HEADER IMMUNE SYSTEM 14-APR-23 8SHV TITLE 38B7 UNLIGANDED COMPND MOL_ID: 1; COMPND 2 MOLECULE: 38B7 LIGHT CHAIN; COMPND 3 CHAIN: L; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: 38B7 HEAVY CHAIN; COMPND 7 CHAIN: H; COMPND 8 ENGINEERED: YES 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 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_COMMON: HUMAN; SOURCE 12 ORGANISM_TAXID: 9606; SOURCE 13 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 14 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM_CELL_LINE: EXPI293 KEYWDS ALLERGY, PEANUT, ANTIBODY, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR B.W.SPILLER,R.A.SHREM REVDAT 1 25-DEC-24 8SHV 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. 1.58 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) : 1.58 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.22 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 3 NUMBER OF REFLECTIONS : 77039 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.165 REMARK 3 R VALUE (WORKING SET) : 0.164 REMARK 3 FREE R VALUE : 0.178 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.850 REMARK 3 FREE R VALUE TEST SET COUNT : 3735 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 30.2200 - 4.7300 0.99 2917 152 0.1786 0.1710 REMARK 3 2 4.7300 - 3.7600 1.00 2812 149 0.1320 0.1350 REMARK 3 3 3.7600 - 3.2900 1.00 2777 129 0.1529 0.1630 REMARK 3 4 3.2900 - 2.9900 1.00 2748 155 0.1570 0.1782 REMARK 3 5 2.9900 - 2.7700 1.00 2790 118 0.1630 0.1615 REMARK 3 6 2.7700 - 2.6100 1.00 2719 151 0.1600 0.1932 REMARK 3 7 2.6100 - 2.4800 1.00 2712 151 0.1637 0.1716 REMARK 3 8 2.4800 - 2.3700 1.00 2732 138 0.1541 0.1722 REMARK 3 9 2.3700 - 2.2800 1.00 2715 131 0.1562 0.1635 REMARK 3 10 2.2800 - 2.2000 1.00 2699 139 0.1552 0.1863 REMARK 3 11 2.2000 - 2.1300 0.99 2736 121 0.1564 0.1867 REMARK 3 12 2.1300 - 2.0700 0.99 2688 147 0.1568 0.1802 REMARK 3 13 2.0700 - 2.0200 1.00 2683 162 0.1590 0.2121 REMARK 3 14 2.0200 - 1.9700 1.00 2698 163 0.1606 0.1644 REMARK 3 15 1.9700 - 1.9200 1.00 2637 162 0.1642 0.1852 REMARK 3 16 1.9200 - 1.8800 1.00 2716 121 0.1664 0.1842 REMARK 3 17 1.8800 - 1.8400 1.00 2744 112 0.1724 0.2010 REMARK 3 18 1.8400 - 1.8100 1.00 2713 124 0.1853 0.2353 REMARK 3 19 1.8100 - 1.7800 1.00 2667 147 0.1996 0.2425 REMARK 3 20 1.7800 - 1.7500 1.00 2730 130 0.2045 0.2452 REMARK 3 21 1.7500 - 1.7200 1.00 2706 139 0.2081 0.2706 REMARK 3 22 1.7200 - 1.6900 1.00 2683 119 0.2135 0.2847 REMARK 3 23 1.6900 - 1.6700 1.00 2683 132 0.2382 0.2584 REMARK 3 24 1.6700 - 1.6400 1.00 2690 137 0.2482 0.2945 REMARK 3 25 1.6400 - 1.6200 1.00 2714 133 0.2664 0.2820 REMARK 3 26 1.6200 - 1.6000 0.99 2650 137 0.2878 0.2949 REMARK 3 27 1.6000 - 1.5800 0.96 2545 136 0.3248 0.3384 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) : 0.169 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.707 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 25.33 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.99 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 : 0.013 3446 REMARK 3 ANGLE : 1.131 4698 REMARK 3 CHIRALITY : 0.076 520 REMARK 3 PLANARITY : 0.010 606 REMARK 3 DIHEDRAL : 6.742 495 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 24 ) REMARK 3 ORIGIN FOR THE GROUP (A): 32.0258 48.9513 94.6627 REMARK 3 T TENSOR REMARK 3 T11: 0.2747 T22: 0.2575 REMARK 3 T33: 0.1812 T12: 0.0584 REMARK 3 T13: -0.0198 T23: 0.0262 REMARK 3 L TENSOR REMARK 3 L11: 8.1212 L22: 7.7519 REMARK 3 L33: 6.2566 L12: 4.1678 REMARK 3 L13: 4.5619 L23: 5.1515 REMARK 3 S TENSOR REMARK 3 S11: 0.0167 S12: -0.0188 S13: -0.2614 REMARK 3 S21: 0.3317 S22: 0.2049 S23: -0.2630 REMARK 3 S31: 0.3314 S32: -0.0272 S33: -0.2724 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 25 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): 36.3205 51.4373 84.9401 REMARK 3 T TENSOR REMARK 3 T11: 0.2025 T22: 0.2322 REMARK 3 T33: 0.1875 T12: 0.0297 REMARK 3 T13: 0.0194 T23: -0.0130 REMARK 3 L TENSOR REMARK 3 L11: 3.1234 L22: 3.7894 REMARK 3 L33: 3.4053 L12: 0.2963 REMARK 3 L13: 0.5928 L23: 0.0302 REMARK 3 S TENSOR REMARK 3 S11: -0.0122 S12: 0.1076 S13: -0.1248 REMARK 3 S21: -0.0504 S22: 0.0481 S23: -0.3257 REMARK 3 S31: 0.0641 S32: 0.0992 S33: -0.0399 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 76 THROUGH 92 ) REMARK 3 ORIGIN FOR THE GROUP (A): 32.6254 55.3330 88.8574 REMARK 3 T TENSOR REMARK 3 T11: 0.2144 T22: 0.1644 REMARK 3 T33: 0.1695 T12: 0.0340 REMARK 3 T13: 0.0115 T23: 0.0199 REMARK 3 L TENSOR REMARK 3 L11: 4.0568 L22: 2.8456 REMARK 3 L33: 4.7084 L12: 0.3277 REMARK 3 L13: 1.9272 L23: 2.0342 REMARK 3 S TENSOR REMARK 3 S11: -0.0652 S12: -0.0810 S13: 0.1251 REMARK 3 S21: -0.1444 S22: 0.0874 S23: -0.1662 REMARK 3 S31: -0.2193 S32: 0.0004 S33: 0.0267 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 93 THROUGH 107 ) REMARK 3 ORIGIN FOR THE GROUP (A): 26.6194 48.3135 84.1883 REMARK 3 T TENSOR REMARK 3 T11: 0.2437 T22: 0.1628 REMARK 3 T33: 0.1851 T12: 0.0038 REMARK 3 T13: 0.0241 T23: 0.0242 REMARK 3 L TENSOR REMARK 3 L11: 3.2151 L22: 3.4449 REMARK 3 L33: 5.7793 L12: -0.2729 REMARK 3 L13: 0.5702 L23: 4.0144 REMARK 3 S TENSOR REMARK 3 S11: -0.0806 S12: 0.0885 S13: -0.1330 REMARK 3 S21: -0.1870 S22: -0.1478 S23: 0.1939 REMARK 3 S31: -0.2310 S32: -0.3438 S33: 0.3385 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 108 THROUGH 151 ) REMARK 3 ORIGIN FOR THE GROUP (A): 8.9642 64.9280 108.4276 REMARK 3 T TENSOR REMARK 3 T11: 0.2183 T22: 0.1756 REMARK 3 T33: 0.1964 T12: -0.0080 REMARK 3 T13: 0.0069 T23: -0.0465 REMARK 3 L TENSOR REMARK 3 L11: 3.1353 L22: 0.8793 REMARK 3 L33: 1.3713 L12: 0.3063 REMARK 3 L13: -0.3886 L23: 0.0577 REMARK 3 S TENSOR REMARK 3 S11: 0.0460 S12: 0.0699 S13: -0.0941 REMARK 3 S21: 0.0665 S22: -0.0302 S23: 0.1192 REMARK 3 S31: 0.0499 S32: -0.0212 S33: 0.0321 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 152 THROUGH 164 ) REMARK 3 ORIGIN FOR THE GROUP (A): 3.0638 57.0506 106.5084 REMARK 3 T TENSOR REMARK 3 T11: 0.2637 T22: 0.1710 REMARK 3 T33: 0.2394 T12: -0.0136 REMARK 3 T13: 0.0154 T23: -0.0440 REMARK 3 L TENSOR REMARK 3 L11: 8.8933 L22: 2.1199 REMARK 3 L33: 2.9791 L12: 3.4938 REMARK 3 L13: -3.3241 L23: -2.4491 REMARK 3 S TENSOR REMARK 3 S11: -0.0018 S12: -0.1225 S13: 0.0448 REMARK 3 S21: 0.0136 S22: 0.0995 S23: 0.1035 REMARK 3 S31: 0.0836 S32: 0.0190 S33: 0.0101 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 165 THROUGH 214 ) REMARK 3 ORIGIN FOR THE GROUP (A): 6.7233 63.5784 110.5737 REMARK 3 T TENSOR REMARK 3 T11: 0.2256 T22: 0.1161 REMARK 3 T33: 0.1898 T12: -0.0113 REMARK 3 T13: 0.0127 T23: -0.0515 REMARK 3 L TENSOR REMARK 3 L11: 8.2917 L22: 0.8821 REMARK 3 L33: 1.4949 L12: -0.1639 REMARK 3 L13: -1.1411 L23: -0.0850 REMARK 3 S TENSOR REMARK 3 S11: 0.0024 S12: -0.2768 S13: -0.0562 REMARK 3 S21: 0.1169 S22: -0.0043 S23: 0.0672 REMARK 3 S31: 0.0856 S32: -0.0104 S33: -0.0024 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): 15.0977 63.7209 72.7046 REMARK 3 T TENSOR REMARK 3 T11: 0.3317 T22: 0.2862 REMARK 3 T33: 0.3273 T12: 0.0861 REMARK 3 T13: -0.0495 T23: -0.0231 REMARK 3 L TENSOR REMARK 3 L11: 2.4272 L22: 1.5199 REMARK 3 L33: 1.9363 L12: 1.5066 REMARK 3 L13: -1.7090 L23: -0.5450 REMARK 3 S TENSOR REMARK 3 S11: 0.0962 S12: 0.3685 S13: 0.4487 REMARK 3 S21: -0.1370 S22: -0.1140 S23: 0.0992 REMARK 3 S31: -0.2558 S32: -0.1746 S33: -0.0685 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 18 THROUGH 60 ) REMARK 3 ORIGIN FOR THE GROUP (A): 23.1273 54.9026 69.9846 REMARK 3 T TENSOR REMARK 3 T11: 0.1998 T22: 0.2516 REMARK 3 T33: 0.1439 T12: 0.0384 REMARK 3 T13: -0.0346 T23: -0.0200 REMARK 3 L TENSOR REMARK 3 L11: 4.3814 L22: 2.3751 REMARK 3 L33: 4.6824 L12: -0.0709 REMARK 3 L13: -1.0460 L23: -0.8362 REMARK 3 S TENSOR REMARK 3 S11: -0.0072 S12: 0.3211 S13: 0.0540 REMARK 3 S21: -0.2332 S22: -0.0858 S23: -0.0340 REMARK 3 S31: -0.0426 S32: 0.1358 S33: 0.1248 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 61 THROUGH 76 ) REMARK 3 ORIGIN FOR THE GROUP (A): 16.9853 53.0082 66.4536 REMARK 3 T TENSOR REMARK 3 T11: 0.3188 T22: 0.3440 REMARK 3 T33: 0.2200 T12: 0.0263 REMARK 3 T13: -0.0484 T23: -0.0317 REMARK 3 L TENSOR REMARK 3 L11: 4.8941 L22: 5.1600 REMARK 3 L33: 4.1973 L12: 4.6960 REMARK 3 L13: -4.2918 L23: -4.6267 REMARK 3 S TENSOR REMARK 3 S11: 0.0250 S12: 0.5198 S13: 0.1812 REMARK 3 S21: -0.4805 S22: 0.0457 S23: 0.3993 REMARK 3 S31: 0.1568 S32: -0.1787 S33: -0.0780 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 77 THROUGH 124 ) REMARK 3 ORIGIN FOR THE GROUP (A): 17.6022 58.4097 75.3640 REMARK 3 T TENSOR REMARK 3 T11: 0.2355 T22: 0.2463 REMARK 3 T33: 0.1721 T12: 0.0130 REMARK 3 T13: -0.0352 T23: -0.0182 REMARK 3 L TENSOR REMARK 3 L11: 1.3541 L22: 1.0407 REMARK 3 L33: 1.7777 L12: -0.5993 REMARK 3 L13: -0.7912 L23: 0.7122 REMARK 3 S TENSOR REMARK 3 S11: 0.0060 S12: 0.1796 S13: 0.0207 REMARK 3 S21: -0.1560 S22: -0.1080 S23: 0.0509 REMARK 3 S31: -0.0153 S32: -0.1511 S33: 0.1175 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 125 THROUGH 139 ) REMARK 3 ORIGIN FOR THE GROUP (A): 4.2623 76.1224 108.9968 REMARK 3 T TENSOR REMARK 3 T11: 0.2359 T22: 0.2486 REMARK 3 T33: 0.2018 T12: 0.0428 REMARK 3 T13: 0.0256 T23: 0.0027 REMARK 3 L TENSOR REMARK 3 L11: 5.4233 L22: 4.6850 REMARK 3 L33: 0.5993 L12: 0.3466 REMARK 3 L13: -1.7844 L23: -0.3505 REMARK 3 S TENSOR REMARK 3 S11: 0.1423 S12: -0.8990 S13: -0.0827 REMARK 3 S21: 0.5167 S22: -0.1206 S23: 0.0485 REMARK 3 S31: 0.4862 S32: -0.2292 S33: 0.0008 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 140 THROUGH 220 ) REMARK 3 ORIGIN FOR THE GROUP (A): 7.9420 76.5020 98.8189 REMARK 3 T TENSOR REMARK 3 T11: 0.1680 T22: 0.1653 REMARK 3 T33: 0.1956 T12: 0.0142 REMARK 3 T13: 0.0086 T23: -0.0069 REMARK 3 L TENSOR REMARK 3 L11: 1.6600 L22: 2.2428 REMARK 3 L33: 3.1060 L12: 0.2111 REMARK 3 L13: 0.8106 L23: 0.9209 REMARK 3 S TENSOR REMARK 3 S11: 0.0217 S12: 0.0338 S13: 0.0215 REMARK 3 S21: -0.0279 S22: -0.0908 S23: 0.0522 REMARK 3 S31: -0.1518 S32: -0.0413 S33: 0.1062 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 8SHV 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_1000273809. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 23-OCT-19 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.5 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-D REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.12713 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 : XIA2 0.5.900-GA3DE5862-DIALS REMARK 200 -1.14, DIALS 1.14.12-G6954CB231- REMARK 200 RELEASE REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 77127 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.580 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 (%) : 99.8 REMARK 200 DATA REDUNDANCY : 7.400 REMARK 200 R MERGE (I) : 0.07000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.58 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.61 REMARK 200 COMPLETENESS FOR SHELL (%) : 96.2 REMARK 200 DATA REDUNDANCY IN SHELL : 6.10 REMARK 200 R MERGE FOR SHELL (I) : 1.40600 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: NULL REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: PLATES REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 58.10 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 4000, 100 MM MES PH 6.5, VAPOR REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 30.99000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.33500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.90500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 68.33500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.99000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 32.90500 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3840 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20070 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 CYS L 215 REMARK 465 SER H 135 REMARK 465 THR H 136 REMARK 465 SER H 137 REMARK 465 CYS H 221 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 HZ1 LYS H 214 O HOH H 301 1.27 REMARK 500 HE ARG L 143 O HOH L 409 1.56 REMARK 500 O HOH L 535 O HOH L 631 1.89 REMARK 500 O HOH L 440 O HOH L 564 1.94 REMARK 500 O HOH L 415 O HOH L 493 1.97 REMARK 500 O HOH L 409 O HOH L 526 1.98 REMARK 500 NZ LYS H 214 O HOH H 301 2.01 REMARK 500 OE1 GLU L 214 O HOH L 401 2.08 REMARK 500 O HOH L 623 O HOH H 497 2.08 REMARK 500 O HOH H 343 O HOH H 489 2.10 REMARK 500 O GLU L 1 O HOH L 402 2.10 REMARK 500 O HOH L 420 O HOH L 580 2.12 REMARK 500 O HOH L 509 O HOH L 564 2.12 REMARK 500 O HOH H 529 O HOH H 535 2.13 REMARK 500 O HOH H 482 O HOH H 520 2.17 REMARK 500 OE2 GLU H 217 O HOH H 302 2.19 REMARK 500 O HOH L 536 O HOH H 495 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 433 O HOH H 485 3646 2.16 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 GLU L 162 CD GLU L 162 OE1 0.074 REMARK 500 SER L 163 CB SER L 163 OG -0.129 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 CYS H 201 CA - CB - SG ANGL. DEV. = 6.7 DEGREES 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 -126.29 56.60 REMARK 500 ASP L 30 -126.47 56.86 REMARK 500 ALA L 51 -34.60 71.75 REMARK 500 TRP L 94 -20.63 71.12 REMARK 500 ASP H 149 60.44 66.79 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH H 541 DISTANCE = 6.04 ANGSTROMS REMARK 525 HOH H 542 DISTANCE = 6.46 ANGSTROMS DBREF 8SHV L 1 215 PDB 8SHV 8SHV 1 215 DBREF 8SHV H 1 221 PDB 8SHV 8SHV 1 221 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 HET EPE L 301 32 HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID HETSYN EPE HEPES FORMUL 3 EPE C8 H18 N2 O4 S FORMUL 4 HOH *489(H2 O) HELIX 1 AA1 GLU L 79 PHE L 83 5 5 HELIX 2 AA2 SER L 122 SER L 128 1 7 HELIX 3 AA3 LYS L 184 GLU L 188 1 5 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 SHEET 1 AA1 4 LEU L 4 THR L 5 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 GLY L 66 -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 GLU L 106 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 GLN L 38 O VAL L 85 SHEET 5 AA2 6 PRO L 44 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 GLU L 106 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 VAL L 134 N PHE L 119 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 GLN L 161 O THR L 179 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 GLU L 196 N GLN L 148 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 MET H 83 N LEU H 18 SHEET 4 AA6 4 PHE H 68 ASP H 73 -1 N THR H 69 O GLU H 82 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 GLU H 46 N ARG H 38 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 LYS H 148 N SER H 125 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 LYS H 148 N SER H 125 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 THR H 210 N HIS H 205 SSBOND 1 CYS L 23 CYS L 88 1555 1555 2.27 SSBOND 2 CYS L 135 CYS L 195 1555 1555 1.99 SSBOND 3 CYS H 22 CYS H 96 1555 1555 2.10 SSBOND 4 CYS H 145 CYS H 201 1555 1555 2.05 CISPEP 1 SER L 7 PRO L 8 0 3.43 CISPEP 2 TYR L 141 PRO L 142 0 1.51 CISPEP 3 PHE H 151 PRO H 152 0 -8.25 CISPEP 4 GLU H 153 PRO H 154 0 0.09 CRYST1 61.980 65.810 136.670 90.00 90.00 90.00 P 21 21 21 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.016134 0.000000 0.000000 0.00000 SCALE2 0.000000 0.015195 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007317 0.00000