER B 25 -1 O SER B 21 N THR B 7 SHEET 3 AA4 4 MET B 80 ASN B 86 -1 O MET B 85 N LEU B 18 SHEET 4 AA4 4 PHE B 70 ASP B 75 -1 N SER B 73 O TYR B 82 SHEET 1 AA5 6 LEU B 11 VAL B 12 0 SHEET 2 AA5 6 THR B 116 VAL B 120 1 O THR B 119 N VAL B 12 SHEET 3 AA5 6 ALA B 94 GLY B 101 -1 N TYR B 96 O THR B 116 SHEET 4 AA5 6 MET B 34 GLN B 39 -1 N VAL B 37 O TYR B 97 SHEET 5 AA5 6 LEU B 45 ILE B 51 -1 O ILE B 51 N MET B 34 SHEET 6 AA5 6 THR B 60 TYR B 62 -1 O TYR B 61 N ARG B 50 SHEET 1 AA6 4 LEU B 11 VAL B 12 0 SHEET 2 AA6 4 THR B 116 VAL B 120 1 O THR B 119 N VAL B 12 SHEET 3 AA6 4 ALA B 94 GLY B 101 -1 N TYR B 96 O THR B 116 SHEET 4 AA6 4 MET B 109 TRP B 112 -1 O TYR B 111 N ARG B 100 SHEET 1 AA7 4 MET C 4 THR C 5 0 SHEET 2 AA7 4 VAL C 19 ALA C 25 -1 O ARG C 24 N THR C 5 SHEET 3 AA7 4 ASP C 70 ILE C 75 -1 O PHE C 71 N CYS C 23 SHEET 4 AA7 4 PHE C 62 SER C 67 -1 N SER C 63 O THR C 74 SHEET 1 AA8 6 SER C 10 ALA C 13 0 SHEET 2 AA8 6 THR C 102 LEU C 106 1 O LYS C 103 N LEU C 11 SHEET 3 AA8 6 THR C 85 GLN C 90 -1 N TYR C 86 O THR C 102 SHEET 4 AA8 6 LEU C 33 GLN C 38 -1 N GLN C 38 O THR C 85 SHEET 5 AA8 6 VAL C 44 TYR C 49 -1 O ILE C 48 N TRP C 35 SHEET 6 AA8 6 ARG C 53 LEU C 54 -1 O ARG C 53 N TYR C 49 SHEET 1 AA9 4 SER C 10 ALA C 13 0 SHEET 2 AA9 4 THR C 102 LEU C 106 1 O LYS C 103 N LEU C 11 SHEET 3 AA9 4 THR C 85 GLN C 90 -1 N TYR C 86 O THR C 102 SHEET 4 AA9 4 THR C 97 PHE C 98 -1 O THR C 97 N GLN C 90 SHEET 1 AB1 4 GLN D 3 THR D 7 0 SHEET 2 AB1 4 SER D 17 SER D 25 -1 O ALA D 23 N VAL D 5 SHEET 3 AB1 4 MET D 80 ASN D 86 -1 O MET D 85 N LEU D 18 SHEET 4 AB1 4 PHE D 70 ASP D 75 -1 N SER D 73 O TYR D 82 SHEET 1 AB2 6 LEU D 11 VAL D 12 0 SHEET 2 AB2 6 THR D 116 VAL D 120 1 O THR D 119 N VAL D 12 SHEET 3 AB2 6 ALA D 94 GLY D 101 -1 N ALA D 94 O VAL D 118 SHEET 4 AB2 6 MET D 34 GLN D 39 -1 N VAL D 37 O TYR D 97 SHEET 5 AB2 6 LEU D 45 ILE D 51 -1 O GLU D 46 N ARG D 38 SHEET 6 AB2 6 THR D 60 TYR D 62 -1 O TYR D 61 N ARG D 50 SHEET 1 AB3 4 LEU D 11 VAL D 12 0 SHEET 2 AB3 4 THR D 116 VAL D 120 1 O THR D 119 N VAL D 12 SHEET 3 AB3 4 ALA D 94 GLY D 101 -1 N ALA D 94 O VAL D 118 SHEET 4 AB3 4 MET D 109 TYR D 111 -1 O TYR D 111 N ARG D 100 SHEET 1 AB4 4 MET E 4 THR E 5 0 SHEET 2 AB4 4 VAL E 19 ALA E 25 -1 O ARG E 24 N THR E 5 SHEET 3 AB4 4 ASP E 70 ILE E 75 -1 O PHE E 71 N CYS E 23 SHEET 4 AB4 4 PHE E 62 SER E 67 -1 N SER E 65 O SER E 72 SHEET 1 AB5 6 SER E 10 ALA E 13 0 SHEET 2 AB5 6 THR E 102 LEU E 106 1 O GLU E 105 N ALA E 13 SHEET 3 AB5 6 THR E 85 GLN E 90 -1 N TYR E 86 O THR E 102 SHEET 4 AB5 6 LEU E 33 GLN E 38 -1 N GLN E 38 O THR E 85 SHEET 5 AB5 6 VAL E 44 TYR E 49 -1 O LYS E 45 N GLN E 37 SHEET 6 AB5 6 ARG E 53 LEU E 54 -1 O ARG E 53 N TYR E 49 SHEET 1 AB6 4 SER E 10 ALA E 13 0 SHEET 2 AB6 4 THR E 102 LEU E 106 1 O GLU E 105 N ALA E 13 SHEET 3 AB6 4 THR E 85 GLN E 90 -1 N TYR E 86 O THR E 102 SHEET 4 AB6 4 THR E 97 PHE E 98 -1 O THR E 97 N GLN E 90 SHEET 1 AB7 4 GLN F 3 THR F 7 0 SHEET 2 AB7 4 LEU F 18 SER F 25 -1 O ALA F 23 N VAL F 5 SHEET 3 AB7 4 MET F 80 MET F 85 -1 O LEU F 83 N LEU F 20 SHEET 4 AB7 4 PHE F 70 ASP F 75 -1 N THR F 71 O GLN F 84 SHEET 1 AB8 6 GLY F 10 VAL F 12 0 SHEET 2 AB8 6 THR F 116 VAL F 120 1 O THR F 119 N GLY F 10 SHEET 3 AB8 6 ALA F 94 GLY F 101 -1 N TYR F 96 O THR F 116 SHEET 4 AB8 6 MET F 34 GLN F 39 -1 N VAL F 37 O TYR F 97 SHEET 5 AB8 6 LEU F 45 ILE F 51 -1 O GLU F 46 N ARG F 38 SHEET 6 AB8 6 THR F 60 TYR F 62 -1 O TYR F 61 N ARG F 50 SHEET 1 AB9 4 GLY F 10 VAL F 12 0 SHEET 2 AB9 4 THR F 116 VAL F 120 1 O THR F 119 N GLY F 10 SHEET 3 AB9 4 ALA F 94 GLY F 101 -1 N TYR F 96 O THR F 116 SHEET 4 AB9 4 MET F 109 TRP F 112 -1 O TYR F 111 N ARG F 100 SHEET 1 AC1 4 MET G 4 THR G 5 0 SHEET 2 AC1 4 VAL G 19 ALA G 25 -1 O ARG G 24 N THR G 5 SHEET 3 AC1 4 ASP G 70 ILE G 75 -1 O ILE G 75 N VAL G 19 SHEET 4 AC1 4 PHE G 62 SER G 67 -1 N SER G 65 O SER G 72 SHEET 1 AC2 2 SER G 10 ALA G 13 0 SHEET 2 AC2 2 LYS G 103 LEU G 106 1 O GLU G 105 N ALA G 13 SHEET 1 AC3 5 ARG G 53 LEU G 54 0 SHEET 2 AC3 5 VAL G 44 TYR G 49 -1 N TYR G 49 O ARG G 53 SHEET 3 AC3 5 LEU G 33 GLN G 38 -1 N TRP G 35 O ILE G 48 SHEET 4 AC3 5 THR G 85 GLN G 90 -1 O GLN G 89 N ASN G 34 SHEET 5 AC3 5 THR G 97 PHE G 98 -1 O THR G 97 N GLN G 90 SHEET 1 AC4 4 GLN H 3 THR H 7 0 SHEET 2 AC4 4 SER H 17 SER H 25 -1 O SER H 21 N THR H 7 SHEET 3 AC4 4 MET H 80 ASN H 86 -1 O LEU H 83 N LEU H 20 SHEET 4 AC4 4 PHE H 70 ASP H 75 -1 N THR H 71 O GLN H 84 SHEET 1 AC5 6 GLY H 10 VAL H 12 0 SHEET 2 AC5 6 THR H 116 VAL H 120 1 O THR H 119 N GLY H 10 SHEET 3 AC5 6 ALA H 94 GLY H 101 -1 N TYR H 96 O THR H 116 SHEET 4 AC5 6 MET H 34 GLN H 39 -1 N VAL H 37 O TYR H 97 SHEET 5 AC5 6 LEU H 45 ILE H 51 -1 O VAL H 48 N TRP H 36 SHEET 6 AC5 6 THR H 60 TYR H 62 -1 O TYR H 61 N ARG H 50 SHEET 1 AC6 4 GLY H 10 VAL H 12 0 SHEET 2 AC6 4 THR H 116 VAL H 120 1 O THR H 119 N GLY H 10 SHEET 3 AC6 4 ALA H 94 GLY H 101 -1 N TYR H 96 O THR H 116 SHEET 4 AC6 4 MET H 109 TRP H 112 -1 O TYR H 111 N ARG H 100 SHEET 1 AC7 4 MET I 4 THR I 5 0 SHEET 2 AC7 4 VAL I 19 ALA I 25 -1 O ARG I 24 N THR I 5 SHEET 3 AC7 4 ASP I 70 ILE I 75 -1 O PHE I 71 N CYS I 23 SHEET 4 AC7 4 PHE I 62 SER I 67 -1 N SER I 63 O THR I 74 SHEET 1 AC8 6 SER I 10 ALA I 13 0 SHEET 2 AC8 6 THR I 102 LEU I 106 1 O LYS I 103 N LEU I 11 SHEET 3 AC8 6 THR I 85 GLN I 90 -1 N TYR I 86 O THR I 102 SHEET 4 AC8 6 LEU I 33 GLN I 38 -1 N GLN I 38 O THR I 85 SHEET 5 AC8 6 VAL I 44 TYR I 49 -1 O ILE I 48 N TRP I 35 SHEET 6 AC8 6 ARG I 53 LEU I 54 -1 O ARG I 53 N TYR I 49 SHEET 1 AC9 4 GLN J 3 THR J 7 0 SHEET 2 AC9 4 SER J 17 SER J 25 -1 O ALA J 23 N VAL J 5 SHEET 3 AC9 4 MET J 80 ASN J 86 -1 O LEU J 83 N LEU J 20 SHEET 4 AC9 4 PHE J 70 ASP J 75 -1 N SER J 73 O TYR J 82 SHEET 1 AD1 6 GLY J 10 VAL J 12 0 SHEET 2 AD1 6 THR J 116 VAL J 120 1 O THR J 119 N GLY J 10 SHEET 3 AD1 6 MET J 95 GLY J 101 -1 N TYR J 96 O THR J 116 SHEET 4 AD1 6 MET J 34 GLN J 39 -1 N VAL J 37 O TYR J 97 SHEET 5 AD1 6 LEU J 45 ILE J 51 -1 O VAL J 48 N TRP J 36 SHEET 6 AD1 6 THR J 60 TYR J 62 -1 O TYR J 61 N ARG J 50 SHEET 1 AD2 4 GLY J 10 VAL J 12 0 SHEET 2 AD2 4 THR J 116 VAL J 120 1 O THR J 119 N GLY J 10 SHEET 3 AD2 4 MET J 95 GLY J 101 -1 N TYR J 96 O THR J 116 SHEET 4 AD2 4 MET J 109 TRP J 112 -1 O TYR J 111 N ARG J 100 SHEET 1 AD3 4 MET K 4 THR K 5 0 SHEET 2 AD3 4 VAL K 19 ALA K 25 -1 O ARG K 24 N THR K 5 SHEET 3 AD3 4 ASP K 70 ILE K 75 -1 O PHE K 71 N CYS K 23 SHEET 4 AD3 4 PHE K 62 SER K 67 -1 N SER K 65 O SER K 72 SHEET 1 AD4 6 SER K 10 ALA K 13 0 SHEET 2 AD4 6 THR K 102 LEU K 106 1 O LYS K 103 N LEU K 11 SHEET 3 AD4 6 THR K 85 GLN K 90 -1 N TYR K 86 O THR K 102 SHEET 4 AD4 6 LEU K 33 GLN K 38 -1 N GLN K 38 O THR K 85 SHEET 5 AD4 6 VAL K 44 TYR K 49 -1 O ILE K 48 N TRP K 35 SHEET 6 AD4 6 ARG K 53 LEU K 54 -1 O ARG K 53 N TYR K 49 SHEET 1 AD5 4 SER K 10 ALA K 13 0 SHEET 2 AD5 4 THR K 102 LEU K 106 1 O LYS K 103 N LEU K 11 SHEET 3 AD5 4 THR K 85 GLN K 90 -1 N TYR K 86 O THR K 102 SHEET 4 AD5 4 THR K 97 PHE K 98 -1 O THR K 97 N GLN K 90 SHEET 1 AD6 4 GLN L 3 THR L 7 0 SHEET 2 AD6 4 GLY L 16 SER L 25 -1 O ALA L 23 N VAL L 5 SHEET 3 AD6 4 MET L 80 LEU L 88 -1 O LEU L 83 N LEU L 20 SHEET 4 AD6 4 PHE L 70 ASP L 75 -1 N SER L 73 O TYR L 82 SHEET 1 AD7 6 LEU L 11 VAL L 12 0 SHEET 2 AD7 6 THR L 116 VAL L 120 1 O THR L 119 N VAL L 12 SHEET 3 AD7 6 ALA L 94 GLY L 101 -1 N TYR L 96 O THR L 116 SHEET 4 AD7 6 MET L 34 GLN L 39 -1 N ASN L 35 O VAL L 99 SHEET 5 AD7 6 LEU L 45 ILE L 51 -1 O ALA L 49 N TRP L 36 SHEET 6 AD7 6 THR L 60 TYR L 62 -1 O TYR L 61 N ARG L 50 SHEET 1 AD8 4 LEU L 11 VAL L 12 0 SHEET 2 AD8 4 THR L 116 VAL L 120 1 O THR L 119 N VAL L 12 SHEET 3 AD8 4 ALA L 94 GLY L 101 -1 N TYR L 96 O THR L 116 SHEET 4 AD8 4 MET L 109 TYR L 111 -1 O ASP L 110 N ARG L 100 SSBOND 1 CYS A 23 CYS A 88 1555 1555 2.04 SSBOND 2 CYS B 22 CYS B 98 1555 1555 2.04 SSBOND 3 CYS C 23 CYS C 88 1555 1555 2.04 SSBOND 4 CYS D 22 CYS D 98 1555 1555 2.04 SSBOND 5 CYS E 23 CYS E 88 1555 1555 2.04 SSBOND 6 CYS F 22 CYS F 98 1555 1555 2.04 SSBOND 7 CYS G 23 CYS G 88 1555 1555 2.04 SSBOND 8 CYS H 22 CYS H 98 1555 1555 2.04 SSBOND 9 CYS I 23 CYS I 88 1555 1555 2.04 SSBOND 10 CYS J 22 CYS J 98 1555 1555 2.04 SSBOND 11 CYS K 23 CYS K 88 1555 1555 2.04 SSBOND 12 CYS L 22 CYS L 98 1555 1555 2.04 LINK OP2 DC N 5 MG MG N 101 1555 1555 2.77 LINK OP2 DC O 5 MG MG O 102 1555 1555 2.65 LINK OP2 DC P 5 MG MG P 102 1555 1555 2.54 CISPEP 1 LEU A 94 PRO A 95 0 3.27 CISPEP 2 LEU C 94 PRO C 95 0 2.77 CISPEP 3 LEU E 94 PRO E 95 0 2.83 CISPEP 4 LEU G 94 PRO G 95 0 3.29 CISPEP 5 LEU I 94 PRO I 95 0 2.50 CISPEP 6 LEU K 94 PRO K 95 0 4.46 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