HEADER PROTEIN BINDING 25-APR-24 8ZAY TITLE CRYSTAL STRUCTURE OF FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: VH-CH1 REGION OF ANTIBODY OF ANTI-RSEP ORTHOLOGUE FROM A COMPND 3 AEOLICUS; COMPND 4 CHAIN: H, I; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: LIGHT CHAIN OF ANTIBODY OF ANTI-RSEP ORTHOLOGUE FROM A COMPND 8 AEOLICUS; COMPND 9 CHAIN: L, M; COMPND 10 ENGINEERED: YES 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 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 8 ORGANISM_TAXID: 10090; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS ANTIBODY, PROTEIN BINDING EXPDTA X-RAY DIFFRACTION AUTHOR Y.ADACHI,T.NOGI REVDAT 1 05-MAR-25 8ZAY 0 JRNL AUTH K.ASAHI,M.HIROSE,R.ARUGA,Y.SHIMIZU,M.TAJIRI,T.TANAKA, JRNL AUTH 2 Y.ADACHI,Y.TANAKA,M.K.KANEKO,Y.KATO,S.AKASHI,Y.AKIYAMA, JRNL AUTH 3 Y.HIZUKURI,T.KATO,T.NOGI JRNL TITL CRYO-EM STRUCTURE OF THE BACTERIAL INTRAMEMBRANE JRNL TITL 2 METALLOPROTEASE RSEP IN THE SUBSTRATE-BOUND STATE. JRNL REF SCI ADV 2025 JRNL REFN ESSN 2375-2548 JRNL DOI 10.1126/SCIADV.ADU0925 REMARK 2 REMARK 2 RESOLUTION. 2.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20.1_4487 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.91 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 42299 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.220 REMARK 3 R VALUE (WORKING SET) : 0.218 REMARK 3 FREE R VALUE : 0.269 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.920 REMARK 3 FREE R VALUE TEST SET COUNT : 4061 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 49.9100 - 7.0600 0.99 2703 123 0.1755 0.2114 REMARK 3 2 7.0600 - 5.6100 1.00 2737 131 0.1791 0.2079 REMARK 3 3 5.6000 - 4.9000 1.00 2709 137 0.1562 0.1597 REMARK 3 4 4.9000 - 4.4500 1.00 2723 112 0.1405 0.1981 REMARK 3 5 4.4500 - 4.1300 1.00 2712 128 0.1552 0.1784 REMARK 3 6 4.1300 - 3.8900 1.00 2685 174 0.1712 0.2443 REMARK 3 7 3.8900 - 3.6900 1.00 2696 132 0.1881 0.2292 REMARK 3 8 3.6900 - 3.5300 1.00 2729 150 0.1918 0.2372 REMARK 3 9 3.5300 - 3.4000 1.00 2667 173 0.2144 0.2853 REMARK 3 10 3.4000 - 3.2800 1.00 2702 134 0.2227 0.2786 REMARK 3 11 3.2800 - 3.1800 1.00 2726 144 0.2322 0.2558 REMARK 3 12 3.1800 - 3.0900 1.00 2701 154 0.2311 0.3003 REMARK 3 13 3.0900 - 3.0100 1.00 2670 141 0.2424 0.2450 REMARK 3 14 3.0100 - 2.9300 1.00 2717 138 0.2308 0.3062 REMARK 3 15 2.9300 - 2.8700 1.00 2719 148 0.2322 0.3440 REMARK 3 16 2.8700 - 2.8000 1.00 2720 134 0.2617 0.3039 REMARK 3 17 2.8000 - 2.7500 1.00 2722 132 0.2787 0.2974 REMARK 3 18 2.7500 - 2.7000 1.00 2683 148 0.2769 0.3544 REMARK 3 19 2.7000 - 2.6500 1.00 2693 114 0.2659 0.2795 REMARK 3 20 2.6500 - 2.6000 1.00 2726 152 0.2618 0.3544 REMARK 3 21 2.6000 - 2.5600 1.00 2725 124 0.2598 0.2773 REMARK 3 22 2.5600 - 2.5200 1.00 2731 149 0.2527 0.3416 REMARK 3 23 2.5200 - 2.4800 1.00 2678 138 0.2616 0.3249 REMARK 3 24 2.4800 - 2.4500 1.00 2726 120 0.2697 0.4028 REMARK 3 25 2.4500 - 2.4200 1.00 2701 157 0.2806 0.3613 REMARK 3 26 2.4200 - 2.3900 1.00 2735 144 0.2890 0.3456 REMARK 3 27 2.3900 - 2.3600 1.00 2588 147 0.3067 0.2887 REMARK 3 28 2.3600 - 2.3300 1.00 2789 155 0.3695 0.4156 REMARK 3 29 2.3300 - 2.3000 1.00 2700 128 0.4035 0.4493 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.367 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.223 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 26.49 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.10 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.002 6822 REMARK 3 ANGLE : 0.441 9295 REMARK 3 CHIRALITY : 0.041 1046 REMARK 3 PLANARITY : 0.003 1187 REMARK 3 DIHEDRAL : 5.186 937 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NUMBER OF UNIQUE REFLECTIONS IS 82574 REMARK 3 WHEN THE BIJVOET PAIRS ARE SEPARATED. REMARK 4 REMARK 4 8ZAY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-APR-24. REMARK 100 THE DEPOSITION ID IS D_1300046995. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 24-JUL-21 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SPRING-8 REMARK 200 BEAMLINE : BL32XU REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43326 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300 REMARK 200 RESOLUTION RANGE LOW (A) : 49.920 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 370.1 REMARK 200 R MERGE (I) : 1.15000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 20.0700 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 50.68 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05M ZINC ACETATE DIHYDRATE, 20% W/V REMARK 280 POLYETHYLENE GLYCOL 3350, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 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,Y+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 35.22000 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 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4260 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19710 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -165.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L 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 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4180 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19700 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -166.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, M 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY H 1 REMARK 465 SER H 2 REMARK 465 GLY H 138 REMARK 465 SER H 139 REMARK 465 ALA H 140 REMARK 465 ALA H 141 REMARK 465 GLN H 142 REMARK 465 THR H 143 REMARK 465 ASN H 144 REMARK 465 GLY I 1 REMARK 465 SER I 2 REMARK 465 SER I 139 REMARK 465 ALA I 140 REMARK 465 ALA I 141 REMARK 465 GLN I 142 REMARK 465 THR I 143 REMARK 465 ASN I 144 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 LYS I 69 -173.44 58.84 REMARK 500 ALA L 51 -37.69 71.99 REMARK 500 ASN L 77 76.22 54.17 REMARK 500 LEU L 83 98.97 -62.77 REMARK 500 ASN L 138 60.18 61.66 REMARK 500 ASN L 190 -72.20 -109.25 REMARK 500 ALA M 51 -30.71 72.65 REMARK 500 ASN M 138 60.64 61.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN H 302 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP H 112 OD2 REMARK 620 2 HOH H 456 O 101.5 REMARK 620 3 HIS L 55 NE2 120.4 107.4 REMARK 620 4 HOH L 465 O 120.0 116.8 91.1 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN H 301 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS H 175 NE2 REMARK 620 2 ASP L 167 OD2 93.2 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN L 302 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP H 218 OD2 REMARK 620 2 GLU L 185 OE1 26.0 REMARK 620 3 HIS L 189 NE2 23.4 5.3 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN M 303 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP H 225 OD1 REMARK 620 2 ASP H 225 OD2 53.7 REMARK 620 3 ASP M 32 OD2 52.9 32.7 REMARK 620 4 HOH M 430 O 55.5 33.5 2.6 REMARK 620 5 HOH M 436 O 53.6 29.8 3.2 3.8 REMARK 620 6 HOH M 446 O 56.0 32.3 3.4 1.5 3.1 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN I 301 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP I 112 OD2 REMARK 620 2 HOH I 435 O 101.9 REMARK 620 3 HIS M 55 NE2 110.5 114.9 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN I 302 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS I 175 NE2 REMARK 620 2 ASP M 167 OD2 100.6 REMARK 620 3 HOH M 413 O 98.7 71.6 REMARK 620 4 HOH M 454 O 86.2 173.1 108.6 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN M 302 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP I 218 OD2 REMARK 620 2 GLU M 185 OE1 23.8 REMARK 620 3 HIS M 189 NE2 24.4 5.6 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN L 301 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP I 225 OD1 REMARK 620 2 ASP I 225 OD2 54.2 REMARK 620 3 ASP L 32 OD2 64.1 40.1 REMARK 620 4 HOH L 427 O 64.5 37.4 3.2 REMARK 620 5 HOH L 446 O 66.7 41.2 2.7 3.9 REMARK 620 6 HOH L 463 O 68.3 41.6 4.3 4.7 1.7 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN M 301 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS L 8 NE2 REMARK 620 2 HOH L 461 O 98.6 REMARK 620 3 GLU M 105 OE2 123.9 118.2 REMARK 620 4 LYS M 142 NZ 103.9 113.7 98.3 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN L 303 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU L 105 OE1 REMARK 620 2 HIS M 8 NE2 138.8 REMARK 620 3 HOH M 460 O 118.4 85.4 REMARK 620 N 1 2 DBREF 8ZAY H 1 226 PDB 8ZAY 8ZAY 1 226 DBREF 8ZAY I 1 226 PDB 8ZAY 8ZAY 1 226 DBREF 8ZAY L 1 214 PDB 8ZAY 8ZAY 1 214 DBREF 8ZAY M 1 214 PDB 8ZAY 8ZAY 1 214 SEQRES 1 H 226 GLY SER GLU VAL LYS LEU VAL GLU SER GLY GLY GLY LEU SEQRES 2 H 226 VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS VAL THR SEQRES 3 H 226 SER GLY PHE THR PHE THR ASP TYR TYR MET SER TRP VAL SEQRES 4 H 226 ARG GLN PRO PRO GLY LYS ALA LEU GLU TRP LEU ALA PHE SEQRES 5 H 226 ILE ARG ASN LYS VAL ASN GLY TYR THR THR GLU TYR ARG SEQRES 6 H 226 ALA SER VAL LYS GLY ARG PHE THR ILE SER ARG ASP SER SEQRES 7 H 226 SER GLN SER ILE LEU TYR LEU GLN VAL ASN THR LEU ARG SEQRES 8 H 226 ALA GLU ASP SER ALA THR TYR TYR CYS ALA ARG ASP ARG SEQRES 9 H 226 GLY GLY ASN GLY VAL TYR PHE ASP TYR TRP GLY GLN GLY SEQRES 10 H 226 THR THR LEU THR VAL SER SER ALA LYS THR THR PRO PRO SEQRES 11 H 226 SER VAL TYR PRO LEU ALA PRO GLY SER ALA ALA GLN THR SEQRES 12 H 226 ASN SER MET VAL THR LEU GLY CYS LEU VAL LYS GLY TYR SEQRES 13 H 226 PHE PRO GLU PRO VAL THR VAL THR TRP ASN SER GLY SER SEQRES 14 H 226 LEU SER SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15 H 226 SER ASP LEU TYR THR LEU SER SER SER VAL THR VAL PRO SEQRES 16 H 226 SER SER THR TRP PRO SER GLU THR VAL THR CYS ASN VAL SEQRES 17 H 226 ALA HIS PRO ALA SER SER THR LYS VAL ASP LYS LYS ILE SEQRES 18 H 226 VAL PRO ARG ASP CYS SEQRES 1 I 226 GLY SER GLU VAL LYS LEU VAL GLU SER GLY GLY GLY LEU SEQRES 2 I 226 VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS VAL THR SEQRES 3 I 226 SER GLY PHE THR PHE THR ASP TYR TYR MET SER TRP VAL SEQRES 4 I 226 ARG GLN PRO PRO GLY LYS ALA LEU GLU TRP LEU ALA PHE SEQRES 5 I 226 ILE ARG ASN LYS VAL ASN GLY TYR THR THR GLU TYR ARG SEQRES 6 I 226 ALA SER VAL LYS GLY ARG PHE THR ILE SER ARG ASP SER SEQRES 7 I 226 SER GLN SER ILE LEU TYR LEU GLN VAL ASN THR LEU ARG SEQRES 8 I 226 ALA GLU ASP SER ALA THR TYR TYR CYS ALA ARG ASP ARG SEQRES 9 I 226 GLY GLY ASN GLY VAL TYR PHE ASP TYR TRP GLY GLN GLY SEQRES 10 I 226 THR THR LEU THR VAL SER SER ALA LYS THR THR PRO PRO SEQRES 11 I 226 SER VAL TYR PRO LEU ALA PRO GLY SER ALA ALA GLN THR SEQRES 12 I 226 ASN SER MET VAL THR LEU GLY CYS LEU VAL LYS GLY TYR SEQRES 13 I 226 PHE PRO GLU PRO VAL THR VAL THR TRP ASN SER GLY SER SEQRES 14 I 226 LEU SER SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15 I 226 SER ASP LEU TYR THR LEU SER SER SER VAL THR VAL PRO SEQRES 16 I 226 SER SER THR TRP PRO SER GLU THR VAL THR CYS ASN VAL SEQRES 17 I 226 ALA HIS PRO ALA SER SER THR LYS VAL ASP LYS LYS ILE SEQRES 18 I 226 VAL PRO ARG ASP CYS SEQRES 1 L 214 ASP ILE VAL MET THR GLN SER HIS LYS PHE MET SER THR SEQRES 2 L 214 SER VAL GLY ASP ARG VAL SER ILE THR CYS LYS ALA SER SEQRES 3 L 214 GLN ASP VAL GLY THR ASP VAL ALA TRP TYR GLN GLN LYS SEQRES 4 L 214 PRO GLY GLN SER PRO LYS LEU LEU ILE TYR TRP ALA SER SEQRES 5 L 214 ILE ARG HIS THR GLY VAL PRO ASP ARG PHE THR GLY SER SEQRES 6 L 214 GLY SER GLY THR ASP PHE THR LEU THR ILE SER ASN VAL SEQRES 7 L 214 GLN SER GLU ASP LEU ALA ASP TYR PHE CYS GLN GLN TYR SEQRES 8 L 214 SER SER TYR PRO LEU THR PHE GLY ALA GLY THR LYS LEU SEQRES 9 L 214 GLU LEU GLU ARG ALA ASP ALA ALA PRO THR VAL SER ILE SEQRES 10 L 214 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SEQRES 11 L 214 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP SEQRES 12 L 214 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN SEQRES 13 L 214 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS SEQRES 14 L 214 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR SEQRES 15 L 214 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU SEQRES 16 L 214 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER SEQRES 17 L 214 PHE ASN ARG ASN GLU CYS SEQRES 1 M 214 ASP ILE VAL MET THR GLN SER HIS LYS PHE MET SER THR SEQRES 2 M 214 SER VAL GLY ASP ARG VAL SER ILE THR CYS LYS ALA SER SEQRES 3 M 214 GLN ASP VAL GLY THR ASP VAL ALA TRP TYR GLN GLN LYS SEQRES 4 M 214 PRO GLY GLN SER PRO LYS LEU LEU ILE TYR TRP ALA SER SEQRES 5 M 214 ILE ARG HIS THR GLY VAL PRO ASP ARG PHE THR GLY SER SEQRES 6 M 214 GLY SER GLY THR ASP PHE THR LEU THR ILE SER ASN VAL SEQRES 7 M 214 GLN SER GLU ASP LEU ALA ASP TYR PHE CYS GLN GLN TYR SEQRES 8 M 214 SER SER TYR PRO LEU THR PHE GLY ALA GLY THR LYS LEU SEQRES 9 M 214 GLU LEU GLU ARG ALA ASP ALA ALA PRO THR VAL SER ILE SEQRES 10 M 214 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SEQRES 11 M 214 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP SEQRES 12 M 214 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN SEQRES 13 M 214 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS SEQRES 14 M 214 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR SEQRES 15 M 214 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU SEQRES 16 M 214 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER SEQRES 17 M 214 PHE ASN ARG ASN GLU CYS HET ZN H 301 1 HET ZN H 302 1 HET ZN I 301 1 HET ZN I 302 1 HET ZN L 301 1 HET ZN L 302 1 HET ZN L 303 1 HET ZN M 301 1 HET ZN M 302 1 HET ZN M 303 1 HETNAM ZN ZINC ION FORMUL 5 ZN 10(ZN 2+) FORMUL 15 HOH *223(H2 O) HELIX 1 AA1 THR H 30 TYR H 34 5 5 HELIX 2 AA2 ASN H 55 GLY H 59 5 5 HELIX 3 AA3 ALA H 66 LYS H 69 5 4 HELIX 4 AA4 ARG H 91 SER H 95 5 5 HELIX 5 AA5 SER H 167 SER H 169 5 3 HELIX 6 AA6 PRO H 211 SER H 214 5 4 HELIX 7 AA7 THR I 30 TYR I 34 5 5 HELIX 8 AA8 ALA I 66 GLY I 70 5 5 HELIX 9 AA9 ARG I 91 SER I 95 5 5 HELIX 10 AB1 PRO I 211 SER I 214 5 4 HELIX 11 AB2 GLN L 79 LEU L 83 5 5 HELIX 12 AB3 SER L 121 GLY L 128 1 8 HELIX 13 AB4 LYS L 183 GLU L 187 1 5 HELIX 14 AB5 ASN L 212 CYS L 214 5 3 HELIX 15 AB6 GLN M 79 LEU M 83 5 5 HELIX 16 AB7 SER M 121 GLY M 128 1 8 HELIX 17 AB8 LYS M 183 ARG M 188 1 6 HELIX 18 AB9 ASN M 212 CYS M 214 5 3 SHEET 1 AA1 4 LYS H 5 SER H 9 0 SHEET 2 AA1 4 LEU H 20 SER H 27 -1 O VAL H 25 N VAL H 7 SHEET 3 AA1 4 ILE H 82 VAL H 87 -1 O LEU H 85 N LEU H 22 SHEET 4 AA1 4 PHE H 72 ARG H 76 -1 N SER H 75 O TYR H 84 SHEET 1 AA2 6 GLY H 12 VAL H 14 0 SHEET 2 AA2 6 THR H 118 VAL H 122 1 O THR H 121 N GLY H 12 SHEET 3 AA2 6 ALA H 96 ARG H 104 -1 N TYR H 98 O THR H 118 SHEET 4 AA2 6 TYR H 35 GLN H 41 -1 N VAL H 39 O TYR H 99 SHEET 5 AA2 6 GLU H 48 ILE H 53 -1 O ILE H 53 N MET H 36 SHEET 6 AA2 6 THR H 62 TYR H 64 -1 O GLU H 63 N PHE H 52 SHEET 1 AA3 4 GLY H 12 VAL H 14 0 SHEET 2 AA3 4 THR H 118 VAL H 122 1 O THR H 121 N GLY H 12 SHEET 3 AA3 4 ALA H 96 ARG H 104 -1 N TYR H 98 O THR H 118 SHEET 4 AA3 4 TYR H 110 TRP H 114 -1 O TYR H 113 N ARG H 102 SHEET 1 AA4 4 SER H 131 LEU H 135 0 SHEET 2 AA4 4 MET H 146 TYR H 156 -1 O LEU H 152 N TYR H 133 SHEET 3 AA4 4 LEU H 185 PRO H 195 -1 O LEU H 188 N VAL H 153 SHEET 4 AA4 4 VAL H 174 THR H 176 -1 N HIS H 175 O SER H 191 SHEET 1 AA5 4 SER H 131 LEU H 135 0 SHEET 2 AA5 4 MET H 146 TYR H 156 -1 O LEU H 152 N TYR H 133 SHEET 3 AA5 4 LEU H 185 PRO H 195 -1 O LEU H 188 N VAL H 153 SHEET 4 AA5 4 VAL H 180 GLN H 182 -1 N GLN H 182 O LEU H 185 SHEET 1 AA6 3 THR H 162 TRP H 165 0 SHEET 2 AA6 3 THR H 205 HIS H 210 -1 O ASN H 207 N THR H 164 SHEET 3 AA6 3 THR H 215 LYS H 220 -1 O VAL H 217 N VAL H 208 SHEET 1 AA7 4 LYS I 5 SER I 9 0 SHEET 2 AA7 4 LEU I 20 SER I 27 -1 O VAL I 25 N VAL I 7 SHEET 3 AA7 4 ILE I 82 VAL I 87 -1 O VAL I 87 N LEU I 20 SHEET 4 AA7 4 PHE I 72 ARG I 76 -1 N THR I 73 O GLN I 86 SHEET 1 AA8 6 GLY I 12 VAL I 14 0 SHEET 2 AA8 6 THR I 118 VAL I 122 1 O THR I 121 N GLY I 12 SHEET 3 AA8 6 THR I 97 ARG I 104 -1 N TYR I 98 O THR I 118 SHEET 4 AA8 6 MET I 36 GLN I 41 -1 N VAL I 39 O TYR I 99 SHEET 5 AA8 6 GLU I 48 ILE I 53 -1 O ILE I 53 N MET I 36 SHEET 6 AA8 6 THR I 62 TYR I 64 -1 O GLU I 63 N PHE I 52 SHEET 1 AA9 4 GLY I 12 VAL I 14 0 SHEET 2 AA9 4 THR I 118 VAL I 122 1 O THR I 121 N GLY I 12 SHEET 3 AA9 4 THR I 97 ARG I 104 -1 N TYR I 98 O THR I 118 SHEET 4 AA9 4 TYR I 110 TRP I 114 -1 O TYR I 113 N ARG I 102 SHEET 1 AB1 4 SER I 131 LEU I 135 0 SHEET 2 AB1 4 MET I 146 TYR I 156 -1 O LYS I 154 N SER I 131 SHEET 3 AB1 4 LEU I 185 PRO I 195 -1 O LEU I 188 N VAL I 153 SHEET 4 AB1 4 VAL I 174 THR I 176 -1 N HIS I 175 O SER I 191 SHEET 1 AB2 4 SER I 131 LEU I 135 0 SHEET 2 AB2 4 MET I 146 TYR I 156 -1 O LYS I 154 N SER I 131 SHEET 3 AB2 4 LEU I 185 PRO I 195 -1 O LEU I 188 N VAL I 153 SHEET 4 AB2 4 VAL I 180 GLN I 182 -1 N GLN I 182 O LEU I 185 SHEET 1 AB3 3 THR I 162 TRP I 165 0 SHEET 2 AB3 3 THR I 205 HIS I 210 -1 O ASN I 207 N THR I 164 SHEET 3 AB3 3 THR I 215 LYS I 220 -1 O THR I 215 N HIS I 210 SHEET 1 AB4 4 MET L 4 THR L 5 0 SHEET 2 AB4 4 VAL L 19 ALA L 25 -1 O LYS L 24 N THR L 5 SHEET 3 AB4 4 ASP L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AB4 4 PHE L 62 SER L 67 -1 N THR L 63 O THR L 74 SHEET 1 AB5 6 PHE L 10 THR L 13 0 SHEET 2 AB5 6 THR L 102 LEU L 106 1 O GLU L 105 N MET L 11 SHEET 3 AB5 6 ASP L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AB5 6 VAL L 33 GLN L 38 -1 N GLN L 38 O ASP L 85 SHEET 5 AB5 6 LYS L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AB5 6 ILE L 53 ARG L 54 -1 O ILE L 53 N TYR L 49 SHEET 1 AB6 4 PHE L 10 THR L 13 0 SHEET 2 AB6 4 THR L 102 LEU L 106 1 O GLU L 105 N MET L 11 SHEET 3 AB6 4 ASP L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AB6 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AB7 4 THR L 114 PHE L 118 0 SHEET 2 AB7 4 GLY L 129 PHE L 139 -1 O PHE L 135 N SER L 116 SHEET 3 AB7 4 TYR L 173 THR L 182 -1 O LEU L 179 N VAL L 132 SHEET 4 AB7 4 VAL L 159 TRP L 163 -1 N SER L 162 O SER L 176 SHEET 1 AB8 4 SER L 153 ARG L 155 0 SHEET 2 AB8 4 ASN L 145 ILE L 150 -1 N ILE L 150 O SER L 153 SHEET 3 AB8 4 SER L 191 THR L 197 -1 O THR L 197 N ASN L 145 SHEET 4 AB8 4 ILE L 205 ASN L 210 -1 O LYS L 207 N CYS L 194 SHEET 1 AB9 4 MET M 4 THR M 5 0 SHEET 2 AB9 4 VAL M 19 ALA M 25 -1 O LYS M 24 N THR M 5 SHEET 3 AB9 4 ASP M 70 ILE M 75 -1 O LEU M 73 N ILE M 21 SHEET 4 AB9 4 PHE M 62 GLY M 66 -1 N THR M 63 O THR M 74 SHEET 1 AC1 6 PHE M 10 THR M 13 0 SHEET 2 AC1 6 THR M 102 LEU M 106 1 O GLU M 105 N THR M 13 SHEET 3 AC1 6 ASP M 85 GLN M 90 -1 N TYR M 86 O THR M 102 SHEET 4 AC1 6 VAL M 33 GLN M 38 -1 N GLN M 38 O ASP M 85 SHEET 5 AC1 6 LYS M 45 TYR M 49 -1 O ILE M 48 N TRP M 35 SHEET 6 AC1 6 ILE M 53 ARG M 54 -1 O ILE M 53 N TYR M 49 SHEET 1 AC2 4 PHE M 10 THR M 13 0 SHEET 2 AC2 4 THR M 102 LEU M 106 1 O GLU M 105 N THR M 13 SHEET 3 AC2 4 ASP M 85 GLN M 90 -1 N TYR M 86 O THR M 102 SHEET 4 AC2 4 THR M 97 PHE M 98 -1 O THR M 97 N GLN M 90 SHEET 1 AC3 4 THR M 114 PHE M 118 0 SHEET 2 AC3 4 GLY M 129 PHE M 139 -1 O PHE M 135 N SER M 116 SHEET 3 AC3 4 TYR M 173 THR M 182 -1 O LEU M 179 N VAL M 132 SHEET 4 AC3 4 VAL M 159 TRP M 163 -1 N SER M 162 O SER M 176 SHEET 1 AC4 4 SER M 153 ARG M 155 0 SHEET 2 AC4 4 ASN M 145 ILE M 150 -1 N ILE M 150 O SER M 153 SHEET 3 AC4 4 SER M 191 THR M 197 -1 O THR M 193 N LYS M 149 SHEET 4 AC4 4 ILE M 205 ASN M 210 -1 O ILE M 205 N ALA M 196 SSBOND 1 CYS H 24 CYS H 100 1555 1555 2.03 SSBOND 2 CYS H 151 CYS H 206 1555 1555 2.03 SSBOND 3 CYS H 226 CYS L 214 1555 1555 2.03 SSBOND 4 CYS I 24 CYS I 100 1555 1555 2.03 SSBOND 5 CYS I 151 CYS I 206 1555 1555 2.03 SSBOND 6 CYS I 226 CYS M 214 1555 1555 2.03 SSBOND 7 CYS L 23 CYS L 88 1555 1555 2.03 SSBOND 8 CYS L 134 CYS L 194 1555 1555 2.03 SSBOND 9 CYS M 23 CYS M 88 1555 1555 2.04 SSBOND 10 CYS M 134 CYS M 194 1555 1555 2.04 LINK OD2 ASP H 112 ZN ZN H 302 1555 1555 2.42 LINK NE2 HIS H 175 ZN ZN H 301 1555 1555 2.30 LINK OD2 ASP H 218 ZN ZN L 302 1555 2745 1.86 LINK OD1 ASP H 225 ZN ZN M 303 1555 2745 2.18 LINK OD2 ASP H 225 ZN ZN M 303 1555 2745 2.61 LINK ZN ZN H 301 OD2 ASP L 167 1555 1555 2.09 LINK ZN ZN H 302 O HOH H 456 1555 1555 2.47 LINK ZN ZN H 302 NE2 HIS L 55 1555 1555 2.29 LINK ZN ZN H 302 O HOH L 465 1555 1555 2.50 LINK OD2 ASP I 112 ZN ZN I 301 1555 1555 2.33 LINK NE2 HIS I 175 ZN ZN I 302 1555 1555 2.30 LINK OD2 ASP I 218 ZN ZN M 302 1555 2756 2.20 LINK OD1 ASP I 225 ZN ZN L 301 1555 2756 2.52 LINK OD2 ASP I 225 ZN ZN L 301 1555 2756 2.28 LINK ZN ZN I 301 O HOH I 435 1555 1555 2.47 LINK ZN ZN I 301 NE2 HIS M 55 1555 1555 2.29 LINK ZN ZN I 302 OD2 ASP M 167 1555 1555 2.07 LINK ZN ZN I 302 O HOH M 413 1555 1555 2.40 LINK ZN ZN I 302 O HOH M 454 1555 1555 2.55 LINK NE2 HIS L 8 ZN ZN M 301 1555 1555 2.29 LINK OD2 ASP L 32 ZN ZN L 301 1555 1555 1.98 LINK OE1 GLU L 105 ZN ZN L 303 1555 1555 2.69 LINK OE1 GLU L 185 ZN ZN L 302 1555 1555 2.18 LINK NE2 HIS L 189 ZN ZN L 302 1555 1555 2.29 LINK ZN ZN L 301 O HOH L 427 1555 1555 2.29 LINK ZN ZN L 301 O HOH L 446 1555 1555 2.30 LINK ZN ZN L 301 O HOH L 463 1555 1555 2.43 LINK ZN ZN L 303 NE2 HIS M 8 1555 1555 2.30 LINK ZN ZN L 303 O HOH M 460 1555 1555 2.19 LINK O HOH L 461 ZN ZN M 301 1555 1555 2.09 LINK OD2 ASP M 32 ZN ZN M 303 1555 1555 2.05 LINK OE2 GLU M 105 ZN ZN M 301 1555 1555 2.23 LINK NZ LYS M 142 ZN ZN M 301 1555 1555 2.08 LINK OE1 GLU M 185 ZN ZN M 302 1555 1555 2.34 LINK NE2 HIS M 189 ZN ZN M 302 1555 1555 2.29 LINK ZN ZN M 303 O HOH M 430 1555 1555 2.35 LINK ZN ZN M 303 O HOH M 436 1555 1555 2.36 LINK ZN ZN M 303 O HOH M 446 1555 1555 2.06 CISPEP 1 PHE H 157 PRO H 158 0 -1.80 CISPEP 2 GLU H 159 PRO H 160 0 1.77 CISPEP 3 TRP H 199 PRO H 200 0 2.66 CISPEP 4 PHE I 157 PRO I 158 0 -3.30 CISPEP 5 GLU I 159 PRO I 160 0 1.48 CISPEP 6 TRP I 199 PRO I 200 0 3.34 CISPEP 7 TYR L 94 PRO L 95 0 1.86 CISPEP 8 TYR L 140 PRO L 141 0 1.99 CISPEP 9 TYR M 94 PRO M 95 0 1.58 CISPEP 10 TYR M 140 PRO M 141 0 1.25 CRYST1 51.780 70.440 132.460 90.00 96.69 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 0.019312 0.000000 0.002265 0.00000 SCALE2 0.000000 0.014196 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007601 0.00000