HEADER IMMUNE SYSTEM 14-APR-23 8SHW TITLE 38B7 WITH HYDROXY-PROLINE PEPTIDE COMPND MOL_ID: 1; COMPND 2 MOLECULE: 38B7 LIGHT CHAIN; COMPND 3 CHAIN: L, A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: 38B7 HEAVY CHAIN; COMPND 7 CHAIN: H, C; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: CONGLUTIN-7; COMPND 11 CHAIN: Q, B; COMPND 12 SYNONYM: 2S PROTEIN 1,SEED STORAGE PROTEIN SSP1,SEED STORAGE PROTEIN COMPND 13 SSP2; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 CELL_LINE: EXPI293; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: EXPI293; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 12 ORGANISM_COMMON: HUMAN; SOURCE 13 ORGANISM_TAXID: 9606; SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 15 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 17 EXPRESSION_SYSTEM_CELL_LINE: EXPI293; SOURCE 18 MOL_ID: 3; SOURCE 19 SYNTHETIC: YES; SOURCE 20 ORGANISM_SCIENTIFIC: ARACHIS HYPOGAEA; SOURCE 21 ORGANISM_COMMON: PEANUT; SOURCE 22 ORGANISM_TAXID: 3818 KEYWDS ALLERGY, PEANUT, ANTIBODY, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR B.W.SPILLER,R.A.SHREM REVDAT 1 25-DEC-24 8SHW 0 JRNL AUTH S.A.SMITH,R.A.SHREM,B.B.C.LANCA,J.ZHANG,J.J.W.WONG,D.CROOTE, JRNL AUTH 2 R.S.PEEBLES JR,B.W.SPILLER JRNL TITL ANTIGENIC DETERMINANTS OF PEANUT INDUCED ANAPHYLAXIS JRNL REF J CLIN IMMUNOL 2024 REMARK 2 REMARK 2 RESOLUTION. 1.95 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) : 1.95 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.74 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6 REMARK 3 NUMBER OF REFLECTIONS : 67972 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.179 REMARK 3 R VALUE (WORKING SET) : 0.178 REMARK 3 FREE R VALUE : 0.205 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.910 REMARK 3 FREE R VALUE TEST SET COUNT : 3336 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 30.7400 - 5.6200 0.98 2752 172 0.1528 0.1636 REMARK 3 2 5.6200 - 4.4600 0.99 2780 129 0.1232 0.1449 REMARK 3 3 4.4600 - 3.9000 0.99 2736 148 0.1417 0.1489 REMARK 3 4 3.9000 - 3.5400 0.99 2741 142 0.1583 0.1709 REMARK 3 5 3.5400 - 3.2900 0.98 2720 116 0.1671 0.2121 REMARK 3 6 3.2900 - 3.1000 0.98 2759 125 0.1938 0.2109 REMARK 3 7 3.1000 - 2.9400 0.98 2698 134 0.1978 0.2181 REMARK 3 8 2.9400 - 2.8100 0.98 2702 148 0.2010 0.2518 REMARK 3 9 2.8100 - 2.7100 0.98 2687 148 0.2009 0.2509 REMARK 3 10 2.7100 - 2.6100 0.98 2703 134 0.2110 0.2406 REMARK 3 11 2.6100 - 2.5300 0.98 2694 128 0.2219 0.2953 REMARK 3 12 2.5300 - 2.4600 0.98 2694 125 0.2085 0.2563 REMARK 3 13 2.4600 - 2.3900 0.97 2694 130 0.2048 0.2397 REMARK 3 14 2.3900 - 2.3400 0.97 2692 137 0.2068 0.2799 REMARK 3 15 2.3400 - 2.2800 0.97 2668 141 0.2042 0.2305 REMARK 3 16 2.2800 - 2.2300 0.97 2684 137 0.1982 0.2632 REMARK 3 17 2.2300 - 2.1900 0.97 2645 136 0.2037 0.2254 REMARK 3 18 2.1900 - 2.1500 0.97 2684 156 0.2077 0.2382 REMARK 3 19 2.1500 - 2.1100 0.97 2666 136 0.2175 0.2570 REMARK 3 20 2.1100 - 2.0700 0.97 2628 128 0.2307 0.2828 REMARK 3 21 2.0700 - 2.0400 0.97 2711 130 0.2324 0.2580 REMARK 3 22 2.0400 - 2.0100 0.97 2628 152 0.2445 0.2787 REMARK 3 23 2.0100 - 1.9800 0.97 2628 166 0.2526 0.3202 REMARK 3 24 1.9800 - 1.9500 0.97 2642 138 0.2611 0.2920 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) : 0.216 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.545 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 33.56 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.41 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 6984 REMARK 3 ANGLE : 0.589 9503 REMARK 3 CHIRALITY : 0.045 1069 REMARK 3 PLANARITY : 0.005 1218 REMARK 3 DIHEDRAL : 12.840 2530 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 13 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 107 ) REMARK 3 ORIGIN FOR THE GROUP (A): 26.3484 -3.6002 24.9849 REMARK 3 T TENSOR REMARK 3 T11: 0.2945 T22: 0.3113 REMARK 3 T33: 0.2946 T12: 0.0274 REMARK 3 T13: 0.0303 T23: -0.0569 REMARK 3 L TENSOR REMARK 3 L11: 2.3593 L22: 3.0612 REMARK 3 L33: 2.5924 L12: 0.4498 REMARK 3 L13: 0.1907 L23: 1.0960 REMARK 3 S TENSOR REMARK 3 S11: -0.0339 S12: 0.0333 S13: -0.0615 REMARK 3 S21: 0.0668 S22: -0.1504 S23: 0.1733 REMARK 3 S31: 0.1312 S32: -0.0706 S33: 0.1721 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 108 THROUGH 214 ) REMARK 3 ORIGIN FOR THE GROUP (A): 55.5818 16.9312 26.9455 REMARK 3 T TENSOR REMARK 3 T11: 0.3287 T22: 0.1298 REMARK 3 T33: 0.5311 T12: 0.0278 REMARK 3 T13: -0.1137 T23: -0.0894 REMARK 3 L TENSOR REMARK 3 L11: 3.7872 L22: 2.1306 REMARK 3 L33: 3.3758 L12: 0.9604 REMARK 3 L13: 0.2678 L23: 0.3616 REMARK 3 S TENSOR REMARK 3 S11: -0.0335 S12: -0.3129 S13: 0.6769 REMARK 3 S21: -0.0445 S22: -0.0139 S23: -0.0761 REMARK 3 S31: -0.5852 S32: 0.1678 S33: -0.2601 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 124 ) REMARK 3 ORIGIN FOR THE GROUP (A): 33.7046 -7.0803 4.8087 REMARK 3 T TENSOR REMARK 3 T11: 0.4854 T22: 0.4690 REMARK 3 T33: 0.3193 T12: -0.0396 REMARK 3 T13: 0.0237 T23: -0.0840 REMARK 3 L TENSOR REMARK 3 L11: 4.9256 L22: 0.7595 REMARK 3 L33: 1.7565 L12: 0.6770 REMARK 3 L13: -0.3228 L23: 0.4458 REMARK 3 S TENSOR REMARK 3 S11: -0.4201 S12: 0.8328 S13: -0.1856 REMARK 3 S21: -0.3579 S22: 0.1032 S23: 0.0978 REMARK 3 S31: 0.0317 S32: -0.1106 S33: 0.1499 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 125 THROUGH 220 ) REMARK 3 ORIGIN FOR THE GROUP (A): 63.6082 4.2922 21.6689 REMARK 3 T TENSOR REMARK 3 T11: 0.3803 T22: 0.3845 REMARK 3 T33: 0.4056 T12: 0.0309 REMARK 3 T13: -0.0255 T23: -0.0005 REMARK 3 L TENSOR REMARK 3 L11: 4.5098 L22: 3.6300 REMARK 3 L33: 3.7092 L12: -0.5928 REMARK 3 L13: 0.3416 L23: -0.6901 REMARK 3 S TENSOR REMARK 3 S11: -0.1635 S12: -0.2206 S13: 0.3385 REMARK 3 S21: 0.0855 S22: 0.0491 S23: -0.3746 REMARK 3 S31: -0.0636 S32: 0.4450 S33: 0.0131 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 18 ) REMARK 3 ORIGIN FOR THE GROUP (A): 84.1045 -33.8337 32.1406 REMARK 3 T TENSOR REMARK 3 T11: 0.1787 T22: 0.1665 REMARK 3 T33: 0.2154 T12: 0.0066 REMARK 3 T13: -0.0237 T23: -0.0617 REMARK 3 L TENSOR REMARK 3 L11: 3.3712 L22: 3.7155 REMARK 3 L33: 2.5140 L12: 0.5128 REMARK 3 L13: -1.2972 L23: -1.1071 REMARK 3 S TENSOR REMARK 3 S11: 0.0253 S12: 0.1228 S13: -0.3629 REMARK 3 S21: -0.0405 S22: -0.0730 S23: -0.1373 REMARK 3 S31: 0.0767 S32: 0.2375 S33: 0.0095 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 19 THROUGH 61 ) REMARK 3 ORIGIN FOR THE GROUP (A): 87.7560 -23.5076 34.2378 REMARK 3 T TENSOR REMARK 3 T11: 0.2327 T22: 0.2391 REMARK 3 T33: 0.2145 T12: 0.0310 REMARK 3 T13: -0.0038 T23: -0.0202 REMARK 3 L TENSOR REMARK 3 L11: 1.0358 L22: 3.4926 REMARK 3 L33: 2.0193 L12: 0.1849 REMARK 3 L13: 0.4569 L23: 0.2057 REMARK 3 S TENSOR REMARK 3 S11: 0.0886 S12: 0.0499 S13: 0.0307 REMARK 3 S21: 0.0265 S22: -0.0650 S23: 0.1190 REMARK 3 S31: -0.1141 S32: -0.0693 S33: -0.0282 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 62 THROUGH 107 ) REMARK 3 ORIGIN FOR THE GROUP (A): 86.9775 -26.5431 31.9373 REMARK 3 T TENSOR REMARK 3 T11: 0.2243 T22: 0.2444 REMARK 3 T33: 0.2453 T12: 0.0492 REMARK 3 T13: 0.0076 T23: -0.0371 REMARK 3 L TENSOR REMARK 3 L11: 1.1970 L22: 1.8349 REMARK 3 L33: 1.5075 L12: 0.1584 REMARK 3 L13: 0.0285 L23: -0.2561 REMARK 3 S TENSOR REMARK 3 S11: 0.1373 S12: 0.0504 S13: -0.0982 REMARK 3 S21: 0.0555 S22: -0.0698 S23: -0.0338 REMARK 3 S31: 0.0188 S32: 0.0235 S33: -0.0226 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 108 THROUGH 214 ) REMARK 3 ORIGIN FOR THE GROUP (A): 58.6824 -42.0988 17.6107 REMARK 3 T TENSOR REMARK 3 T11: 0.4570 T22: 0.8414 REMARK 3 T33: 0.6901 T12: -0.0276 REMARK 3 T13: -0.0528 T23: -0.4393 REMARK 3 L TENSOR REMARK 3 L11: 1.9374 L22: 2.8714 REMARK 3 L33: 2.0364 L12: 1.5564 REMARK 3 L13: -0.4377 L23: -0.5622 REMARK 3 S TENSOR REMARK 3 S11: -0.0442 S12: 1.1148 S13: -1.0031 REMARK 3 S21: -0.5344 S22: 0.2785 S23: 0.0280 REMARK 3 S31: 0.3658 S32: -0.0070 S33: -0.1760 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 33 ) REMARK 3 ORIGIN FOR THE GROUP (A): 79.9657 -5.7922 20.7090 REMARK 3 T TENSOR REMARK 3 T11: 0.4514 T22: 0.3897 REMARK 3 T33: 0.3747 T12: 0.1121 REMARK 3 T13: -0.0340 T23: 0.0425 REMARK 3 L TENSOR REMARK 3 L11: 3.9867 L22: 3.1358 REMARK 3 L33: 2.5741 L12: 0.7414 REMARK 3 L13: 0.1505 L23: 0.9715 REMARK 3 S TENSOR REMARK 3 S11: -0.0527 S12: 0.0373 S13: 0.4132 REMARK 3 S21: -0.1288 S22: -0.0400 S23: 0.1797 REMARK 3 S31: -0.4773 S32: -0.4855 S33: 0.0439 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 34 THROUGH 124 ) REMARK 3 ORIGIN FOR THE GROUP (A): 82.9672 -12.5240 17.4675 REMARK 3 T TENSOR REMARK 3 T11: 0.3072 T22: 0.2880 REMARK 3 T33: 0.1730 T12: 0.0322 REMARK 3 T13: 0.0018 T23: 0.0109 REMARK 3 L TENSOR REMARK 3 L11: 2.6034 L22: 1.2068 REMARK 3 L33: 1.6894 L12: -0.0726 REMARK 3 L13: -0.4245 L23: -0.7262 REMARK 3 S TENSOR REMARK 3 S11: -0.0840 S12: 0.4168 S13: 0.2241 REMARK 3 S21: -0.3040 S22: 0.0555 S23: -0.0245 REMARK 3 S31: -0.1900 S32: -0.2243 S33: 0.2918 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 125 THROUGH 220 ) REMARK 3 ORIGIN FOR THE GROUP (A): 51.0141 -27.8678 19.6842 REMARK 3 T TENSOR REMARK 3 T11: 0.2358 T22: 0.6614 REMARK 3 T33: 0.4068 T12: -0.0308 REMARK 3 T13: -0.0526 T23: -0.0826 REMARK 3 L TENSOR REMARK 3 L11: 0.8406 L22: 3.1190 REMARK 3 L33: 3.0272 L12: -0.0738 REMARK 3 L13: -0.0001 L23: 0.5327 REMARK 3 S TENSOR REMARK 3 S11: -0.0694 S12: 0.9814 S13: -0.0181 REMARK 3 S21: -0.2009 S22: -0.0287 S23: 0.8644 REMARK 3 S31: 0.0202 S32: -0.4123 S33: 0.0326 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'Q' AND (RESID 37 THROUGH 44 ) REMARK 3 ORIGIN FOR THE GROUP (A): 14.8500 -12.8704 5.0956 REMARK 3 T TENSOR REMARK 3 T11: 0.4994 T22: 0.9484 REMARK 3 T33: 0.6896 T12: -0.1413 REMARK 3 T13: -0.1103 T23: -0.5618 REMARK 3 L TENSOR REMARK 3 L11: 3.5783 L22: 1.7252 REMARK 3 L33: 2.8396 L12: 0.9290 REMARK 3 L13: 1.7316 L23: 0.3704 REMARK 3 S TENSOR REMARK 3 S11: -0.0755 S12: 0.2701 S13: -0.1514 REMARK 3 S21: -0.4244 S22: 0.0303 S23: 0.9607 REMARK 3 S31: 0.3069 S32: -1.1057 S33: 0.1555 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 37 THROUGH 44 ) REMARK 3 ORIGIN FOR THE GROUP (A): 100.2489 -7.3444 25.4747 REMARK 3 T TENSOR REMARK 3 T11: 0.4335 T22: 0.5180 REMARK 3 T33: 0.4793 T12: -0.0064 REMARK 3 T13: -0.0087 T23: 0.0700 REMARK 3 L TENSOR REMARK 3 L11: 8.2329 L22: 3.2727 REMARK 3 L33: 7.3290 L12: -1.4445 REMARK 3 L13: 0.1765 L23: -0.7537 REMARK 3 S TENSOR REMARK 3 S11: -0.6138 S12: 0.3093 S13: 0.1253 REMARK 3 S21: 0.0028 S22: 0.3974 S23: -0.4950 REMARK 3 S31: 0.2629 S32: 1.1320 S33: 0.3890 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : 3 REMARK 3 NCS GROUP : ens_1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "A" and (resid 1 through 41 or REMARK 3 resid 43 through 66 or resid 68 through REMARK 3 214 or resid 215)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "L" and (resid 1 through 41 or REMARK 3 resid 43 through 66 or resid 68 through REMARK 3 215)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : ens_2 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "B" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "Q" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : ens_3 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "C" and (resid 1 through 95 or REMARK 3 resid 97 through 186 or resid 188 through REMARK 3 190 or resid 192 through 220)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "H" and (resid 1 through 95 or REMARK 3 resid 97 through 132 or resid 138 through REMARK 3 186 or resid 188 through 190 or resid 192 REMARK 3 through 220)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 8SHW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-APR-23. REMARK 100 THE DEPOSITION ID IS D_1000273813. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 02-JUN-22 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 21-ID-G REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97857 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS 20220820 REMARK 200 DATA SCALING SOFTWARE : POINTLESS 1.12.12 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 67997 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6 REMARK 200 DATA REDUNDANCY : 4.300 REMARK 200 R MERGE (I) : 0.05000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 15.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02 REMARK 200 COMPLETENESS FOR SHELL (%) : 96.6 REMARK 200 DATA REDUNDANCY IN SHELL : 4.40 REMARK 200 R MERGE FOR SHELL (I) : 0.65000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.400 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: NULL REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 50.26 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM NACITRATE PH 5.6, 20% ISOPROPYL REMARK 280 ALCOHOL, 20% PEG 4000, 10 MM CDCL2, VAPOR DIFFUSION, HANGING REMARK 280 DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z REMARK 290 4555 -X+1/2,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 64.01050 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.89200 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 64.01050 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 45.89200 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, Q, 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: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, 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 CYS L 215 REMARK 465 SER H 135 REMARK 465 THR H 136 REMARK 465 SER H 137 REMARK 465 CYS H 221 REMARK 465 CYS A 215 REMARK 465 SER C 133 REMARK 465 LYS C 134 REMARK 465 SER C 135 REMARK 465 THR C 136 REMARK 465 SER C 137 REMARK 465 CYS C 221 REMARK 465 GLU Q 32 REMARK 465 ASP Q 33 REMARK 465 SER Q 34 REMARK 465 TYR Q 35 REMARK 465 GLU Q 36 REMARK 465 ASP Q 45 REMARK 465 GLU B 32 REMARK 465 ASP B 33 REMARK 465 SER B 34 REMARK 465 TYR B 35 REMARK 465 GLU B 36 REMARK 465 ASP B 45 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 H 398 O HOH H 400 1.81 REMARK 500 O HOH A 533 O HOH A 545 1.87 REMARK 500 O HOH A 531 O HOH A 551 2.00 REMARK 500 O HOH C 311 O HOH C 417 2.01 REMARK 500 O HOH H 357 O HOH H 431 2.02 REMARK 500 O HOH H 308 O HOH H 408 2.05 REMARK 500 OG SER A 177 O HOH A 401 2.06 REMARK 500 O HOH L 410 O HOH L 442 2.07 REMARK 500 O HOH L 430 O HOH L 444 2.09 REMARK 500 O HOH A 423 O HOH A 477 2.11 REMARK 500 O HOH L 419 O HOH L 441 2.11 REMARK 500 O HOH C 440 O HOH C 443 2.12 REMARK 500 O HOH C 370 O HOH C 379 2.15 REMARK 500 O HOH A 424 O HOH C 414 2.16 REMARK 500 O SER A 209 O HOH A 402 2.18 REMARK 500 O VAL H 23 O HOH H 301 2.19 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 O HOH L 464 O HOH A 547 3455 1.92 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 L 30 -123.10 56.96 REMARK 500 ALA L 51 -35.67 72.43 REMARK 500 TRP L 94 -23.68 68.66 REMARK 500 ASN L 139 73.98 52.23 REMARK 500 SER H 101 -14.69 -142.63 REMARK 500 ASP H 149 64.53 64.51 REMARK 500 ASP A 30 -122.87 58.61 REMARK 500 ALA A 51 -34.89 70.61 REMARK 500 ALA A 84 -178.64 -171.09 REMARK 500 TRP A 94 -20.58 69.41 REMARK 500 LYS A 170 -64.84 -97.73 REMARK 500 SER C 101 -14.49 -142.37 REMARK 500 ASP C 149 65.32 63.32 REMARK 500 REMARK 500 REMARK: NULL DBREF 8SHW L 1 215 PDB 8SHW 8SHW 1 215 DBREF 8SHW H 1 221 PDB 8SHW 8SHW 1 221 DBREF 8SHW A 1 215 PDB 8SHW 8SHW 1 215 DBREF 8SHW C 1 221 PDB 8SHW 8SHW 1 221 DBREF 8SHW Q 32 45 UNP Q6PSU2 CONG7_ARAHY 57 70 DBREF 8SHW B 32 45 UNP Q6PSU2 CONG7_ARAHY 57 70 SEQADV 8SHW GLU Q 36 UNP Q6PSU2 GLY 61 CONFLICT SEQADV 8SHW GLU B 36 UNP Q6PSU2 GLY 61 CONFLICT SEQRES 1 L 215 GLU ILE VAL LEU THR GLN SER PRO ALA THR LEU SER LEU SEQRES 2 L 215 SER PRO GLY ALA ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 L 215 GLN SER VAL ASP THR TYR LEU ALA TRP TYR GLN GLN ARG SEQRES 4 L 215 ARG GLY GLN SER PRO ARG LEU LEU ILE TYR ASP ALA SER SEQRES 5 L 215 LYS ARG ALA THR GLY ILE PRO ALA ARG PHE SER GLY SER SEQRES 6 L 215 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 215 GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN ARG SEQRES 8 L 215 ASN ASN TRP ARG THR TRP THR PHE GLY GLN GLY THR LYS SEQRES 9 L 215 VAL GLU ILE ASN 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 221 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL GLN SEQRES 2 H 221 PRO GLY ARG SER LEU ARG LEU SER CYS VAL GLY SER GLY SEQRES 3 H 221 PHE THR PHE ARG ARG ASP ALA LYS TYR TRP VAL ARG GLN SEQRES 4 H 221 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ALA ILE SER SEQRES 5 H 221 HIS ASP GLY GLY GLU GLU ASP TYR ALA GLU SER VAL LYS SEQRES 6 H 221 GLY ARG PHE THR ILE SER ARG ASP ASN SER ARG GLU THR SEQRES 7 H 221 VAL TYR LEU GLU MET ASN SER LEU ARG PRO GLU ASP THR SEQRES 8 H 221 ALA VAL TYR TYR CYS ALA THR THR ARG SER GLY TRP TYR SEQRES 9 H 221 PHE ASP TYR TRP GLY GLN GLY ALA LEU VAL THR VAL SER SEQRES 10 H 221 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 11 H 221 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU SEQRES 12 H 221 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR SEQRES 13 H 221 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS SEQRES 14 H 221 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER SEQRES 15 H 221 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY SEQRES 16 H 221 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER SEQRES 17 H 221 ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 1 A 215 GLU ILE VAL LEU THR GLN SER PRO ALA THR LEU SER LEU SEQRES 2 A 215 SER PRO GLY ALA ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 A 215 GLN SER VAL ASP THR TYR LEU ALA TRP TYR GLN GLN ARG SEQRES 4 A 215 ARG GLY GLN SER PRO ARG LEU LEU ILE TYR ASP ALA SER SEQRES 5 A 215 LYS ARG ALA THR GLY ILE PRO ALA ARG PHE SER GLY SER SEQRES 6 A 215 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 A 215 GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN ARG SEQRES 8 A 215 ASN ASN TRP ARG THR TRP THR PHE GLY GLN GLY THR LYS SEQRES 9 A 215 VAL GLU ILE ASN ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 A 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 A 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 A 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 A 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 A 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 A 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 A 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 A 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 C 221 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL GLN SEQRES 2 C 221 PRO GLY ARG SER LEU ARG LEU SER CYS VAL GLY SER GLY SEQRES 3 C 221 PHE THR PHE ARG ARG ASP ALA LYS TYR TRP VAL ARG GLN SEQRES 4 C 221 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ALA ILE SER SEQRES 5 C 221 HIS ASP GLY GLY GLU GLU ASP TYR ALA GLU SER VAL LYS SEQRES 6 C 221 GLY ARG PHE THR ILE SER ARG ASP ASN SER ARG GLU THR SEQRES 7 C 221 VAL TYR LEU GLU MET ASN SER LEU ARG PRO GLU ASP THR SEQRES 8 C 221 ALA VAL TYR TYR CYS ALA THR THR ARG SER GLY TRP TYR SEQRES 9 C 221 PHE ASP TYR TRP GLY GLN GLY ALA LEU VAL THR VAL SER SEQRES 10 C 221 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 11 C 221 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU SEQRES 12 C 221 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR SEQRES 13 C 221 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS SEQRES 14 C 221 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER SEQRES 15 C 221 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY SEQRES 16 C 221 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER SEQRES 17 C 221 ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 1 Q 14 GLU ASP SER TYR GLU ARG ASP PRO TYR SER HYP SER GLN SEQRES 2 Q 14 ASP SEQRES 1 B 14 GLU ASP SER TYR GLU ARG ASP PRO TYR SER HYP SER GLN SEQRES 2 B 14 ASP MODRES 8SHW HYP Q 42 PRO MODIFIED RESIDUE MODRES 8SHW HYP B 42 PRO MODIFIED RESIDUE HET HYP Q 42 8 HET HYP B 42 8 HET NAG D 1 14 HET NAG D 2 14 HET BMA D 3 11 HET MAN D 4 11 HET NAG A 301 14 HETNAM HYP 4-HYDROXYPROLINE HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETSYN HYP HYDROXYPROLINE 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 HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 5 HYP 2(C5 H9 N O3) FORMUL 7 NAG 3(C8 H15 N O6) FORMUL 7 BMA C6 H12 O6 FORMUL 7 MAN C6 H12 O6 FORMUL 9 HOH *651(H2 O) HELIX 1 AA1 GLU L 79 PHE L 83 5 5 HELIX 2 AA2 SER L 122 LYS L 127 1 6 HELIX 3 AA3 LYS L 184 LYS L 189 1 6 HELIX 4 AA4 THR H 28 ASP H 32 5 5 HELIX 5 AA5 ASN H 74 ARG H 76 5 3 HELIX 6 AA6 ARG H 87 THR H 91 5 5 HELIX 7 AA7 SER H 161 ALA H 163 5 3 HELIX 8 AA8 SER H 192 LEU H 194 5 3 HELIX 9 AA9 LYS H 206 ASN H 209 5 4 HELIX 10 AB1 GLU A 79 PHE A 83 5 5 HELIX 11 AB2 SER A 122 LYS A 127 1 6 HELIX 12 AB3 LYS A 184 GLU A 188 1 5 HELIX 13 AB4 THR C 28 ASP C 32 5 5 HELIX 14 AB5 ASN C 74 ARG C 76 5 3 HELIX 15 AB6 ARG C 87 THR C 91 5 5 HELIX 16 AB7 SER C 161 ALA C 163 5 3 HELIX 17 AB8 SER C 192 LEU C 194 5 3 HELIX 18 AB9 LYS C 206 ASN C 209 5 4 SHEET 1 AA1 4 LEU L 4 SER L 7 0 SHEET 2 AA1 4 ALA L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AA1 4 ASP L 70 ILE L 75 -1 O LEU L 73 N LEU L 21 SHEET 4 AA1 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AA2 6 THR L 10 LEU L 13 0 SHEET 2 AA2 6 THR L 103 ILE L 107 1 O LYS L 104 N LEU L 11 SHEET 3 AA2 6 VAL L 85 ASN L 92 -1 N TYR L 86 O THR L 103 SHEET 4 AA2 6 ALA L 34 GLN L 38 -1 N TYR L 36 O TYR L 87 SHEET 5 AA2 6 ARG L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AA2 6 LYS L 53 ARG L 54 -1 O LYS L 53 N TYR L 49 SHEET 1 AA3 4 THR L 10 LEU L 13 0 SHEET 2 AA3 4 THR L 103 ILE L 107 1 O LYS L 104 N LEU L 11 SHEET 3 AA3 4 VAL L 85 ASN L 92 -1 N TYR L 86 O THR L 103 SHEET 4 AA3 4 THR L 96 PHE L 99 -1 O THR L 98 N GLN L 90 SHEET 1 AA4 4 SER L 115 PHE L 119 0 SHEET 2 AA4 4 THR L 130 PHE L 140 -1 O LEU L 136 N PHE L 117 SHEET 3 AA4 4 TYR L 174 SER L 183 -1 O LEU L 180 N VAL L 133 SHEET 4 AA4 4 SER L 160 VAL L 164 -1 N SER L 163 O SER L 177 SHEET 1 AA5 4 ALA L 154 LEU L 155 0 SHEET 2 AA5 4 LYS L 146 VAL L 151 -1 N VAL L 151 O ALA L 154 SHEET 3 AA5 4 VAL L 192 THR L 198 -1 O ALA L 194 N LYS L 150 SHEET 4 AA5 4 VAL L 206 ASN L 211 -1 O VAL L 206 N VAL L 197 SHEET 1 AA6 4 GLN H 3 SER H 7 0 SHEET 2 AA6 4 LEU H 18 SER H 25 -1 O SER H 21 N SER H 7 SHEET 3 AA6 4 THR H 78 MET H 83 -1 O LEU H 81 N LEU H 20 SHEET 4 AA6 4 PHE H 68 ASP H 73 -1 N SER H 71 O TYR H 80 SHEET 1 AA7 6 GLY H 10 VAL H 12 0 SHEET 2 AA7 6 ALA H 112 VAL H 116 1 O THR H 115 N VAL H 12 SHEET 3 AA7 6 ALA H 92 THR H 98 -1 N TYR H 94 O ALA H 112 SHEET 4 AA7 6 LYS H 34 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AA7 6 LEU H 45 ILE H 51 -1 O VAL H 48 N TRP H 36 SHEET 6 AA7 6 GLU H 58 TYR H 60 -1 O ASP H 59 N ALA H 50 SHEET 1 AA8 4 GLY H 10 VAL H 12 0 SHEET 2 AA8 4 ALA H 112 VAL H 116 1 O THR H 115 N VAL H 12 SHEET 3 AA8 4 ALA H 92 THR H 98 -1 N TYR H 94 O ALA H 112 SHEET 4 AA8 4 TYR H 107 TRP H 108 -1 O TYR H 107 N THR H 98 SHEET 1 AA9 4 SER H 125 LEU H 129 0 SHEET 2 AA9 4 THR H 140 TYR H 150 -1 O LEU H 146 N PHE H 127 SHEET 3 AA9 4 TYR H 181 PRO H 190 -1 O LEU H 183 N VAL H 147 SHEET 4 AA9 4 VAL H 168 THR H 170 -1 N HIS H 169 O VAL H 186 SHEET 1 AB1 4 SER H 125 LEU H 129 0 SHEET 2 AB1 4 THR H 140 TYR H 150 -1 O LEU H 146 N PHE H 127 SHEET 3 AB1 4 TYR H 181 PRO H 190 -1 O LEU H 183 N VAL H 147 SHEET 4 AB1 4 VAL H 174 LEU H 175 -1 N VAL H 174 O SER H 182 SHEET 1 AB2 3 THR H 156 TRP H 159 0 SHEET 2 AB2 3 ILE H 200 HIS H 205 -1 O ASN H 202 N SER H 158 SHEET 3 AB2 3 THR H 210 LYS H 215 -1 O VAL H 212 N VAL H 203 SHEET 1 AB3 4 LEU A 4 SER A 7 0 SHEET 2 AB3 4 ALA A 19 ALA A 25 -1 O ARG A 24 N THR A 5 SHEET 3 AB3 4 ASP A 70 ILE A 75 -1 O LEU A 73 N LEU A 21 SHEET 4 AB3 4 PHE A 62 SER A 67 -1 N SER A 63 O THR A 74 SHEET 1 AB4 6 THR A 10 LEU A 13 0 SHEET 2 AB4 6 THR A 103 ILE A 107 1 O LYS A 104 N LEU A 11 SHEET 3 AB4 6 VAL A 85 ASN A 92 -1 N TYR A 86 O THR A 103 SHEET 4 AB4 6 ALA A 34 GLN A 38 -1 N TYR A 36 O TYR A 87 SHEET 5 AB4 6 ARG A 45 TYR A 49 -1 O LEU A 47 N TRP A 35 SHEET 6 AB4 6 LYS A 53 ARG A 54 -1 O LYS A 53 N TYR A 49 SHEET 1 AB5 4 THR A 10 LEU A 13 0 SHEET 2 AB5 4 THR A 103 ILE A 107 1 O LYS A 104 N LEU A 11 SHEET 3 AB5 4 VAL A 85 ASN A 92 -1 N TYR A 86 O THR A 103 SHEET 4 AB5 4 THR A 96 PHE A 99 -1 O THR A 98 N GLN A 90 SHEET 1 AB6 4 SER A 115 PHE A 119 0 SHEET 2 AB6 4 THR A 130 PHE A 140 -1 O LEU A 136 N PHE A 117 SHEET 3 AB6 4 TYR A 174 SER A 183 -1 O LEU A 182 N ALA A 131 SHEET 4 AB6 4 SER A 160 VAL A 164 -1 N SER A 163 O SER A 177 SHEET 1 AB7 3 LYS A 146 VAL A 151 0 SHEET 2 AB7 3 VAL A 192 THR A 198 -1 O GLU A 196 N GLN A 148 SHEET 3 AB7 3 VAL A 206 ASN A 211 -1 O VAL A 206 N VAL A 197 SHEET 1 AB8 4 GLN C 3 SER C 7 0 SHEET 2 AB8 4 LEU C 18 SER C 25 -1 O SER C 21 N SER C 7 SHEET 3 AB8 4 THR C 78 MET C 83 -1 O MET C 83 N LEU C 18 SHEET 4 AB8 4 PHE C 68 ASP C 73 -1 N SER C 71 O TYR C 80 SHEET 1 AB9 6 GLY C 10 VAL C 12 0 SHEET 2 AB9 6 ALA C 112 VAL C 116 1 O THR C 115 N VAL C 12 SHEET 3 AB9 6 ALA C 92 THR C 98 -1 N TYR C 94 O ALA C 112 SHEET 4 AB9 6 LYS C 34 GLN C 39 -1 N VAL C 37 O TYR C 95 SHEET 5 AB9 6 LEU C 45 ILE C 51 -1 O GLU C 46 N ARG C 38 SHEET 6 AB9 6 GLU C 58 TYR C 60 -1 O ASP C 59 N ALA C 50 SHEET 1 AC1 4 GLY C 10 VAL C 12 0 SHEET 2 AC1 4 ALA C 112 VAL C 116 1 O THR C 115 N VAL C 12 SHEET 3 AC1 4 ALA C 92 THR C 98 -1 N TYR C 94 O ALA C 112 SHEET 4 AC1 4 TYR C 107 TRP C 108 -1 O TYR C 107 N THR C 98 SHEET 1 AC2 4 SER C 125 LEU C 129 0 SHEET 2 AC2 4 THR C 140 TYR C 150 -1 O LEU C 146 N PHE C 127 SHEET 3 AC2 4 TYR C 181 PRO C 190 -1 O TYR C 181 N TYR C 150 SHEET 4 AC2 4 VAL C 168 THR C 170 -1 N HIS C 169 O VAL C 186 SHEET 1 AC3 4 SER C 125 LEU C 129 0 SHEET 2 AC3 4 THR C 140 TYR C 150 -1 O LEU C 146 N PHE C 127 SHEET 3 AC3 4 TYR C 181 PRO C 190 -1 O TYR C 181 N TYR C 150 SHEET 4 AC3 4 VAL C 174 LEU C 175 -1 N VAL C 174 O SER C 182 SHEET 1 AC4 3 THR C 156 TRP C 159 0 SHEET 2 AC4 3 ILE C 200 HIS C 205 -1 O ASN C 202 N SER C 158 SHEET 3 AC4 3 THR C 210 LYS C 215 -1 O THR C 210 N HIS C 205 SSBOND 1 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 2 CYS L 135 CYS L 195 1555 1555 2.03 SSBOND 3 CYS H 22 CYS H 96 1555 1555 2.03 SSBOND 4 CYS H 145 CYS H 201 1555 1555 2.03 SSBOND 5 CYS A 23 CYS A 88 1555 1555 2.04 SSBOND 6 CYS A 135 CYS A 195 1555 1555 2.03 SSBOND 7 CYS C 22 CYS C 96 1555 1555 2.03 SSBOND 8 CYS C 145 CYS C 201 1555 1555 2.03 LINK ND2 ASN L 108 C1 NAG D 1 1555 1555 1.44 LINK ND2 ASN A 108 C1 NAG A 301 1555 1555 1.45 LINK C SER Q 41 N HYP Q 42 1555 1555 1.33 LINK C HYP Q 42 N SER Q 43 1555 1555 1.33 LINK C SER B 41 N HYP B 42 1555 1555 1.33 LINK C HYP B 42 N SER B 43 1555 1555 1.33 LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.46 LINK O4 NAG D 2 C1 BMA D 3 1555 1555 1.46 LINK O6 BMA D 3 C1 MAN D 4 1555 1555 1.45 CISPEP 1 SER L 7 PRO L 8 0 -3.58 CISPEP 2 TYR L 141 PRO L 142 0 4.35 CISPEP 3 PHE H 151 PRO H 152 0 -4.54 CISPEP 4 GLU H 153 PRO H 154 0 0.45 CISPEP 5 SER A 7 PRO A 8 0 -3.81 CISPEP 6 TYR A 141 PRO A 142 0 5.86 CISPEP 7 PHE C 151 PRO C 152 0 -4.52 CISPEP 8 GLU C 153 PRO C 154 0 0.73 CRYST1 128.021 91.784 82.946 90.00 93.22 90.00 C 1 2 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 0.007811 0.000000 0.000439 0.00000 SCALE2 0.000000 0.010895 0.000000 0.00000 SCALE3 0.000000 0.000000 0.012075 0.00000 MTRIX1 1 -0.986587 0.053735 -0.154138 118.39768 1 MTRIX2 1 0.051720 -0.792715 -0.607394 -8.88418 1 MTRIX3 1 -0.154826 -0.607219 0.779303 -3.24858 1 MTRIX1 2 -0.889612 0.169698 -0.424019 116.06952 1 MTRIX2 2 0.047083 -0.889386 -0.454726 -12.53578 1 MTRIX3 2 -0.454283 -0.424494 0.783219 27.56252 1 MTRIX1 3 -0.985785 0.053872 -0.159143 118.29384 1 MTRIX2 3 0.055289 -0.790432 -0.610050 -8.95926 1 MTRIX3 3 -0.158657 -0.610176 0.776217 -2.97245 1