HEADER CELL INVASION 02-OCT-25 9YIO TITLE CRYSTAL STRUCTURE OF 5B3 FAB IN COMPLEX WITH PVRIPR EGF7-8 COMPND MOL_ID: 1; COMPND 2 MOLECULE: PVRIPR EGF7-8; COMPND 3 CHAIN: B; COMPND 4 ENGINEERED: YES; COMPND 5 MUTATION: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: 5B3 KAPPA CHAIN; COMPND 8 CHAIN: C; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: 5B3 HEAVY CHAIN; COMPND 12 CHAIN: D; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PLASMODIUM VIVAX; SOURCE 3 ORGANISM_COMMON: MALARIA PARASITE P. VIVAX; SOURCE 4 ORGANISM_TAXID: 5855; SOURCE 5 GENE: PVP01_0816800; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 11 ORGANISM_COMMON: MOUSE; SOURCE 12 ORGANISM_TAXID: 10090; SOURCE 13 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 14 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 16 MOL_ID: 3; SOURCE 17 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 18 ORGANISM_COMMON: MOUSE; SOURCE 19 ORGANISM_TAXID: 10090; SOURCE 20 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 21 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 22 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS PLASMODIUM VIVAX, INVASION, ANTIBODY-ANTIGEN COMPLEX, CELL INVASION EXPDTA X-RAY DIFFRACTION AUTHOR X.XIAO,A.F.COWMAN,S.W.SCALLY REVDAT 1 04-FEB-26 9YIO 0 JRNL AUTH B.A.SEAGER,P.S.LIM,X.XIAO,K.H.LAI,L.B.FEUFACK-DONFACK, JRNL AUTH 2 S.DASS,N.C.JUNG,A.ABRAHAM,M.J.GRIGG,N.M.ANSTEY,T.WILLIAM, JRNL AUTH 3 J.SATTABONGKOT,A.LEIS,R.J.LONGLEY,M.T.DURAISINGH,J.POPOVICI, JRNL AUTH 4 D.W.WILSON,A.F.COWMAN,S.W.SCALLY JRNL TITL PTRAMP, CSS AND RIPR FORM A CONSERVED COMPLEX REQUIRED FOR JRNL TITL 2 MEROZOITE INVASION OF PLASMODIUM SPECIES INTO ERYTHROCYTES JRNL REF NAT COMMUN 2026 JRNL REFN ESSN 2041-1723 JRNL DOI 10.1038/S41467-026-68486-1 REMARK 2 REMARK 2 RESOLUTION. 2.08 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21_5207 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) : 2.08 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.64 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2 REMARK 3 NUMBER OF REFLECTIONS : 36935 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.206 REMARK 3 R VALUE (WORKING SET) : 0.204 REMARK 3 FREE R VALUE : 0.235 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.410 REMARK 3 FREE R VALUE TEST SET COUNT : 2000 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 48.6400 - 5.0100 0.98 2659 154 0.1914 0.1982 REMARK 3 2 5.0000 - 3.9700 0.99 2546 142 0.1592 0.1849 REMARK 3 3 3.9700 - 3.4700 0.99 2538 148 0.1790 0.2276 REMARK 3 4 3.4700 - 3.1500 1.00 2505 148 0.1957 0.2324 REMARK 3 5 3.1500 - 2.9300 1.00 2505 140 0.2093 0.2539 REMARK 3 6 2.9300 - 2.7600 0.99 2498 149 0.2173 0.2416 REMARK 3 7 2.7600 - 2.6200 1.00 2488 136 0.2239 0.2685 REMARK 3 8 2.6200 - 2.5000 1.00 2494 140 0.2180 0.2443 REMARK 3 9 2.5000 - 2.4100 1.00 2472 143 0.2296 0.2746 REMARK 3 10 2.4100 - 2.3200 1.00 2492 148 0.2352 0.2585 REMARK 3 11 2.3200 - 2.2500 1.00 2472 140 0.2484 0.3007 REMARK 3 12 2.2500 - 2.1900 1.00 2476 144 0.2690 0.3183 REMARK 3 13 2.1900 - 2.1300 0.99 2464 132 0.2828 0.2964 REMARK 3 14 2.1300 - 2.0800 0.94 2326 136 0.3063 0.3193 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) : 0.240 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.568 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 32.47 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.06 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 : 0.003 4066 REMARK 3 ANGLE : 0.615 5522 REMARK 3 CHIRALITY : 0.046 611 REMARK 3 PLANARITY : 0.005 702 REMARK 3 DIHEDRAL : 13.563 1474 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 6 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ( CHAIN B AND RESID 763:803 ) REMARK 3 ORIGIN FOR THE GROUP (A): -9.023 35.452 -59.409 REMARK 3 T TENSOR REMARK 3 T11: 0.3114 T22: 0.2843 REMARK 3 T33: 0.5077 T12: -0.0243 REMARK 3 T13: 0.0677 T23: 0.0340 REMARK 3 L TENSOR REMARK 3 L11: 2.7751 L22: 5.3101 REMARK 3 L33: 1.6717 L12: -3.9188 REMARK 3 L13: -1.3603 L23: 2.1196 REMARK 3 S TENSOR REMARK 3 S11: 0.2424 S12: 0.0123 S13: 0.8408 REMARK 3 S21: -0.6304 S22: -0.0619 S23: -0.7484 REMARK 3 S31: -0.4032 S32: -0.0107 S33: -0.1985 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: ( CHAIN B AND RESID 804:843 ) REMARK 3 ORIGIN FOR THE GROUP (A): -8.805 11.578 -72.689 REMARK 3 T TENSOR REMARK 3 T11: 0.5794 T22: 0.7278 REMARK 3 T33: 0.3787 T12: -0.0459 REMARK 3 T13: -0.1029 T23: 0.0332 REMARK 3 L TENSOR REMARK 3 L11: 8.0299 L22: 8.5204 REMARK 3 L33: 9.5472 L12: 2.3013 REMARK 3 L13: 1.4743 L23: 5.7198 REMARK 3 S TENSOR REMARK 3 S11: 0.0555 S12: 1.6755 S13: -0.1310 REMARK 3 S21: -1.2401 S22: -0.1184 S23: 0.4886 REMARK 3 S31: 0.4664 S32: -0.3894 S33: 0.1084 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: ( CHAIN C AND RESID 1:107 ) REMARK 3 ORIGIN FOR THE GROUP (A): -4.814 10.524 -37.456 REMARK 3 T TENSOR REMARK 3 T11: 0.1993 T22: 0.1613 REMARK 3 T33: 0.3951 T12: 0.0147 REMARK 3 T13: -0.0075 T23: 0.0464 REMARK 3 L TENSOR REMARK 3 L11: 3.3307 L22: 2.8116 REMARK 3 L33: 4.7361 L12: -0.2291 REMARK 3 L13: 0.8617 L23: -0.1038 REMARK 3 S TENSOR REMARK 3 S11: -0.0798 S12: -0.1332 S13: -0.0772 REMARK 3 S21: 0.1508 S22: -0.0867 S23: -0.6271 REMARK 3 S31: 0.1794 S32: 0.3554 S33: 0.1530 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: ( CHAIN C AND RESID 108:209 ) REMARK 3 ORIGIN FOR THE GROUP (A): -20.860 9.394 -6.368 REMARK 3 T TENSOR REMARK 3 T11: 0.7022 T22: 1.3339 REMARK 3 T33: 0.8004 T12: 0.0182 REMARK 3 T13: -0.1252 T23: 0.5863 REMARK 3 L TENSOR REMARK 3 L11: 5.1761 L22: 1.5068 REMARK 3 L33: 3.9207 L12: -0.2308 REMARK 3 L13: -2.3393 L23: 0.0773 REMARK 3 S TENSOR REMARK 3 S11: -0.3423 S12: -2.5081 S13: -1.6587 REMARK 3 S21: 0.5122 S22: 0.4610 S23: 0.1800 REMARK 3 S31: 0.4789 S32: -0.1125 S33: -0.0478 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: ( CHAIN D AND RESID 1:113 ) REMARK 3 ORIGIN FOR THE GROUP (A): -20.987 24.259 -43.142 REMARK 3 T TENSOR REMARK 3 T11: 0.1689 T22: 0.1385 REMARK 3 T33: 0.2583 T12: 0.0199 REMARK 3 T13: -0.0465 T23: 0.0329 REMARK 3 L TENSOR REMARK 3 L11: 3.0981 L22: 1.0751 REMARK 3 L33: 3.7772 L12: 0.2990 REMARK 3 L13: -2.8103 L23: 0.0488 REMARK 3 S TENSOR REMARK 3 S11: 0.0329 S12: 0.0304 S13: 0.1657 REMARK 3 S21: 0.0614 S22: -0.0128 S23: -0.0804 REMARK 3 S31: -0.1523 S32: -0.0061 S33: 0.0058 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: ( CHAIN D AND RESID 114:214 ) REMARK 3 ORIGIN FOR THE GROUP (A): -20.501 25.148 -6.955 REMARK 3 T TENSOR REMARK 3 T11: 0.5807 T22: 0.9948 REMARK 3 T33: 0.4220 T12: 0.0026 REMARK 3 T13: -0.0845 T23: -0.1798 REMARK 3 L TENSOR REMARK 3 L11: 4.4766 L22: 2.6362 REMARK 3 L33: 6.6771 L12: -0.9165 REMARK 3 L13: 2.6284 L23: -0.8428 REMARK 3 S TENSOR REMARK 3 S11: -0.4402 S12: -2.0789 S13: 0.7230 REMARK 3 S21: 0.7846 S22: 0.2369 S23: -0.4310 REMARK 3 S31: -0.6912 S32: 0.0711 S33: 0.2093 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 9YIO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-OCT-25. REMARK 100 THE DEPOSITION ID IS D_1000300627. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 03-AUG-24 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 4.4 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON REMARK 200 BEAMLINE : MX2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.95365 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 : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36982 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.078 REMARK 200 RESOLUTION RANGE LOW (A) : 48.640 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 200 DATA REDUNDANCY : 6.300 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 7.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.08 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.13 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: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 53.69 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M (NH4)2SO4, 20% PEG-3,350 AND 0.1M REMARK 280 SODIUM ACETATE BUFFER PH 4.4, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 295K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -X+1/2,Y+1/2,-Z REMARK 290 4555 X+1/2,-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 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 40.13500 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.87300 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 40.13500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.87300 REMARK 290 SMTRY3 4 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: B, C, D 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 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH C 369 LIES ON A SPECIAL POSITION. REMARK 375 HOH C 370 LIES ON A SPECIAL POSITION. 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 ASN C 211 REMARK 465 ARG C 212 REMARK 465 GLY C 213 REMARK 465 GLU C 214 REMARK 465 SER D 215 REMARK 465 CYS D 216 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 D 471 O HOH D 517 2.14 REMARK 500 O HOH B 1013 O HOH B 1050 2.18 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 HIS B 762 -1.94 80.69 REMARK 500 ASN B 790 -7.85 76.87 REMARK 500 ASP B 815 49.26 -88.80 REMARK 500 TRP C 47 -51.81 -126.79 REMARK 500 THR C 51 -52.95 73.73 REMARK 500 ALA C 84 -177.47 -174.82 REMARK 500 SER C 92 -179.22 -172.95 REMARK 500 TRP C 96 3.21 91.12 REMARK 500 LYS C 190 -45.98 -136.90 REMARK 500 PRO C 204 108.58 -47.24 REMARK 500 SER D 132 89.29 -155.27 REMARK 500 ASP D 144 62.77 63.97 REMARK 500 SER D 187 31.99 -85.26 REMARK 500 PRO D 213 -175.04 -69.68 REMARK 500 REMARK 500 REMARK: NULL DBREF1 9YIO B 764 843 UNP A0A564ZTL5_PLAVI DBREF2 9YIO B A0A564ZTL5 764 843 DBREF 9YIO C 1 214 PDB 9YIO 9YIO 1 214 DBREF 9YIO D 1 216 PDB 9YIO 9YIO 1 216 SEQADV 9YIO GLY B 761 UNP A0A564ZTL EXPRESSION TAG SEQADV 9YIO HIS B 762 UNP A0A564ZTL EXPRESSION TAG SEQADV 9YIO MET B 763 UNP A0A564ZTL EXPRESSION TAG SEQADV 9YIO GLN B 767 UNP A0A564ZTL ASN 767 ENGINEERED MUTATION SEQADV 9YIO GLN B 780 UNP A0A564ZTL ASN 780 ENGINEERED MUTATION SEQRES 1 B 83 GLY HIS MET TYR CYS LYS GLN VAL THR CYS LYS GLU ASN SEQRES 2 B 83 GLU ILE CYS LYS VAL VAL GLN ASN THR PRO THR CYS GLU SEQRES 3 B 83 CYS LYS GLU ASN LEU LYS ARG ASP SER ASN ASN GLU CYS SEQRES 4 B 83 VAL PHE ASN ASN MET CYS LEU VAL ASN LYS GLY ASN CYS SEQRES 5 B 83 PRO ILE ASP SER GLU CYS ILE TYR HIS GLU LYS LYS ARG SEQRES 6 B 83 HIS GLN CYS LEU CYS HIS LYS LYS GLY LEU VAL ALA ILE SEQRES 7 B 83 ASN GLY LYS CYS VAL SEQRES 1 C 213 GLN ILE VAL LEU SER GLN SER PRO ALA ILE LEU SER ALA SEQRES 2 C 213 SER PRO GLY GLU LYS VAL THR MET THR CYS ARG ALA SER SEQRES 3 C 213 SER SER VAL ASN TYR MET HIS TRP TYR GLN GLN LYS PRO SEQRES 4 C 213 GLY SER SER PRO LYS PRO TRP ILE TYR ALA THR SER ASN SEQRES 5 C 213 LEU ALA SER GLY VAL PRO THR ARG PHE SER GLY SER GLY SEQRES 6 C 213 SER GLY THR SER TYR SER LEU THR ILE SER ARG VAL GLU SEQRES 7 C 213 ALA GLU ASP ALA ALA THR TYR TYR CYS GLN GLN TRP SER SEQRES 8 C 213 PRO ASN PRO TRP THR PHE GLY GLY GLY THR LYS LEU GLU SEQRES 9 C 213 ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE SEQRES 10 C 213 PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SER SEQRES 11 C 213 VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA SEQRES 12 C 213 LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY SEQRES 13 C 213 ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SEQRES 14 C 213 SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS SEQRES 15 C 213 ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL SEQRES 16 C 213 THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE SEQRES 17 C 213 ASN ASN ARG GLY GLU SEQRES 1 D 224 GLU VAL GLN VAL GLN GLN SER GLY THR GLU LEU VAL ARG SEQRES 2 D 224 PRO GLY ALA VAL VAL LYS LEU SER CYS ILE VAL SER GLY SEQRES 3 D 224 PHE SER ILE LYS ASP TYR TYR ILE HIS TRP VAL LYS GLN SEQRES 4 D 224 ARG PRO GLU LYS GLY LEU GLU TRP ILE GLY TRP ILE ASP SEQRES 5 D 224 PRO GLU ASN GLY LYS THR ILE TYR ASP PRO LYS PHE GLN SEQRES 6 D 224 GLY LYS ALA SER ILE THR ALA ASP ARG SER PHE ASN THR SEQRES 7 D 224 ALA TYR LEU HIS ILE SER ARG PRO THR SER GLU ASP THR SEQRES 8 D 224 ALA VAL TYR TYR CYS ALA ARG SER TYR TYR TYR GLY SER SEQRES 9 D 224 SER ASP ALA MET ASP ASN TRP GLY GLN GLY THR SER VAL SEQRES 10 D 224 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 D 224 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12 D 224 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 D 224 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 D 224 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 D 224 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 D 224 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17 D 224 LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO SEQRES 18 D 224 LYS SER CYS HET GOL B 901 6 HET GOL D 301 6 HET GOL D 302 6 HET SO4 D 303 5 HET SO4 D 304 5 HETNAM GOL GLYCEROL HETNAM SO4 SULFATE ION HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 4 GOL 3(C3 H8 O3) FORMUL 7 SO4 2(O4 S 2-) FORMUL 9 HOH *238(H2 O) HELIX 1 AA1 ASN B 803 CYS B 812 5 10 HELIX 2 AA2 GLU C 79 ALA C 83 5 5 HELIX 3 AA3 GLU C 123 GLY C 128 1 6 HELIX 4 AA4 LYS C 183 LYS C 188 1 6 HELIX 5 AA5 SER D 28 TYR D 32 5 5 HELIX 6 AA6 THR D 83 THR D 87 5 5 HELIX 7 AA7 SER D 127 THR D 131 5 5 HELIX 8 AA8 SER D 156 ALA D 158 5 3 HELIX 9 AA9 PRO D 185 LEU D 189 5 5 HELIX 10 AB1 LYS D 201 ASN D 204 5 4 SHEET 1 AA1 2 GLU B 774 VAL B 779 0 SHEET 2 AA1 2 THR B 782 CYS B 787 -1 O THR B 784 N LYS B 777 SHEET 1 AA2 2 LEU B 791 ARG B 793 0 SHEET 2 AA2 2 CYS B 799 PHE B 801 -1 O VAL B 800 N LYS B 792 SHEET 1 AA3 2 SER B 816 ILE B 819 0 SHEET 2 AA3 2 GLN B 827 CYS B 830 -1 O LEU B 829 N GLU B 817 SHEET 1 AA4 2 VAL B 836 ALA B 837 0 SHEET 2 AA4 2 CYS B 842 VAL B 843 -1 O VAL B 843 N VAL B 836 SHEET 1 AA5 4 LEU C 4 SER C 7 0 SHEET 2 AA5 4 VAL C 19 ALA C 25 -1 O ARG C 24 N SER C 5 SHEET 3 AA5 4 SER C 70 ILE C 75 -1 O LEU C 73 N MET C 21 SHEET 4 AA5 4 PHE C 62 SER C 67 -1 N SER C 63 O THR C 74 SHEET 1 AA6 6 ILE C 10 ALA C 13 0 SHEET 2 AA6 6 THR C 102 ILE C 106 1 O GLU C 105 N LEU C 11 SHEET 3 AA6 6 ALA C 84 TRP C 91 -1 N TYR C 86 O THR C 102 SHEET 4 AA6 6 TYR C 32 GLN C 38 -1 N HIS C 34 O GLN C 89 SHEET 5 AA6 6 LYS C 45 TYR C 49 -1 O LYS C 45 N GLN C 37 SHEET 6 AA6 6 ASN C 53 LEU C 54 -1 O ASN C 53 N TYR C 49 SHEET 1 AA7 4 PHE C 116 PHE C 118 0 SHEET 2 AA7 4 THR C 129 PHE C 139 -1 O LEU C 135 N PHE C 116 SHEET 3 AA7 4 TYR C 173 SER C 182 -1 O LEU C 179 N VAL C 132 SHEET 4 AA7 4 SER C 159 VAL C 163 -1 N GLN C 160 O THR C 178 SHEET 1 AA8 4 ALA C 153 GLN C 155 0 SHEET 2 AA8 4 LYS C 145 VAL C 150 -1 N TRP C 148 O GLN C 155 SHEET 3 AA8 4 TYR C 192 THR C 197 -1 O ALA C 193 N LYS C 149 SHEET 4 AA8 4 VAL C 205 PHE C 209 -1 O VAL C 205 N VAL C 196 SHEET 1 AA9 4 GLN D 3 GLY D 8 0 SHEET 2 AA9 4 VAL D 18 SER D 25 -1 O ILE D 23 N GLN D 5 SHEET 3 AA9 4 THR D 77 ILE D 82 -1 O LEU D 80 N LEU D 20 SHEET 4 AA9 4 ALA D 67 ASP D 72 -1 N THR D 70 O TYR D 79 SHEET 1 AB1 6 LEU D 11 VAL D 12 0 SHEET 2 AB1 6 THR D 107 VAL D 111 1 O THR D 110 N VAL D 12 SHEET 3 AB1 6 ALA D 88 SER D 95 -1 N ALA D 88 O VAL D 109 SHEET 4 AB1 6 TYR D 33 GLN D 39 -1 N HIS D 35 O ALA D 93 SHEET 5 AB1 6 LEU D 45 ILE D 51 -1 O GLU D 46 N LYS D 38 SHEET 6 AB1 6 THR D 57 TYR D 59 -1 O ILE D 58 N TRP D 50 SHEET 1 AB2 4 SER D 120 LEU D 124 0 SHEET 2 AB2 4 ALA D 136 TYR D 145 -1 O GLY D 139 N LEU D 124 SHEET 3 AB2 4 TYR D 176 VAL D 184 -1 O VAL D 184 N ALA D 136 SHEET 4 AB2 4 VAL D 163 THR D 165 -1 N HIS D 164 O VAL D 181 SHEET 1 AB3 4 SER D 120 LEU D 124 0 SHEET 2 AB3 4 ALA D 136 TYR D 145 -1 O GLY D 139 N LEU D 124 SHEET 3 AB3 4 TYR D 176 VAL D 184 -1 O VAL D 184 N ALA D 136 SHEET 4 AB3 4 VAL D 169 LEU D 170 -1 N VAL D 169 O SER D 177 SHEET 1 AB4 3 THR D 151 TRP D 154 0 SHEET 2 AB4 3 ILE D 195 HIS D 200 -1 O ASN D 197 N SER D 153 SHEET 3 AB4 3 THR D 205 LYS D 210 -1 O THR D 205 N HIS D 200 SSBOND 1 CYS B 765 CYS B 776 1555 1555 2.05 SSBOND 2 CYS B 770 CYS B 785 1555 1555 2.05 SSBOND 3 CYS B 787 CYS B 799 1555 1555 2.05 SSBOND 4 CYS B 805 CYS B 818 1555 1555 2.04 SSBOND 5 CYS B 812 CYS B 828 1555 1555 2.04 SSBOND 6 CYS B 830 CYS B 842 1555 1555 2.04 SSBOND 7 CYS C 23 CYS C 88 1555 1555 2.05 SSBOND 8 CYS C 134 CYS C 194 1555 1555 2.03 SSBOND 9 CYS D 22 CYS D 92 1555 1555 2.04 SSBOND 10 CYS D 140 CYS D 196 1555 1555 2.03 CISPEP 1 SER C 7 PRO C 8 0 -6.84 CISPEP 2 TYR C 140 PRO C 141 0 1.58 CISPEP 3 PHE D 146 PRO D 147 0 -5.78 CISPEP 4 GLU D 148 PRO D 149 0 2.21 CRYST1 80.270 81.746 92.149 90.00 90.00 90.00 P 21 21 2 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 0.012458 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012233 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010852 0.00000