HEADER IMMUNE SYSTEM 31-JAN-25 9LRF TITLE KILLER IMMUNOGLOBULIN RECEPTOR KIR2DL2 IN COMPLEX WITH TITLE 2 KIR2DL2_KIR2DL2/3 AGONIST 61-FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: KILLER CELL IMMUNOGLOBULIN-LIKE RECEPTOR 2DL2; COMPND 3 CHAIN: K; COMPND 4 SYNONYM: CD158 ANTIGEN-LIKE FAMILY MEMBER B1,NATURAL KILLER- COMPND 5 ASSOCIATED TRANSCRIPT 6,NKAT-6,P58 NATURAL KILLER CELL RECEPTOR CLONE COMPND 6 CL-43,P58 NK RECEPTOR CL-43; COMPND 7 ENGINEERED: YES; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: KIR2DL2_KIR2DL2/3 AGONIST 61 FAB FRAGMENT HEAVY CHAIN; COMPND 10 CHAIN: H; COMPND 11 ENGINEERED: YES; COMPND 12 MOL_ID: 3; COMPND 13 MOLECULE: KIR2DL2_KIR2DL2/3 AGONIST 61 FAB FRAGMENT LIGHT CHAIN; COMPND 14 CHAIN: L; COMPND 15 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: KIR2DL2, CD158B1, NKAT6; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_TAXID: 9606; SOURCE 11 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 13 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 14 MOL_ID: 3; SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 16 ORGANISM_TAXID: 9606; SOURCE 17 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 18 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 19 EXPRESSION_SYSTEM_CELL_LINE: HEK293 KEYWDS KIR, NATURAL KILLER RECEPTOR, INHIBITORY RECEPTOR, 2DL2, KEYWDS 2 IMMUNOGLOBULIN, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR Y.NISHIKAWA REVDAT 1 15-OCT-25 9LRF 0 JRNL AUTH S.HIURA,Y.KUWASAKI,Y.NISHIKAWA,T.KIMURA,S.YOSHIDA, JRNL AUTH 2 M.NAKAYAMA,T.MAKINO,S.UENO JRNL TITL SELECTIVE AGONISTS OF KIR AND NKG2A TO EVADE MISSING SELF JRNL TITL 2 RESPONSE OF NATURAL KILLER CELLS. JRNL REF SCI REP V. 15 33550 2025 JRNL REFN ESSN 2045-2322 JRNL PMID 41023081 JRNL DOI 10.1038/S41598-025-18394-Z REMARK 2 REMARK 2 RESOLUTION. 2.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.19.2_4158: ???) 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) : 2.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.08 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7 REMARK 3 NUMBER OF REFLECTIONS : 29353 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.236 REMARK 3 R VALUE (WORKING SET) : 0.234 REMARK 3 FREE R VALUE : 0.274 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.950 REMARK 3 FREE R VALUE TEST SET COUNT : 1454 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 38.0800 - 5.3800 0.98 2843 147 0.2068 0.2535 REMARK 3 2 5.3800 - 4.2700 0.97 2747 160 0.1702 0.1989 REMARK 3 3 4.2700 - 3.7300 0.98 2781 146 0.2114 0.2550 REMARK 3 4 3.7300 - 3.3900 0.98 2752 142 0.2619 0.2862 REMARK 3 5 3.3900 - 3.1500 0.99 2782 165 0.2806 0.3454 REMARK 3 6 3.1500 - 2.9600 0.99 2808 137 0.3018 0.3871 REMARK 3 7 2.9600 - 2.8200 0.99 2799 136 0.3298 0.3737 REMARK 3 8 2.8200 - 2.6900 0.99 2772 143 0.3321 0.3370 REMARK 3 9 2.6900 - 2.5900 0.99 2810 141 0.3480 0.4141 REMARK 3 10 2.5900 - 2.5000 0.99 2805 137 0.3841 0.3948 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) : 0.460 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.820 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 : 0.002 4776 REMARK 3 ANGLE : 0.524 6510 REMARK 3 CHIRALITY : 0.043 738 REMARK 3 PLANARITY : 0.005 836 REMARK 3 DIHEDRAL : 15.640 1662 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 11 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'K' AND (RESID 25 THROUGH 73 ) REMARK 3 ORIGIN FOR THE GROUP (A): 49.8206 54.3333 -3.8523 REMARK 3 T TENSOR REMARK 3 T11: 0.7376 T22: 0.5654 REMARK 3 T33: 1.1463 T12: 0.0438 REMARK 3 T13: 0.0920 T23: 0.0349 REMARK 3 L TENSOR REMARK 3 L11: 3.3151 L22: 3.3535 REMARK 3 L33: 1.7094 L12: 0.8345 REMARK 3 L13: 0.0380 L23: -1.3942 REMARK 3 S TENSOR REMARK 3 S11: 0.0212 S12: 0.0784 S13: 1.0421 REMARK 3 S21: -0.0163 S22: -0.3232 S23: -0.4912 REMARK 3 S31: -0.4993 S32: 0.0902 S33: 0.0581 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'K' AND (RESID 74 THROUGH 103 ) REMARK 3 ORIGIN FOR THE GROUP (A): 51.6178 53.6665 -5.0903 REMARK 3 T TENSOR REMARK 3 T11: 0.6845 T22: 0.7061 REMARK 3 T33: 1.3260 T12: 0.0933 REMARK 3 T13: 0.1035 T23: 0.1665 REMARK 3 L TENSOR REMARK 3 L11: 1.0460 L22: 0.4296 REMARK 3 L33: 2.8311 L12: -0.3684 REMARK 3 L13: -0.3814 L23: 0.3407 REMARK 3 S TENSOR REMARK 3 S11: 0.2790 S12: 0.2995 S13: 1.2528 REMARK 3 S21: -0.4446 S22: 0.0464 S23: -0.6684 REMARK 3 S31: -0.3115 S32: 0.5036 S33: 0.0682 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'K' AND (RESID 104 THROUGH 117 ) REMARK 3 ORIGIN FOR THE GROUP (A): 53.4855 60.3324 5.6230 REMARK 3 T TENSOR REMARK 3 T11: 0.8215 T22: 0.9127 REMARK 3 T33: 1.3009 T12: 0.0046 REMARK 3 T13: 0.0251 T23: -0.1129 REMARK 3 L TENSOR REMARK 3 L11: 1.5039 L22: 9.2505 REMARK 3 L33: 5.7517 L12: -2.0970 REMARK 3 L13: -2.6750 L23: 1.1970 REMARK 3 S TENSOR REMARK 3 S11: 0.5033 S12: 0.9470 S13: 2.2713 REMARK 3 S21: 0.7352 S22: -0.0411 S23: -1.7351 REMARK 3 S31: 0.1065 S32: 1.5323 S33: 0.1643 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'K' AND (RESID 118 THROUGH 162 ) REMARK 3 ORIGIN FOR THE GROUP (A): 27.3567 42.4246 -16.0651 REMARK 3 T TENSOR REMARK 3 T11: 0.8876 T22: 0.8243 REMARK 3 T33: 0.7649 T12: 0.0746 REMARK 3 T13: -0.1403 T23: -0.0099 REMARK 3 L TENSOR REMARK 3 L11: 3.3980 L22: 1.4953 REMARK 3 L33: 1.1623 L12: 0.9678 REMARK 3 L13: 1.4544 L23: -0.4557 REMARK 3 S TENSOR REMARK 3 S11: -0.0310 S12: -0.0170 S13: 0.2135 REMARK 3 S21: -0.8016 S22: -0.0895 S23: -0.2264 REMARK 3 S31: 0.2131 S32: -0.2019 S33: -0.1081 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'K' AND (RESID 163 THROUGH 180 ) REMARK 3 ORIGIN FOR THE GROUP (A): 23.9129 39.9203 -10.6742 REMARK 3 T TENSOR REMARK 3 T11: 0.8862 T22: 1.2013 REMARK 3 T33: 1.0612 T12: -0.0547 REMARK 3 T13: -0.1388 T23: -0.1613 REMARK 3 L TENSOR REMARK 3 L11: 2.3508 L22: 1.5836 REMARK 3 L33: 3.5289 L12: -1.0757 REMARK 3 L13: 0.3329 L23: -1.5997 REMARK 3 S TENSOR REMARK 3 S11: 0.0483 S12: 0.5943 S13: -0.7789 REMARK 3 S21: -1.3245 S22: -1.1280 S23: 0.1198 REMARK 3 S31: -0.1222 S32: -0.4970 S33: -0.1149 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'K' AND (RESID 181 THROUGH 221 ) REMARK 3 ORIGIN FOR THE GROUP (A): 28.4695 44.5934 -15.6521 REMARK 3 T TENSOR REMARK 3 T11: 0.8242 T22: 0.7343 REMARK 3 T33: 0.6653 T12: 0.1152 REMARK 3 T13: -0.0660 T23: -0.0216 REMARK 3 L TENSOR REMARK 3 L11: 2.8198 L22: 2.6553 REMARK 3 L33: 2.0846 L12: 0.8964 REMARK 3 L13: 0.4042 L23: -0.6373 REMARK 3 S TENSOR REMARK 3 S11: 0.0278 S12: 0.4952 S13: 0.0055 REMARK 3 S21: -0.6412 S22: -0.2234 S23: 0.2002 REMARK 3 S31: 0.1539 S32: 0.3377 S33: 0.1044 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 73 ) REMARK 3 ORIGIN FOR THE GROUP (A): 55.7015 36.6528 16.3431 REMARK 3 T TENSOR REMARK 3 T11: 0.7825 T22: 0.6799 REMARK 3 T33: 0.6741 T12: 0.0283 REMARK 3 T13: -0.0603 T23: -0.1771 REMARK 3 L TENSOR REMARK 3 L11: 3.9451 L22: 2.8447 REMARK 3 L33: 4.5464 L12: -2.1357 REMARK 3 L13: -0.1662 L23: -0.7637 REMARK 3 S TENSOR REMARK 3 S11: -0.2205 S12: -0.6386 S13: 0.8510 REMARK 3 S21: 1.0817 S22: 0.2439 S23: 0.0975 REMARK 3 S31: -0.1980 S32: -0.2214 S33: -0.0787 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 74 THROUGH 129 ) REMARK 3 ORIGIN FOR THE GROUP (A): 57.4758 32.2818 17.4362 REMARK 3 T TENSOR REMARK 3 T11: 0.8042 T22: 0.7732 REMARK 3 T33: 0.7369 T12: 0.0537 REMARK 3 T13: -0.0527 T23: -0.1599 REMARK 3 L TENSOR REMARK 3 L11: 1.5527 L22: 3.1870 REMARK 3 L33: 1.7493 L12: -0.6131 REMARK 3 L13: 0.2839 L23: -2.2096 REMARK 3 S TENSOR REMARK 3 S11: -0.2177 S12: -0.4008 S13: 0.3707 REMARK 3 S21: 0.9814 S22: 0.1911 S23: -0.3262 REMARK 3 S31: -0.6323 S32: -0.6092 S33: 0.0662 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 130 THROUGH 224 ) REMARK 3 ORIGIN FOR THE GROUP (A): 64.5299 2.7524 51.7679 REMARK 3 T TENSOR REMARK 3 T11: 0.5814 T22: 0.7341 REMARK 3 T33: 0.7113 T12: -0.0328 REMARK 3 T13: -0.0628 T23: -0.0873 REMARK 3 L TENSOR REMARK 3 L11: 2.8048 L22: 2.8626 REMARK 3 L33: 3.6092 L12: 0.6914 REMARK 3 L13: -0.1966 L23: 1.7265 REMARK 3 S TENSOR REMARK 3 S11: -0.2966 S12: 0.2301 S13: -0.0929 REMARK 3 S21: -0.1628 S22: 0.2112 S23: 0.1109 REMARK 3 S31: -0.0692 S32: -0.3746 S33: 0.0487 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 111 ) REMARK 3 ORIGIN FOR THE GROUP (A): 65.3372 22.7711 0.6269 REMARK 3 T TENSOR REMARK 3 T11: 0.4312 T22: 0.4988 REMARK 3 T33: 0.5494 T12: -0.0091 REMARK 3 T13: 0.0201 T23: -0.0566 REMARK 3 L TENSOR REMARK 3 L11: 4.2000 L22: 6.0408 REMARK 3 L33: 1.6056 L12: -0.6381 REMARK 3 L13: 0.2074 L23: -0.5546 REMARK 3 S TENSOR REMARK 3 S11: 0.0775 S12: 0.3170 S13: 0.0957 REMARK 3 S21: -0.3640 S22: -0.0186 S23: -0.8244 REMARK 3 S31: 0.0497 S32: 0.2816 S33: -0.0326 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 112 THROUGH 210 ) REMARK 3 ORIGIN FOR THE GROUP (A): 90.5760 -5.7234 19.6161 REMARK 3 T TENSOR REMARK 3 T11: 0.6940 T22: 0.8018 REMARK 3 T33: 0.8127 T12: 0.1514 REMARK 3 T13: 0.1474 T23: 0.1301 REMARK 3 L TENSOR REMARK 3 L11: 4.0495 L22: 4.5051 REMARK 3 L33: 3.5507 L12: 0.5273 REMARK 3 L13: 0.1149 L23: -0.8878 REMARK 3 S TENSOR REMARK 3 S11: -0.2963 S12: -0.5546 S13: -0.4957 REMARK 3 S21: 0.5585 S22: 0.1156 S23: 0.1846 REMARK 3 S31: 0.4047 S32: 0.0924 S33: 0.2541 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 9LRF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-FEB-25. REMARK 100 THE DEPOSITION ID IS D_1300056289. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 05-JUN-23 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : PHOTON FACTORY REMARK 200 BEAMLINE : BL-17A REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9800 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 : 29367 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500 REMARK 200 RESOLUTION RANGE LOW (A) : 48.330 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9 REMARK 200 DATA REDUNDANCY : 3.400 REMARK 200 R MERGE (I) : 0.06900 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.60 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : 3.60 REMARK 200 R MERGE FOR SHELL (I) : 1.08500 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: 2DL2 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 60.06 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.08 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM IMIDAZOLE-HCL PH7.5, 200MM REMARK 280 CALCIUM ACETATE, 10% PEG3350, VAPOR DIFFUSION, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 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 85.05450 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.62200 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 85.05450 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 39.62200 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3900 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 29700 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, 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 HIS K 22 REMARK 465 GLU K 23 REMARK 465 GLY K 24 REMARK 465 GLY K 222 REMARK 465 ASN K 223 REMARK 465 PRO K 224 REMARK 465 SER K 225 REMARK 465 HIS K 226 REMARK 465 HIS K 227 REMARK 465 HIS K 228 REMARK 465 HIS K 229 REMARK 465 HIS K 230 REMARK 465 HIS K 231 REMARK 465 SER H 137 REMARK 465 SER H 138 REMARK 465 LYS H 139 REMARK 465 SER H 140 REMARK 465 THR H 141 REMARK 465 SER H 142 REMARK 465 GLY H 143 REMARK 465 GLY H 144 REMARK 465 SER H 225 REMARK 465 CYS H 226 REMARK 465 ASP H 227 REMARK 465 LYS H 228 REMARK 465 THR H 229 REMARK 465 HIS H 230 REMARK 465 GLU L 211 REMARK 465 CYS L 212 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 VAL K 25 CG1 CG2 REMARK 470 LYS K 28 NZ REMARK 470 ARG K 54 NH1 NH2 REMARK 470 LYS K 65 NZ REMARK 470 LYS K 82 CE NZ REMARK 470 SER K 103 OG REMARK 470 GLN K 110 CG CD OE1 NE2 REMARK 470 SER K 130 OG REMARK 470 GLU K 163 CG CD OE1 OE2 REMARK 470 GLU K 165 CG CD OE1 OE2 REMARK 470 HIS K 167 CG ND1 CD2 CE1 NE2 REMARK 470 GLN H 3 CD OE1 NE2 REMARK 470 LYS H 12 NZ REMARK 470 LYS H 13 CG CD CE NZ REMARK 470 SER H 16 OG REMARK 470 SER H 17 OG REMARK 470 LYS H 19 CG CD CE NZ REMARK 470 SER H 21 OG REMARK 470 SER H 30 OG REMARK 470 ILE H 52 CG1 CG2 CD1 REMARK 470 VAL H 121 CG1 CG2 REMARK 470 SER H 122 OG REMARK 470 SER H 123 OG REMARK 470 LYS H 211 CG CD CE NZ REMARK 470 LYS H 216 CE NZ REMARK 470 LYS H 219 NZ REMARK 470 LYS H 224 CG CD CE NZ REMARK 470 THR L 94 OG1 CG2 REMARK 470 LYS L 107 CE NZ REMARK 470 LYS L 124 CG CD CE NZ REMARK 470 ARG L 140 CG CD NE CZ NH1 NH2 REMARK 470 GLU L 141 CG CD OE1 OE2 REMARK 470 LYS L 143 CG CD CE NZ REMARK 470 LEU L 152 CG CD1 CD2 REMARK 470 GLU L 159 CG CD OE1 OE2 REMARK 470 GLU L 163 CD OE1 OE2 REMARK 470 LYS L 167 CG CD 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 ASP K 78 -126.17 56.80 REMARK 500 SER K 154 57.64 -91.62 REMARK 500 PRO H 53 -72.55 -56.09 REMARK 500 THR H 102 -154.61 -118.70 REMARK 500 ASP H 154 74.09 56.95 REMARK 500 ALA L 51 -43.82 65.45 REMARK 500 PRO L 95 72.69 -66.66 REMARK 500 ASN L 136 71.68 57.49 REMARK 500 ASP L 149 -120.10 57.29 REMARK 500 SER L 154 -68.45 -127.65 REMARK 500 SER L 169 66.08 -61.68 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 9LRA RELATED DB: PDB DBREF 9LRF K 22 225 UNP P43627 KI2L2_HUMAN 22 225 DBREF 9LRF H 1 230 PDB 9LRF 9LRF 1 230 DBREF 9LRF L 1 212 PDB 9LRF 9LRF 1 212 SEQADV 9LRF HIS K 226 UNP P43627 EXPRESSION TAG SEQADV 9LRF HIS K 227 UNP P43627 EXPRESSION TAG SEQADV 9LRF HIS K 228 UNP P43627 EXPRESSION TAG SEQADV 9LRF HIS K 229 UNP P43627 EXPRESSION TAG SEQADV 9LRF HIS K 230 UNP P43627 EXPRESSION TAG SEQADV 9LRF HIS K 231 UNP P43627 EXPRESSION TAG SEQRES 1 K 210 HIS GLU GLY VAL HIS ARG LYS PRO SER LEU LEU ALA HIS SEQRES 2 K 210 PRO GLY ARG LEU VAL LYS SER GLU GLU THR VAL ILE LEU SEQRES 3 K 210 GLN CYS TRP SER ASP VAL ARG PHE GLU HIS PHE LEU LEU SEQRES 4 K 210 HIS ARG GLU GLY LYS PHE LYS ASP THR LEU HIS LEU ILE SEQRES 5 K 210 GLY GLU HIS HIS ASP GLY VAL SER LYS ALA ASN PHE SER SEQRES 6 K 210 ILE GLY PRO MET MET GLN ASP LEU ALA GLY THR TYR ARG SEQRES 7 K 210 CYS TYR GLY SER VAL THR HIS SER PRO TYR GLN LEU SER SEQRES 8 K 210 ALA PRO SER ASP PRO LEU ASP ILE VAL ILE THR GLY LEU SEQRES 9 K 210 TYR GLU LYS PRO SER LEU SER ALA GLN PRO GLY PRO THR SEQRES 10 K 210 VAL LEU ALA GLY GLU SER VAL THR LEU SER CYS SER SER SEQRES 11 K 210 ARG SER SER TYR ASP MET TYR HIS LEU SER ARG GLU GLY SEQRES 12 K 210 GLU ALA HIS GLU CYS ARG PHE SER ALA GLY PRO LYS VAL SEQRES 13 K 210 ASN GLY THR PHE GLN ALA ASP PHE PRO LEU GLY PRO ALA SEQRES 14 K 210 THR HIS GLY GLY THR TYR ARG CYS PHE GLY SER PHE ARG SEQRES 15 K 210 ASP SER PRO TYR GLU TRP SER ASN SER SER ASP PRO LEU SEQRES 16 K 210 LEU VAL SER VAL ILE GLY ASN PRO SER HIS HIS HIS HIS SEQRES 17 K 210 HIS HIS SEQRES 1 H 230 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 230 PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 H 230 GLY THR PHE SER SER PHE ALA ILE SER TRP VAL ARG GLN SEQRES 4 H 230 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY ILE ILE SEQRES 5 H 230 PRO ILE PHE GLY THR ALA ASN TYR ALA GLN LYS PHE GLN SEQRES 6 H 230 GLY ARG VAL THR ILE THR ALA ASP GLU SER THR SER THR SEQRES 7 H 230 ALA TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 H 230 ALA VAL TYR TYR CYS ALA ARG VAL SER GLY THR THR GLY SEQRES 9 H 230 GLY TYR TYR TYR GLY MET ASP VAL TRP GLY GLN GLY THR SEQRES 10 H 230 LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER SEQRES 11 H 230 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY SEQRES 12 H 230 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE SEQRES 13 H 230 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU SEQRES 14 H 230 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SEQRES 15 H 230 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SEQRES 16 H 230 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL SEQRES 17 H 230 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL SEQRES 18 H 230 GLU PRO LYS SER CYS ASP LYS THR HIS SEQRES 1 L 212 ALA ILE ARG MET THR GLN SER PRO SER SER VAL SER ALA SEQRES 2 L 212 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 L 212 GLN GLY ILE GLY ASN TRP LEU ALA TRP TYR GLN GLN LYS SEQRES 4 L 212 PRO GLY ARG ALA PRO LYS LEU LEU ILE SER THR ALA SER SEQRES 5 L 212 SER LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY GLY SEQRES 6 L 212 GLY SER GLY ARG GLY PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 212 GLN LEU GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER SEQRES 8 L 212 TYR ILE THR PRO TRP THR PHE GLY GLN GLY THR LYS VAL SEQRES 9 L 212 GLU ILE LYS VAL ALA ALA PRO SER VAL PHE ILE PHE PRO SEQRES 10 L 212 PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SER VAL SEQRES 11 L 212 VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA LYS SEQRES 12 L 212 VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY ASN SEQRES 13 L 212 SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SER SEQRES 14 L 212 THR TYR SER LEU SER SER THR LEU THR LEU SER LYS ALA SEQRES 15 L 212 ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL THR SEQRES 16 L 212 HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE ASN SEQRES 17 L 212 ARG GLY GLU CYS HET NAG K 301 14 HET NAG K 302 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE FORMUL 4 NAG 2(C8 H15 N O6) FORMUL 6 HOH *14(H2 O) HELIX 1 AA1 MET K 91 LEU K 94 5 4 HELIX 2 AA2 THR H 28 PHE H 32 5 5 HELIX 3 AA3 ARG H 87 THR H 91 5 5 HELIX 4 AA4 THR H 103 GLY H 105 5 3 HELIX 5 AA5 SER H 166 ALA H 168 5 3 HELIX 6 AA6 PRO H 195 LEU H 199 5 5 HELIX 7 AA7 LYS H 211 ASN H 214 5 4 HELIX 8 AA8 GLN L 79 PHE L 83 5 5 HELIX 9 AA9 SER L 119 SER L 125 1 7 HELIX 10 AB1 LYS L 181 HIS L 187 1 7 SHEET 1 AA1 4 SER K 30 HIS K 34 0 SHEET 2 AA1 4 VAL K 45 SER K 51 -1 O ILE K 46 N HIS K 34 SHEET 3 AA1 4 VAL K 80 ILE K 87 -1 O ILE K 87 N VAL K 45 SHEET 4 AA1 4 GLU K 75 HIS K 77 -1 N HIS K 77 O VAL K 80 SHEET 1 AA2 5 LEU K 38 LYS K 40 0 SHEET 2 AA2 5 LEU K 118 THR K 123 1 O VAL K 121 N VAL K 39 SHEET 3 AA2 5 GLY K 96 SER K 103 -1 N TYR K 98 O LEU K 118 SHEET 4 AA2 5 HIS K 57 GLY K 64 -1 N HIS K 57 O SER K 103 SHEET 5 AA2 5 ASP K 68 ILE K 73 -1 O LEU K 70 N LEU K 60 SHEET 1 AA3 3 SER K 130 GLN K 134 0 SHEET 2 AA3 3 SER K 144 SER K 151 -1 O SER K 150 N SER K 130 SHEET 3 AA3 3 PHE K 181 PRO K 189 -1 O PHE K 185 N LEU K 147 SHEET 1 AA4 2 THR K 138 LEU K 140 0 SHEET 2 AA4 2 SER K 219 ILE K 221 1 O SER K 219 N VAL K 139 SHEET 1 AA5 4 GLU K 168 PHE K 171 0 SHEET 2 AA5 4 MET K 157 ARG K 162 -1 N LEU K 160 O GLU K 168 SHEET 3 AA5 4 THR K 195 SER K 201 -1 O PHE K 199 N HIS K 159 SHEET 4 AA5 4 LEU K 216 LEU K 217 -1 O LEU K 216 N TYR K 196 SHEET 1 AA6 4 GLN H 3 GLN H 6 0 SHEET 2 AA6 4 VAL H 18 SER H 25 -1 O LYS H 23 N VAL H 5 SHEET 3 AA6 4 THR H 78 LEU H 83 -1 O ALA H 79 N CYS H 22 SHEET 4 AA6 4 VAL H 68 ASP H 73 -1 N THR H 71 O TYR H 80 SHEET 1 AA7 6 GLU H 10 LYS H 12 0 SHEET 2 AA7 6 THR H 117 VAL H 121 1 O LEU H 118 N GLU H 10 SHEET 3 AA7 6 ALA H 92 GLY H 101 -1 N TYR H 94 O THR H 117 SHEET 4 AA7 6 ALA H 33 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AA7 6 LEU H 45 ILE H 51 -1 O GLY H 49 N TRP H 36 SHEET 6 AA7 6 ALA H 58 TYR H 60 -1 O ASN H 59 N GLY H 50 SHEET 1 AA8 4 GLU H 10 LYS H 12 0 SHEET 2 AA8 4 THR H 117 VAL H 121 1 O LEU H 118 N GLU H 10 SHEET 3 AA8 4 ALA H 92 GLY H 101 -1 N TYR H 94 O THR H 117 SHEET 4 AA8 4 TYR H 107 TRP H 113 -1 O GLY H 109 N SER H 100 SHEET 1 AA9 4 SER H 130 LEU H 134 0 SHEET 2 AA9 4 ALA H 146 TYR H 155 -1 O LEU H 151 N PHE H 132 SHEET 3 AA9 4 TYR H 186 VAL H 194 -1 O VAL H 192 N LEU H 148 SHEET 4 AA9 4 VAL H 173 THR H 175 -1 N HIS H 174 O VAL H 191 SHEET 1 AB1 4 SER H 130 LEU H 134 0 SHEET 2 AB1 4 ALA H 146 TYR H 155 -1 O LEU H 151 N PHE H 132 SHEET 3 AB1 4 TYR H 186 VAL H 194 -1 O VAL H 192 N LEU H 148 SHEET 4 AB1 4 VAL H 179 LEU H 180 -1 N VAL H 179 O SER H 187 SHEET 1 AB2 3 THR H 161 TRP H 164 0 SHEET 2 AB2 3 ILE H 205 HIS H 210 -1 O ASN H 207 N SER H 163 SHEET 3 AB2 3 THR H 215 LYS H 220 -1 O VAL H 217 N VAL H 208 SHEET 1 AB3 4 MET L 4 SER L 7 0 SHEET 2 AB3 4 VAL L 19 ALA L 25 -1 O THR L 22 N SER L 7 SHEET 3 AB3 4 GLY L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AB3 4 PHE L 62 SER L 67 -1 N GLY L 65 O THR L 72 SHEET 1 AB4 6 SER L 10 ALA L 13 0 SHEET 2 AB4 6 THR L 102 ILE L 106 1 O GLU L 105 N VAL L 11 SHEET 3 AB4 6 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AB4 6 LEU L 33 GLN L 38 -1 N TYR L 36 O TYR L 87 SHEET 5 AB4 6 LYS L 45 SER L 49 -1 O LYS L 45 N GLN L 37 SHEET 6 AB4 6 SER L 53 LEU L 54 -1 O SER L 53 N SER L 49 SHEET 1 AB5 4 SER L 112 PHE L 116 0 SHEET 2 AB5 4 THR L 127 PHE L 137 -1 O LEU L 133 N PHE L 114 SHEET 3 AB5 4 TYR L 171 SER L 180 -1 O LEU L 177 N VAL L 130 SHEET 4 AB5 4 SER L 157 VAL L 161 -1 N GLN L 158 O THR L 176 SHEET 1 AB6 4 ALA L 151 LEU L 152 0 SHEET 2 AB6 4 LYS L 143 VAL L 148 -1 N VAL L 148 O ALA L 151 SHEET 3 AB6 4 VAL L 189 THR L 195 -1 O GLU L 193 N GLN L 145 SHEET 4 AB6 4 VAL L 203 ASN L 208 -1 O VAL L 203 N VAL L 194 SSBOND 1 CYS K 49 CYS K 100 1555 1555 2.03 SSBOND 2 CYS K 149 CYS K 198 1555 1555 2.03 SSBOND 3 CYS H 22 CYS H 96 1555 1555 2.03 SSBOND 4 CYS H 150 CYS H 206 1555 1555 2.03 SSBOND 5 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 6 CYS L 132 CYS L 192 1555 1555 2.03 LINK ND2 ASN K 84 C1 NAG K 301 1555 1555 1.44 LINK ND2 ASN K 211 C1 NAG K 302 1555 1555 1.44 CISPEP 1 HIS K 34 PRO K 35 0 1.92 CISPEP 2 GLN K 134 PRO K 135 0 5.48 CISPEP 3 PHE H 156 PRO H 157 0 -4.14 CISPEP 4 GLU H 158 PRO H 159 0 3.03 CISPEP 5 SER L 7 PRO L 8 0 -0.34 CISPEP 6 TYR L 138 PRO L 139 0 2.26 CRYST1 170.109 79.244 64.364 90.00 92.39 90.00 C 1 2 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 0.005879 0.000000 0.000245 0.00000 SCALE2 0.000000 0.012619 0.000000 0.00000 SCALE3 0.000000 0.000000 0.015550 0.00000