HEADER IMMUNE SYSTEM 01-JUN-23 8T0O TITLE FAB FROM MAB RB2AT_87 COMPND MOL_ID: 1; COMPND 2 MOLECULE: RB2AT_87 FAB LIGHT CHAIN; COMPND 3 CHAIN: L; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: RB2AT_87 FAB HEAVY CHAIN; COMPND 7 CHAIN: H; COMPND 8 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_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS; SOURCE 8 ORGANISM_TAXID: 9986; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS FAB FRAGMENT, MONOCLONAL ANTIBODY, DE NOVO PROTEIN, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR A.G.KREUTZER,R.J.MALONIS,J.R.LAI,J.S.NOWICK REVDAT 1 27-MAR-24 8T0O 0 JRNL AUTH A.G.KREUTZER,R.J.MALONIS,C.M.T.PARROCHA,K.TONG, JRNL AUTH 2 G.GUAGLIANONE,J.T.NGUYEN,M.N.DIAB,J.R.LAI,J.S.NOWICK JRNL TITL GENERATION AND STUDY OF ANTIBODIES AGAINST TWO TRIANGULAR JRNL TITL 2 TRIMERS DERIVED FROM ABETA JRNL REF PEPTIDE SCIENCE 24333 2023 JRNL REFN ISSN 1344-7661 JRNL DOI 10.1002/PEP2.24333 REMARK 2 REMARK 2 RESOLUTION. 2.30 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) : 2.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.45 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 91.3 REMARK 3 NUMBER OF REFLECTIONS : 44577 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.219 REMARK 3 R VALUE (WORKING SET) : 0.215 REMARK 3 FREE R VALUE : 0.257 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.560 REMARK 3 FREE R VALUE TEST SET COUNT : 3815 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 36.4500 - 6.8900 1.00 1642 158 0.1650 0.1945 REMARK 3 2 6.8800 - 5.4700 1.00 1640 168 0.1867 0.2271 REMARK 3 3 5.4700 - 4.7800 1.00 1653 162 0.1468 0.2071 REMARK 3 4 4.7800 - 4.3500 1.00 1663 150 0.1260 0.1841 REMARK 3 5 4.3400 - 4.0400 1.00 1626 156 0.1591 0.2044 REMARK 3 6 4.0300 - 3.8000 0.99 1635 157 0.1959 0.2393 REMARK 3 7 3.8000 - 3.6100 1.00 1645 162 0.2004 0.2125 REMARK 3 8 3.6100 - 3.4500 0.99 1651 158 0.1944 0.2630 REMARK 3 9 3.4500 - 3.3200 0.99 1646 148 0.2416 0.2476 REMARK 3 10 3.3200 - 3.2000 1.00 1652 162 0.2481 0.3302 REMARK 3 11 3.2000 - 3.1000 1.00 1644 142 0.2540 0.2559 REMARK 3 12 3.1000 - 3.0100 1.00 1657 156 0.2576 0.3262 REMARK 3 13 3.0100 - 2.9300 1.00 1626 148 0.2684 0.2766 REMARK 3 14 2.9300 - 2.8600 1.00 1674 162 0.3002 0.3679 REMARK 3 15 2.8600 - 2.8000 1.00 1680 148 0.3162 0.3864 REMARK 3 16 2.8000 - 2.7400 1.00 1644 142 0.3484 0.3825 REMARK 3 17 2.7400 - 2.6800 0.98 1613 149 0.4167 0.4400 REMARK 3 18 2.6800 - 2.6300 0.97 1607 144 0.3955 0.4647 REMARK 3 19 2.6300 - 2.5900 1.00 1647 157 0.3461 0.3843 REMARK 3 20 2.5900 - 2.5400 1.00 1617 150 0.3391 0.3840 REMARK 3 21 2.5400 - 2.5000 0.93 1592 151 0.3445 0.3499 REMARK 3 22 2.5000 - 2.4600 0.91 1489 136 0.3497 0.4203 REMARK 3 23 2.4600 - 2.4300 0.99 1611 159 0.3503 0.3432 REMARK 3 24 2.4300 - 2.4000 0.94 1384 124 0.3459 0.3430 REMARK 3 25 2.3300 - 2.3300 0.90 265 23 0.3729 0.3415 REMARK 3 26 2.3300 - 2.3000 0.93 1559 143 0.3805 0.4213 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 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) : 0.400 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 33.650 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 : 0.008 NULL REMARK 3 ANGLE : 0.945 NULL REMARK 3 CHIRALITY : 0.052 526 REMARK 3 PLANARITY : 0.007 574 REMARK 3 DIHEDRAL : 10.430 459 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 10 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 38 ) REMARK 3 ORIGIN FOR THE GROUP (A): 43.3955 27.9576 7.8119 REMARK 3 T TENSOR REMARK 3 T11: 0.3429 T22: 0.4279 REMARK 3 T33: 0.4082 T12: 0.0259 REMARK 3 T13: -0.0671 T23: -0.0190 REMARK 3 L TENSOR REMARK 3 L11: 5.4004 L22: 5.2280 REMARK 3 L33: 5.1422 L12: -1.3085 REMARK 3 L13: -1.3540 L23: 1.7963 REMARK 3 S TENSOR REMARK 3 S11: -0.0696 S12: -0.3903 S13: 0.2045 REMARK 3 S21: 0.3947 S22: 0.2579 S23: -0.8359 REMARK 3 S31: 0.2732 S32: 0.7929 S33: -0.2570 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 39 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): 38.2074 25.0241 0.7544 REMARK 3 T TENSOR REMARK 3 T11: 0.4482 T22: 0.4530 REMARK 3 T33: 0.4415 T12: 0.0885 REMARK 3 T13: -0.0128 T23: -0.0029 REMARK 3 L TENSOR REMARK 3 L11: 2.4318 L22: 7.2631 REMARK 3 L33: 8.8465 L12: 1.6599 REMARK 3 L13: -0.4526 L23: -0.7882 REMARK 3 S TENSOR REMARK 3 S11: 0.2883 S12: 0.1471 S13: -0.2480 REMARK 3 S21: -0.0814 S22: -0.1826 S23: 0.0446 REMARK 3 S31: 0.2244 S32: 0.4863 S33: -0.0152 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 76 THROUGH 112 ) REMARK 3 ORIGIN FOR THE GROUP (A): 38.9078 25.5811 8.7291 REMARK 3 T TENSOR REMARK 3 T11: 0.2877 T22: 0.4034 REMARK 3 T33: 0.3139 T12: 0.0456 REMARK 3 T13: -0.0655 T23: -0.0498 REMARK 3 L TENSOR REMARK 3 L11: 5.0645 L22: 6.7703 REMARK 3 L33: 4.9583 L12: -1.0437 REMARK 3 L13: -2.2183 L23: 0.6209 REMARK 3 S TENSOR REMARK 3 S11: 0.1256 S12: -0.0216 S13: -0.2403 REMARK 3 S21: -0.0768 S22: -0.0410 S23: 0.3248 REMARK 3 S31: 0.1249 S32: 0.4945 S33: -0.0717 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 113 THROUGH 211 ) REMARK 3 ORIGIN FOR THE GROUP (A): 18.1710 45.1049 26.4783 REMARK 3 T TENSOR REMARK 3 T11: 0.3903 T22: 0.3381 REMARK 3 T33: 0.3997 T12: 0.0992 REMARK 3 T13: -0.0697 T23: 0.0163 REMARK 3 L TENSOR REMARK 3 L11: 3.7768 L22: 1.7829 REMARK 3 L33: 7.7123 L12: 0.4205 REMARK 3 L13: -4.3014 L23: -0.2152 REMARK 3 S TENSOR REMARK 3 S11: 0.1236 S12: -0.1900 S13: 0.0350 REMARK 3 S21: 0.1554 S22: -0.0392 S23: 0.0246 REMARK 3 S31: -0.2430 S32: -0.0196 S33: -0.0590 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 212 THROUGH 217 ) REMARK 3 ORIGIN FOR THE GROUP (A): 8.8975 51.5402 33.0824 REMARK 3 T TENSOR REMARK 3 T11: 0.7420 T22: 0.7825 REMARK 3 T33: 0.8209 T12: 0.2286 REMARK 3 T13: 0.1765 T23: -0.1677 REMARK 3 L TENSOR REMARK 3 L11: 5.2250 L22: 4.7418 REMARK 3 L33: 7.6328 L12: -3.3852 REMARK 3 L13: -2.6433 L23: 4.2617 REMARK 3 S TENSOR REMARK 3 S11: 0.3245 S12: -0.1252 S13: 0.1530 REMARK 3 S21: 0.5707 S22: 0.4216 S23: 0.9230 REMARK 3 S31: -0.8058 S32: -0.7737 S33: -0.6430 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 18 ) REMARK 3 ORIGIN FOR THE GROUP (A): 25.0970 9.9463 23.1464 REMARK 3 T TENSOR REMARK 3 T11: 0.9365 T22: 0.5832 REMARK 3 T33: 0.8615 T12: 0.0410 REMARK 3 T13: 0.0813 T23: 0.1823 REMARK 3 L TENSOR REMARK 3 L11: 5.6192 L22: 7.3896 REMARK 3 L33: 2.8104 L12: 0.0061 REMARK 3 L13: -3.2415 L23: 2.7636 REMARK 3 S TENSOR REMARK 3 S11: -0.3968 S12: 0.3997 S13: -0.5784 REMARK 3 S21: -0.3852 S22: 0.1830 S23: 0.9625 REMARK 3 S31: 2.1513 S32: -0.3110 S33: 0.0416 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 19 THROUGH 32 ) REMARK 3 ORIGIN FOR THE GROUP (A): 29.2715 4.1937 8.0532 REMARK 3 T TENSOR REMARK 3 T11: 0.9727 T22: 0.4720 REMARK 3 T33: 1.0115 T12: 0.1379 REMARK 3 T13: -0.1290 T23: 0.0329 REMARK 3 L TENSOR REMARK 3 L11: 5.3365 L22: 6.0750 REMARK 3 L33: 8.1360 L12: 4.4544 REMARK 3 L13: 5.0607 L23: 1.9260 REMARK 3 S TENSOR REMARK 3 S11: -0.1380 S12: 1.3060 S13: -1.4816 REMARK 3 S21: -1.6014 S22: 0.6269 S23: 0.5074 REMARK 3 S31: 1.8171 S32: 0.1974 S33: -0.5236 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 33 THROUGH 65 ) REMARK 3 ORIGIN FOR THE GROUP (A): 38.0260 12.5998 18.1166 REMARK 3 T TENSOR REMARK 3 T11: 0.5118 T22: 0.5090 REMARK 3 T33: 0.4017 T12: 0.1999 REMARK 3 T13: -0.0257 T23: 0.1010 REMARK 3 L TENSOR REMARK 3 L11: 7.0293 L22: 8.1899 REMARK 3 L33: 5.1366 L12: -0.3700 REMARK 3 L13: -0.1734 L23: -2.4377 REMARK 3 S TENSOR REMARK 3 S11: -0.3361 S12: -0.8189 S13: 0.0462 REMARK 3 S21: 0.7858 S22: 0.1087 S23: -0.1478 REMARK 3 S31: 0.3434 S32: 0.9185 S33: 0.0297 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 66 THROUGH 137 ) REMARK 3 ORIGIN FOR THE GROUP (A): 24.9890 17.7454 19.7744 REMARK 3 T TENSOR REMARK 3 T11: 0.5367 T22: 0.2953 REMARK 3 T33: 0.4665 T12: -0.0252 REMARK 3 T13: -0.0138 T23: 0.0557 REMARK 3 L TENSOR REMARK 3 L11: 3.0870 L22: 1.3176 REMARK 3 L33: 3.5541 L12: -1.4799 REMARK 3 L13: -1.4037 L23: 1.1784 REMARK 3 S TENSOR REMARK 3 S11: -0.2371 S12: -0.2193 S13: -0.2278 REMARK 3 S21: 0.1253 S22: 0.1491 S23: 0.1133 REMARK 3 S31: 0.8242 S32: 0.1225 S33: 0.1259 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 138 THROUGH 217 ) REMARK 3 ORIGIN FOR THE GROUP (A): 8.8356 31.6154 21.7085 REMARK 3 T TENSOR REMARK 3 T11: 0.3961 T22: 0.4551 REMARK 3 T33: 0.3487 T12: -0.0304 REMARK 3 T13: -0.0033 T23: -0.0177 REMARK 3 L TENSOR REMARK 3 L11: 5.0587 L22: 8.1225 REMARK 3 L33: 5.8167 L12: -3.1902 REMARK 3 L13: 1.3469 L23: -3.5034 REMARK 3 S TENSOR REMARK 3 S11: 0.0525 S12: -0.1862 S13: -0.1900 REMARK 3 S21: -0.3578 S22: -0.0284 S23: 0.2640 REMARK 3 S31: 0.3509 S32: -0.3675 S33: -0.0397 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 8T0O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JUN-23. REMARK 100 THE DEPOSITION ID IS D_1000274902. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 14-DEC-20 REMARK 200 TEMPERATURE (KELVIN) : 113 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRL REMARK 200 BEAMLINE : BL12-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44577 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300 REMARK 200 RESOLUTION RANGE LOW (A) : 36.450 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 91.6 REMARK 200 DATA REDUNDANCY : 30.00 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.1100 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL 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 (%): 60.03 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.08 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS AT PH 8.0 AND 2.0 M REMARK 280 (NH4)2SO4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+1/3 REMARK 290 3555 -X+Y,-X,Z+2/3 REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z+2/3 REMARK 290 6555 -X,-X+Y,-Z+1/3 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 26.38533 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 52.77067 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 52.77067 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 26.38533 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: 4070 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18950 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 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 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 OG1 THR L 72 O HOH L 301 1.82 REMARK 500 OD1 ASN H 104 O HOH H 401 1.98 REMARK 500 NE2 GLN L 27 OD1 ASP L 98 2.14 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 199 CA - CB - SG ANGL. DEV. = 7.3 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 SER L 26 -74.59 -48.13 REMARK 500 TYR L 30 -127.99 54.04 REMARK 500 ALA L 51 -42.17 76.37 REMARK 500 PRO L 60 1.18 -64.52 REMARK 500 ASN L 143 70.53 49.85 REMARK 500 ALA L 149 127.96 -173.53 REMARK 500 LYS L 174 -60.09 -106.00 REMARK 500 ARG L 216 108.26 -52.74 REMARK 500 SER H 53 -39.32 -34.71 REMARK 500 THR H 72 46.08 -69.33 REMARK 500 ASN H 73 52.65 -119.88 REMARK 500 GLU H 74 51.67 71.53 REMARK 500 ALA H 86 -74.50 -55.36 REMARK 500 ALA H 90 173.72 178.92 REMARK 500 ASN H 104 119.36 -166.18 REMARK 500 LEU H 127 78.19 -110.23 REMARK 500 ASP H 147 64.76 63.79 REMARK 500 PHE H 149 135.44 -172.61 REMARK 500 REMARK 500 REMARK: NULL DBREF 8T0O L 1 217 PDB 8T0O 8T0O 1 217 DBREF 8T0O H 1 217 PDB 8T0O 8T0O 1 217 SEQRES 1 L 217 GLU LEU ASP MET THR GLN THR PRO ALA SER VAL GLU ALA SEQRES 2 L 217 ALA VAL GLY GLY THR VAL THR ILE LYS CYS GLN ALA SER SEQRES 3 L 217 GLN SER ILE TYR SER TYR LEU ALA TRP TYR GLN GLN GLU SEQRES 4 L 217 PRO GLY GLN PRO PRO LYS ARG LEU ILE TYR LYS ALA SER SEQRES 5 L 217 THR LEU ALA SER GLY VAL PRO PRO ARG PHE LYS GLY SER SEQRES 6 L 217 GLY SER GLY THR GLU PHE THR LEU THR ILE SER ASP LEU SEQRES 7 L 217 GLU CYS ALA ASP ALA ALA THR TYR TYR CYS GLN SER ASN SEQRES 8 L 217 LEU TYR SER ILE ASN SER ASP TYR GLY ALA ALA PHE GLY SEQRES 9 L 217 GLY GLY THR GLU VAL VAL VAL LYS ARG THR VAL ALA ALA SEQRES 10 L 217 PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU SEQRES 11 L 217 LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN SEQRES 12 L 217 PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP SEQRES 13 L 217 ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR SEQRES 14 L 217 GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER SEQRES 15 L 217 THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS SEQRES 16 L 217 VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER SEQRES 17 L 217 PRO VAL THR LYS SER PHE ASN ARG GLY SEQRES 1 H 217 GLN SER VAL LYS GLU SER GLU GLY GLY LEU PHE LYS PRO SEQRES 2 H 217 THR ASP THR LEU THR LEU THR CYS THR VAL SER GLY PHE SEQRES 3 H 217 SER LEU SER SER ASN ALA ILE SER TRP VAL ARG GLN ALA SEQRES 4 H 217 PRO GLY ASN GLY LEU GLU TRP ILE GLY THR ILE GLY GLY SEQRES 5 H 217 SER GLY ASN THR TYR TYR ALA SER TRP ALA LYS SER ARG SEQRES 6 H 217 SER THR ILE THR ARG ASN THR ASN GLU ASN THR VAL THR SEQRES 7 H 217 LEU LYS MET THR SER LEU THR ALA ALA ASP THR ALA THR SEQRES 8 H 217 TYR PHE CYS ALA ARG ASP SER ALA THR THR ASP SER ASN SEQRES 9 H 217 ILE TRP GLY PRO GLY THR LEU VAL THR VAL SER SER ALA SEQRES 10 H 217 SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SEQRES 11 H 217 SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS SEQRES 12 H 217 LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER SEQRES 13 H 217 TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE SEQRES 14 H 217 PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SEQRES 15 H 217 SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN SEQRES 16 H 217 THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR SEQRES 17 H 217 LYS VAL ASP LYS LYS VAL GLU PRO LYS HET CL H 301 1 HETNAM CL CHLORIDE ION FORMUL 3 CL CL 1- FORMUL 4 HOH *23(H2 O) HELIX 1 AA1 GLU L 79 ALA L 83 5 5 HELIX 2 AA2 SER L 126 LYS L 131 1 6 HELIX 3 AA3 LYS L 188 GLU L 192 1 5 HELIX 4 AA4 LEU H 84 THR H 89 1 6 HELIX 5 AA5 SER H 130 LYS H 132 5 3 HELIX 6 AA6 SER H 190 LEU H 192 5 3 HELIX 7 AA7 LYS H 204 ASN H 207 5 4 SHEET 1 AA1 4 MET L 4 THR L 7 0 SHEET 2 AA1 4 VAL L 19 ALA L 25 -1 O LYS L 22 N THR L 7 SHEET 3 AA1 4 GLU L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AA1 4 PHE L 62 SER L 67 -1 N LYS L 63 O THR L 74 SHEET 1 AA2 6 SER L 10 ALA L 13 0 SHEET 2 AA2 6 THR L 107 VAL L 111 1 O VAL L 110 N VAL L 11 SHEET 3 AA2 6 THR L 85 SER L 90 -1 N TYR L 86 O THR L 107 SHEET 4 AA2 6 LEU L 33 GLN L 38 -1 N TYR L 36 O TYR L 87 SHEET 5 AA2 6 LYS L 45 TYR L 49 -1 O LYS L 45 N GLN L 37 SHEET 6 AA2 6 THR L 53 LEU L 54 -1 O THR L 53 N TYR L 49 SHEET 1 AA3 4 SER L 119 PHE L 123 0 SHEET 2 AA3 4 THR L 134 PHE L 144 -1 O LEU L 140 N PHE L 121 SHEET 3 AA3 4 TYR L 178 SER L 187 -1 O LEU L 186 N ALA L 135 SHEET 4 AA3 4 SER L 164 VAL L 168 -1 N SER L 167 O SER L 181 SHEET 1 AA4 4 ALA L 158 GLN L 160 0 SHEET 2 AA4 4 LYS L 150 VAL L 155 -1 N TRP L 153 O GLN L 160 SHEET 3 AA4 4 VAL L 196 THR L 202 -1 O GLU L 200 N GLN L 152 SHEET 4 AA4 4 VAL L 210 ASN L 215 -1 O VAL L 210 N VAL L 201 SHEET 1 AA5 4 VAL H 3 LYS H 4 0 SHEET 2 AA5 4 LEU H 17 VAL H 23 -1 O THR H 22 N LYS H 4 SHEET 3 AA5 4 ASN H 75 LYS H 80 -1 O THR H 76 N CYS H 21 SHEET 4 AA5 4 SER H 66 ASN H 71 -1 N THR H 69 O VAL H 77 SHEET 1 AA6 6 GLY H 9 PHE H 11 0 SHEET 2 AA6 6 THR H 110 VAL H 114 1 O THR H 113 N PHE H 11 SHEET 3 AA6 6 ALA H 90 ASP H 97 -1 N TYR H 92 O THR H 110 SHEET 4 AA6 6 ILE H 33 GLN H 38 -1 N VAL H 36 O PHE H 93 SHEET 5 AA6 6 LEU H 44 ILE H 50 -1 O GLY H 48 N TRP H 35 SHEET 6 AA6 6 THR H 56 TYR H 58 -1 O TYR H 57 N THR H 49 SHEET 1 AA7 4 GLY H 9 PHE H 11 0 SHEET 2 AA7 4 THR H 110 VAL H 114 1 O THR H 113 N PHE H 11 SHEET 3 AA7 4 ALA H 90 ASP H 97 -1 N TYR H 92 O THR H 110 SHEET 4 AA7 4 ASN H 104 TRP H 106 -1 O ILE H 105 N ARG H 96 SHEET 1 AA8 4 SER H 123 LEU H 127 0 SHEET 2 AA8 4 THR H 138 TYR H 148 -1 O LEU H 144 N PHE H 125 SHEET 3 AA8 4 TYR H 179 PRO H 188 -1 O SER H 183 N CYS H 143 SHEET 4 AA8 4 VAL H 166 THR H 168 -1 N HIS H 167 O VAL H 184 SHEET 1 AA9 4 THR H 134 SER H 135 0 SHEET 2 AA9 4 THR H 138 TYR H 148 -1 O THR H 138 N SER H 135 SHEET 3 AA9 4 TYR H 179 PRO H 188 -1 O SER H 183 N CYS H 143 SHEET 4 AA9 4 VAL H 172 LEU H 173 -1 N VAL H 172 O SER H 180 SHEET 1 AB1 3 THR H 154 TRP H 157 0 SHEET 2 AB1 3 ILE H 198 HIS H 203 -1 O ASN H 200 N SER H 156 SHEET 3 AB1 3 THR H 208 LYS H 213 -1 O VAL H 210 N VAL H 201 SSBOND 1 CYS L 23 CYS L 88 1555 1555 2.07 SSBOND 2 CYS L 139 CYS L 199 1555 1555 2.07 SSBOND 3 CYS H 21 CYS H 94 1555 1555 2.06 SSBOND 4 CYS H 143 CYS H 199 1555 1555 2.04 CISPEP 1 THR L 7 PRO L 8 0 -1.75 CISPEP 2 TYR L 145 PRO L 146 0 -2.43 CISPEP 3 PHE H 149 PRO H 150 0 -4.68 CISPEP 4 GLU H 151 PRO H 152 0 0.98 CRYST1 111.358 111.358 79.156 90.00 90.00 120.00 P 31 2 1 6 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 0.008980 0.005185 0.000000 0.00000 SCALE2 0.000000 0.010369 0.000000 0.00000 SCALE3 0.000000 0.000000 0.012633 0.00000