HEADER HYDROLASE 16-MAY-25 9UZB TITLE CRYSTAL STRUCTURE OF KASOKERO VIRUS CAP-SNATCHING ENDONUCLEASE IN APO TITLE 2 FORM COMPND MOL_ID: 1; COMPND 2 MOLECULE: RNA-DIRECTED RNA POLYMERASE L; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: LARGE STRUCTURAL PROTEIN,REPLICASE,TRANSCRIPTASE; COMPND 5 EC: 2.7.7.48; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: MAB 2E9 FAB HEAVY CHAIN; COMPND 9 CHAIN: H; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: MAB 2E9 FAB LIGHT CHAIN; COMPND 13 CHAIN: L; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: KASOKERO VIRUS; SOURCE 3 ORGANISM_TAXID: 1712570; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008; 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; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 13 ORGANISM_TAXID: 10090; SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS CAP-SNATCHING ENDONUCLEASE, HYDROLASE EXPDTA X-RAY DIFFRACTION AUTHOR Z.DENG,W.KUANG,Z.TIAN REVDAT 1 31-DEC-25 9UZB 0 JRNL AUTH W.KUANG,Z.TIAN,G.ZHANG,F.WU,J.LI,J.TANG,H.ZHANG,X.ZHUO,Z.HU, JRNL AUTH 2 M.WANG,H.ZHAO,Z.DENG JRNL TITL STRUCTURE AND FUNCTION OF THE NAIROVIRUS CAP-SNATCHING JRNL TITL 2 ENDONUCLEASE JRNL REF NUCLEIC ACIDS RES. 2025 JRNL REFN ESSN 1362-4962 REMARK 2 REMARK 2 RESOLUTION. 1.90 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 : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.50 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 3 NUMBER OF REFLECTIONS : 53439 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.184 REMARK 3 R VALUE (WORKING SET) : 0.182 REMARK 3 FREE R VALUE : 0.221 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.180 REMARK 3 FREE R VALUE TEST SET COUNT : 2766 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 27.5000 - 5.1500 0.97 2556 134 0.1716 0.1933 REMARK 3 2 5.1500 - 4.0900 0.99 2564 114 0.1385 0.1692 REMARK 3 3 4.0900 - 3.5700 0.99 2564 137 0.1506 0.1504 REMARK 3 4 3.5700 - 3.2500 0.99 2520 151 0.1646 0.1963 REMARK 3 5 3.2500 - 3.0200 1.00 2564 135 0.1861 0.2320 REMARK 3 6 3.0200 - 2.8400 1.00 2516 141 0.1898 0.2663 REMARK 3 7 2.8400 - 2.7000 1.00 2527 138 0.2022 0.2535 REMARK 3 8 2.7000 - 2.5800 1.00 2567 137 0.1995 0.2634 REMARK 3 9 2.5800 - 2.4800 1.00 2492 138 0.1974 0.2269 REMARK 3 10 2.4800 - 2.3900 0.99 2521 166 0.1935 0.2173 REMARK 3 11 2.3900 - 2.3200 1.00 2503 133 0.1903 0.2218 REMARK 3 12 2.3200 - 2.2500 1.00 2561 137 0.1927 0.2142 REMARK 3 13 2.2500 - 2.1900 1.00 2491 139 0.1941 0.2269 REMARK 3 14 2.1900 - 2.1400 1.00 2572 124 0.1921 0.2879 REMARK 3 15 2.1400 - 2.0900 1.00 2541 137 0.1982 0.2572 REMARK 3 16 2.0900 - 2.0500 1.00 2485 152 0.2057 0.2365 REMARK 3 17 2.0500 - 2.0100 1.00 2553 144 0.2073 0.2607 REMARK 3 18 2.0100 - 1.9700 1.00 2489 141 0.2011 0.2434 REMARK 3 19 1.9700 - 1.9300 1.00 2538 124 0.2162 0.2596 REMARK 3 20 1.9300 - 1.9000 0.99 2549 144 0.2264 0.2707 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) : 0.190 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.910 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL 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 : 0.008 5366 REMARK 3 ANGLE : 1.080 7279 REMARK 3 CHIRALITY : 0.067 810 REMARK 3 PLANARITY : 0.009 930 REMARK 3 DIHEDRAL : 6.086 726 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: NULL REMARK 4 REMARK 4 9UZB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 20-MAY-25. REMARK 100 THE DEPOSITION ID IS D_1300059490. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 27-SEP-24 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 : SSRF REMARK 200 BEAMLINE : BL10U2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2 REMARK 200 DATA SCALING SOFTWARE : XIA2 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53558 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900 REMARK 200 RESOLUTION RANGE LOW (A) : 28.410 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 200 DATA REDUNDANCY : 3.300 REMARK 200 R MERGE (I) : 0.14100 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.94 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3 REMARK 200 DATA REDUNDANCY IN SHELL : 3.30 REMARK 200 R MERGE FOR SHELL (I) : 0.45100 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: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 41.19 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 25% VOL/VOL JEFFAMINE ED2003, 0.2 M REMARK 280 NACL, AND 0.1 M MES-NAOH PH 6.0, EVAPORATION, TEMPERATURE 289K 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 40.45300 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 ILE A 727 REMARK 465 PHE A 728 REMARK 465 LYS A 729 REMARK 465 SER A 730 REMARK 465 ASP A 731 REMARK 465 ARG A 732 REMARK 465 LEU A 733 REMARK 465 ASN A 734 REMARK 465 ARG A 735 REMARK 465 SER A 736 REMARK 465 ASN A 737 REMARK 465 VAL A 738 REMARK 465 ALA A 739 REMARK 465 VAL A 740 REMARK 465 SER A 741 REMARK 465 ARG A 742 REMARK 465 GLY A 743 REMARK 465 LYS A 744 REMARK 465 ASP A 745 REMARK 465 LYS A 746 REMARK 465 GLY A 747 REMARK 465 GLY A 748 REMARK 465 LYS A 749 REMARK 465 LYS A 750 REMARK 465 LYS A 751 REMARK 465 GLU A 752 REMARK 465 THR A 753 REMARK 465 THR A 754 REMARK 465 VAL A 755 REMARK 465 ASN A 756 REMARK 465 LYS A 757 REMARK 465 ASP A 758 REMARK 465 GLN A 759 REMARK 465 ASP A 760 REMARK 465 ASP A 761 REMARK 465 ASP A 762 REMARK 465 ALA A 763 REMARK 465 GLN A 764 REMARK 465 SER A 765 REMARK 465 ALA A 766 REMARK 465 VAL A 767 REMARK 465 LEU A 768 REMARK 465 LEU A 769 REMARK 465 SER A 770 REMARK 465 HIS A 771 REMARK 465 LYS A 772 REMARK 465 LYS A 773 REMARK 465 ARG A 774 REMARK 465 PHE A 775 REMARK 465 PRO A 776 REMARK 465 MET A 777 REMARK 465 PRO A 778 REMARK 465 GLU A 779 REMARK 465 ILE A 780 REMARK 465 SER A 904 REMARK 465 SER H 220 REMARK 465 CYS H 221 REMARK 465 ASP H 222 REMARK 465 LYS H 223 REMARK 465 THR H 224 REMARK 465 HIS H 225 REMARK 465 HIS H 226 REMARK 465 HIS H 227 REMARK 465 HIS H 228 REMARK 465 HIS H 229 REMARK 465 HIS H 230 REMARK 465 CYS L 219 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 LEU A 620 CG CD1 CD2 REMARK 470 SER A 654 OG REMARK 470 ARG A 678 CG CD NE CZ NH1 NH2 REMARK 470 LEU A 709 CG CD1 CD2 REMARK 470 SER A 786 OG REMARK 470 ARG A 876 CG CD NE CZ NH1 NH2 REMARK 470 LEU A 901 CG CD1 CD2 REMARK 470 LYS H 219 CG CD CE NZ REMARK 470 LEU L 9 CG CD1 CD2 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 O HOH A 1023 O HOH A 1151 1.74 REMARK 500 NZ LYS A 814 O HOH A 1001 1.77 REMARK 500 O HOH H 391 O HOH L 476 1.89 REMARK 500 O HOH H 516 O HOH H 571 1.90 REMARK 500 OG SER L 94 O HOH L 301 1.92 REMARK 500 O HOH L 331 O HOH L 507 1.95 REMARK 500 O SER A 800 O HOH A 1002 1.95 REMARK 500 OG SER A 789 O HOH A 1003 1.95 REMARK 500 OG SER H 177 O HOH H 301 1.96 REMARK 500 O HOH A 1146 O HOH A 1154 2.04 REMARK 500 CB LEU A 620 O HOH A 1160 2.05 REMARK 500 O HOH H 382 O HOH H 491 2.05 REMARK 500 O HOH H 471 O HOH L 476 2.07 REMARK 500 O HOH H 500 O HOH H 535 2.09 REMARK 500 CG ARG A 724 O HOH A 1134 2.10 REMARK 500 O HOH A 1147 O HOH A 1157 2.11 REMARK 500 O HOH H 356 O HOH H 501 2.12 REMARK 500 O HOH A 1062 O HOH A 1141 2.12 REMARK 500 NH2 ARG A 887 O HOH A 1004 2.12 REMARK 500 O HOH L 437 O HOH L 527 2.12 REMARK 500 OE1 GLN L 27 O HOH L 302 2.12 REMARK 500 OE1 GLU H 153 O HOH H 302 2.13 REMARK 500 O HOH H 501 O HOH H 558 2.13 REMARK 500 O HOH H 305 O HOH H 403 2.13 REMARK 500 O HOH L 306 O HOH L 523 2.13 REMARK 500 O HOH H 362 O HOH H 542 2.13 REMARK 500 O HOH A 1046 O HOH A 1171 2.15 REMARK 500 O HOH A 1126 O HOH A 1162 2.15 REMARK 500 O HOH H 513 O HOH L 507 2.16 REMARK 500 CB SER A 789 O HOH A 1003 2.16 REMARK 500 O HOH A 1006 O HOH A 1148 2.17 REMARK 500 O LEU H 194 O HOH H 303 2.17 REMARK 500 O HOH H 563 O HOH H 581 2.17 REMARK 500 NH2 ARG A 706 O HOH A 1005 2.17 REMARK 500 O HOH A 1021 O HOH A 1134 2.17 REMARK 500 OG1 THR H 140 O HOH H 304 2.17 REMARK 500 O HOH L 316 O HOH L 490 2.17 REMARK 500 NE ARG L 24 O HOH L 303 2.17 REMARK 500 O LEU L 30 O HOH A 1001 2.18 REMARK 500 O HOH L 475 O HOH L 502 2.18 REMARK 500 CD ARG A 724 O HOH A 1134 2.19 REMARK 500 O HOH L 456 O HOH L 517 2.19 REMARK 500 O VAL A 832 O HOH A 1006 2.19 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 H 154 C - N - CD ANGL. DEV. = -17.8 DEGREES REMARK 500 LEU L 38 CA - CB - CG ANGL. DEV. = -17.1 DEGREES REMARK 500 LEU L 88 CA - CB - CG ANGL. DEV. = 16.3 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 LYS A 814 -124.07 47.68 REMARK 500 SER A 892 -91.12 -114.73 REMARK 500 GLU A 902 2.80 -63.50 REMARK 500 GLU H 153 -166.51 -66.33 REMARK 500 PRO H 154 98.23 42.33 REMARK 500 LYS L 55 59.82 39.67 REMARK 500 VAL L 56 -49.50 82.84 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 GLU H 153 PRO H 154 -124.41 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 GLU H 153 -10.64 REMARK 500 REMARK 500 REMARK: NULL DBREF1 9UZB A 610 904 UNP A0A0M5KLS1_9VIRU DBREF2 9UZB A A0A0M5KLS1 610 904 DBREF 9UZB H 1 230 PDB 9UZB 9UZB 1 230 DBREF 9UZB L 1 219 PDB 9UZB 9UZB 1 219 SEQRES 1 A 295 LYS LYS PRO ILE ALA LEU ILE CYS ALA GLU LEU TYR LYS SEQRES 2 A 295 PRO PHE GLN ASP LEU PHE ALA ALA LEU PRO LYS ASP CYS SEQRES 3 A 295 SER GLU GLU CYS GLN THR LEU PHE GLU ASP ILE ARG ASN SEQRES 4 A 295 SER GLU SER HIS ALA SER ALA TRP SER SER ALA LEU ARG SEQRES 5 A 295 ILE LYS GLY VAL ALA TYR GLU GLY PHE PHE SER LEU THR SEQRES 6 A 295 ASN SER TRP ARG TYR ILE PRO GLU ASP LEU LYS PRO THR SEQRES 7 A 295 LEU GLY MET ALA ILE GLN THR VAL PHE PRO ASP LYS PHE SEQRES 8 A 295 GLU LYS PHE LEU GLU ARG THR HIS LEU HIS PRO GLU TYR SEQRES 9 A 295 ARG ASP PHE THR PRO ASP TYR LEU MET CYS ARG SER ARG SEQRES 10 A 295 ILE PHE LYS SER ASP ARG LEU ASN ARG SER ASN VAL ALA SEQRES 11 A 295 VAL SER ARG GLY LYS ASP LYS GLY GLY LYS LYS LYS GLU SEQRES 12 A 295 THR THR VAL ASN LYS ASP GLN ASP ASP ASP ALA GLN SER SEQRES 13 A 295 ALA VAL LEU LEU SER HIS LYS LYS ARG PHE PRO MET PRO SEQRES 14 A 295 GLU ILE ALA VAL GLN GLU VAL SER SER VAL SER ALA VAL SEQRES 15 A 295 VAL ASP ARG PHE LYS SER LYS SER SER GLU LYS GLY ARG SEQRES 16 A 295 PRO ILE ARG GLN GLU GLU SER ARG PRO LYS THR GLU SER SEQRES 17 A 295 MET GLN GLU ASP ILE GLU VAL ASP GLU LEU LEU ILE VAL SEQRES 18 A 295 GLU VAL GLY TYR GLN THR ASP ILE GLU GLY LYS VAL ILE SEQRES 19 A 295 SER ASP ILE GLU LYS TRP LYS GLY VAL VAL ASN LEU MET SEQRES 20 A 295 SER HIS LEU GLY ILE LYS VAL ASN VAL LEU THR CYS ALA SEQRES 21 A 295 ASP ASN SER GLN THR PRO ARG THR ASP TRP TRP ILE ASP SEQRES 22 A 295 GLU LYS TYR VAL ARG LEU LEU LEU ASN SER ILE SER TYR SEQRES 23 A 295 LEU PHE LYS GLU LEU LEU GLU ASN SER SEQRES 1 H 230 GLU VAL LYS LEU GLU GLU SER GLY GLY GLY LEU VAL ARG SEQRES 2 H 230 PRO GLY GLY SER ARG LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 H 230 PHE THR PHE SER SER TYR GLY MET GLN TRP VAL ARG GLN SEQRES 4 H 230 ALA PRO GLU LYS GLY LEU GLU TRP VAL ALA TYR ILE SER SEQRES 5 H 230 SER GLY SER ARG THR ILE TYR TYR ALA ASP THR VAL LYS SEQRES 6 H 230 GLY ARG PHE THR ILE SER ARG ASP ASN PRO LYS ASN THR SEQRES 7 H 230 LEU PHE LEU GLN MET THR SER LEU ARG SER GLU ASP THR SEQRES 8 H 230 ALA MET TYR TYR CYS ALA THR GLY TYR GLY GLY THR TRP SEQRES 9 H 230 PHE ALA TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 10 H 230 ALA ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 11 H 230 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU SEQRES 12 H 230 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR SEQRES 13 H 230 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS SEQRES 14 H 230 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER SEQRES 15 H 230 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY SEQRES 16 H 230 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER SEQRES 17 H 230 ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 18 H 230 ASP LYS THR HIS HIS HIS HIS HIS HIS SEQRES 1 L 219 GLN ILE VAL LEU SER GLN SER PRO LEU SER LEU PRO VAL SEQRES 2 L 219 SER LEU GLY ASP GLN ALA SER ILE SER CYS ARG SER SER SEQRES 3 L 219 GLN SER LEU LEU HIS SER ASN GLY ASN THR TYR LEU HIS SEQRES 4 L 219 TRP TYR LEU GLN LYS PRO GLY GLN SER PRO LYS LEU LEU SEQRES 5 L 219 ILE TYR LYS VAL SER ASN ARG PHE SER GLY VAL PRO ASP SEQRES 6 L 219 ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU SEQRES 7 L 219 LYS ILE SER ARG VAL GLU ALA GLU ASP LEU GLY VAL TYR SEQRES 8 L 219 PHE CYS SER GLN SER THR HIS VAL PRO TYR THR PHE GLY SEQRES 9 L 219 GLY GLY THR LYS LEU GLU ILE LYS ARG THR VAL ALA ALA SEQRES 10 L 219 PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU SEQRES 11 L 219 LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN SEQRES 12 L 219 PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP SEQRES 13 L 219 ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR SEQRES 14 L 219 GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER SEQRES 15 L 219 THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS SEQRES 16 L 219 VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER SEQRES 17 L 219 PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS FORMUL 4 HOH *714(H2 O) HELIX 1 AA1 PRO A 612 LEU A 620 1 9 HELIX 2 AA2 LEU A 620 LEU A 631 1 12 HELIX 3 AA3 PRO A 632 ASN A 648 1 17 HELIX 4 AA4 SER A 651 SER A 676 1 26 HELIX 5 AA5 PRO A 681 LYS A 685 5 5 HELIX 6 AA6 THR A 687 PHE A 696 1 10 HELIX 7 AA7 PHE A 696 THR A 707 1 12 HELIX 8 AA8 HIS A 710 PHE A 716 5 7 HELIX 9 AA9 SER A 787 GLY A 803 1 17 HELIX 10 AB1 ASP A 837 GLY A 860 1 24 HELIX 11 AB2 PRO A 875 TRP A 879 5 5 HELIX 12 AB3 ASP A 882 SER A 892 1 11 HELIX 13 AB4 SER A 892 GLU A 902 1 11 HELIX 14 AB5 THR H 28 TYR H 32 5 5 HELIX 15 AB6 ASP H 62 LYS H 65 5 4 HELIX 16 AB7 ASN H 74 LYS H 76 5 3 HELIX 17 AB8 ARG H 87 THR H 91 5 5 HELIX 18 AB9 SER H 132 LYS H 134 5 3 HELIX 19 AC1 SER H 161 ALA H 163 5 3 HELIX 20 AC2 SER H 192 LEU H 194 5 3 HELIX 21 AC3 LYS H 206 ASN H 209 5 4 HELIX 22 AC4 GLU L 84 LEU L 88 5 5 HELIX 23 AC5 SER L 126 SER L 132 1 7 HELIX 24 AC6 LYS L 188 LYS L 193 1 6 SHEET 1 AA1 5 GLN A 783 VAL A 785 0 SHEET 2 AA1 5 TYR A 720 ARG A 724 1 N CYS A 723 O VAL A 785 SHEET 3 AA1 5 GLU A 826 GLU A 831 -1 O LEU A 828 N MET A 722 SHEET 4 AA1 5 LYS A 862 CYS A 868 1 O ASN A 864 N ILE A 829 SHEET 5 AA1 5 ILE A 806 GLU A 810 -1 N GLU A 809 O VAL A 865 SHEET 1 AA2 4 LYS H 3 SER H 7 0 SHEET 2 AA2 4 ARG H 18 SER H 25 -1 O ALA H 23 N GLU H 5 SHEET 3 AA2 4 THR H 78 MET H 83 -1 O MET H 83 N ARG H 18 SHEET 4 AA2 4 PHE H 68 ASP H 73 -1 N SER H 71 O PHE H 80 SHEET 1 AA3 6 GLY H 10 VAL H 12 0 SHEET 2 AA3 6 THR H 112 VAL H 116 1 O THR H 115 N VAL H 12 SHEET 3 AA3 6 ALA H 92 THR H 98 -1 N TYR H 94 O THR H 112 SHEET 4 AA3 6 MET H 34 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AA3 6 LEU H 45 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AA3 6 ILE H 58 TYR H 60 -1 O TYR H 59 N TYR H 50 SHEET 1 AA4 4 GLY H 10 VAL H 12 0 SHEET 2 AA4 4 THR H 112 VAL H 116 1 O THR H 115 N VAL H 12 SHEET 3 AA4 4 ALA H 92 THR H 98 -1 N TYR H 94 O THR H 112 SHEET 4 AA4 4 TYR H 107 TRP H 108 -1 O TYR H 107 N THR H 98 SHEET 1 AA5 4 SER H 125 LEU H 129 0 SHEET 2 AA5 4 THR H 140 TYR H 150 -1 O LEU H 146 N PHE H 127 SHEET 3 AA5 4 TYR H 181 PRO H 190 -1 O LEU H 183 N VAL H 147 SHEET 4 AA5 4 VAL H 168 THR H 170 -1 N HIS H 169 O VAL H 186 SHEET 1 AA6 4 THR H 136 SER H 137 0 SHEET 2 AA6 4 THR H 140 TYR H 150 -1 O THR H 140 N SER H 137 SHEET 3 AA6 4 TYR H 181 PRO H 190 -1 O LEU H 183 N VAL H 147 SHEET 4 AA6 4 VAL H 174 LEU H 175 -1 N VAL H 174 O SER H 182 SHEET 1 AA7 3 THR H 156 TRP H 159 0 SHEET 2 AA7 3 TYR H 199 HIS H 205 -1 O ASN H 204 N THR H 156 SHEET 3 AA7 3 THR H 210 VAL H 216 -1 O VAL H 212 N VAL H 203 SHEET 1 AA8 4 LEU L 4 SER L 7 0 SHEET 2 AA8 4 ALA L 19 SER L 25 -1 O SER L 22 N SER L 7 SHEET 3 AA8 4 ASP L 75 ILE L 80 -1 O PHE L 76 N CYS L 23 SHEET 4 AA8 4 PHE L 67 SER L 72 -1 N SER L 68 O LYS L 79 SHEET 1 AA9 6 SER L 10 VAL L 13 0 SHEET 2 AA9 6 THR L 107 ILE L 111 1 O LYS L 108 N LEU L 11 SHEET 3 AA9 6 GLY L 89 GLN L 95 -1 N GLY L 89 O LEU L 109 SHEET 4 AA9 6 LEU L 38 GLN L 43 -1 N GLN L 43 O VAL L 90 SHEET 5 AA9 6 LYS L 50 TYR L 54 -1 O LEU L 52 N TRP L 40 SHEET 6 AA9 6 ASN L 58 ARG L 59 -1 O ASN L 58 N TYR L 54 SHEET 1 AB1 4 SER L 10 VAL L 13 0 SHEET 2 AB1 4 THR L 107 ILE L 111 1 O LYS L 108 N LEU L 11 SHEET 3 AB1 4 GLY L 89 GLN L 95 -1 N GLY L 89 O LEU L 109 SHEET 4 AB1 4 THR L 102 PHE L 103 -1 O THR L 102 N GLN L 95 SHEET 1 AB2 4 SER L 119 PHE L 123 0 SHEET 2 AB2 4 THR L 134 PHE L 144 -1 O LEU L 140 N PHE L 121 SHEET 3 AB2 4 TYR L 178 SER L 187 -1 O LEU L 184 N VAL L 137 SHEET 4 AB2 4 SER L 164 VAL L 168 -1 N GLN L 165 O THR L 183 SHEET 1 AB3 4 ALA L 158 LEU L 159 0 SHEET 2 AB3 4 LYS L 150 VAL L 155 -1 N VAL L 155 O ALA L 158 SHEET 3 AB3 4 VAL L 196 THR L 202 -1 O GLU L 200 N GLN L 152 SHEET 4 AB3 4 VAL L 210 ASN L 215 -1 O VAL L 210 N VAL L 201 SSBOND 1 CYS H 22 CYS H 96 1555 1555 2.08 SSBOND 2 CYS H 145 CYS H 201 1555 1555 2.03 SSBOND 3 CYS L 23 CYS L 93 1555 1555 2.09 SSBOND 4 CYS L 139 CYS L 199 1555 1555 2.03 CISPEP 1 PHE H 151 PRO H 152 0 -11.20 CISPEP 2 SER L 7 PRO L 8 0 -1.69 CISPEP 3 VAL L 99 PRO L 100 0 -1.80 CISPEP 4 TYR L 145 PRO L 146 0 -2.01 CRYST1 37.162 80.906 115.184 90.00 93.47 90.00 P 1 21 1 2 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 0.026909 0.000000 0.001632 0.00000 SCALE2 0.000000 0.012360 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008698 0.00000