HEADER MEMBRANE PROTEIN/IMMUNE SYSTEM 28-FEB-24 8YHZ TITLE THE CO-CRYSTAL STRUCTURE OF THE FAB FRAGMENT OF AB-1080 WITH NAV1.7 TITLE 2 VSDII PEPTIDE COMPND MOL_ID: 1; COMPND 2 MOLECULE: LIGHT CHAIN OF 1080 FAB; COMPND 3 CHAIN: L; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: HEAVY CHAIN OF 1080 FAB; COMPND 7 CHAIN: H; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: SODIUM CHANNEL PROTEIN TYPE 9 SUBUNIT ALPHA; COMPND 11 CHAIN: P; COMPND 12 SYNONYM: NAV1.7 VSDII PEPTIDE,NEUROENDOCRINE SODIUM CHANNEL,HNE-NA, COMPND 13 PERIPHERAL SODIUM CHANNEL 1,PN1,SODIUM CHANNEL PROTEIN TYPE IX COMPND 14 SUBUNIT ALPHA,VOLTAGE-GATED SODIUM CHANNEL SUBUNIT ALPHA NAV1.7; COMPND 15 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS; SOURCE 3 ORGANISM_TAXID: 9986; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS; SOURCE 9 ORGANISM_TAXID: 9986; SOURCE 10 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 11 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 13 MOL_ID: 3; SOURCE 14 SYNTHETIC: YES; SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 16 ORGANISM_COMMON: HUMAN; SOURCE 17 ORGANISM_TAXID: 9606 KEYWDS INHIBITOR, NAV1.7, MEMBRANE PROTEIN/IMMUNE SYSTEM, MEMBRANE PROTEIN- KEYWDS 2 IMMUNE SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR D.JUANJUAN,Z.YANING,Z.RUI,D.YANCHAO REVDAT 1 23-OCT-24 8YHZ 0 JRNL AUTH D.JUANJUAN JRNL TITL THE CO-CRYSTAL STRUCTURE OF THE FAB FRAGMENT OF AB-1080 WITH JRNL TITL 2 NAV1.7 VSDII PEPTIDE JRNL REF CELL REP MED JRNL REFN ESSN 2666-3791 JRNL DOI 10.1016/J.XCRM.2024.101800 REMARK 2 REMARK 2 RESOLUTION. 1.62 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 : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.62 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.65 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3 REMARK 3 NUMBER OF REFLECTIONS : 58921 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.194 REMARK 3 R VALUE (WORKING SET) : 0.194 REMARK 3 FREE R VALUE : 0.210 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.390 REMARK 3 FREE R VALUE TEST SET COUNT : 2000 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 28.6500 - 3.9000 1.00 4443 156 0.1609 0.1602 REMARK 3 2 3.9000 - 3.1000 1.00 4234 149 0.1753 0.2044 REMARK 3 3 3.1000 - 2.7000 1.00 4189 147 0.2105 0.2330 REMARK 3 4 2.7000 - 2.4600 1.00 4142 145 0.2206 0.2556 REMARK 3 5 2.4600 - 2.2800 1.00 4139 146 0.2126 0.2396 REMARK 3 6 2.2800 - 2.1500 1.00 4084 143 0.2065 0.2115 REMARK 3 7 2.1500 - 2.0400 1.00 4116 145 0.2067 0.2134 REMARK 3 8 2.0400 - 1.9500 0.99 4064 142 0.2275 0.2502 REMARK 3 9 1.9500 - 1.8800 0.99 4038 143 0.2217 0.2539 REMARK 3 10 1.8800 - 1.8100 0.99 4019 141 0.2251 0.2293 REMARK 3 11 1.8100 - 1.7500 0.97 3966 139 0.2340 0.2804 REMARK 3 12 1.7500 - 1.7000 0.96 3930 139 0.2530 0.2799 REMARK 3 13 1.7000 - 1.6600 0.95 3847 135 0.2773 0.2798 REMARK 3 14 1.6600 - 1.6200 0.92 3710 130 0.2984 0.3091 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) : 0.210 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.750 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.007 NULL REMARK 3 ANGLE : 1.026 NULL REMARK 3 CHIRALITY : 0.063 534 REMARK 3 PLANARITY : 0.007 584 REMARK 3 DIHEDRAL : 14.848 1191 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 0 THROUGH 23 ) REMARK 3 ORIGIN FOR THE GROUP (A): -3.0022 -19.1995 -20.5806 REMARK 3 T TENSOR REMARK 3 T11: 0.2643 T22: 0.2933 REMARK 3 T33: 0.3196 T12: 0.0149 REMARK 3 T13: -0.0063 T23: 0.0222 REMARK 3 L TENSOR REMARK 3 L11: 1.2606 L22: 1.6800 REMARK 3 L33: 1.2340 L12: 0.3951 REMARK 3 L13: -0.1576 L23: -0.2437 REMARK 3 S TENSOR REMARK 3 S11: 0.0565 S12: -0.2925 S13: -0.2699 REMARK 3 S21: 0.0378 S22: -0.1208 S23: -0.2627 REMARK 3 S31: 0.0545 S32: 0.1724 S33: 0.0753 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 24 THROUGH 61 ) REMARK 3 ORIGIN FOR THE GROUP (A): -12.9771 -20.0153 -28.9390 REMARK 3 T TENSOR REMARK 3 T11: 0.2586 T22: 0.2512 REMARK 3 T33: 0.2586 T12: 0.0045 REMARK 3 T13: -0.0024 T23: -0.0140 REMARK 3 L TENSOR REMARK 3 L11: 1.8062 L22: 1.5208 REMARK 3 L33: 1.4740 L12: 0.0554 REMARK 3 L13: 0.2608 L23: 0.4265 REMARK 3 S TENSOR REMARK 3 S11: -0.0401 S12: 0.0464 S13: 0.0129 REMARK 3 S21: -0.2670 S22: 0.0030 S23: 0.1921 REMARK 3 S31: 0.0667 S32: 0.0202 S33: 0.0647 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 62 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): -5.8957 -25.4616 -26.6979 REMARK 3 T TENSOR REMARK 3 T11: 0.2873 T22: 0.2618 REMARK 3 T33: 0.3322 T12: 0.0300 REMARK 3 T13: 0.0114 T23: 0.0036 REMARK 3 L TENSOR REMARK 3 L11: 2.7957 L22: 5.3954 REMARK 3 L33: 2.5385 L12: 3.2495 REMARK 3 L13: -1.8590 L23: -2.7270 REMARK 3 S TENSOR REMARK 3 S11: -0.1911 S12: -0.1257 S13: -0.3261 REMARK 3 S21: -0.1538 S22: -0.0895 S23: -0.2681 REMARK 3 S31: 0.2996 S32: 0.1043 S33: 0.3131 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 76 THROUGH 111 ) REMARK 3 ORIGIN FOR THE GROUP (A): -10.4151 -17.2618 -23.1342 REMARK 3 T TENSOR REMARK 3 T11: 0.2409 T22: 0.2197 REMARK 3 T33: 0.2136 T12: 0.0021 REMARK 3 T13: -0.0146 T23: 0.0059 REMARK 3 L TENSOR REMARK 3 L11: 2.5568 L22: 1.6030 REMARK 3 L33: 0.7673 L12: 0.5374 REMARK 3 L13: -0.2626 L23: 0.1922 REMARK 3 S TENSOR REMARK 3 S11: -0.1051 S12: 0.0609 S13: 0.1074 REMARK 3 S21: -0.1822 S22: 0.0614 S23: -0.0126 REMARK 3 S31: 0.0885 S32: 0.0280 S33: 0.0172 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 112 THROUGH 125 ) REMARK 3 ORIGIN FOR THE GROUP (A): 4.8228 11.6547 -18.3005 REMARK 3 T TENSOR REMARK 3 T11: 0.3637 T22: 0.2783 REMARK 3 T33: 0.3361 T12: -0.0268 REMARK 3 T13: -0.0014 T23: 0.0061 REMARK 3 L TENSOR REMARK 3 L11: 0.3489 L22: 1.8189 REMARK 3 L33: 0.5528 L12: -0.2151 REMARK 3 L13: -0.1705 L23: 0.2820 REMARK 3 S TENSOR REMARK 3 S11: 0.2619 S12: -0.0151 S13: 0.1276 REMARK 3 S21: -0.0407 S22: -0.2000 S23: -0.3063 REMARK 3 S31: -0.2082 S32: -0.1321 S33: -0.0081 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 126 THROUGH 141 ) REMARK 3 ORIGIN FOR THE GROUP (A): -6.3889 20.3770 -11.4490 REMARK 3 T TENSOR REMARK 3 T11: 0.4399 T22: 0.3588 REMARK 3 T33: 0.3781 T12: 0.0263 REMARK 3 T13: -0.0035 T23: -0.1058 REMARK 3 L TENSOR REMARK 3 L11: 2.9693 L22: 3.1014 REMARK 3 L33: 2.2852 L12: -1.2737 REMARK 3 L13: -1.1961 L23: 1.3236 REMARK 3 S TENSOR REMARK 3 S11: 0.0786 S12: -0.3659 S13: 0.3127 REMARK 3 S21: 0.0925 S22: -0.2996 S23: 0.3689 REMARK 3 S31: -0.4402 S32: -0.2392 S33: 0.2308 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 142 THROUGH 154 ) REMARK 3 ORIGIN FOR THE GROUP (A): 5.1898 6.1131 -11.5911 REMARK 3 T TENSOR REMARK 3 T11: 0.4131 T22: 0.3632 REMARK 3 T33: 0.3152 T12: -0.0170 REMARK 3 T13: -0.0240 T23: 0.0185 REMARK 3 L TENSOR REMARK 3 L11: 0.5612 L22: 2.6167 REMARK 3 L33: 1.7237 L12: -0.9765 REMARK 3 L13: -0.9858 L23: 1.7646 REMARK 3 S TENSOR REMARK 3 S11: -0.0203 S12: -0.3016 S13: -0.0577 REMARK 3 S21: 0.6113 S22: 0.1000 S23: -0.1566 REMARK 3 S31: 0.3920 S32: 0.2043 S33: 0.0364 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 155 THROUGH 178 ) REMARK 3 ORIGIN FOR THE GROUP (A): 0.1245 6.2803 -13.6908 REMARK 3 T TENSOR REMARK 3 T11: 0.3705 T22: 0.3832 REMARK 3 T33: 0.2970 T12: -0.0246 REMARK 3 T13: -0.0411 T23: 0.0370 REMARK 3 L TENSOR REMARK 3 L11: 1.1784 L22: 1.8998 REMARK 3 L33: 1.8733 L12: -0.2813 REMARK 3 L13: -0.7325 L23: 1.1000 REMARK 3 S TENSOR REMARK 3 S11: 0.0746 S12: -0.3119 S13: -0.0369 REMARK 3 S21: 0.2033 S22: -0.1459 S23: -0.0243 REMARK 3 S31: 0.0116 S32: 0.1075 S33: 0.1043 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 179 THROUGH 217 ) REMARK 3 ORIGIN FOR THE GROUP (A): 3.4454 17.8246 -7.6326 REMARK 3 T TENSOR REMARK 3 T11: 0.3571 T22: 0.3571 REMARK 3 T33: 0.3336 T12: -0.0338 REMARK 3 T13: -0.0379 T23: -0.0591 REMARK 3 L TENSOR REMARK 3 L11: 1.6010 L22: 1.6824 REMARK 3 L33: 1.7771 L12: 0.1646 REMARK 3 L13: -0.1909 L23: 0.5069 REMARK 3 S TENSOR REMARK 3 S11: 0.1947 S12: -0.4344 S13: 0.3274 REMARK 3 S21: 0.2481 S22: -0.0267 S23: -0.1651 REMARK 3 S31: -0.0721 S32: -0.1861 S33: -0.1389 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 118 ) REMARK 3 ORIGIN FOR THE GROUP (A): -28.1260 -9.4047 -20.7041 REMARK 3 T TENSOR REMARK 3 T11: 0.2573 T22: 0.2677 REMARK 3 T33: 0.2597 T12: -0.0006 REMARK 3 T13: -0.0031 T23: -0.0130 REMARK 3 L TENSOR REMARK 3 L11: 0.8647 L22: 1.6831 REMARK 3 L33: 0.6250 L12: 0.4317 REMARK 3 L13: 0.0872 L23: 0.6697 REMARK 3 S TENSOR REMARK 3 S11: 0.0262 S12: 0.0421 S13: 0.0083 REMARK 3 S21: 0.0462 S22: -0.0460 S23: 0.1037 REMARK 3 S31: -0.0690 S32: -0.0780 S33: 0.0118 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 119 THROUGH 133 ) REMARK 3 ORIGIN FOR THE GROUP (A): -0.8586 21.6531 -20.0970 REMARK 3 T TENSOR REMARK 3 T11: 0.3818 T22: 0.4739 REMARK 3 T33: 0.4859 T12: -0.0294 REMARK 3 T13: 0.0765 T23: -0.1463 REMARK 3 L TENSOR REMARK 3 L11: 1.5767 L22: 2.7353 REMARK 3 L33: 3.1808 L12: -0.4442 REMARK 3 L13: -1.2040 L23: 0.5583 REMARK 3 S TENSOR REMARK 3 S11: 0.0246 S12: -0.1990 S13: -0.1457 REMARK 3 S21: -0.1719 S22: 0.2491 S23: -0.9131 REMARK 3 S31: -0.0581 S32: 0.9109 S33: -0.1177 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 134 THROUGH 214 ) REMARK 3 ORIGIN FOR THE GROUP (A): -11.2064 15.0284 -21.9129 REMARK 3 T TENSOR REMARK 3 T11: 0.3222 T22: 0.2840 REMARK 3 T33: 0.2460 T12: 0.0400 REMARK 3 T13: 0.0134 T23: 0.0262 REMARK 3 L TENSOR REMARK 3 L11: 2.9019 L22: 1.3523 REMARK 3 L33: 1.1694 L12: 0.8131 REMARK 3 L13: -0.1807 L23: 0.4465 REMARK 3 S TENSOR REMARK 3 S11: 0.1024 S12: 0.2465 S13: 0.2726 REMARK 3 S21: -0.0705 S22: -0.0508 S23: 0.0122 REMARK 3 S31: -0.2155 S32: 0.0316 S33: -0.0007 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'P' AND (RESID 210 THROUGH 219 ) REMARK 3 ORIGIN FOR THE GROUP (A): -31.8076 -28.1967 -27.7797 REMARK 3 T TENSOR REMARK 3 T11: 0.4747 T22: 0.3922 REMARK 3 T33: 0.4964 T12: -0.0683 REMARK 3 T13: -0.0300 T23: -0.0596 REMARK 3 L TENSOR REMARK 3 L11: 0.9870 L22: 4.2119 REMARK 3 L33: 5.5909 L12: -2.0128 REMARK 3 L13: -0.1306 L23: 0.6964 REMARK 3 S TENSOR REMARK 3 S11: 0.1286 S12: 0.4959 S13: -0.5045 REMARK 3 S21: -0.4275 S22: -0.1059 S23: 0.7759 REMARK 3 S31: 0.6449 S32: -0.8658 S33: 0.3570 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 8YHZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 01-MAR-24. REMARK 100 THE DEPOSITION ID IS D_1300045140. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-JAN-20 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 : SSRF REMARK 200 BEAMLINE : BL17U1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97950 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59782 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.620 REMARK 200 RESOLUTION RANGE LOW (A) : 28.670 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 7.900 REMARK 200 R MERGE (I) : 0.10700 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 29.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.62 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.68 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.10700 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 49.12 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M POTASSIUM THIOCYANATE, 25% W/V REMARK 280 POLYETHYLENE GLYCOL 3,350, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 291.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4 REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4 REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4 REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4 REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 73.52400 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 39.48250 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 39.48250 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 36.76200 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 39.48250 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 39.48250 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 110.28600 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 39.48250 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.48250 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 36.76200 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 39.48250 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.48250 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 110.28600 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 73.52400 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4610 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19300 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, P 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 GLU P 209 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 GLU L 217 CG CD OE1 OE2 REMARK 470 LYS H 213 CG CD CE NZ REMARK 470 SER H 214 OG 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 434 O HOH H 538 1.82 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 ASN L 30 -2.74 65.82 REMARK 500 ALA L 51 -22.84 71.43 REMARK 500 GLU H 14 -7.48 74.27 REMARK 500 THR H 71 -167.90 -116.84 REMARK 500 LYS H 128 21.19 -141.78 REMARK 500 ASP H 143 64.74 64.46 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 L 553 DISTANCE = 5.92 ANGSTROMS REMARK 525 HOH H 548 DISTANCE = 6.09 ANGSTROMS DBREF 8YHZ L 0 217 PDB 8YHZ 8YHZ 0 217 DBREF 8YHZ H 1 214 PDB 8YHZ 8YHZ 1 214 DBREF 8YHZ P 209 219 UNP Q15858 SCN9A_HUMAN 764 774 SEQRES 1 L 218 GLN VAL LEU THR GLN THR ALA SER PRO VAL SER ALA ALA SEQRES 2 L 218 VAL GLY ASN THR VAL THR ILE THR CYS GLN SER SER GLN SEQRES 3 L 218 SER VAL TRP LYS ASN ASN ASP LEU SER TRP TYR GLN GLN SEQRES 4 L 218 LYS LEU GLY GLN PRO PRO LYS LEU LEU ILE TYR TYR ALA SEQRES 5 L 218 SER THR LEU ALA SER GLY VAL SER SER ARG PHE LYS ALA SEQRES 6 L 218 SER GLY SER GLY THR GLN PHE THR LEU THR ILE SER ASP SEQRES 7 L 218 VAL GLN CYS ASP ASP ALA GLY THR TYR TYR CYS VAL GLY SEQRES 8 L 218 SER TYR ASP CYS SER SER ALA ASP CYS ASN ALA PHE GLY SEQRES 9 L 218 GLY GLY THR LYS VAL VAL VAL LYS ARG THR VAL ALA ALA SEQRES 10 L 218 PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU SEQRES 11 L 218 LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN SEQRES 12 L 218 PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP SEQRES 13 L 218 ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR SEQRES 14 L 218 GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER SEQRES 15 L 218 THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS SEQRES 16 L 218 VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER SEQRES 17 L 218 PRO VAL THR LYS SER PHE ASN ARG GLY GLU SEQRES 1 H 214 GLN SER GLU GLU GLU SER GLY GLY ARG LEU VAL THR PRO SEQRES 2 H 214 GLU THR PRO LEU THR LEU THR CYS THR ALA SER GLY ILE SEQRES 3 H 214 ASP LEU SER LYS TRP PRO MET THR TRP VAL ARG GLN ALA SEQRES 4 H 214 PRO GLY LYS GLY LEU GLU TRP ILE GLY ILE ILE GLY ARG SEQRES 5 H 214 SER GLY SER THR ASN TYR ALA SER TRP ALA LYS GLY ARG SEQRES 6 H 214 PHE THR ILE SER LYS THR SER THR THR VAL ASP LEU LYS SEQRES 7 H 214 MET THR SER PRO THR THR GLU ASP THR ALA THR TYR PHE SEQRES 8 H 214 CYS ALA ARG GLY GLY SER TYR TYR ASP LEU TRP GLY GLN SEQRES 9 H 214 GLY THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY SEQRES 10 H 214 PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SEQRES 11 H 214 SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP SEQRES 12 H 214 TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SEQRES 13 H 214 ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 14 H 214 GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR SEQRES 15 H 214 VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS SEQRES 16 H 214 ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS SEQRES 17 H 214 LYS VAL GLU PRO LYS SER SEQRES 1 P 11 GLU HIS HIS PRO MET THR GLU GLU PHE LYS ASN FORMUL 4 HOH *507(H2 O) HELIX 1 AA1 VAL L 27 ASN L 31 5 5 HELIX 2 AA2 GLN L 79 ALA L 83 5 5 HELIX 3 AA3 SER L 125 LYS L 130 1 6 HELIX 4 AA4 LYS L 187 GLU L 191 1 5 HELIX 5 AA5 ASP H 27 TRP H 31 5 5 HELIX 6 AA6 SER H 60 LYS H 63 5 4 HELIX 7 AA7 THR H 83 THR H 87 5 5 HELIX 8 AA8 SER H 155 ALA H 157 5 3 HELIX 9 AA9 SER H 186 LEU H 188 5 3 HELIX 10 AB1 LYS H 200 ASN H 203 5 4 HELIX 11 AB2 PRO P 212 LYS P 218 1 7 SHEET 1 AA1 4 LEU L 2 GLN L 4 0 SHEET 2 AA1 4 VAL L 17 SER L 23 -1 O GLN L 22 N THR L 3 SHEET 3 AA1 4 GLN L 70 ILE L 75 -1 O ILE L 75 N VAL L 17 SHEET 4 AA1 4 PHE L 62 SER L 67 -1 N LYS L 63 O THR L 74 SHEET 1 AA2 6 VAL L 9 ALA L 12 0 SHEET 2 AA2 6 THR L 106 LYS L 111 1 O VAL L 109 N VAL L 9 SHEET 3 AA2 6 GLY L 84 SER L 91 -1 N GLY L 84 O VAL L 108 SHEET 4 AA2 6 LEU L 33 GLN L 38 -1 N GLN L 38 O THR L 85 SHEET 5 AA2 6 LYS L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AA2 6 THR L 53 LEU L 54 -1 O THR L 53 N TYR L 49 SHEET 1 AA3 4 VAL L 9 ALA L 12 0 SHEET 2 AA3 4 THR L 106 LYS L 111 1 O VAL L 109 N VAL L 9 SHEET 3 AA3 4 GLY L 84 SER L 91 -1 N GLY L 84 O VAL L 108 SHEET 4 AA3 4 ASN L 100 PHE L 102 -1 O ALA L 101 N GLY L 90 SHEET 1 AA4 4 SER L 118 PHE L 122 0 SHEET 2 AA4 4 THR L 133 PHE L 143 -1 O LEU L 139 N PHE L 120 SHEET 3 AA4 4 TYR L 177 SER L 186 -1 O TYR L 177 N PHE L 143 SHEET 4 AA4 4 SER L 163 VAL L 167 -1 N GLN L 164 O THR L 182 SHEET 1 AA5 4 ALA L 157 LEU L 158 0 SHEET 2 AA5 4 LYS L 149 VAL L 154 -1 N VAL L 154 O ALA L 157 SHEET 3 AA5 4 VAL L 195 THR L 201 -1 O GLU L 199 N GLN L 151 SHEET 4 AA5 4 VAL L 209 ASN L 214 -1 O LYS L 211 N CYS L 198 SHEET 1 AA6 4 SER H 2 SER H 6 0 SHEET 2 AA6 4 LEU H 17 SER H 24 -1 O THR H 22 N GLU H 4 SHEET 3 AA6 4 THR H 74 MET H 79 -1 O MET H 79 N LEU H 17 SHEET 4 AA6 4 PHE H 66 LYS H 70 -1 N THR H 67 O LYS H 78 SHEET 1 AA7 6 LEU H 10 VAL H 11 0 SHEET 2 AA7 6 THR H 106 VAL H 110 1 O THR H 109 N VAL H 11 SHEET 3 AA7 6 ALA H 88 ARG H 94 -1 N TYR H 90 O THR H 106 SHEET 4 AA7 6 MET H 33 GLN H 38 -1 N VAL H 36 O PHE H 91 SHEET 5 AA7 6 LEU H 44 ILE H 50 -1 O GLU H 45 N ARG H 37 SHEET 6 AA7 6 THR H 56 TYR H 58 -1 O ASN H 57 N ILE H 49 SHEET 1 AA8 4 LEU H 10 VAL H 11 0 SHEET 2 AA8 4 THR H 106 VAL H 110 1 O THR H 109 N VAL H 11 SHEET 3 AA8 4 ALA H 88 ARG H 94 -1 N TYR H 90 O THR H 106 SHEET 4 AA8 4 LEU H 101 TRP H 102 -1 O LEU H 101 N ARG H 94 SHEET 1 AA9 4 SER H 119 LEU H 123 0 SHEET 2 AA9 4 THR H 134 TYR H 144 -1 O LEU H 140 N PHE H 121 SHEET 3 AA9 4 TYR H 175 PRO H 184 -1 O TYR H 175 N TYR H 144 SHEET 4 AA9 4 VAL H 162 THR H 164 -1 N HIS H 163 O VAL H 180 SHEET 1 AB1 4 SER H 119 LEU H 123 0 SHEET 2 AB1 4 THR H 134 TYR H 144 -1 O LEU H 140 N PHE H 121 SHEET 3 AB1 4 TYR H 175 PRO H 184 -1 O TYR H 175 N TYR H 144 SHEET 4 AB1 4 VAL H 168 LEU H 169 -1 N VAL H 168 O SER H 176 SHEET 1 AB2 3 THR H 150 TRP H 153 0 SHEET 2 AB2 3 TYR H 193 HIS H 199 -1 O ASN H 196 N SER H 152 SHEET 3 AB2 3 THR H 204 VAL H 210 -1 O VAL H 206 N VAL H 197 SSBOND 1 CYS L 21 CYS L 88 1555 1555 2.07 SSBOND 2 CYS L 94 CYS L 99 1555 1555 2.08 SSBOND 3 CYS L 138 CYS L 198 1555 1555 2.02 SSBOND 4 CYS H 21 CYS H 92 1555 1555 2.05 SSBOND 5 CYS H 139 CYS H 195 1555 1555 2.04 CISPEP 1 SER L 7 PRO L 8 0 -6.59 CISPEP 2 TYR L 144 PRO L 145 0 0.87 CISPEP 3 PHE H 145 PRO H 146 0 -6.67 CISPEP 4 GLU H 147 PRO H 148 0 1.45 CRYST1 78.965 78.965 147.048 90.00 90.00 90.00 P 41 21 2 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 0.012664 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012664 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006801 0.00000