HEADER SIGNALING PROTEIN 24-MAR-25 9NWU TITLE CRYSTAL STRUCTURE OF A HIGH AFFINITY VL-VH TETRABODY FOR THE TITLE 2 ERYTHROPOIETIN RECEPTOR COMPND MOL_ID: 1; COMPND 2 MOLECULE: DIABODY; COMPND 3 CHAIN: C, D, A, B; COMPND 4 ENGINEERED: YES; COMPND 5 OTHER_DETAILS: N-TERMINAL LIGHT CHAIN, C-TERMINAL HEAVY CHAIN SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: EXPI293; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PSCSTA KEYWDS DIABODY, DIMER, HIGH-AFFINITY BINDING, AGONIST, SIGNALING PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR A.U.SINGER,H.A.BRUCE,N.YANG,L.L.BLAZER,J.J.ADAMS,S.S.SIDHU REVDAT 1 01-OCT-25 9NWU 0 JRNL AUTH J.J.ADAMS,L.L.BLAZER,J.CHUNG,M.KARIMI,T.DAVIDSON,H.A.BRUCE, JRNL AUTH 2 A.U.SINGER,N.YANG,L.CARDARELLI,I.POT,L.COLOMBO,L.J.HUANG, JRNL AUTH 3 Y.MA,S.W.MICHNICK,O.W.MOE,S.S.SIDHU JRNL TITL AN ASYMMETRIC TETRABODY IS A POTENT AND EFFICACIOUS AGONIST JRNL TITL 2 OF THE ERYTHROPOIETIN RECEPTOR IN VITRO AND IN VIVO. JRNL REF PROTEIN SCI. V. 34 70292 2025 JRNL REFN ESSN 1469-896X JRNL PMID 40960423 JRNL DOI 10.1002/PRO.70292 REMARK 2 REMARK 2 RESOLUTION. 1.96 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) : 1.96 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 70.89 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 94.7 REMARK 3 NUMBER OF REFLECTIONS : 65633 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.169 REMARK 3 R VALUE (WORKING SET) : 0.167 REMARK 3 FREE R VALUE : 0.215 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.110 REMARK 3 FREE R VALUE TEST SET COUNT : 3354 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 70.8900 - 5.6500 0.97 2699 157 0.1512 0.1644 REMARK 3 2 5.6500 - 4.4900 0.98 2692 175 0.1226 0.1451 REMARK 3 3 4.4900 - 3.9200 0.97 2724 99 0.1296 0.1786 REMARK 3 4 3.9200 - 3.5600 0.96 2600 169 0.1515 0.2104 REMARK 3 5 3.5600 - 3.3100 0.98 2727 128 0.1527 0.2383 REMARK 3 6 3.3100 - 3.1100 0.99 2704 153 0.1770 0.2406 REMARK 3 7 3.1100 - 2.9600 0.99 2757 113 0.1895 0.2415 REMARK 3 8 2.9600 - 2.8300 1.00 2715 156 0.1788 0.2523 REMARK 3 9 2.8300 - 2.7200 0.98 2657 176 0.1726 0.2416 REMARK 3 10 2.7200 - 2.6200 0.98 2653 161 0.1794 0.2202 REMARK 3 11 2.6200 - 2.5400 0.99 2749 137 0.1971 0.2526 REMARK 3 12 2.5400 - 2.4700 0.99 2705 152 0.1900 0.2565 REMARK 3 13 2.4700 - 2.4000 0.99 2727 117 0.1961 0.2528 REMARK 3 14 2.4000 - 2.3500 0.99 2707 152 0.2006 0.2509 REMARK 3 15 2.3500 - 2.2900 0.99 2748 103 0.1934 0.2815 REMARK 3 16 2.2900 - 2.2400 0.99 2721 138 0.1950 0.2455 REMARK 3 17 2.2400 - 2.2000 1.00 2710 161 0.1882 0.2542 REMARK 3 18 2.2000 - 2.1600 0.99 2700 152 0.2003 0.2300 REMARK 3 19 2.1600 - 2.1200 0.98 2677 133 0.2033 0.2622 REMARK 3 20 2.1200 - 2.0800 0.91 2498 141 0.2174 0.2784 REMARK 3 21 2.0800 - 2.0500 0.86 2349 103 0.2397 0.2672 REMARK 3 22 2.0500 - 2.0200 0.79 2153 150 0.2570 0.3459 REMARK 3 23 2.0200 - 1.9900 0.75 2037 135 0.2829 0.3502 REMARK 3 24 1.9900 - 1.9600 0.69 1870 93 0.3203 0.3140 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) : 0.251 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.991 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 36.10 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.23 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 : 0.008 7156 REMARK 3 ANGLE : 0.978 9744 REMARK 3 CHIRALITY : 0.060 1058 REMARK 3 PLANARITY : 0.009 1236 REMARK 3 DIHEDRAL : 8.994 1069 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 14 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 91 ) REMARK 3 ORIGIN FOR THE GROUP (A): 49.3822 -10.2103 62.1203 REMARK 3 T TENSOR REMARK 3 T11: 0.3508 T22: 0.4641 REMARK 3 T33: 0.2599 T12: -0.1491 REMARK 3 T13: 0.0193 T23: 0.0216 REMARK 3 L TENSOR REMARK 3 L11: 3.5888 L22: 4.7513 REMARK 3 L33: 2.5571 L12: 0.5660 REMARK 3 L13: -0.3758 L23: -1.1847 REMARK 3 S TENSOR REMARK 3 S11: -0.3796 S12: 0.5140 S13: 0.0557 REMARK 3 S21: -0.3634 S22: 0.2673 S23: -0.2473 REMARK 3 S31: -0.2720 S32: 0.3678 S33: 0.1122 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 92 THROUGH 119 ) REMARK 3 ORIGIN FOR THE GROUP (A): 39.5951 -6.8236 61.5664 REMARK 3 T TENSOR REMARK 3 T11: 0.3790 T22: 0.3186 REMARK 3 T33: 0.3293 T12: -0.0578 REMARK 3 T13: 0.0489 T23: -0.0314 REMARK 3 L TENSOR REMARK 3 L11: 4.9386 L22: 3.3040 REMARK 3 L33: 8.6840 L12: -2.9418 REMARK 3 L13: 5.9805 L23: -4.9400 REMARK 3 S TENSOR REMARK 3 S11: -0.3444 S12: 0.3085 S13: 0.5427 REMARK 3 S21: 0.1860 S22: -0.4116 S23: -0.4825 REMARK 3 S31: -0.5749 S32: 0.7249 S33: 0.8732 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 120 THROUGH 228 ) REMARK 3 ORIGIN FOR THE GROUP (A): 15.3666 -1.3231 45.6316 REMARK 3 T TENSOR REMARK 3 T11: 0.3435 T22: 0.1914 REMARK 3 T33: 0.2965 T12: -0.0023 REMARK 3 T13: 0.0885 T23: -0.0453 REMARK 3 L TENSOR REMARK 3 L11: 4.2253 L22: 2.5287 REMARK 3 L33: 3.5964 L12: -0.1849 REMARK 3 L13: 0.5582 L23: -0.8619 REMARK 3 S TENSOR REMARK 3 S11: 0.1419 S12: -0.0365 S13: 0.4183 REMARK 3 S21: 0.1234 S22: -0.0161 S23: 0.1357 REMARK 3 S31: -0.3623 S32: 0.0186 S33: -0.1344 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 91 ) REMARK 3 ORIGIN FOR THE GROUP (A): 26.3897 -20.1844 37.8403 REMARK 3 T TENSOR REMARK 3 T11: 0.2576 T22: 0.3006 REMARK 3 T33: 0.2729 T12: -0.0067 REMARK 3 T13: 0.0252 T23: -0.0712 REMARK 3 L TENSOR REMARK 3 L11: 3.0537 L22: 2.7145 REMARK 3 L33: 3.0386 L12: -0.8311 REMARK 3 L13: 1.1789 L23: -0.7143 REMARK 3 S TENSOR REMARK 3 S11: 0.0436 S12: 0.2674 S13: -0.1707 REMARK 3 S21: 0.0655 S22: -0.0014 S23: -0.0299 REMARK 3 S31: -0.0274 S32: 0.1298 S33: -0.0452 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 92 THROUGH 114 ) REMARK 3 ORIGIN FOR THE GROUP (A): 23.5871 -20.3742 44.2619 REMARK 3 T TENSOR REMARK 3 T11: 0.3223 T22: 0.3242 REMARK 3 T33: 0.3036 T12: 0.0164 REMARK 3 T13: 0.0096 T23: -0.0467 REMARK 3 L TENSOR REMARK 3 L11: 6.7691 L22: 5.9833 REMARK 3 L33: 6.6695 L12: -6.6474 REMARK 3 L13: 6.7407 L23: -5.6506 REMARK 3 S TENSOR REMARK 3 S11: 0.1870 S12: 0.3097 S13: -0.4721 REMARK 3 S21: 0.0545 S22: -0.0399 S23: 0.2978 REMARK 3 S31: -0.0711 S32: 0.2655 S33: -0.0640 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 115 THROUGH 203 ) REMARK 3 ORIGIN FOR THE GROUP (A): 38.2215 -26.9473 76.2654 REMARK 3 T TENSOR REMARK 3 T11: 0.2588 T22: 0.2747 REMARK 3 T33: 0.2353 T12: -0.0770 REMARK 3 T13: 0.0561 T23: -0.0363 REMARK 3 L TENSOR REMARK 3 L11: 3.1892 L22: 2.5002 REMARK 3 L33: 3.6017 L12: 0.2093 REMARK 3 L13: -0.0758 L23: 0.1421 REMARK 3 S TENSOR REMARK 3 S11: -0.1427 S12: 0.1004 S13: -0.2808 REMARK 3 S21: 0.0200 S22: -0.0490 S23: 0.0078 REMARK 3 S31: 0.4254 S32: -0.3007 S33: 0.1882 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 204 THROUGH 229 ) REMARK 3 ORIGIN FOR THE GROUP (A): 38.7633 -23.5921 68.8355 REMARK 3 T TENSOR REMARK 3 T11: 0.2541 T22: 0.3499 REMARK 3 T33: 0.1965 T12: -0.0707 REMARK 3 T13: 0.0267 T23: 0.0006 REMARK 3 L TENSOR REMARK 3 L11: 4.7260 L22: 5.7921 REMARK 3 L33: 7.0603 L12: -1.4664 REMARK 3 L13: -0.2690 L23: 0.9880 REMARK 3 S TENSOR REMARK 3 S11: 0.0454 S12: 0.6544 S13: -0.3500 REMARK 3 S21: -0.3318 S22: -0.2043 S23: -0.1948 REMARK 3 S31: 0.0582 S32: -0.1545 S33: 0.1343 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 102 ) REMARK 3 ORIGIN FOR THE GROUP (A): 49.9917 13.8972 57.1351 REMARK 3 T TENSOR REMARK 3 T11: 0.2335 T22: 0.2718 REMARK 3 T33: 0.2635 T12: 0.0499 REMARK 3 T13: -0.0365 T23: 0.0091 REMARK 3 L TENSOR REMARK 3 L11: 4.0808 L22: 4.1382 REMARK 3 L33: 4.1710 L12: 0.7319 REMARK 3 L13: 0.5679 L23: -0.8523 REMARK 3 S TENSOR REMARK 3 S11: 0.0587 S12: 0.2292 S13: -0.0808 REMARK 3 S21: -0.0856 S22: 0.1571 S23: -0.0012 REMARK 3 S31: 0.2498 S32: -0.0760 S33: -0.2002 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 103 THROUGH 124 ) REMARK 3 ORIGIN FOR THE GROUP (A): 29.6002 6.1456 67.4139 REMARK 3 T TENSOR REMARK 3 T11: 0.5001 T22: 0.3518 REMARK 3 T33: 0.5496 T12: 0.1179 REMARK 3 T13: -0.0500 T23: -0.0626 REMARK 3 L TENSOR REMARK 3 L11: 1.4703 L22: 0.3478 REMARK 3 L33: 1.9588 L12: 0.3485 REMARK 3 L13: -1.7063 L23: -0.1448 REMARK 3 S TENSOR REMARK 3 S11: -0.2100 S12: -0.2045 S13: 0.1687 REMARK 3 S21: 0.1123 S22: -0.2933 S23: -0.3436 REMARK 3 S31: 0.0290 S32: 0.3194 S33: 0.4853 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 125 THROUGH 229 ) REMARK 3 ORIGIN FOR THE GROUP (A): 16.0283 10.5213 72.2570 REMARK 3 T TENSOR REMARK 3 T11: 0.2663 T22: 0.1759 REMARK 3 T33: 0.2752 T12: 0.0428 REMARK 3 T13: -0.0536 T23: -0.0578 REMARK 3 L TENSOR REMARK 3 L11: 3.2123 L22: 2.2109 REMARK 3 L33: 3.0413 L12: -0.1697 REMARK 3 L13: 1.1163 L23: -0.2007 REMARK 3 S TENSOR REMARK 3 S11: 0.2239 S12: -0.0207 S13: -0.4000 REMARK 3 S21: 0.0209 S22: 0.0086 S23: -0.0773 REMARK 3 S31: 0.4267 S32: 0.1014 S33: -0.2054 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 91 ) REMARK 3 ORIGIN FOR THE GROUP (A): 27.3714 27.8756 82.2737 REMARK 3 T TENSOR REMARK 3 T11: 0.2074 T22: 0.1687 REMARK 3 T33: 0.2527 T12: 0.0378 REMARK 3 T13: -0.0140 T23: -0.0488 REMARK 3 L TENSOR REMARK 3 L11: 2.6073 L22: 2.4188 REMARK 3 L33: 3.1004 L12: 1.1347 REMARK 3 L13: 0.4291 L23: -0.5568 REMARK 3 S TENSOR REMARK 3 S11: 0.0002 S12: 0.0758 S13: -0.0662 REMARK 3 S21: -0.0732 S22: -0.0012 S23: 0.0498 REMARK 3 S31: -0.0821 S32: 0.0155 S33: 0.0055 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 92 THROUGH 114 ) REMARK 3 ORIGIN FOR THE GROUP (A): 25.1361 28.6615 75.5344 REMARK 3 T TENSOR REMARK 3 T11: 0.2857 T22: 0.2405 REMARK 3 T33: 0.2302 T12: 0.0433 REMARK 3 T13: -0.0726 T23: -0.0088 REMARK 3 L TENSOR REMARK 3 L11: 7.7240 L22: 1.5808 REMARK 3 L33: 3.8746 L12: 1.6090 REMARK 3 L13: -3.0659 L23: 0.5504 REMARK 3 S TENSOR REMARK 3 S11: 0.4591 S12: -0.3375 S13: 0.6147 REMARK 3 S21: 0.1506 S22: -0.2281 S23: 0.2474 REMARK 3 S31: -0.3245 S32: 0.4196 S33: -0.2357 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 115 THROUGH 203 ) REMARK 3 ORIGIN FOR THE GROUP (A): 40.6077 32.0471 44.7193 REMARK 3 T TENSOR REMARK 3 T11: 0.2546 T22: 0.1935 REMARK 3 T33: 0.2671 T12: 0.0252 REMARK 3 T13: -0.0163 T23: 0.0056 REMARK 3 L TENSOR REMARK 3 L11: 4.5241 L22: 1.7604 REMARK 3 L33: 3.7908 L12: 0.0917 REMARK 3 L13: 1.1374 L23: -0.4369 REMARK 3 S TENSOR REMARK 3 S11: -0.0413 S12: -0.1829 S13: 0.2301 REMARK 3 S21: 0.0759 S22: -0.0697 S23: -0.0998 REMARK 3 S31: -0.3273 S32: 0.1310 S33: 0.1301 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 204 THROUGH 229 ) REMARK 3 ORIGIN FOR THE GROUP (A): 40.3117 27.9209 51.8054 REMARK 3 T TENSOR REMARK 3 T11: 0.2802 T22: 0.2588 REMARK 3 T33: 0.2814 T12: 0.0686 REMARK 3 T13: 0.0107 T23: 0.0442 REMARK 3 L TENSOR REMARK 3 L11: 5.0738 L22: 4.4989 REMARK 3 L33: 7.2438 L12: 1.4607 REMARK 3 L13: 2.5513 L23: 0.6172 REMARK 3 S TENSOR REMARK 3 S11: -0.1358 S12: -0.6539 S13: 0.3871 REMARK 3 S21: 0.2164 S22: -0.0253 S23: -0.1275 REMARK 3 S31: -0.0782 S32: 0.0662 S33: 0.2054 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 9NWU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-MAR-25. REMARK 100 THE DEPOSITION ID IS D_1000294298. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 04-NOV-22 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 9.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 24-ID-E REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOPROC REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 65686 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.960 REMARK 200 RESOLUTION RANGE LOW (A) : 141.780 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.9 REMARK 200 DATA REDUNDANCY : 3.300 REMARK 200 R MERGE (I) : 0.05000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 14.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.96 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.01 REMARK 200 COMPLETENESS FOR SHELL (%) : 71.3 REMARK 200 DATA REDUNDANCY IN SHELL : 2.30 REMARK 200 R MERGE FOR SHELL (I) : 0.71600 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.300 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 (%): 50.77 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG8000, 100 MM CHES PH 9.5, WITH REMARK 280 MICROSEEDING. CRYSTALS CRYOPROTECTED WITH THE SAME REMARK 280 CRYSTALLIZATION LIQUOR PLUS 25% ETHYLENE GLYCOL, VAPOR DIFFUSION, REMARK 280 SITTING DROP, TEMPERATURE 295K 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 70.88950 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, 3 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: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, A, B 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3720 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20540 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -57.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4480 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20950 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -71.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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 C 108 REMARK 465 GLY C 109 REMARK 465 GLY C 110 REMARK 465 GLY C 111 REMARK 465 GLY C 112 REMARK 465 SER C 229 REMARK 465 GLY D 109 REMARK 465 GLY D 110 REMARK 465 GLY D 111 REMARK 465 GLY A 108 REMARK 465 GLY B 108 REMARK 465 GLY B 109 REMARK 465 GLY B 110 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 C 56 OG REMARK 470 LYS C 103 CE NZ REMARK 470 LYS C 107 CG CD CE NZ REMARK 470 GLU C 113 CG CD OE1 OE2 REMARK 470 ASN C 140 CG OD1 ND2 REMARK 470 LYS C 155 CE NZ REMARK 470 LYS C 177 CD CE NZ REMARK 470 GLN C 221 CG CD OE1 NE2 REMARK 470 LYS D 42 CE NZ REMARK 470 LYS D 45 CD CE NZ REMARK 470 LYS D 107 CE NZ REMARK 470 GLU D 113 CG CD OE1 OE2 REMARK 470 ARG D 142 CG CD NE CZ NH1 NH2 REMARK 470 LYS D 155 NZ REMARK 470 GLN D 221 CG CD OE1 NE2 REMARK 470 ASP A 1 CG OD1 OD2 REMARK 470 LYS A 42 CD CE NZ REMARK 470 TYR A 93 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ARG A 142 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 155 CE NZ REMARK 470 GLN A 221 CD OE1 NE2 REMARK 470 LYS B 42 CE NZ REMARK 470 LYS B 45 CD CE NZ REMARK 470 LYS B 103 NZ REMARK 470 GLU B 113 CG CD OE1 OE2 REMARK 470 LYS B 155 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 O HOH D 531 O HOH D 546 2.17 REMARK 500 O HOH D 488 O HOH D 517 2.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 GLN C 27 -149.59 -123.90 REMARK 500 SER C 28 133.66 -35.48 REMARK 500 ALA C 51 -25.36 69.55 REMARK 500 TYR C 166 -24.45 67.55 REMARK 500 SER C 197 57.73 39.91 REMARK 500 GLN D 27 -152.05 -124.28 REMARK 500 ALA D 51 -24.77 69.40 REMARK 500 SER D 92 -166.11 -118.51 REMARK 500 LYS D 155 -169.58 -118.61 REMARK 500 TYR D 166 -18.25 67.81 REMARK 500 GLN A 27 -148.08 -138.19 REMARK 500 SER A 28 136.06 -35.50 REMARK 500 ALA A 51 -24.72 70.30 REMARK 500 TYR A 166 -20.63 66.05 REMARK 500 ALA A 204 167.59 179.74 REMARK 500 GLN B 27 -147.50 -135.63 REMARK 500 SER B 28 152.33 -49.79 REMARK 500 ALA B 51 -27.81 70.44 REMARK 500 SER B 52 -6.08 -142.14 REMARK 500 ALA B 84 -178.86 -177.44 REMARK 500 SER B 92 -168.60 -118.45 REMARK 500 TYR B 166 -21.97 66.48 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA D 303 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 SER D 175 O REMARK 620 2 LYS D 177 O 134.8 REMARK 620 N 1 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 8VUI RELATED DB: PDB REMARK 900 FAB-EPR-1 IS THE FAB VERSION OF THIS ANTIBODY REMARK 900 RELATED ID: 8VTP RELATED DB: PDB REMARK 900 FAB-EPR-1 IS THE FAB VERSION OF THIS ANTIBODY DBREF 9NWU C 1 229 PDB 9NWU 9NWU 1 229 DBREF 9NWU D 1 229 PDB 9NWU 9NWU 1 229 DBREF 9NWU A 1 229 PDB 9NWU 9NWU 1 229 DBREF 9NWU B 1 229 PDB 9NWU 9NWU 1 229 SEQRES 1 C 229 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 C 229 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 C 229 GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN LYS SEQRES 4 C 229 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SER SEQRES 5 C 229 SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 C 229 ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 C 229 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER SEQRES 8 C 229 SER TYR SER LEU ILE THR PHE GLY GLN GLY THR LYS VAL SEQRES 9 C 229 GLU ILE LYS GLY GLY GLY GLY GLY GLU VAL GLN LEU VAL SEQRES 10 C 229 GLU SER GLY GLY GLY LEU VAL GLN PRO GLY GLY SER LEU SEQRES 11 C 229 ARG LEU SER CYS ALA ALA SER GLY PHE ASN LEU ARG SER SEQRES 12 C 229 TYR TYR MET HIS TRP VAL ARG GLN ALA PRO GLY LYS GLY SEQRES 13 C 229 LEU GLU TRP VAL ALA SER ILE SER PRO TYR TYR SER TYR SEQRES 14 C 229 THR TYR TYR ALA ASP SER VAL LYS GLY ARG PHE THR ILE SEQRES 15 C 229 SER ALA ASP THR SER LYS ASN THR ALA TYR LEU GLN MET SEQRES 16 C 229 ASN SER LEU ARG ALA GLU ASP THR ALA VAL TYR TYR CYS SEQRES 17 C 229 ALA ARG HIS GLY TYR GLY ALA MET ASP TYR TRP GLY GLN SEQRES 18 C 229 GLY THR LEU VAL THR VAL SER SER SEQRES 1 D 229 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 D 229 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 D 229 GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN LYS SEQRES 4 D 229 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SER SEQRES 5 D 229 SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 D 229 ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 D 229 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER SEQRES 8 D 229 SER TYR SER LEU ILE THR PHE GLY GLN GLY THR LYS VAL SEQRES 9 D 229 GLU ILE LYS GLY GLY GLY GLY GLY GLU VAL GLN LEU VAL SEQRES 10 D 229 GLU SER GLY GLY GLY LEU VAL GLN PRO GLY GLY SER LEU SEQRES 11 D 229 ARG LEU SER CYS ALA ALA SER GLY PHE ASN LEU ARG SER SEQRES 12 D 229 TYR TYR MET HIS TRP VAL ARG GLN ALA PRO GLY LYS GLY SEQRES 13 D 229 LEU GLU TRP VAL ALA SER ILE SER PRO TYR TYR SER TYR SEQRES 14 D 229 THR TYR TYR ALA ASP SER VAL LYS GLY ARG PHE THR ILE SEQRES 15 D 229 SER ALA ASP THR SER LYS ASN THR ALA TYR LEU GLN MET SEQRES 16 D 229 ASN SER LEU ARG ALA GLU ASP THR ALA VAL TYR TYR CYS SEQRES 17 D 229 ALA ARG HIS GLY TYR GLY ALA MET ASP TYR TRP GLY GLN SEQRES 18 D 229 GLY THR LEU VAL THR VAL SER SER SEQRES 1 A 229 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 A 229 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 A 229 GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN LYS SEQRES 4 A 229 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SER SEQRES 5 A 229 SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 A 229 ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 A 229 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER SEQRES 8 A 229 SER TYR SER LEU ILE THR PHE GLY GLN GLY THR LYS VAL SEQRES 9 A 229 GLU ILE LYS GLY GLY GLY GLY GLY GLU VAL GLN LEU VAL SEQRES 10 A 229 GLU SER GLY GLY GLY LEU VAL GLN PRO GLY GLY SER LEU SEQRES 11 A 229 ARG LEU SER CYS ALA ALA SER GLY PHE ASN LEU ARG SER SEQRES 12 A 229 TYR TYR MET HIS TRP VAL ARG GLN ALA PRO GLY LYS GLY SEQRES 13 A 229 LEU GLU TRP VAL ALA SER ILE SER PRO TYR TYR SER TYR SEQRES 14 A 229 THR TYR TYR ALA ASP SER VAL LYS GLY ARG PHE THR ILE SEQRES 15 A 229 SER ALA ASP THR SER LYS ASN THR ALA TYR LEU GLN MET SEQRES 16 A 229 ASN SER LEU ARG ALA GLU ASP THR ALA VAL TYR TYR CYS SEQRES 17 A 229 ALA ARG HIS GLY TYR GLY ALA MET ASP TYR TRP GLY GLN SEQRES 18 A 229 GLY THR LEU VAL THR VAL SER SER SEQRES 1 B 229 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 B 229 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 B 229 GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN LYS SEQRES 4 B 229 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SER SEQRES 5 B 229 SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 B 229 ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 B 229 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER SEQRES 8 B 229 SER TYR SER LEU ILE THR PHE GLY GLN GLY THR LYS VAL SEQRES 9 B 229 GLU ILE LYS GLY GLY GLY GLY GLY GLU VAL GLN LEU VAL SEQRES 10 B 229 GLU SER GLY GLY GLY LEU VAL GLN PRO GLY GLY SER LEU SEQRES 11 B 229 ARG LEU SER CYS ALA ALA SER GLY PHE ASN LEU ARG SER SEQRES 12 B 229 TYR TYR MET HIS TRP VAL ARG GLN ALA PRO GLY LYS GLY SEQRES 13 B 229 LEU GLU TRP VAL ALA SER ILE SER PRO TYR TYR SER TYR SEQRES 14 B 229 THR TYR TYR ALA ASP SER VAL LYS GLY ARG PHE THR ILE SEQRES 15 B 229 SER ALA ASP THR SER LYS ASN THR ALA TYR LEU GLN MET SEQRES 16 B 229 ASN SER LEU ARG ALA GLU ASP THR ALA VAL TYR TYR CYS SEQRES 17 B 229 ALA ARG HIS GLY TYR GLY ALA MET ASP TYR TRP GLY GLN SEQRES 18 B 229 GLY THR LEU VAL THR VAL SER SER HET NHE C 301 13 HET CL C 302 1 HET NHE D 301 13 HET SO4 D 302 5 HET NA D 303 1 HET NHE A 301 13 HET CL A 302 2 HET CL A 303 1 HET NHE B 301 26 HET CL B 302 1 HET CL B 303 1 HET CL B 304 1 HET CL B 305 1 HET NA B 306 1 HETNAM NHE 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID HETNAM CL CHLORIDE ION HETNAM SO4 SULFATE ION HETNAM NA SODIUM ION HETSYN NHE N-CYCLOHEXYLTAURINE; CHES FORMUL 5 NHE 4(C8 H17 N O3 S) FORMUL 6 CL 7(CL 1-) FORMUL 8 SO4 O4 S 2- FORMUL 9 NA 2(NA 1+) FORMUL 19 HOH *586(H2 O) HELIX 1 AA1 GLN C 79 PHE C 83 5 5 HELIX 2 AA2 ASN C 140 TYR C 144 5 5 HELIX 3 AA3 ARG C 199 THR C 203 5 5 HELIX 4 AA4 GLN D 79 PHE D 83 5 5 HELIX 5 AA5 ASN D 140 TYR D 144 5 5 HELIX 6 AA6 ASP D 174 LYS D 177 5 4 HELIX 7 AA7 THR D 186 LYS D 188 5 3 HELIX 8 AA8 ARG D 199 THR D 203 5 5 HELIX 9 AA9 GLN A 79 PHE A 83 5 5 HELIX 10 AB1 ASN A 140 TYR A 144 5 5 HELIX 11 AB2 ASP A 174 LYS A 177 5 4 HELIX 12 AB3 THR A 186 LYS A 188 5 3 HELIX 13 AB4 ARG A 199 THR A 203 5 5 HELIX 14 AB5 GLN B 79 PHE B 83 5 5 HELIX 15 AB6 ASN B 140 TYR B 144 5 5 HELIX 16 AB7 ASP B 174 LYS B 177 5 4 HELIX 17 AB8 ARG B 199 THR B 203 5 5 SHEET 1 AA1 4 MET C 4 SER C 7 0 SHEET 2 AA1 4 VAL C 19 ALA C 25 -1 O ARG C 24 N THR C 5 SHEET 3 AA1 4 ASP C 70 ILE C 75 -1 O ILE C 75 N VAL C 19 SHEET 4 AA1 4 PHE C 62 SER C 67 -1 N SER C 67 O ASP C 70 SHEET 1 AA212 SER C 53 LEU C 54 0 SHEET 2 AA212 LYS C 45 TYR C 49 -1 N TYR C 49 O SER C 53 SHEET 3 AA212 VAL C 33 GLN C 38 -1 N TRP C 35 O LEU C 47 SHEET 4 AA212 THR C 85 SER C 91 -1 O THR C 85 N GLN C 38 SHEET 5 AA212 THR C 102 GLU C 105 -1 O THR C 102 N TYR C 86 SHEET 6 AA212 SER C 10 SER C 12 1 N LEU C 11 O GLU C 105 SHEET 7 AA212 SER A 10 ALA A 13 -1 O SER A 10 N SER C 12 SHEET 8 AA212 THR A 102 ILE A 106 1 O GLU A 105 N LEU A 11 SHEET 9 AA212 THR A 85 SER A 91 -1 N TYR A 86 O THR A 102 SHEET 10 AA212 VAL A 33 GLN A 38 -1 N TYR A 36 O TYR A 87 SHEET 11 AA212 LYS A 45 TYR A 49 -1 O LEU A 47 N TRP A 35 SHEET 12 AA212 SER A 53 LEU A 54 -1 O SER A 53 N TYR A 49 SHEET 1 AA3 8 ILE C 96 PHE C 98 0 SHEET 2 AA3 8 THR C 85 SER C 91 -1 N GLN C 90 O THR C 97 SHEET 3 AA3 8 THR C 102 GLU C 105 -1 O THR C 102 N TYR C 86 SHEET 4 AA3 8 SER C 10 SER C 12 1 N LEU C 11 O GLU C 105 SHEET 5 AA3 8 SER A 10 ALA A 13 -1 O SER A 10 N SER C 12 SHEET 6 AA3 8 THR A 102 ILE A 106 1 O GLU A 105 N LEU A 11 SHEET 7 AA3 8 THR A 85 SER A 91 -1 N TYR A 86 O THR A 102 SHEET 8 AA3 8 ILE A 96 PHE A 98 -1 O THR A 97 N GLN A 90 SHEET 1 AA4 4 GLN C 115 SER C 119 0 SHEET 2 AA4 4 LEU C 130 SER C 137 -1 O ALA C 135 N VAL C 117 SHEET 3 AA4 4 THR C 190 MET C 195 -1 O MET C 195 N LEU C 130 SHEET 4 AA4 4 PHE C 180 ASP C 185 -1 N THR C 181 O GLN C 194 SHEET 1 AA5 6 GLY C 122 VAL C 124 0 SHEET 2 AA5 6 THR C 223 VAL C 227 1 O THR C 226 N VAL C 124 SHEET 3 AA5 6 ALA C 204 GLY C 212 -1 N TYR C 206 O THR C 223 SHEET 4 AA5 6 MET C 146 GLN C 151 -1 N VAL C 149 O TYR C 207 SHEET 5 AA5 6 GLU C 158 ILE C 163 -1 O ALA C 161 N TRP C 148 SHEET 6 AA5 6 THR C 170 TYR C 172 -1 O TYR C 171 N SER C 162 SHEET 1 AA6 4 GLY C 122 VAL C 124 0 SHEET 2 AA6 4 THR C 223 VAL C 227 1 O THR C 226 N VAL C 124 SHEET 3 AA6 4 ALA C 204 GLY C 212 -1 N TYR C 206 O THR C 223 SHEET 4 AA6 4 ALA C 215 TRP C 219 -1 O TYR C 218 N ARG C 210 SHEET 1 AA7 4 MET D 4 SER D 7 0 SHEET 2 AA7 4 VAL D 19 ALA D 25 -1 O ARG D 24 N THR D 5 SHEET 3 AA7 4 ASP D 70 ILE D 75 -1 O PHE D 71 N CYS D 23 SHEET 4 AA7 4 PHE D 62 SER D 67 -1 N SER D 63 O THR D 74 SHEET 1 AA8 6 SER D 10 ALA D 13 0 SHEET 2 AA8 6 THR D 102 ILE D 106 1 O GLU D 105 N LEU D 11 SHEET 3 AA8 6 THR D 85 SER D 91 -1 N TYR D 86 O THR D 102 SHEET 4 AA8 6 VAL D 33 GLN D 38 -1 N GLN D 38 O THR D 85 SHEET 5 AA8 6 LYS D 45 TYR D 49 -1 O LEU D 47 N TRP D 35 SHEET 6 AA8 6 SER D 53 LEU D 54 -1 O SER D 53 N TYR D 49 SHEET 1 AA9 4 SER D 10 ALA D 13 0 SHEET 2 AA9 4 THR D 102 ILE D 106 1 O GLU D 105 N LEU D 11 SHEET 3 AA9 4 THR D 85 SER D 91 -1 N TYR D 86 O THR D 102 SHEET 4 AA9 4 ILE D 96 PHE D 98 -1 O THR D 97 N GLN D 90 SHEET 1 AB1 4 GLN D 115 SER D 119 0 SHEET 2 AB1 4 LEU D 130 SER D 137 -1 O SER D 133 N SER D 119 SHEET 3 AB1 4 THR D 190 MET D 195 -1 O MET D 195 N LEU D 130 SHEET 4 AB1 4 PHE D 180 ASP D 185 -1 N SER D 183 O TYR D 192 SHEET 1 AB2 6 LEU D 123 VAL D 124 0 SHEET 2 AB2 6 THR D 223 VAL D 227 1 O THR D 226 N VAL D 124 SHEET 3 AB2 6 ALA D 204 GLY D 212 -1 N TYR D 206 O THR D 223 SHEET 4 AB2 6 MET D 146 GLN D 151 -1 N VAL D 149 O TYR D 207 SHEET 5 AB2 6 LEU D 157 ILE D 163 -1 O ALA D 161 N TRP D 148 SHEET 6 AB2 6 THR D 170 TYR D 172 -1 O TYR D 171 N SER D 162 SHEET 1 AB3 4 LEU D 123 VAL D 124 0 SHEET 2 AB3 4 THR D 223 VAL D 227 1 O THR D 226 N VAL D 124 SHEET 3 AB3 4 ALA D 204 GLY D 212 -1 N TYR D 206 O THR D 223 SHEET 4 AB3 4 ALA D 215 TRP D 219 -1 O ALA D 215 N GLY D 212 SHEET 1 AB4 4 MET A 4 SER A 7 0 SHEET 2 AB4 4 VAL A 19 ALA A 25 -1 O THR A 22 N SER A 7 SHEET 3 AB4 4 ASP A 70 ILE A 75 -1 O PHE A 71 N CYS A 23 SHEET 4 AB4 4 PHE A 62 SER A 67 -1 N SER A 63 O THR A 74 SHEET 1 AB5 4 GLN A 115 SER A 119 0 SHEET 2 AB5 4 LEU A 130 SER A 137 -1 O SER A 133 N SER A 119 SHEET 3 AB5 4 THR A 190 MET A 195 -1 O MET A 195 N LEU A 130 SHEET 4 AB5 4 PHE A 180 ASP A 185 -1 N THR A 181 O GLN A 194 SHEET 1 AB6 6 GLY A 122 VAL A 124 0 SHEET 2 AB6 6 THR A 223 VAL A 227 1 O THR A 226 N VAL A 124 SHEET 3 AB6 6 ALA A 204 GLY A 212 -1 N TYR A 206 O THR A 223 SHEET 4 AB6 6 MET A 146 GLN A 151 -1 N VAL A 149 O TYR A 207 SHEET 5 AB6 6 LEU A 157 ILE A 163 -1 O GLU A 158 N ARG A 150 SHEET 6 AB6 6 THR A 170 TYR A 172 -1 O TYR A 171 N SER A 162 SHEET 1 AB7 4 GLY A 122 VAL A 124 0 SHEET 2 AB7 4 THR A 223 VAL A 227 1 O THR A 226 N VAL A 124 SHEET 3 AB7 4 ALA A 204 GLY A 212 -1 N TYR A 206 O THR A 223 SHEET 4 AB7 4 ALA A 215 TRP A 219 -1 O ALA A 215 N GLY A 212 SHEET 1 AB8 4 MET B 4 SER B 7 0 SHEET 2 AB8 4 VAL B 19 ALA B 25 -1 O ARG B 24 N THR B 5 SHEET 3 AB8 4 ASP B 70 ILE B 75 -1 O PHE B 71 N CYS B 23 SHEET 4 AB8 4 PHE B 62 SER B 67 -1 N SER B 63 O THR B 74 SHEET 1 AB9 6 SER B 10 ALA B 13 0 SHEET 2 AB9 6 THR B 102 ILE B 106 1 O GLU B 105 N LEU B 11 SHEET 3 AB9 6 ALA B 84 SER B 91 -1 N ALA B 84 O VAL B 104 SHEET 4 AB9 6 VAL B 33 GLN B 38 -1 N GLN B 38 O THR B 85 SHEET 5 AB9 6 LYS B 45 TYR B 49 -1 O LEU B 47 N TRP B 35 SHEET 6 AB9 6 SER B 53 LEU B 54 -1 O SER B 53 N TYR B 49 SHEET 1 AC1 4 SER B 10 ALA B 13 0 SHEET 2 AC1 4 THR B 102 ILE B 106 1 O GLU B 105 N LEU B 11 SHEET 3 AC1 4 ALA B 84 SER B 91 -1 N ALA B 84 O VAL B 104 SHEET 4 AC1 4 ILE B 96 PHE B 98 -1 O THR B 97 N GLN B 90 SHEET 1 AC2 4 GLN B 115 SER B 119 0 SHEET 2 AC2 4 LEU B 130 SER B 137 -1 O SER B 133 N SER B 119 SHEET 3 AC2 4 THR B 190 MET B 195 -1 O MET B 195 N LEU B 130 SHEET 4 AC2 4 PHE B 180 ASP B 185 -1 N THR B 181 O GLN B 194 SHEET 1 AC3 6 LEU B 123 VAL B 124 0 SHEET 2 AC3 6 THR B 223 VAL B 227 1 O THR B 226 N VAL B 124 SHEET 3 AC3 6 ALA B 204 GLY B 212 -1 N TYR B 206 O THR B 223 SHEET 4 AC3 6 MET B 146 GLN B 151 -1 N VAL B 149 O TYR B 207 SHEET 5 AC3 6 LEU B 157 ILE B 163 -1 O GLU B 158 N ARG B 150 SHEET 6 AC3 6 THR B 170 TYR B 172 -1 O TYR B 171 N SER B 162 SHEET 1 AC4 4 LEU B 123 VAL B 124 0 SHEET 2 AC4 4 THR B 223 VAL B 227 1 O THR B 226 N VAL B 124 SHEET 3 AC4 4 ALA B 204 GLY B 212 -1 N TYR B 206 O THR B 223 SHEET 4 AC4 4 ALA B 215 TRP B 219 -1 O ALA B 215 N GLY B 212 SSBOND 1 CYS C 23 CYS C 88 1555 1555 2.05 SSBOND 2 CYS C 134 CYS C 208 1555 1555 2.05 SSBOND 3 CYS D 23 CYS D 88 1555 1555 2.02 SSBOND 4 CYS D 134 CYS D 208 1555 1555 2.04 SSBOND 5 CYS A 23 CYS A 88 1555 1555 2.04 SSBOND 6 CYS A 134 CYS A 208 1555 1555 2.04 SSBOND 7 CYS B 23 CYS B 88 1555 1555 2.05 SSBOND 8 CYS B 134 CYS B 208 1555 1555 2.04 LINK O SER D 175 NA NA D 303 1555 1555 3.15 LINK O LYS D 177 NA NA D 303 1555 1555 2.70 CISPEP 1 SER C 7 PRO C 8 0 -5.96 CISPEP 2 SER D 7 PRO D 8 0 -3.62 CISPEP 3 SER A 7 PRO A 8 0 -4.00 CISPEP 4 SER B 7 PRO B 8 0 -6.14 CRYST1 57.355 141.779 60.651 90.00 90.76 90.00 P 1 21 1 8 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 0.017435 0.000000 0.000231 0.00000 SCALE2 0.000000 0.007053 0.000000 0.00000 SCALE3 0.000000 0.000000 0.016489 0.00000