HEADER IMMUNE SYSTEM 18-JUL-25 9VX3 TITLE CRYSTAL STRUCTURE OF THE PEPTIDE-BOUND FORM OF HISMAB-1 FV-CLASP COMPND MOL_ID: 1; COMPND 2 MOLECULE: HISMAB-1VH(S112C),SERINE/THREONINE-PROTEIN KINASE 4 18KDA COMPND 3 SUBUNIT; COMPND 4 CHAIN: A, D; COMPND 5 SYNONYM: MST1/C; COMPND 6 ENGINEERED: YES; COMPND 7 OTHER_DETAILS: HISMAB-1VH(S112C)-SARAH; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: HISMAB-1VL,SERINE/THREONINE-PROTEIN KINASE 4 18KDA SUBUNIT; COMPND 10 CHAIN: B, E; COMPND 11 SYNONYM: MST1/C; COMPND 12 ENGINEERED: YES; COMPND 13 MUTATION: YES; COMPND 14 OTHER_DETAILS: HISMAB-1VL-SARAH(S37C); COMPND 15 MOL_ID: 3; COMPND 16 MOLECULE: POLYHISTIDINE PEPTIDE; COMPND 17 CHAIN: C, F; COMPND 18 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS, HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 10090, 9606; SOURCE 5 GENE: STK4, KRS2, MST1; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: MUS MUSCULUS, HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 10090, 9606; SOURCE 12 GENE: STK4, KRS2, MST1; SOURCE 13 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 15 MOL_ID: 3; SOURCE 16 SYNTHETIC: YES; SOURCE 17 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 18 ORGANISM_TAXID: 32630 KEYWDS HISMAB-1, FV-CLASP, HIS-TAG, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR N.HITOMI,A.HARADA-HIKITA,T.ARIMORI REVDAT 1 17-DEC-25 9VX3 0 JRNL AUTH N.HITOMI,S.HOSHI,M.K.KANEKO,R.KATO,K.IWASAKI,J.TAKAGI, JRNL AUTH 2 Y.KATO,A.HARADA-HIKITA,T.ARIMORI JRNL TITL FUNCTIONAL AND STRUCTURAL CHARACTERIZATION OF A NOVEL JRNL TITL 2 ANTI-HIS-TAG ANTIBODY, HISMAB-1. JRNL REF J.MOL.BIOL. 69574 2025 JRNL REFN ESSN 1089-8638 JRNL PMID 41349762 JRNL DOI 10.1016/J.JMB.2025.169574 REMARK 2 REMARK 2 RESOLUTION. 2.39 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) : 2.39 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.57 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0 REMARK 3 NUMBER OF REFLECTIONS : 27174 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.198 REMARK 3 R VALUE (WORKING SET) : 0.196 REMARK 3 FREE R VALUE : 0.237 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1358 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 39.5700 - 5.1500 0.98 2641 138 0.1622 0.1751 REMARK 3 2 5.1500 - 4.0900 0.99 2604 137 0.1459 0.1796 REMARK 3 3 4.0900 - 3.5800 0.99 2599 137 0.1849 0.2354 REMARK 3 4 3.5800 - 3.2500 0.99 2589 136 0.2072 0.2937 REMARK 3 5 3.2500 - 3.0200 0.99 2560 135 0.2478 0.3015 REMARK 3 6 3.0200 - 2.8400 0.99 2583 136 0.2545 0.3235 REMARK 3 7 2.8400 - 2.7000 1.00 2599 137 0.2627 0.3045 REMARK 3 8 2.7000 - 2.5800 1.00 2557 134 0.3246 0.3890 REMARK 3 9 2.5800 - 2.4800 1.00 2594 137 0.3536 0.3613 REMARK 3 10 2.4800 - 2.3900 0.96 2490 131 0.3625 0.3996 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 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) : 0.427 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.895 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 69.00 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 79.99 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 : 0.006 5320 REMARK 3 ANGLE : 0.819 7176 REMARK 3 CHIRALITY : 0.045 781 REMARK 3 PLANARITY : 0.005 918 REMARK 3 DIHEDRAL : 13.676 1986 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 12 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ( CHAIN A AND RESID 1:103 ) REMARK 3 ORIGIN FOR THE GROUP (A): 20.147 30.516 15.570 REMARK 3 T TENSOR REMARK 3 T11: 0.4084 T22: 0.4363 REMARK 3 T33: 0.4062 T12: 0.1091 REMARK 3 T13: 0.0428 T23: 0.0023 REMARK 3 L TENSOR REMARK 3 L11: 3.5880 L22: 7.1031 REMARK 3 L33: 2.4016 L12: 3.0529 REMARK 3 L13: 0.4378 L23: 0.6456 REMARK 3 S TENSOR REMARK 3 S11: 0.0843 S12: 0.0072 S13: -0.0758 REMARK 3 S21: 0.0259 S22: -0.0985 S23: 0.2273 REMARK 3 S31: 0.0255 S32: -0.1464 S33: 0.0123 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: ( CHAIN A AND RESID 104:164 ) REMARK 3 ORIGIN FOR THE GROUP (A): 7.721 24.126 -10.608 REMARK 3 T TENSOR REMARK 3 T11: 0.5612 T22: 0.6359 REMARK 3 T33: 0.7517 T12: -0.0766 REMARK 3 T13: -0.0198 T23: -0.0120 REMARK 3 L TENSOR REMARK 3 L11: 3.0599 L22: 4.6711 REMARK 3 L33: 0.1382 L12: 3.3499 REMARK 3 L13: 0.4839 L23: 0.5583 REMARK 3 S TENSOR REMARK 3 S11: -0.4861 S12: 0.0613 S13: 0.2101 REMARK 3 S21: -0.5393 S22: 0.5884 S23: 0.6935 REMARK 3 S31: 0.1121 S32: -0.5679 S33: -0.1223 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: ( CHAIN B AND RESID 1:100 ) REMARK 3 ORIGIN FOR THE GROUP (A): 14.409 50.857 9.749 REMARK 3 T TENSOR REMARK 3 T11: 0.6442 T22: 0.4894 REMARK 3 T33: 0.6849 T12: 0.1488 REMARK 3 T13: -0.0280 T23: -0.0338 REMARK 3 L TENSOR REMARK 3 L11: 3.1018 L22: 5.9005 REMARK 3 L33: 3.8626 L12: 0.4720 REMARK 3 L13: 0.5275 L23: 0.0536 REMARK 3 S TENSOR REMARK 3 S11: 0.1203 S12: 0.2688 S13: 0.2916 REMARK 3 S21: -0.5242 S22: -0.2357 S23: 0.9688 REMARK 3 S31: -0.6504 S32: -0.3556 S33: 0.0768 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: ( CHAIN B AND RESID 101:119 ) REMARK 3 ORIGIN FOR THE GROUP (A): 10.647 51.739 -10.386 REMARK 3 T TENSOR REMARK 3 T11: 0.7744 T22: 0.9151 REMARK 3 T33: 0.8256 T12: 0.0978 REMARK 3 T13: -0.0527 T23: 0.1030 REMARK 3 L TENSOR REMARK 3 L11: 4.6584 L22: 0.5736 REMARK 3 L33: 2.5794 L12: -1.2004 REMARK 3 L13: 3.3209 L23: -0.7955 REMARK 3 S TENSOR REMARK 3 S11: -0.8006 S12: 0.3431 S13: 0.6413 REMARK 3 S21: 0.7155 S22: 0.7473 S23: -0.1645 REMARK 3 S31: -0.7508 S32: -0.9867 S33: -0.0391 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: ( CHAIN B AND RESID 120:158 ) REMARK 3 ORIGIN FOR THE GROUP (A): 12.809 27.706 -7.359 REMARK 3 T TENSOR REMARK 3 T11: 0.9946 T22: 0.7061 REMARK 3 T33: 0.7572 T12: -0.2798 REMARK 3 T13: 0.0312 T23: -0.0305 REMARK 3 L TENSOR REMARK 3 L11: 7.2651 L22: 7.7428 REMARK 3 L33: 1.4761 L12: 8.6508 REMARK 3 L13: -2.8275 L23: -4.1661 REMARK 3 S TENSOR REMARK 3 S11: 0.5740 S12: -0.6533 S13: 0.5202 REMARK 3 S21: 1.2613 S22: -0.6143 S23: 0.5239 REMARK 3 S31: -0.0489 S32: 0.0521 S33: 0.1482 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: ( CHAIN C AND RESID 1:6 ) REMARK 3 ORIGIN FOR THE GROUP (A): 20.601 43.635 26.033 REMARK 3 T TENSOR REMARK 3 T11: 0.6135 T22: 0.7271 REMARK 3 T33: 0.7431 T12: 0.0190 REMARK 3 T13: 0.0051 T23: -0.0372 REMARK 3 L TENSOR REMARK 3 L11: 3.5189 L22: 8.4554 REMARK 3 L33: 3.9764 L12: 3.8600 REMARK 3 L13: -3.6108 L23: -4.4394 REMARK 3 S TENSOR REMARK 3 S11: 0.1540 S12: -0.9846 S13: -1.6784 REMARK 3 S21: 0.2875 S22: -1.0524 S23: 0.6185 REMARK 3 S31: -0.3075 S32: 0.1653 S33: 0.8001 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: ( CHAIN D AND RESID 1:82 ) REMARK 3 ORIGIN FOR THE GROUP (A): 9.301 31.507 -45.663 REMARK 3 T TENSOR REMARK 3 T11: 0.6031 T22: 0.6836 REMARK 3 T33: 0.5568 T12: 0.0885 REMARK 3 T13: -0.0839 T23: 0.0031 REMARK 3 L TENSOR REMARK 3 L11: 3.4903 L22: 5.0035 REMARK 3 L33: 3.6649 L12: 1.7707 REMARK 3 L13: -0.5751 L23: -0.5266 REMARK 3 S TENSOR REMARK 3 S11: 0.2181 S12: -0.0184 S13: 0.2372 REMARK 3 S21: -0.2510 S22: -0.2401 S23: 0.7392 REMARK 3 S31: -0.0866 S32: -0.2947 S33: 0.0640 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: ( CHAIN D AND RESID 83:124 ) REMARK 3 ORIGIN FOR THE GROUP (A): 13.094 21.442 -37.833 REMARK 3 T TENSOR REMARK 3 T11: 0.7264 T22: 0.7580 REMARK 3 T33: 0.7340 T12: 0.0395 REMARK 3 T13: -0.0393 T23: 0.0632 REMARK 3 L TENSOR REMARK 3 L11: 0.5744 L22: 6.9530 REMARK 3 L33: 2.5660 L12: 0.7188 REMARK 3 L13: -0.1409 L23: -2.8389 REMARK 3 S TENSOR REMARK 3 S11: 0.2010 S12: 0.0502 S13: -0.3606 REMARK 3 S21: -0.0549 S22: -0.1947 S23: 0.0878 REMARK 3 S31: 0.0023 S32: 0.0076 S33: -0.0649 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: ( CHAIN D AND RESID 125:164 ) REMARK 3 ORIGIN FOR THE GROUP (A): 22.107 21.619 -14.792 REMARK 3 T TENSOR REMARK 3 T11: 0.6777 T22: 0.6186 REMARK 3 T33: 0.6813 T12: -0.1342 REMARK 3 T13: 0.0344 T23: -0.0335 REMARK 3 L TENSOR REMARK 3 L11: 3.5719 L22: 4.8264 REMARK 3 L33: -0.5459 L12: 5.2345 REMARK 3 L13: 2.8058 L23: 2.0670 REMARK 3 S TENSOR REMARK 3 S11: 0.2836 S12: -0.0731 S13: 0.1120 REMARK 3 S21: 1.0896 S22: -0.3430 S23: 0.2184 REMARK 3 S31: 0.0326 S32: 0.0484 S33: 0.0308 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: ( CHAIN E AND RESID 0:102 ) REMARK 3 ORIGIN FOR THE GROUP (A): 30.341 41.008 -43.476 REMARK 3 T TENSOR REMARK 3 T11: 0.6742 T22: 0.7642 REMARK 3 T33: 0.4590 T12: -0.1006 REMARK 3 T13: 0.0503 T23: -0.0010 REMARK 3 L TENSOR REMARK 3 L11: 3.1837 L22: 3.4526 REMARK 3 L33: 7.6533 L12: 0.7572 REMARK 3 L13: 1.3474 L23: 0.0494 REMARK 3 S TENSOR REMARK 3 S11: 0.1668 S12: -0.3717 S13: 0.1618 REMARK 3 S21: -0.0553 S22: -0.1002 S23: -0.3016 REMARK 3 S31: -0.6188 S32: 0.9700 S33: -0.0641 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: ( CHAIN E AND RESID 103:157 ) REMARK 3 ORIGIN FOR THE GROUP (A): 21.820 28.502 -22.604 REMARK 3 T TENSOR REMARK 3 T11: 0.6041 T22: 0.6366 REMARK 3 T33: 0.6688 T12: 0.0026 REMARK 3 T13: -0.0193 T23: 0.0206 REMARK 3 L TENSOR REMARK 3 L11: 2.6668 L22: 7.0332 REMARK 3 L33: 1.8880 L12: 3.8692 REMARK 3 L13: 1.2299 L23: 1.4543 REMARK 3 S TENSOR REMARK 3 S11: -0.1987 S12: 0.5141 S13: 0.3362 REMARK 3 S21: 0.0264 S22: 0.4908 S23: 0.5790 REMARK 3 S31: -0.1924 S32: 0.2662 S33: -0.2778 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: ( CHAIN F AND RESID 1:6 ) REMARK 3 ORIGIN FOR THE GROUP (A): 17.317 40.951 -57.153 REMARK 3 T TENSOR REMARK 3 T11: 1.0452 T22: 0.6341 REMARK 3 T33: 0.6810 T12: 0.1358 REMARK 3 T13: -0.0661 T23: 0.0603 REMARK 3 L TENSOR REMARK 3 L11: 4.5991 L22: 4.8384 REMARK 3 L33: 5.2687 L12: -0.4313 REMARK 3 L13: -3.2094 L23: 4.1081 REMARK 3 S TENSOR REMARK 3 S11: 0.3815 S12: 1.0998 S13: -0.3120 REMARK 3 S21: -0.7650 S22: -1.1086 S23: 0.5871 REMARK 3 S31: -2.8238 S32: -0.1556 S33: 0.4944 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 9VX3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-JUL-25. REMARK 100 THE DEPOSITION ID IS D_1300061363. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-JUL-22 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 : BL44XU REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9 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 : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 94322 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.390 REMARK 200 RESOLUTION RANGE LOW (A) : 48.130 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0 REMARK 200 DATA REDUNDANCY : 3.470 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.06300 REMARK 200 FOR THE DATA SET : 11.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.39 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.54 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.3 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 1.04300 REMARK 200 FOR SHELL : 1.210 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 (%): 44.91 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 16% (W/V) POLYETHYLENE GLYCOL 3350, REMARK 280 0.1M HEPES (PH 7.0), 0.2M MGCL2, 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 34.75600 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5840 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 16320 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -45.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5790 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 16670 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F 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 A -1 REMARK 465 ARG A 0 REMARK 465 SER A 115 REMARK 465 ASP A 116 REMARK 465 TYR A 117 REMARK 465 GLY A 165 REMARK 465 THR A 166 REMARK 465 LEU A 167 REMARK 465 LEU A 168 REMARK 465 GLY A 169 REMARK 465 GLY B -1 REMARK 465 ARG B 0 REMARK 465 GLY B 109 REMARK 465 SER B 110 REMARK 465 ASP B 111 REMARK 465 TYR B 112 REMARK 465 GLU B 113 REMARK 465 PHE B 114 REMARK 465 LYS B 159 REMARK 465 GLY D -1 REMARK 465 ARG D 0 REMARK 465 GLY D 42 REMARK 465 LYS D 43 REMARK 465 GLY D 114 REMARK 465 GLY D 165 REMARK 465 THR D 166 REMARK 465 LEU D 167 REMARK 465 LEU D 168 REMARK 465 GLY D 169 REMARK 465 GLY E -1 REMARK 465 ARG E 108 REMARK 465 GLY E 109 REMARK 465 SER E 110 REMARK 465 ASP E 111 REMARK 465 TYR E 112 REMARK 465 GLU E 113 REMARK 465 PHE E 114 REMARK 465 ALA E 158 REMARK 465 LYS E 159 REMARK 480 REMARK 480 ZERO OCCUPANCY ATOM REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 480 M RES C SSEQI ATOMS REMARK 480 LYS B 103 CE NZ REMARK 480 LYS E 103 CE NZ 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 ALA A 99 -147.58 61.07 REMARK 500 LEU B 11 106.68 -164.17 REMARK 500 TYR B 32 71.79 -103.30 REMARK 500 ALA B 51 -34.24 79.45 REMARK 500 HIS C 4 -10.84 -157.26 REMARK 500 ALA D 88 178.61 178.94 REMARK 500 ALA D 99 -154.91 61.24 REMARK 500 ALA E 51 -25.56 64.44 REMARK 500 ALA E 84 -179.01 176.88 REMARK 500 HIS E 92 -63.69 -99.94 REMARK 500 HIS F 4 -14.66 -156.22 REMARK 500 REMARK 500 REMARK: NULL DBREF 9VX3 A -1 115 PDB 9VX3 9VX3 -1 115 DBREF 9VX3 A 116 164 UNP Q13043 STK4_HUMAN 432 480 DBREF 9VX3 B -1 110 PDB 9VX3 9VX3 -1 110 DBREF 9VX3 B 111 159 UNP Q13043 STK4_HUMAN 432 480 DBREF 9VX3 C 1 6 PDB 9VX3 9VX3 1 6 DBREF 9VX3 D -1 115 PDB 9VX3 9VX3 -1 115 DBREF 9VX3 D 116 164 UNP Q13043 STK4_HUMAN 432 480 DBREF 9VX3 E -1 110 PDB 9VX3 9VX3 -1 110 DBREF 9VX3 E 111 159 UNP Q13043 STK4_HUMAN 432 480 DBREF 9VX3 F 1 6 PDB 9VX3 9VX3 1 6 SEQADV 9VX3 GLY A 165 UNP Q13043 EXPRESSION TAG SEQADV 9VX3 THR A 166 UNP Q13043 EXPRESSION TAG SEQADV 9VX3 LEU A 167 UNP Q13043 EXPRESSION TAG SEQADV 9VX3 LEU A 168 UNP Q13043 EXPRESSION TAG SEQADV 9VX3 GLY A 169 UNP Q13043 EXPRESSION TAG SEQADV 9VX3 CYS B 147 UNP Q13043 SER 468 ENGINEERED MUTATION SEQADV 9VX3 GLY D 165 UNP Q13043 EXPRESSION TAG SEQADV 9VX3 THR D 166 UNP Q13043 EXPRESSION TAG SEQADV 9VX3 LEU D 167 UNP Q13043 EXPRESSION TAG SEQADV 9VX3 LEU D 168 UNP Q13043 EXPRESSION TAG SEQADV 9VX3 GLY D 169 UNP Q13043 EXPRESSION TAG SEQADV 9VX3 CYS E 147 UNP Q13043 SER 468 ENGINEERED MUTATION SEQRES 1 A 175 GLY ARG GLU VAL GLN LEU GLN GLN PHE GLY ALA GLU LEU SEQRES 2 A 175 VAL LYS PRO GLY ALA SER VAL LYS ILE SER CYS LYS ALA SEQRES 3 A 175 SER GLY TYR THR PHE THR ASP TYR ASN MET ASP TRP VAL SEQRES 4 A 175 LYS GLN SER HIS GLY LYS SER LEU GLU TRP ILE GLY ASP SEQRES 5 A 175 ILE ASN PRO ASN TYR ASP SER THR VAL TYR ASN GLN LYS SEQRES 6 A 175 PHE LYS GLY LYS ALA THR LEU THR VAL ASP LYS SER SER SEQRES 7 A 175 SER THR ALA TYR MET GLU LEU ARG SER LEU THR SER GLU SEQRES 8 A 175 ASP THR ALA ILE TYR TYR CYS ALA ARG ASP GLY ALA TYR SEQRES 9 A 175 ALA MET ASP HIS TRP GLY GLN GLY THR SER VAL THR VAL SEQRES 10 A 175 CYS SER GLY SER ASP TYR GLU PHE LEU LYS SER TRP THR SEQRES 11 A 175 VAL GLU ASP LEU GLN LYS ARG LEU LEU ALA LEU ASP PRO SEQRES 12 A 175 MET MET GLU GLN GLU ILE GLU GLU ILE ARG GLN LYS TYR SEQRES 13 A 175 GLN SER LYS ARG GLN PRO ILE LEU ASP ALA ILE GLU ALA SEQRES 14 A 175 LYS GLY THR LEU LEU GLY SEQRES 1 B 167 GLY ARG ASP ILE VAL MET THR GLN SER PRO SER SER LEU SEQRES 2 B 167 SER VAL SER ALA GLY GLU LYS VAL THR MET SER CYS LYS SEQRES 3 B 167 SER SER GLN SER LEU LEU ASN SER GLY HIS GLN LYS ASN SEQRES 4 B 167 TYR LEU ALA TRP TYR GLN GLN LYS PRO GLY GLN PRO PRO SEQRES 5 B 167 LYS LEU LEU ILE SER GLY ALA SER THR ARG GLU SER GLY SEQRES 6 B 167 VAL PRO ASP ARG PHE THR GLY SER GLY SER GLY THR ASP SEQRES 7 B 167 PHE THR LEU THR ILE SER SER VAL GLN ALA GLU ASP LEU SEQRES 8 B 167 ALA VAL TYR TYR CYS GLN ASN ASP HIS ARG TYR PRO LEU SEQRES 9 B 167 THR PHE GLY ALA GLY THR LYS LEU GLU LEU LYS ARG GLY SEQRES 10 B 167 SER ASP TYR GLU PHE LEU LYS SER TRP THR VAL GLU ASP SEQRES 11 B 167 LEU GLN LYS ARG LEU LEU ALA LEU ASP PRO MET MET GLU SEQRES 12 B 167 GLN GLU ILE GLU GLU ILE ARG GLN LYS TYR GLN CYS LYS SEQRES 13 B 167 ARG GLN PRO ILE LEU ASP ALA ILE GLU ALA LYS SEQRES 1 C 6 HIS HIS HIS HIS HIS HIS SEQRES 1 D 175 GLY ARG GLU VAL GLN LEU GLN GLN PHE GLY ALA GLU LEU SEQRES 2 D 175 VAL LYS PRO GLY ALA SER VAL LYS ILE SER CYS LYS ALA SEQRES 3 D 175 SER GLY TYR THR PHE THR ASP TYR ASN MET ASP TRP VAL SEQRES 4 D 175 LYS GLN SER HIS GLY LYS SER LEU GLU TRP ILE GLY ASP SEQRES 5 D 175 ILE ASN PRO ASN TYR ASP SER THR VAL TYR ASN GLN LYS SEQRES 6 D 175 PHE LYS GLY LYS ALA THR LEU THR VAL ASP LYS SER SER SEQRES 7 D 175 SER THR ALA TYR MET GLU LEU ARG SER LEU THR SER GLU SEQRES 8 D 175 ASP THR ALA ILE TYR TYR CYS ALA ARG ASP GLY ALA TYR SEQRES 9 D 175 ALA MET ASP HIS TRP GLY GLN GLY THR SER VAL THR VAL SEQRES 10 D 175 CYS SER GLY SER ASP TYR GLU PHE LEU LYS SER TRP THR SEQRES 11 D 175 VAL GLU ASP LEU GLN LYS ARG LEU LEU ALA LEU ASP PRO SEQRES 12 D 175 MET MET GLU GLN GLU ILE GLU GLU ILE ARG GLN LYS TYR SEQRES 13 D 175 GLN SER LYS ARG GLN PRO ILE LEU ASP ALA ILE GLU ALA SEQRES 14 D 175 LYS GLY THR LEU LEU GLY SEQRES 1 E 167 GLY ARG ASP ILE VAL MET THR GLN SER PRO SER SER LEU SEQRES 2 E 167 SER VAL SER ALA GLY GLU LYS VAL THR MET SER CYS LYS SEQRES 3 E 167 SER SER GLN SER LEU LEU ASN SER GLY HIS GLN LYS ASN SEQRES 4 E 167 TYR LEU ALA TRP TYR GLN GLN LYS PRO GLY GLN PRO PRO SEQRES 5 E 167 LYS LEU LEU ILE SER GLY ALA SER THR ARG GLU SER GLY SEQRES 6 E 167 VAL PRO ASP ARG PHE THR GLY SER GLY SER GLY THR ASP SEQRES 7 E 167 PHE THR LEU THR ILE SER SER VAL GLN ALA GLU ASP LEU SEQRES 8 E 167 ALA VAL TYR TYR CYS GLN ASN ASP HIS ARG TYR PRO LEU SEQRES 9 E 167 THR PHE GLY ALA GLY THR LYS LEU GLU LEU LYS ARG GLY SEQRES 10 E 167 SER ASP TYR GLU PHE LEU LYS SER TRP THR VAL GLU ASP SEQRES 11 E 167 LEU GLN LYS ARG LEU LEU ALA LEU ASP PRO MET MET GLU SEQRES 12 E 167 GLN GLU ILE GLU GLU ILE ARG GLN LYS TYR GLN CYS LYS SEQRES 13 E 167 ARG GLN PRO ILE LEU ASP ALA ILE GLU ALA LYS SEQRES 1 F 6 HIS HIS HIS HIS HIS HIS FORMUL 7 HOH *12(H2 O) HELIX 1 AA1 THR A 28 TYR A 32 5 5 HELIX 2 AA2 GLN A 61 LYS A 64 5 4 HELIX 3 AA3 LYS A 73 SER A 75 5 3 HELIX 4 AA4 THR A 83 THR A 87 5 5 HELIX 5 AA5 GLU A 118 TRP A 123 5 6 HELIX 6 AA6 THR A 124 LYS A 164 1 41 HELIX 7 AA7 GLN B 79 LEU B 83 5 5 HELIX 8 AA8 THR B 119 GLU B 157 1 39 HELIX 9 AA9 THR D 28 TYR D 32 5 5 HELIX 10 AB1 GLN D 61 LYS D 64 5 4 HELIX 11 AB2 THR D 83 THR D 87 5 5 HELIX 12 AB3 ASP D 116 LYS D 121 1 6 HELIX 13 AB4 THR D 124 LYS D 164 1 41 HELIX 14 AB5 GLN E 79 LEU E 83 5 5 HELIX 15 AB6 THR E 119 ARG E 149 1 31 HELIX 16 AB7 ARG E 149 GLU E 157 1 9 SHEET 1 AA1 4 GLN A 3 PHE A 7 0 SHEET 2 AA1 4 VAL A 18 SER A 25 -1 O LYS A 23 N GLN A 5 SHEET 3 AA1 4 THR A 77 LEU A 82 -1 O MET A 80 N ILE A 20 SHEET 4 AA1 4 ALA A 67 ASP A 72 -1 N ASP A 72 O THR A 77 SHEET 1 AA2 6 LEU A 11 VAL A 12 0 SHEET 2 AA2 6 THR A 107 VAL A 111 1 O THR A 110 N VAL A 12 SHEET 3 AA2 6 ALA A 88 ASP A 95 -1 N ALA A 88 O VAL A 109 SHEET 4 AA2 6 ASN A 33 GLN A 39 -1 N VAL A 37 O TYR A 91 SHEET 5 AA2 6 LEU A 45 ASN A 52 -1 O ILE A 48 N TRP A 36 SHEET 6 AA2 6 SER A 56 TYR A 59 -1 O SER A 56 N ASN A 52 SHEET 1 AA3 4 LEU A 11 VAL A 12 0 SHEET 2 AA3 4 THR A 107 VAL A 111 1 O THR A 110 N VAL A 12 SHEET 3 AA3 4 ALA A 88 ASP A 95 -1 N ALA A 88 O VAL A 109 SHEET 4 AA3 4 MET A 100 TRP A 103 -1 O HIS A 102 N ARG A 94 SHEET 1 AA4 4 MET B 4 SER B 7 0 SHEET 2 AA4 4 VAL B 19 SER B 25 -1 O SER B 22 N SER B 7 SHEET 3 AA4 4 ASP B 70 ILE B 75 -1 O PHE B 71 N CYS B 23 SHEET 4 AA4 4 PHE B 62 SER B 67 -1 N SER B 65 O THR B 72 SHEET 1 AA5 2 LEU B 30 ASN B 30A 0 SHEET 2 AA5 2 LYS B 30F ASN B 31 -1 O LYS B 30F N ASN B 30A SHEET 1 AA6 5 THR B 53 ARG B 54 0 SHEET 2 AA6 5 LYS B 45 SER B 49 -1 N SER B 49 O THR B 53 SHEET 3 AA6 5 LEU B 33 GLN B 38 -1 N TRP B 35 O LEU B 47 SHEET 4 AA6 5 VAL B 85 ASN B 90 -1 O TYR B 87 N TYR B 36 SHEET 5 AA6 5 THR B 102 LYS B 103 -1 O THR B 102 N TYR B 86 SHEET 1 AA7 4 GLN D 3 PHE D 7 0 SHEET 2 AA7 4 SER D 17 SER D 25 -1 O SER D 25 N GLN D 3 SHEET 3 AA7 4 THR D 77 ARG D 82A-1 O MET D 80 N ILE D 20 SHEET 4 AA7 4 ALA D 67 ASP D 72 -1 N THR D 70 O TYR D 79 SHEET 1 AA8 6 LEU D 11 VAL D 12 0 SHEET 2 AA8 6 THR D 107 VAL D 111 1 O THR D 110 N VAL D 12 SHEET 3 AA8 6 ALA D 88 ASP D 95 -1 N ALA D 88 O VAL D 109 SHEET 4 AA8 6 ASN D 33 GLN D 39 -1 N ASP D 35 O ALA D 93 SHEET 5 AA8 6 LEU D 45 ASN D 52 -1 O GLU D 46 N LYS D 38 SHEET 6 AA8 6 SER D 56 TYR D 59 -1 O SER D 56 N ASN D 52 SHEET 1 AA9 4 LEU D 11 VAL D 12 0 SHEET 2 AA9 4 THR D 107 VAL D 111 1 O THR D 110 N VAL D 12 SHEET 3 AA9 4 ALA D 88 ASP D 95 -1 N ALA D 88 O VAL D 109 SHEET 4 AA9 4 MET D 100 TRP D 103 -1 O HIS D 102 N ARG D 94 SHEET 1 AB1 4 MET E 4 SER E 7 0 SHEET 2 AB1 4 VAL E 19 SER E 25 -1 O LYS E 24 N THR E 5 SHEET 3 AB1 4 ASP E 70 ILE E 75 -1 O PHE E 71 N CYS E 23 SHEET 4 AB1 4 PHE E 62 SER E 67 -1 N SER E 65 O THR E 72 SHEET 1 AB2 6 SER E 10 VAL E 13 0 SHEET 2 AB2 6 THR E 102 LEU E 106 1 O GLU E 105 N VAL E 13 SHEET 3 AB2 6 VAL E 85 ASN E 90 -1 N TYR E 86 O THR E 102 SHEET 4 AB2 6 LEU E 33 GLN E 38 -1 N TYR E 36 O TYR E 87 SHEET 5 AB2 6 LYS E 45 SER E 49 -1 O LYS E 45 N GLN E 37 SHEET 6 AB2 6 THR E 53 ARG E 54 -1 O THR E 53 N SER E 49 SHEET 1 AB3 4 SER E 10 VAL E 13 0 SHEET 2 AB3 4 THR E 102 LEU E 106 1 O GLU E 105 N VAL E 13 SHEET 3 AB3 4 VAL E 85 ASN E 90 -1 N TYR E 86 O THR E 102 SHEET 4 AB3 4 THR E 97 PHE E 98 -1 O THR E 97 N ASN E 90 SHEET 1 AB4 2 LEU E 30 ASN E 30A 0 SHEET 2 AB4 2 LYS E 30F ASN E 31 -1 O LYS E 30F N ASN E 30A SSBOND 1 CYS A 22 CYS A 92 1555 1555 2.05 SSBOND 2 CYS A 112 CYS B 147 1555 1555 2.03 SSBOND 3 CYS B 23 CYS B 88 1555 1555 2.06 SSBOND 4 CYS D 22 CYS D 92 1555 1555 2.03 SSBOND 5 CYS D 112 CYS E 147 1555 1555 2.04 SSBOND 6 CYS E 23 CYS E 88 1555 1555 2.05 CISPEP 1 SER B 7 PRO B 8 0 -6.20 CISPEP 2 TYR B 94 PRO B 95 0 3.70 CISPEP 3 SER E 7 PRO E 8 0 0.00 CISPEP 4 TYR E 94 PRO E 95 0 -6.10 CRYST1 54.139 69.512 93.396 90.00 93.78 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 0.018471 0.000000 0.001220 0.00000 SCALE2 0.000000 0.014386 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010730 0.00000