HEADER IMMUNE SYSTEM 31-JAN-25 9LRH TITLE KILLER IMMUNOGLOBULIN RECEPTOR KIR2DL2 IN COMPLEX WITH TITLE 2 KIR2DL2_KIR2DL2/3 AGONIST 61-SCFV 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 SCFV; COMPND 10 CHAIN: H, L; COMPND 11 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: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562 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 9LRH 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. 3.40 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.21.1_5286: ???) 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) : 3.40 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.38 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 3 NUMBER OF REFLECTIONS : 14289 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.228 REMARK 3 R VALUE (WORKING SET) : 0.227 REMARK 3 FREE R VALUE : 0.253 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.940 REMARK 3 FREE R VALUE TEST SET COUNT : 706 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 44.3800 - 5.8100 0.99 2863 150 0.2177 0.2377 REMARK 3 2 5.8100 - 4.6100 1.00 2741 144 0.2019 0.2183 REMARK 3 3 4.6100 - 4.0300 1.00 2666 160 0.1954 0.2474 REMARK 3 4 4.0300 - 3.6600 1.00 2671 138 0.2900 0.3454 REMARK 3 5 3.6600 - 3.4000 0.99 2642 114 0.3809 0.4263 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) : 0.580 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.670 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 : 0.003 NULL REMARK 3 ANGLE : 0.522 NULL REMARK 3 CHIRALITY : 0.042 504 REMARK 3 PLANARITY : 0.004 586 REMARK 3 DIHEDRAL : 10.798 1202 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 9 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'K' AND (RESID 25 THROUGH 51 ) REMARK 3 ORIGIN FOR THE GROUP (A): 13.0292 29.1184 37.2730 REMARK 3 T TENSOR REMARK 3 T11: 1.0635 T22: 1.4167 REMARK 3 T33: 1.8917 T12: 0.0571 REMARK 3 T13: 0.0520 T23: 0.2991 REMARK 3 L TENSOR REMARK 3 L11: 4.6687 L22: 6.2463 REMARK 3 L33: 7.6420 L12: -2.2724 REMARK 3 L13: -4.8228 L23: 1.6549 REMARK 3 S TENSOR REMARK 3 S11: -0.9119 S12: 0.9638 S13: 0.7537 REMARK 3 S21: 0.3454 S22: 0.4812 S23: 2.3078 REMARK 3 S31: 1.1695 S32: -1.4750 S33: 0.3459 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'K' AND (RESID 52 THROUGH 73 ) REMARK 3 ORIGIN FOR THE GROUP (A): 13.3861 40.7193 36.2915 REMARK 3 T TENSOR REMARK 3 T11: 0.7816 T22: 1.4916 REMARK 3 T33: 1.5082 T12: 0.0345 REMARK 3 T13: -0.0234 T23: 0.2775 REMARK 3 L TENSOR REMARK 3 L11: 1.6466 L22: 5.2535 REMARK 3 L33: 6.1357 L12: 0.2207 REMARK 3 L13: 0.2489 L23: 5.7095 REMARK 3 S TENSOR REMARK 3 S11: -1.4369 S12: 0.6705 S13: -0.0337 REMARK 3 S21: 0.9567 S22: 0.2880 S23: 2.4607 REMARK 3 S31: 0.1574 S32: -1.4585 S33: 1.4773 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'K' AND (RESID 74 THROUGH 134 ) REMARK 3 ORIGIN FOR THE GROUP (A): 16.2255 32.3298 37.3344 REMARK 3 T TENSOR REMARK 3 T11: 1.0160 T22: 1.2269 REMARK 3 T33: 1.2465 T12: -0.0239 REMARK 3 T13: -0.0896 T23: 0.1013 REMARK 3 L TENSOR REMARK 3 L11: 3.4105 L22: 9.2657 REMARK 3 L33: 3.4971 L12: -3.8692 REMARK 3 L13: 1.1727 L23: -2.1595 REMARK 3 S TENSOR REMARK 3 S11: -0.0547 S12: 0.0806 S13: -0.0083 REMARK 3 S21: 0.3357 S22: 0.1951 S23: 0.6781 REMARK 3 S31: -0.1344 S32: -0.3285 S33: -0.1899 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'K' AND (RESID 135 THROUGH 201 ) REMARK 3 ORIGIN FOR THE GROUP (A): 28.7357 11.2197 46.3502 REMARK 3 T TENSOR REMARK 3 T11: 1.1430 T22: 1.2354 REMARK 3 T33: 1.2086 T12: 0.0022 REMARK 3 T13: -0.0351 T23: -0.0576 REMARK 3 L TENSOR REMARK 3 L11: 5.2726 L22: 7.0806 REMARK 3 L33: 7.3741 L12: 3.1180 REMARK 3 L13: -1.2620 L23: -2.9001 REMARK 3 S TENSOR REMARK 3 S11: -0.1193 S12: 0.0886 S13: 0.5420 REMARK 3 S21: 0.1464 S22: 0.2023 S23: 0.1111 REMARK 3 S31: 0.5875 S32: -0.2041 S33: 0.0463 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'K' AND (RESID 202 THROUGH 223 ) REMARK 3 ORIGIN FOR THE GROUP (A): 26.8694 14.9262 40.7153 REMARK 3 T TENSOR REMARK 3 T11: 1.3732 T22: 1.1901 REMARK 3 T33: 1.2220 T12: 0.1245 REMARK 3 T13: -0.0617 T23: -0.2173 REMARK 3 L TENSOR REMARK 3 L11: 6.0968 L22: 6.6264 REMARK 3 L33: 4.4174 L12: 1.6806 REMARK 3 L13: -0.3600 L23: -3.3268 REMARK 3 S TENSOR REMARK 3 S11: -0.5116 S12: 0.2906 S13: 1.4104 REMARK 3 S21: -0.4851 S22: 0.5719 S23: 0.4222 REMARK 3 S31: 0.3731 S32: 0.5044 S33: -0.2447 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 25 ) REMARK 3 ORIGIN FOR THE GROUP (A): 32.8018 61.5655 27.9732 REMARK 3 T TENSOR REMARK 3 T11: 1.3650 T22: 1.1085 REMARK 3 T33: 1.3465 T12: -0.0209 REMARK 3 T13: 0.0500 T23: 0.0795 REMARK 3 L TENSOR REMARK 3 L11: 2.7158 L22: 7.0263 REMARK 3 L33: 6.7913 L12: 2.1502 REMARK 3 L13: -3.8543 L23: -0.3671 REMARK 3 S TENSOR REMARK 3 S11: 0.7736 S12: -0.4746 S13: 1.7064 REMARK 3 S21: 1.1503 S22: -0.0295 S23: 1.1336 REMARK 3 S31: -0.7413 S32: -0.3715 S33: -1.1537 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 26 THROUGH 123 ) REMARK 3 ORIGIN FOR THE GROUP (A): 31.4075 51.4790 28.3112 REMARK 3 T TENSOR REMARK 3 T11: 0.9671 T22: 1.2053 REMARK 3 T33: 1.2649 T12: 0.0568 REMARK 3 T13: 0.1486 T23: -0.0649 REMARK 3 L TENSOR REMARK 3 L11: 4.7171 L22: 6.4853 REMARK 3 L33: 4.4125 L12: 3.1726 REMARK 3 L13: -0.7054 L23: -2.2291 REMARK 3 S TENSOR REMARK 3 S11: 0.4904 S12: -0.0188 S13: 0.2126 REMARK 3 S21: 0.2474 S22: -0.0173 S23: 0.1327 REMARK 3 S31: -0.3617 S32: 0.0132 S33: -0.4160 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'L' AND (RESID -7 THROUGH 3 ) REMARK 3 ORIGIN FOR THE GROUP (A): 39.6687 30.7549 27.2828 REMARK 3 T TENSOR REMARK 3 T11: 2.2371 T22: 1.6964 REMARK 3 T33: 1.8452 T12: -0.1301 REMARK 3 T13: 0.1370 T23: -0.3196 REMARK 3 L TENSOR REMARK 3 L11: 6.3210 L22: 3.4027 REMARK 3 L33: 9.3435 L12: 2.2924 REMARK 3 L13: 3.7709 L23: -1.1555 REMARK 3 S TENSOR REMARK 3 S11: 2.9189 S12: -1.2536 S13: 2.6340 REMARK 3 S21: 4.2709 S22: 1.3657 S23: -1.1514 REMARK 3 S31: -0.7019 S32: 2.0628 S33: -2.2768 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 4 THROUGH 108 ) REMARK 3 ORIGIN FOR THE GROUP (A): 31.7628 42.6217 8.9606 REMARK 3 T TENSOR REMARK 3 T11: 1.1440 T22: 1.1087 REMARK 3 T33: 0.9990 T12: -0.0579 REMARK 3 T13: -0.0683 T23: 0.0239 REMARK 3 L TENSOR REMARK 3 L11: 5.9832 L22: 2.7843 REMARK 3 L33: 2.7944 L12: -1.3572 REMARK 3 L13: -1.1502 L23: 1.9392 REMARK 3 S TENSOR REMARK 3 S11: 0.0106 S12: 0.6133 S13: -0.3005 REMARK 3 S21: -1.0183 S22: 0.3003 S23: 0.1091 REMARK 3 S31: 0.3003 S32: -0.1964 S33: -0.2647 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 9LRH 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_1300056291. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 11-SEP-23 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SLS REMARK 200 BEAMLINE : X06SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000 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 : 14337 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.400 REMARK 200 RESOLUTION RANGE LOW (A) : 49.430 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 13.50 REMARK 200 R MERGE (I) : 0.20900 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.67 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : 14.10 REMARK 200 R MERGE FOR SHELL (I) : 3.36400 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 (%): 62.05 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.24 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM BIS-TRIS PROPANE PH7.0, 29% REMARK 280 TACSIMATE PH7.0, VAPOR DIFFUSION, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 3555 -Y,X+1/2,Z+1/4 REMARK 290 4555 Y+1/2,-X,Z+3/4 REMARK 290 5555 -X+1/2,Y,-Z+3/4 REMARK 290 6555 X,-Y+1/2,-Z+1/4 REMARK 290 7555 Y+1/2,X+1/2,-Z+1/2 REMARK 290 8555 -Y,-X,-Z REMARK 290 9555 X+1/2,Y+1/2,Z+1/2 REMARK 290 10555 -X,-Y,Z REMARK 290 11555 -Y+1/2,X,Z+3/4 REMARK 290 12555 Y,-X+1/2,Z+1/4 REMARK 290 13555 -X,Y+1/2,-Z+1/4 REMARK 290 14555 X+1/2,-Y,-Z+3/4 REMARK 290 15555 Y,X,-Z REMARK 290 16555 -Y+1/2,-X+1/2,-Z+1/2 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 49.42750 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 49.42750 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 201.53800 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 49.42750 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 100.76900 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 49.42750 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 302.30700 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 49.42750 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 302.30700 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 49.42750 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 100.76900 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 49.42750 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 49.42750 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 201.53800 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 49.42750 REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 49.42750 REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 201.53800 REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 49.42750 REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 302.30700 REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 49.42750 REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 100.76900 REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 49.42750 REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 100.76900 REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 49.42750 REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 302.30700 REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 49.42750 REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 49.42750 REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 201.53800 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: 4240 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19680 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 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 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 GLY H 124 REMARK 465 GLY H 125 REMARK 465 GLY H 126 REMARK 465 GLY H 127 REMARK 465 SER H 128 REMARK 465 GLY H 129 REMARK 465 GLY H 130 REMARK 465 GLY H 131 REMARK 465 GLY H 132 REMARK 465 SER H 133 REMARK 465 GLY H 134 REMARK 465 GLY H 135 REMARK 465 GLY H 136 REMARK 465 GLY H 137 REMARK 465 SER H 138 REMARK 465 ALA H 139 REMARK 465 ILE H 140 REMARK 465 ARG H 141 REMARK 465 MET H 142 REMARK 465 THR H 143 REMARK 465 GLN H 144 REMARK 465 SER H 145 REMARK 465 PRO H 146 REMARK 465 SER H 147 REMARK 465 SER H 148 REMARK 465 VAL H 149 REMARK 465 SER H 150 REMARK 465 ALA H 151 REMARK 465 SER H 152 REMARK 465 VAL H 153 REMARK 465 GLY H 154 REMARK 465 ASP H 155 REMARK 465 ARG H 156 REMARK 465 VAL H 157 REMARK 465 THR H 158 REMARK 465 ILE H 159 REMARK 465 THR H 160 REMARK 465 CYS H 161 REMARK 465 ARG H 162 REMARK 465 ALA H 163 REMARK 465 SER H 164 REMARK 465 GLN H 165 REMARK 465 GLY H 166 REMARK 465 ILE H 167 REMARK 465 GLY H 168 REMARK 465 ASN H 169 REMARK 465 TRP H 170 REMARK 465 LEU H 171 REMARK 465 ALA H 172 REMARK 465 TRP H 173 REMARK 465 TYR H 174 REMARK 465 GLN H 175 REMARK 465 GLN H 176 REMARK 465 LYS H 177 REMARK 465 PRO H 178 REMARK 465 GLY H 179 REMARK 465 ARG H 180 REMARK 465 ALA H 181 REMARK 465 PRO H 182 REMARK 465 LYS H 183 REMARK 465 LEU H 184 REMARK 465 LEU H 185 REMARK 465 ILE H 186 REMARK 465 SER H 187 REMARK 465 THR H 188 REMARK 465 ALA H 189 REMARK 465 SER H 190 REMARK 465 SER H 191 REMARK 465 LEU H 192 REMARK 465 GLN H 193 REMARK 465 SER H 194 REMARK 465 GLY H 195 REMARK 465 VAL H 196 REMARK 465 PRO H 197 REMARK 465 SER H 198 REMARK 465 ARG H 199 REMARK 465 PHE H 200 REMARK 465 SER H 201 REMARK 465 GLY H 202 REMARK 465 GLY H 203 REMARK 465 GLY H 204 REMARK 465 SER H 205 REMARK 465 GLY H 206 REMARK 465 ARG H 207 REMARK 465 GLY H 208 REMARK 465 PHE H 209 REMARK 465 THR H 210 REMARK 465 LEU H 211 REMARK 465 THR H 212 REMARK 465 ILE H 213 REMARK 465 SER H 214 REMARK 465 SER H 215 REMARK 465 LEU H 216 REMARK 465 GLN H 217 REMARK 465 LEU H 218 REMARK 465 GLU H 219 REMARK 465 ASP H 220 REMARK 465 PHE H 221 REMARK 465 ALA H 222 REMARK 465 THR H 223 REMARK 465 TYR H 224 REMARK 465 TYR H 225 REMARK 465 CYS H 226 REMARK 465 GLN H 227 REMARK 465 GLN H 228 REMARK 465 SER H 229 REMARK 465 TYR H 230 REMARK 465 ILE H 231 REMARK 465 THR H 232 REMARK 465 PRO H 233 REMARK 465 TRP H 234 REMARK 465 THR H 235 REMARK 465 PHE H 236 REMARK 465 GLY H 237 REMARK 465 GLN H 238 REMARK 465 GLY H 239 REMARK 465 THR H 240 REMARK 465 LYS H 241 REMARK 465 VAL H 242 REMARK 465 GLU H 243 REMARK 465 ILE H 244 REMARK 465 LYS H 245 REMARK 465 GLY H 246 REMARK 465 ALA H 247 REMARK 465 LEU H 248 REMARK 465 GLU H 249 REMARK 465 VAL H 250 REMARK 465 LEU H 251 REMARK 465 PHE H 252 REMARK 465 GLN H 253 REMARK 465 GLN L -137 REMARK 465 VAL L -136 REMARK 465 GLN L -135 REMARK 465 LEU L -134 REMARK 465 VAL L -133 REMARK 465 GLN L -132 REMARK 465 SER L -131 REMARK 465 GLY L -130 REMARK 465 ALA L -129 REMARK 465 GLU L -128 REMARK 465 VAL L -127 REMARK 465 LYS L -126 REMARK 465 LYS L -125 REMARK 465 PRO L -124 REMARK 465 GLY L -123 REMARK 465 SER L -122 REMARK 465 SER L -121 REMARK 465 VAL L -120 REMARK 465 LYS L -119 REMARK 465 VAL L -118 REMARK 465 SER L -117 REMARK 465 CYS L -116 REMARK 465 LYS L -115 REMARK 465 ALA L -114 REMARK 465 SER L -113 REMARK 465 GLY L -112 REMARK 465 GLY L -111 REMARK 465 THR L -110 REMARK 465 PHE L -109 REMARK 465 SER L -108 REMARK 465 SER L -107 REMARK 465 PHE L -106 REMARK 465 ALA L -105 REMARK 465 ILE L -104 REMARK 465 SER L -103 REMARK 465 TRP L -102 REMARK 465 VAL L -101 REMARK 465 ARG L -100 REMARK 465 GLN L -99 REMARK 465 ALA L -98 REMARK 465 PRO L -97 REMARK 465 GLY L -96 REMARK 465 GLN L -95 REMARK 465 GLY L -94 REMARK 465 LEU L -93 REMARK 465 GLU L -92 REMARK 465 TRP L -91 REMARK 465 MET L -90 REMARK 465 GLY L -89 REMARK 465 GLY L -88 REMARK 465 ILE L -87 REMARK 465 ILE L -86 REMARK 465 PRO L -85 REMARK 465 ILE L -84 REMARK 465 PHE L -83 REMARK 465 GLY L -82 REMARK 465 THR L -81 REMARK 465 ALA L -80 REMARK 465 ASN L -79 REMARK 465 TYR L -78 REMARK 465 ALA L -77 REMARK 465 GLN L -76 REMARK 465 LYS L -75 REMARK 465 PHE L -74 REMARK 465 GLN L -73 REMARK 465 GLY L -72 REMARK 465 ARG L -71 REMARK 465 VAL L -70 REMARK 465 THR L -69 REMARK 465 ILE L -68 REMARK 465 THR L -67 REMARK 465 ALA L -66 REMARK 465 ASP L -65 REMARK 465 GLU L -64 REMARK 465 SER L -63 REMARK 465 THR L -62 REMARK 465 SER L -61 REMARK 465 THR L -60 REMARK 465 ALA L -59 REMARK 465 TYR L -58 REMARK 465 MET L -57 REMARK 465 GLU L -56 REMARK 465 LEU L -55 REMARK 465 SER L -54 REMARK 465 SER L -53 REMARK 465 LEU L -52 REMARK 465 ARG L -51 REMARK 465 SER L -50 REMARK 465 GLU L -49 REMARK 465 ASP L -48 REMARK 465 THR L -47 REMARK 465 ALA L -46 REMARK 465 VAL L -45 REMARK 465 TYR L -44 REMARK 465 TYR L -43 REMARK 465 CYS L -42 REMARK 465 ALA L -41 REMARK 465 ARG L -40 REMARK 465 VAL L -39 REMARK 465 SER L -38 REMARK 465 GLY L -37 REMARK 465 THR L -36 REMARK 465 THR L -35 REMARK 465 GLY L -34 REMARK 465 GLY L -33 REMARK 465 TYR L -32 REMARK 465 TYR L -31 REMARK 465 TYR L -30 REMARK 465 GLY L -29 REMARK 465 MET L -28 REMARK 465 ASP L -27 REMARK 465 VAL L -26 REMARK 465 TRP L -25 REMARK 465 GLY L -24 REMARK 465 GLN L -23 REMARK 465 GLY L -22 REMARK 465 THR L -21 REMARK 465 LEU L -20 REMARK 465 VAL L -19 REMARK 465 THR L -18 REMARK 465 VAL L -17 REMARK 465 SER L -16 REMARK 465 SER L -15 REMARK 465 GLY L -14 REMARK 465 GLY L -13 REMARK 465 GLY L -12 REMARK 465 GLY L -11 REMARK 465 SER L -10 REMARK 465 GLY L -9 REMARK 465 GLY L -8 REMARK 465 ALA L 109 REMARK 465 LEU L 110 REMARK 465 GLU L 111 REMARK 465 VAL L 112 REMARK 465 LEU L 113 REMARK 465 PHE L 114 REMARK 465 GLN L 115 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 HIS K 26 CG ND1 CD2 CE1 NE2 REMARK 470 ARG K 27 CG CD NE CZ NH1 NH2 REMARK 470 ARG K 54 NH1 NH2 REMARK 470 LYS K 82 CE NZ REMARK 470 GLN K 110 CG CD OE1 NE2 REMARK 470 SER K 130 OG REMARK 470 ARG K 152 CG CD NE CZ NH1 NH2 REMARK 470 GLU K 165 CG CD OE1 OE2 REMARK 470 HIS K 167 CG ND1 CD2 CE1 NE2 REMARK 470 PHE K 171 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ASN K 223 CG OD1 ND2 REMARK 470 GLN H 1 CG CD OE1 NE2 REMARK 470 GLN H 3 CD OE1 NE2 REMARK 470 LYS H 13 CG CD CE NZ REMARK 470 SER H 16 OG REMARK 470 SER H 17 OG REMARK 470 SER H 21 OG REMARK 470 SER H 122 OG REMARK 470 SER H 123 OG REMARK 470 SER L -5 OG REMARK 470 LYS L 107 CE NZ 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 OG SER L 7 OG1 THR L 22 2.09 REMARK 500 O GLU K 127 OH TYR K 155 2.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 OG1 THR L 20 OG1 THR L 20 15555 2.14 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 ASP K 78 -125.39 58.55 REMARK 500 HIS K 106 -89.47 -109.83 REMARK 500 GLN K 110 106.08 -53.37 REMARK 500 PRO K 175 103.70 -54.64 REMARK 500 PRO H 41 104.84 -56.52 REMARK 500 ALA L 51 -47.43 68.75 REMARK 500 ALA L 84 -156.49 -167.65 REMARK 500 TYR L 92 -93.09 -72.14 REMARK 500 PRO L 95 75.48 -58.37 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 9LRA RELATED DB: PDB REMARK 900 RELATED ID: 9LRF RELATED DB: PDB DBREF 9LRH K 22 225 UNP P43627 KI2L2_HUMAN 22 225 DBREF 9LRH H 1 253 PDB 9LRH 9LRH 1 253 DBREF 9LRH L -137 115 PDB 9LRH 9LRH -137 115 SEQADV 9LRH HIS K 226 UNP P43627 EXPRESSION TAG SEQADV 9LRH HIS K 227 UNP P43627 EXPRESSION TAG SEQADV 9LRH HIS K 228 UNP P43627 EXPRESSION TAG SEQADV 9LRH HIS K 229 UNP P43627 EXPRESSION TAG SEQADV 9LRH HIS K 230 UNP P43627 EXPRESSION TAG SEQADV 9LRH 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 253 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 253 PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 H 253 GLY THR PHE SER SER PHE ALA ILE SER TRP VAL ARG GLN SEQRES 4 H 253 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY ILE ILE SEQRES 5 H 253 PRO ILE PHE GLY THR ALA ASN TYR ALA GLN LYS PHE GLN SEQRES 6 H 253 GLY ARG VAL THR ILE THR ALA ASP GLU SER THR SER THR SEQRES 7 H 253 ALA TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 H 253 ALA VAL TYR TYR CYS ALA ARG VAL SER GLY THR THR GLY SEQRES 9 H 253 GLY TYR TYR TYR GLY MET ASP VAL TRP GLY GLN GLY THR SEQRES 10 H 253 LEU VAL THR VAL SER SER GLY GLY GLY GLY SER GLY GLY SEQRES 11 H 253 GLY GLY SER GLY GLY GLY GLY SER ALA ILE ARG MET THR SEQRES 12 H 253 GLN SER PRO SER SER VAL SER ALA SER VAL GLY ASP ARG SEQRES 13 H 253 VAL THR ILE THR CYS ARG ALA SER GLN GLY ILE GLY ASN SEQRES 14 H 253 TRP LEU ALA TRP TYR GLN GLN LYS PRO GLY ARG ALA PRO SEQRES 15 H 253 LYS LEU LEU ILE SER THR ALA SER SER LEU GLN SER GLY SEQRES 16 H 253 VAL PRO SER ARG PHE SER GLY GLY GLY SER GLY ARG GLY SEQRES 17 H 253 PHE THR LEU THR ILE SER SER LEU GLN LEU GLU ASP PHE SEQRES 18 H 253 ALA THR TYR TYR CYS GLN GLN SER TYR ILE THR PRO TRP SEQRES 19 H 253 THR PHE GLY GLN GLY THR LYS VAL GLU ILE LYS GLY ALA SEQRES 20 H 253 LEU GLU VAL LEU PHE GLN SEQRES 1 L 253 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 L 253 PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 L 253 GLY THR PHE SER SER PHE ALA ILE SER TRP VAL ARG GLN SEQRES 4 L 253 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY ILE ILE SEQRES 5 L 253 PRO ILE PHE GLY THR ALA ASN TYR ALA GLN LYS PHE GLN SEQRES 6 L 253 GLY ARG VAL THR ILE THR ALA ASP GLU SER THR SER THR SEQRES 7 L 253 ALA TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 L 253 ALA VAL TYR TYR CYS ALA ARG VAL SER GLY THR THR GLY SEQRES 9 L 253 GLY TYR TYR TYR GLY MET ASP VAL TRP GLY GLN GLY THR SEQRES 10 L 253 LEU VAL THR VAL SER SER GLY GLY GLY GLY SER GLY GLY SEQRES 11 L 253 GLY GLY SER GLY GLY GLY GLY SER ALA ILE ARG MET THR SEQRES 12 L 253 GLN SER PRO SER SER VAL SER ALA SER VAL GLY ASP ARG SEQRES 13 L 253 VAL THR ILE THR CYS ARG ALA SER GLN GLY ILE GLY ASN SEQRES 14 L 253 TRP LEU ALA TRP TYR GLN GLN LYS PRO GLY ARG ALA PRO SEQRES 15 L 253 LYS LEU LEU ILE SER THR ALA SER SER LEU GLN SER GLY SEQRES 16 L 253 VAL PRO SER ARG PHE SER GLY GLY GLY SER GLY ARG GLY SEQRES 17 L 253 PHE THR LEU THR ILE SER SER LEU GLN LEU GLU ASP PHE SEQRES 18 L 253 ALA THR TYR TYR CYS GLN GLN SER TYR ILE THR PRO TRP SEQRES 19 L 253 THR PHE GLY GLN GLY THR LYS VAL GLU ILE LYS GLY ALA SEQRES 20 L 253 LEU GLU VAL LEU PHE GLN 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 *5(H2 O) HELIX 1 AA1 MET K 91 ALA K 95 5 5 HELIX 2 AA2 ARG H 87 THR H 91 5 5 HELIX 3 AA3 THR H 103 GLY H 105 5 3 HELIX 4 AA4 GLN L 79 PHE L 83 5 5 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 PHE K 85 N LEU K 47 SHEET 4 AA1 4 GLU K 75 HIS K 77 -1 N GLU K 75 O LYS K 82 SHEET 1 AA2 5 LEU K 38 LYS K 40 0 SHEET 2 AA2 5 LEU K 118 TYR K 126 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 GLU K 63 -1 N LEU K 59 O TYR K 101 SHEET 5 AA2 5 THR K 69 ILE K 73 -1 O LEU K 70 N LEU K 60 SHEET 1 AA3 3 LEU K 38 LYS K 40 0 SHEET 2 AA3 3 LEU K 118 TYR K 126 1 O VAL K 121 N VAL K 39 SHEET 3 AA3 3 GLU K 208 SER K 210 1 O TRP K 209 N ILE K 122 SHEET 1 AA4 3 SER K 130 GLN K 134 0 SHEET 2 AA4 3 SER K 144 SER K 151 -1 O THR K 146 N GLN K 134 SHEET 3 AA4 3 PHE K 181 PRO K 189 -1 O PHE K 185 N LEU K 147 SHEET 1 AA5 5 THR K 138 LEU K 140 0 SHEET 2 AA5 5 LEU K 216 ILE K 221 1 O SER K 219 N VAL K 139 SHEET 3 AA5 5 GLY K 194 SER K 201 -1 N GLY K 194 O VAL K 218 SHEET 4 AA5 5 MET K 157 ARG K 162 -1 N SER K 161 O ARG K 197 SHEET 5 AA5 5 GLU K 168 PHE K 171 -1 O ARG K 170 N TYR K 158 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 ILE H 34 ALA H 40 -1 N SER H 35 O ALA H 97 SHEET 5 AA7 6 GLN H 43 ILE H 51 -1 O GLN H 43 N ALA H 40 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 MET L 4 SER L 7 0 SHEET 2 AA9 4 VAL L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AA9 4 GLY L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AA9 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AB1 6 SER L 10 ALA L 13 0 SHEET 2 AB1 6 THR L 102 ILE L 106 1 O LYS L 103 N VAL L 11 SHEET 3 AB1 6 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AB1 6 LEU L 33 GLN L 38 -1 N GLN L 38 O THR L 85 SHEET 5 AB1 6 LYS L 45 SER L 49 -1 O LYS L 45 N GLN L 37 SHEET 6 AB1 6 SER L 53 LEU L 54 -1 O SER L 53 N SER L 49 SSBOND 1 CYS K 49 CYS K 100 1555 1555 2.03 SSBOND 2 CYS K 149 CYS K 198 1555 1555 2.04 SSBOND 3 CYS H 22 CYS H 96 1555 1555 2.03 SSBOND 4 CYS L 23 CYS L 88 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 2.65 CISPEP 2 GLN K 134 PRO K 135 0 5.78 CISPEP 3 SER L 7 PRO L 8 0 -0.97 CRYST1 98.855 98.855 403.076 90.00 90.00 90.00 I 41 2 2 32 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 0.010116 0.000000 0.000000 0.00000 SCALE2 0.000000 0.010116 0.000000 0.00000 SCALE3 0.000000 0.000000 0.002481 0.00000