HEADER IMMUNE SYSTEM 30-JAN-25 9LRA TITLE KILLER IMMUNOGLOBULIN RECEPTOR KIR2DL2 IN COMPLEX WITH PAN2D 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: PAN2D FAB FRAGMENT LIGHT CHAIN; COMPND 10 CHAIN: L; COMPND 11 ENGINEERED: YES; COMPND 12 MOL_ID: 3; COMPND 13 MOLECULE: PAN2D FAB FRAGMENT HEAVY CHAIN; COMPND 14 CHAIN: H; 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: HEK293F; 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: HEK293F 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 9LRA 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. 2.60 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) : 2.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.20 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 25257 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.222 REMARK 3 R VALUE (WORKING SET) : 0.220 REMARK 3 FREE R VALUE : 0.252 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.630 REMARK 3 FREE R VALUE TEST SET COUNT : 1169 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 49.2000 - 5.2000 1.00 3171 164 0.2013 0.2132 REMARK 3 2 5.2000 - 4.1300 1.00 3035 152 0.1535 0.1990 REMARK 3 3 4.1300 - 3.6100 1.00 2998 154 0.2078 0.2118 REMARK 3 4 3.6000 - 3.2800 1.00 2951 175 0.2304 0.2932 REMARK 3 5 3.2800 - 3.0400 1.00 3013 108 0.2653 0.3234 REMARK 3 6 3.0400 - 2.8600 1.00 3003 129 0.2992 0.3312 REMARK 3 7 2.8600 - 2.7200 1.00 2921 164 0.3064 0.3590 REMARK 3 8 2.7200 - 2.6000 1.00 2996 123 0.3261 0.3663 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) : 0.350 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.370 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 4929 REMARK 3 ANGLE : 0.535 6712 REMARK 3 CHIRALITY : 0.041 756 REMARK 3 PLANARITY : 0.004 856 REMARK 3 DIHEDRAL : 14.735 1745 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 24 THROUGH 134 ) REMARK 3 ORIGIN FOR THE GROUP (A): -44.2518 -21.3821 16.8042 REMARK 3 T TENSOR REMARK 3 T11: 0.3817 T22: 0.4200 REMARK 3 T33: 0.3880 T12: -0.0479 REMARK 3 T13: -0.0277 T23: -0.0621 REMARK 3 L TENSOR REMARK 3 L11: 1.0294 L22: 1.2612 REMARK 3 L33: 1.2873 L12: -0.2869 REMARK 3 L13: 0.5709 L23: -0.7925 REMARK 3 S TENSOR REMARK 3 S11: 0.1369 S12: -0.1190 S13: 0.0276 REMARK 3 S21: -0.0849 S22: 0.0148 S23: 0.0807 REMARK 3 S31: 0.1802 S32: -0.2396 S33: 0.0000 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'K' AND (RESID 135 THROUGH 224 ) REMARK 3 ORIGIN FOR THE GROUP (A): -27.2566 -32.1360 36.8359 REMARK 3 T TENSOR REMARK 3 T11: 0.4148 T22: 0.4298 REMARK 3 T33: 0.3851 T12: -0.0412 REMARK 3 T13: 0.0154 T23: -0.0214 REMARK 3 L TENSOR REMARK 3 L11: 0.5473 L22: 0.9873 REMARK 3 L33: 0.9655 L12: 0.4419 REMARK 3 L13: -0.2825 L23: -0.1029 REMARK 3 S TENSOR REMARK 3 S11: 0.1169 S12: -0.1162 S13: 0.1305 REMARK 3 S21: 0.1063 S22: -0.2826 S23: 0.1982 REMARK 3 S31: -0.0140 S32: -0.0341 S33: -0.0000 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 18 ) REMARK 3 ORIGIN FOR THE GROUP (A): -16.3325 9.4341 22.3691 REMARK 3 T TENSOR REMARK 3 T11: 0.4003 T22: 0.3905 REMARK 3 T33: 0.5717 T12: 0.0427 REMARK 3 T13: 0.0260 T23: -0.0948 REMARK 3 L TENSOR REMARK 3 L11: 0.1434 L22: 0.5709 REMARK 3 L33: 0.3421 L12: 0.1237 REMARK 3 L13: -0.0015 L23: -0.4468 REMARK 3 S TENSOR REMARK 3 S11: 0.0815 S12: 0.3305 S13: 0.8484 REMARK 3 S21: -0.4871 S22: 0.1876 S23: 0.7797 REMARK 3 S31: -0.0373 S32: -0.1466 S33: 0.0920 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 19 THROUGH 129 ) REMARK 3 ORIGIN FOR THE GROUP (A): -10.6457 4.9703 21.7446 REMARK 3 T TENSOR REMARK 3 T11: 0.3494 T22: 0.3027 REMARK 3 T33: 0.3554 T12: 0.0211 REMARK 3 T13: 0.0175 T23: -0.0205 REMARK 3 L TENSOR REMARK 3 L11: 0.3299 L22: 1.3415 REMARK 3 L33: 0.7067 L12: 0.4526 REMARK 3 L13: 0.1595 L23: 0.1424 REMARK 3 S TENSOR REMARK 3 S11: 0.0815 S12: -0.1390 S13: 0.2447 REMARK 3 S21: -0.1317 S22: -0.1246 S23: 0.3129 REMARK 3 S31: -0.0769 S32: -0.0121 S33: -0.0030 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 130 THROUGH 151 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.9687 19.7894 0.4898 REMARK 3 T TENSOR REMARK 3 T11: 0.5884 T22: 0.4654 REMARK 3 T33: 0.6029 T12: 0.0378 REMARK 3 T13: -0.0239 T23: 0.1521 REMARK 3 L TENSOR REMARK 3 L11: 1.1439 L22: 0.8775 REMARK 3 L33: 2.4207 L12: 0.6465 REMARK 3 L13: -0.8448 L23: 0.3961 REMARK 3 S TENSOR REMARK 3 S11: 0.1381 S12: 0.3385 S13: 0.8870 REMARK 3 S21: -0.1337 S22: 0.1798 S23: 0.7465 REMARK 3 S31: -0.2124 S32: -0.5330 S33: 0.0231 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 152 THROUGH 164 ) REMARK 3 ORIGIN FOR THE GROUP (A): -5.4243 17.6683 -7.8144 REMARK 3 T TENSOR REMARK 3 T11: 0.5674 T22: 0.6802 REMARK 3 T33: 0.9318 T12: 0.0046 REMARK 3 T13: -0.2715 T23: 0.1944 REMARK 3 L TENSOR REMARK 3 L11: 0.1802 L22: 0.7739 REMARK 3 L33: 0.6350 L12: -0.2999 REMARK 3 L13: 0.1654 L23: -0.6617 REMARK 3 S TENSOR REMARK 3 S11: -0.1509 S12: -0.1666 S13: 0.7283 REMARK 3 S21: -0.5344 S22: 0.0391 S23: 0.1544 REMARK 3 S31: 0.3355 S32: -0.4673 S33: -0.2430 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 165 THROUGH 214 ) REMARK 3 ORIGIN FOR THE GROUP (A): 0.7735 21.0129 -2.8805 REMARK 3 T TENSOR REMARK 3 T11: 0.5973 T22: 0.4595 REMARK 3 T33: 0.5910 T12: -0.0352 REMARK 3 T13: 0.0579 T23: 0.1576 REMARK 3 L TENSOR REMARK 3 L11: 1.5250 L22: 1.0937 REMARK 3 L33: 0.4729 L12: 0.4164 REMARK 3 L13: -0.6537 L23: 0.1597 REMARK 3 S TENSOR REMARK 3 S11: 0.0122 S12: 0.1125 S13: 0.4124 REMARK 3 S21: -0.2083 S22: 0.2880 S23: -0.0713 REMARK 3 S31: -0.4991 S32: -0.0137 S33: -0.0398 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 119 ) REMARK 3 ORIGIN FOR THE GROUP (A): -8.5693 -15.7938 16.0591 REMARK 3 T TENSOR REMARK 3 T11: 0.3622 T22: 0.3710 REMARK 3 T33: 0.3476 T12: 0.0564 REMARK 3 T13: 0.0460 T23: 0.0121 REMARK 3 L TENSOR REMARK 3 L11: 0.7290 L22: 0.8843 REMARK 3 L33: 1.4323 L12: 0.8787 REMARK 3 L13: -0.2340 L23: 0.1227 REMARK 3 S TENSOR REMARK 3 S11: -0.0906 S12: 0.0224 S13: -0.1298 REMARK 3 S21: -0.3021 S22: 0.0099 S23: -0.0869 REMARK 3 S31: 0.0413 S32: 0.0401 S33: 0.0000 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 120 THROUGH 142 ) REMARK 3 ORIGIN FOR THE GROUP (A): 9.0799 6.9838 -5.0369 REMARK 3 T TENSOR REMARK 3 T11: 0.8450 T22: 0.6759 REMARK 3 T33: 0.6761 T12: -0.0922 REMARK 3 T13: 0.2709 T23: -0.0179 REMARK 3 L TENSOR REMARK 3 L11: 2.5482 L22: 0.1498 REMARK 3 L33: 1.1559 L12: -0.5001 REMARK 3 L13: 1.0610 L23: -0.0320 REMARK 3 S TENSOR REMARK 3 S11: 0.1491 S12: 0.7383 S13: 0.5138 REMARK 3 S21: -0.6954 S22: -0.3142 S23: -0.1915 REMARK 3 S31: -0.1720 S32: 0.0880 S33: -0.7373 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 143 THROUGH 208 ) REMARK 3 ORIGIN FOR THE GROUP (A): 11.0256 9.4260 2.2261 REMARK 3 T TENSOR REMARK 3 T11: 0.5800 T22: 0.5838 REMARK 3 T33: 0.5409 T12: -0.1067 REMARK 3 T13: 0.0471 T23: 0.0212 REMARK 3 L TENSOR REMARK 3 L11: 0.4131 L22: 0.2690 REMARK 3 L33: 0.8976 L12: 0.2053 REMARK 3 L13: -0.7918 L23: -0.2909 REMARK 3 S TENSOR REMARK 3 S11: -0.2301 S12: 0.0765 S13: -0.2338 REMARK 3 S21: -0.4561 S22: 0.2309 S23: -0.5112 REMARK 3 S31: 0.0140 S32: 0.3773 S33: 0.0000 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 209 THROUGH 223 ) REMARK 3 ORIGIN FOR THE GROUP (A): 17.2418 5.6323 -2.9471 REMARK 3 T TENSOR REMARK 3 T11: 0.7860 T22: 0.7308 REMARK 3 T33: 0.9416 T12: 0.0699 REMARK 3 T13: 0.2327 T23: 0.0104 REMARK 3 L TENSOR REMARK 3 L11: 0.1138 L22: 0.0670 REMARK 3 L33: 0.1785 L12: -0.1018 REMARK 3 L13: -0.0297 L23: 0.0913 REMARK 3 S TENSOR REMARK 3 S11: -0.3069 S12: 0.8030 S13: -0.2982 REMARK 3 S21: -0.1525 S22: 0.2887 S23: -0.1016 REMARK 3 S31: -0.0111 S32: 0.3556 S33: 0.0003 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 9LRA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 31-JAN-25. REMARK 100 THE DEPOSITION ID IS D_1300054120. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 03-DEC-21 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 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-1A REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.045 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 4M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25315 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600 REMARK 200 RESOLUTION RANGE LOW (A) : 49.200 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 13.70 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 10.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69 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: 2DL2 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 57.84 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM SODIUM MALONATE PH5.0, 19% REMARK 280 PEG3350, VAPOR DIFFUSION, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 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 39.62650 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.70000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.75750 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.70000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.62650 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.75750 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: 5590 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 28440 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, L, H 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 PRO K 108 REMARK 465 GLY K 164 REMARK 465 GLU K 165 REMARK 465 ALA K 166 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 CYS L 215 REMARK 465 LYS H 137 REMARK 465 SER H 138 REMARK 465 THR H 139 REMARK 465 SER H 140 REMARK 465 CYS H 224 REMARK 465 ASP H 225 REMARK 465 LYS H 226 REMARK 465 THR H 227 REMARK 465 HIS H 228 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 SER K 107 OG REMARK 470 HIS K 192 CG ND1 CD2 CE1 NE2 REMARK 470 GLU L 124 CG CD OE1 OE2 REMARK 470 LYS L 127 CG CD CE NZ REMARK 470 SER L 177 OG REMARK 470 LYS L 189 CG CD CE NZ REMARK 470 LYS L 191 CG CD CE NZ REMARK 470 SER L 203 OG REMARK 470 SER L 204 OG REMARK 470 SER L 209 OG REMARK 470 GLU L 214 CG CD OE1 OE2 REMARK 470 GLU H 1 CG CD OE1 OE2 REMARK 470 GLN H 3 CD OE1 NE2 REMARK 470 SER H 128 OG REMARK 470 SER H 135 OG REMARK 470 SER H 136 OG REMARK 470 THR H 168 OG1 CG2 REMARK 470 LYS H 209 CG CD CE NZ REMARK 470 LYS H 222 CG CD CE NZ REMARK 470 SER H 223 OG 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 SER K 151 145.96 -170.00 REMARK 500 LYS K 176 -149.50 -114.39 REMARK 500 ALA K 190 52.33 -114.75 REMARK 500 HIS K 192 -1.22 64.77 REMARK 500 THR L 52 -54.94 68.61 REMARK 500 ASN L 139 70.65 55.18 REMARK 500 LYS L 191 -68.16 -94.46 REMARK 500 ALA H 16 -158.50 -98.39 REMARK 500 MET H 108 91.56 -68.34 REMARK 500 PRO H 155 -161.59 -79.65 REMARK 500 REMARK 500 REMARK: NULL DBREF 9LRA K 22 225 UNP P43627 KI2L2_HUMAN 22 225 DBREF 9LRA L 1 215 PDB 9LRA 9LRA 1 215 DBREF 9LRA H 1 228 PDB 9LRA 9LRA 1 228 SEQADV 9LRA HIS K 226 UNP P43627 EXPRESSION TAG SEQADV 9LRA HIS K 227 UNP P43627 EXPRESSION TAG SEQADV 9LRA HIS K 228 UNP P43627 EXPRESSION TAG SEQADV 9LRA HIS K 229 UNP P43627 EXPRESSION TAG SEQADV 9LRA HIS K 230 UNP P43627 EXPRESSION TAG SEQADV 9LRA 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 L 215 GLN ILE VAL LEU THR GLN SER PRO ALA SER MET SER ALA SEQRES 2 L 215 SER LEU GLY GLU ARG VAL THR MET THR CYS THR ALA SER SEQRES 3 L 215 SER SER VAL SER SER SER TYR LEU TYR TRP TYR GLN GLN SEQRES 4 L 215 LYS PRO GLY SER SER PRO LYS LEU TRP ILE TYR SER THR SEQRES 5 L 215 SER ASN LEU ALA SER GLY VAL PRO ALA ARG PHE SER GLY SEQRES 6 L 215 SER GLY SER GLY THR SER TYR SER LEU THR ILE SER SER SEQRES 7 L 215 MET GLU ALA GLU ASP ALA ALA THR TYR TYR CYS HIS GLN SEQRES 8 L 215 TYR HIS ARG SER PRO PRO THR PHE GLY GLY GLY THR LYS SEQRES 9 L 215 LEU GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 L 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 L 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 L 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 L 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 L 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 L 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 L 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 L 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 H 228 GLU VAL GLN LEU GLN GLN SER GLY THR VAL LEU ALA ARG SEQRES 2 H 228 PRO GLY ALA SER VAL LYS MET SER CYS LYS ALA SER GLY SEQRES 3 H 228 TYR THR PHE THR SER TYR TRP MET HIS TRP MET LYS GLN SEQRES 4 H 228 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY THR ILE TYR SEQRES 5 H 228 PRO GLY ASN SER ASP THR ASN TYR ASN GLN LYS PHE LYS SEQRES 6 H 228 GLY LYS ALA LYS LEU THR ALA VAL THR SER THR ASN THR SEQRES 7 H 228 ALA TYR MET GLU LEU SER SER LEU THR ASN GLU ASP SER SEQRES 8 H 228 ALA VAL TYR TYR CYS SER ARG PRO THR THR ALA THR ARG SEQRES 9 H 228 SER SER ALA MET ASP TYR TRP GLY GLN GLY THR SER VAL SEQRES 10 H 228 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 H 228 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12 H 228 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 H 228 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 H 228 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 H 228 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 H 228 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17 H 228 LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO SEQRES 18 H 228 LYS SER CYS ASP LYS THR HIS HET NAG K 301 14 HET NAG K 302 14 HET NAG K 303 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 3(C8 H15 N O6) FORMUL 7 HOH *208(H2 O) HELIX 1 AA1 MET K 91 LEU K 94 5 4 HELIX 2 AA2 LYS K 176 THR K 180 5 5 HELIX 3 AA3 SER L 30 SER L 32 5 3 HELIX 4 AA4 GLU L 80 ALA L 84 5 5 HELIX 5 AA5 SER L 122 LYS L 127 1 6 HELIX 6 AA6 LYS L 184 GLU L 188 1 5 HELIX 7 AA7 THR H 28 TYR H 32 5 5 HELIX 8 AA8 GLN H 62 LYS H 65 5 4 HELIX 9 AA9 THR H 74 THR H 76 5 3 HELIX 10 AB1 THR H 87 SER H 91 5 5 HELIX 11 AB2 SER H 164 ALA H 166 5 3 HELIX 12 AB3 SER H 195 GLN H 200 1 6 SHEET 1 AA1 4 SER K 30 HIS K 34 0 SHEET 2 AA1 4 VAL K 45 SER K 51 -1 O TRP K 50 N SER K 30 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 GLU K 63 O THR K 97 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 THR K 146 SER K 151 -1 O SER K 150 N SER K 130 SHEET 3 AA3 3 PHE K 181 PRO K 186 -1 O PHE K 185 N LEU K 147 SHEET 1 AA4 5 THR K 138 LEU K 140 0 SHEET 2 AA4 5 LEU K 216 ILE K 221 1 O ILE K 221 N VAL K 139 SHEET 3 AA4 5 GLY K 194 PHE K 202 -1 N GLY K 194 O VAL K 218 SHEET 4 AA4 5 MET K 157 ARG K 162 -1 N HIS K 159 O PHE K 199 SHEET 5 AA4 5 GLU K 168 PHE K 171 -1 O GLU K 168 N LEU K 160 SHEET 1 AA5 4 THR K 138 LEU K 140 0 SHEET 2 AA5 4 LEU K 216 ILE K 221 1 O ILE K 221 N VAL K 139 SHEET 3 AA5 4 GLY K 194 PHE K 202 -1 N GLY K 194 O VAL K 218 SHEET 4 AA5 4 SER K 205 TRP K 209 -1 O SER K 205 N PHE K 202 SHEET 1 AA6 4 LEU L 4 SER L 7 0 SHEET 2 AA6 4 VAL L 19 ALA L 25 -1 O THR L 24 N THR L 5 SHEET 3 AA6 4 SER L 71 ILE L 76 -1 O TYR L 72 N CYS L 23 SHEET 4 AA6 4 PHE L 63 SER L 68 -1 N SER L 66 O SER L 73 SHEET 1 AA7 6 SER L 10 ALA L 13 0 SHEET 2 AA7 6 THR L 103 ILE L 107 1 O LYS L 104 N MET L 11 SHEET 3 AA7 6 THR L 86 GLN L 91 -1 N TYR L 87 O THR L 103 SHEET 4 AA7 6 LEU L 34 GLN L 39 -1 N TYR L 35 O HIS L 90 SHEET 5 AA7 6 LYS L 46 TYR L 50 -1 O ILE L 49 N TRP L 36 SHEET 6 AA7 6 ASN L 54 LEU L 55 -1 O ASN L 54 N TYR L 50 SHEET 1 AA8 4 SER L 10 ALA L 13 0 SHEET 2 AA8 4 THR L 103 ILE L 107 1 O LYS L 104 N MET L 11 SHEET 3 AA8 4 THR L 86 GLN L 91 -1 N TYR L 87 O THR L 103 SHEET 4 AA8 4 THR L 98 PHE L 99 -1 O THR L 98 N GLN L 91 SHEET 1 AA9 4 SER L 115 PHE L 119 0 SHEET 2 AA9 4 THR L 130 PHE L 140 -1 O VAL L 134 N PHE L 119 SHEET 3 AA9 4 TYR L 174 SER L 183 -1 O LEU L 182 N ALA L 131 SHEET 4 AA9 4 SER L 160 VAL L 164 -1 N GLN L 161 O THR L 179 SHEET 1 AB1 3 LYS L 146 VAL L 151 0 SHEET 2 AB1 3 VAL L 192 THR L 198 -1 O GLU L 196 N GLN L 148 SHEET 3 AB1 3 VAL L 206 ASN L 211 -1 O PHE L 210 N TYR L 193 SHEET 1 AB2 4 GLN H 3 GLN H 6 0 SHEET 2 AB2 4 VAL H 18 SER H 25 -1 O LYS H 23 N GLN H 5 SHEET 3 AB2 4 THR H 78 LEU H 83 -1 O ALA H 79 N CYS H 22 SHEET 4 AB2 4 ALA H 68 VAL H 73 -1 N VAL H 73 O THR H 78 SHEET 1 AB3 6 VAL H 10 ALA H 12 0 SHEET 2 AB3 6 THR H 115 VAL H 119 1 O THR H 118 N ALA H 12 SHEET 3 AB3 6 ALA H 92 PRO H 99 -1 N TYR H 94 O THR H 115 SHEET 4 AB3 6 MET H 34 GLN H 39 -1 N HIS H 35 O SER H 97 SHEET 5 AB3 6 LEU H 45 ILE H 51 -1 O GLU H 46 N LYS H 38 SHEET 6 AB3 6 THR H 58 TYR H 60 -1 O ASN H 59 N THR H 50 SHEET 1 AB4 4 VAL H 10 ALA H 12 0 SHEET 2 AB4 4 THR H 115 VAL H 119 1 O THR H 118 N ALA H 12 SHEET 3 AB4 4 ALA H 92 PRO H 99 -1 N TYR H 94 O THR H 115 SHEET 4 AB4 4 MET H 108 TRP H 111 -1 O TYR H 110 N ARG H 98 SHEET 1 AB5 4 SER H 128 LEU H 132 0 SHEET 2 AB5 4 THR H 143 TYR H 153 -1 O LEU H 149 N PHE H 130 SHEET 3 AB5 4 TYR H 184 PRO H 193 -1 O TYR H 184 N TYR H 153 SHEET 4 AB5 4 VAL H 171 THR H 173 -1 N HIS H 172 O VAL H 189 SHEET 1 AB6 4 SER H 128 LEU H 132 0 SHEET 2 AB6 4 THR H 143 TYR H 153 -1 O LEU H 149 N PHE H 130 SHEET 3 AB6 4 TYR H 184 PRO H 193 -1 O TYR H 184 N TYR H 153 SHEET 4 AB6 4 VAL H 177 LEU H 178 -1 N VAL H 177 O SER H 185 SHEET 1 AB7 3 THR H 159 TRP H 162 0 SHEET 2 AB7 3 TYR H 202 HIS H 208 -1 O ASN H 205 N SER H 161 SHEET 3 AB7 3 THR H 213 VAL H 219 -1 O THR H 213 N HIS H 208 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 L 23 CYS L 89 1555 1555 2.03 SSBOND 4 CYS L 135 CYS L 195 1555 1555 2.03 SSBOND 5 CYS H 22 CYS H 96 1555 1555 2.03 SSBOND 6 CYS H 148 CYS H 204 1555 1555 2.03 LINK ND2 ASN K 84 C1 NAG K 303 1555 1555 1.44 LINK ND2 ASN K 178 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 5.72 CISPEP 2 GLY K 88 PRO K 89 0 -1.78 CISPEP 3 GLN K 134 PRO K 135 0 1.72 CISPEP 4 SER L 7 PRO L 8 0 -3.52 CISPEP 5 SER L 95 PRO L 96 0 2.80 CISPEP 6 TYR L 141 PRO L 142 0 -0.55 CISPEP 7 PHE H 154 PRO H 155 0 0.17 CRYST1 79.253 81.515 123.400 90.00 90.00 90.00 P 21 21 21 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 0.012618 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012268 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008104 0.00000