HEADER IMMUNE SYSTEM 28-FEB-23 8GBX TITLE CRYSTAL STRUCTURE OF PC39-50I, AN ANTI-HIV BROADLY NEUTRALIZING TITLE 2 ANTIBODY COMPND MOL_ID: 1; COMPND 2 MOLECULE: PC39-50I FAB HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: PC39-50I FAB LIGHT CHAIN; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES; COMPND 9 OTHER_DETAILS: THE N-TERMINAL RESIDUE PAIR "VH" ORIGINATES FROM THE COMPND 10 SIGNAL PEPTIDE SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS ANTIBODY, BROADLY NEUTRALIZING, HIV-1, V3 GLYCAN, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR S.MURRELL,O.OMORODION,I.A.WILSON REVDAT 1 07-JUN-23 8GBX 0 JRNL AUTH C.JOYCE,S.MURRELL,B.MURRELL,O.OMORODION,L.S.VER,N.CARRICO, JRNL AUTH 2 R.ROUZEAU,R.BASTIDAS,R.NEDELLEC,M.BICK,J.WOEHL,F.ZHAO, JRNL AUTH 3 A.BURNS,S.BARMAN,M.APPEL,A.RAMOS,L.WICKRAMASINGHE,K.EREN, JRNL AUTH 4 T.VOLLBRECHT,D.M.SMITH,S.L.KOSAKOVSKY POND,R.MCBRIDE, JRNL AUTH 5 C.WORTH,J.C.PAULSON,F.BATISTA,D.SOK,P.POIGNARD,B.BRINEY, JRNL AUTH 6 I.A.WILSON,E.LANDAIS,D.R.BURTON JRNL TITL ANTIGEN PRESSURE FROM TWO FOUNDER VIRUSES INDUCES MULTIPLE JRNL TITL 2 INSERTIONS AT A SINGLE POSITION TO GENERATE BROADLY JRNL TITL 3 NEUTRALIZING HIV ANTIBODIES JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.19.2_4158 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) : 2.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.81 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 3 NUMBER OF REFLECTIONS : 17601 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.214 REMARK 3 R VALUE (WORKING SET) : 0.212 REMARK 3 FREE R VALUE : 0.244 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020 REMARK 3 FREE R VALUE TEST SET COUNT : 884 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 45.8100 - 4.9000 1.00 2916 161 0.1930 0.2256 REMARK 3 2 4.9000 - 3.8900 1.00 2802 152 0.1784 0.2217 REMARK 3 3 3.8900 - 3.4000 1.00 2762 151 0.2185 0.2560 REMARK 3 4 3.4000 - 3.0900 1.00 2766 142 0.2303 0.2537 REMARK 3 5 3.0900 - 2.8700 1.00 2756 141 0.2775 0.2636 REMARK 3 6 2.8700 - 2.7000 0.98 2715 137 0.3086 0.3478 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) : 0.360 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.860 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 57.11 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 63.40 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 : 0.002 3637 REMARK 3 ANGLE : 0.561 4950 REMARK 3 CHIRALITY : 0.044 547 REMARK 3 PLANARITY : 0.005 636 REMARK 3 DIHEDRAL : 17.871 1322 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 10 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): 1.8327 -5.2624 -18.3714 REMARK 3 T TENSOR REMARK 3 T11: 0.7016 T22: 0.6761 REMARK 3 T33: 0.6569 T12: -0.0044 REMARK 3 T13: 0.0489 T23: -0.0069 REMARK 3 L TENSOR REMARK 3 L11: 6.2128 L22: 2.0138 REMARK 3 L33: 0.1009 L12: -9.6716 REMARK 3 L13: 0.6974 L23: -0.9273 REMARK 3 S TENSOR REMARK 3 S11: 0.9009 S12: 0.8296 S13: -0.5926 REMARK 3 S21: -2.4358 S22: -1.1088 S23: 1.0441 REMARK 3 S31: -0.0211 S32: -0.6405 S33: 0.2633 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 18 THROUGH 111 ) REMARK 3 ORIGIN FOR THE GROUP (A): 5.2800 -16.4274 -11.0403 REMARK 3 T TENSOR REMARK 3 T11: 0.6950 T22: 0.3906 REMARK 3 T33: 0.3508 T12: -0.0020 REMARK 3 T13: -0.1258 T23: -0.0429 REMARK 3 L TENSOR REMARK 3 L11: 2.1246 L22: 6.1971 REMARK 3 L33: 2.9082 L12: -1.6962 REMARK 3 L13: -0.8921 L23: -1.2135 REMARK 3 S TENSOR REMARK 3 S11: 0.0144 S12: 0.1983 S13: -0.3367 REMARK 3 S21: -0.2966 S22: -0.0076 S23: 0.5299 REMARK 3 S31: 0.5390 S32: -0.0880 S33: 0.0018 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 112 THROUGH 216 ) REMARK 3 ORIGIN FOR THE GROUP (A): 19.0475 15.0571 -30.6062 REMARK 3 T TENSOR REMARK 3 T11: 0.5954 T22: 0.3706 REMARK 3 T33: 0.3332 T12: -0.0777 REMARK 3 T13: -0.0323 T23: 0.0315 REMARK 3 L TENSOR REMARK 3 L11: 7.4982 L22: 2.5974 REMARK 3 L33: 2.8659 L12: 3.2155 REMARK 3 L13: -1.7208 L23: -1.0650 REMARK 3 S TENSOR REMARK 3 S11: -0.1766 S12: 0.6257 S13: 0.4357 REMARK 3 S21: -0.3782 S22: 0.2148 S23: 0.1035 REMARK 3 S31: -0.2692 S32: 0.4035 S33: -0.0132 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'L' AND (RESID -1 THROUGH 29 ) REMARK 3 ORIGIN FOR THE GROUP (A): 27.7610 -10.6354 -2.7315 REMARK 3 T TENSOR REMARK 3 T11: 0.4543 T22: 0.4448 REMARK 3 T33: 0.5270 T12: 0.1222 REMARK 3 T13: -0.0849 T23: 0.0431 REMARK 3 L TENSOR REMARK 3 L11: 6.1287 L22: 5.2015 REMARK 3 L33: 7.3523 L12: 3.0133 REMARK 3 L13: -1.7398 L23: -4.0020 REMARK 3 S TENSOR REMARK 3 S11: 0.3207 S12: 0.3718 S13: 0.1304 REMARK 3 S21: 0.1693 S22: -0.5748 S23: -0.6724 REMARK 3 S31: -0.1859 S32: 0.5216 S33: 0.2156 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 30 THROUGH 61 ) REMARK 3 ORIGIN FOR THE GROUP (A): 22.8158 -19.0848 -11.9784 REMARK 3 T TENSOR REMARK 3 T11: 0.7862 T22: 0.4486 REMARK 3 T33: 0.4248 T12: 0.1893 REMARK 3 T13: -0.0044 T23: -0.0509 REMARK 3 L TENSOR REMARK 3 L11: 7.7357 L22: 6.9367 REMARK 3 L33: 5.6067 L12: 1.3439 REMARK 3 L13: -2.3871 L23: 1.7186 REMARK 3 S TENSOR REMARK 3 S11: -0.1187 S12: 0.5927 S13: -0.3994 REMARK 3 S21: -0.6835 S22: -0.2682 S23: -0.3952 REMARK 3 S31: 1.0805 S32: 0.5292 S33: 0.3789 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 62 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): 30.0581 -18.1837 -3.8368 REMARK 3 T TENSOR REMARK 3 T11: 0.6391 T22: 0.6476 REMARK 3 T33: 0.6852 T12: 0.2418 REMARK 3 T13: -0.1151 T23: 0.0693 REMARK 3 L TENSOR REMARK 3 L11: 8.2865 L22: 6.8283 REMARK 3 L33: 2.0002 L12: 0.8840 REMARK 3 L13: -5.8744 L23: 0.6454 REMARK 3 S TENSOR REMARK 3 S11: 0.0531 S12: -0.8004 S13: -0.3596 REMARK 3 S21: 0.3679 S22: -0.2318 S23: -1.3256 REMARK 3 S31: 1.1650 S32: 1.6432 S33: 0.1896 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 76 THROUGH 113 ) REMARK 3 ORIGIN FOR THE GROUP (A): 27.1102 -9.0979 -11.6645 REMARK 3 T TENSOR REMARK 3 T11: 0.6458 T22: 0.6370 REMARK 3 T33: 0.3848 T12: 0.1858 REMARK 3 T13: 0.0088 T23: 0.0553 REMARK 3 L TENSOR REMARK 3 L11: 4.0459 L22: 5.7800 REMARK 3 L33: 0.9712 L12: 3.3146 REMARK 3 L13: -0.5589 L23: -1.2303 REMARK 3 S TENSOR REMARK 3 S11: 0.0551 S12: -0.0425 S13: -0.2542 REMARK 3 S21: -0.5114 S22: -0.3001 S23: -0.6712 REMARK 3 S31: 0.5357 S32: 0.7418 S33: 0.1962 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 114 THROUGH 150 ) REMARK 3 ORIGIN FOR THE GROUP (A): 27.0611 20.0897 -21.2335 REMARK 3 T TENSOR REMARK 3 T11: 0.5131 T22: 0.5523 REMARK 3 T33: 0.4029 T12: -0.1634 REMARK 3 T13: 0.0814 T23: 0.0842 REMARK 3 L TENSOR REMARK 3 L11: 5.0468 L22: 9.3291 REMARK 3 L33: 2.8707 L12: -4.5867 REMARK 3 L13: -0.3148 L23: 0.3007 REMARK 3 S TENSOR REMARK 3 S11: -0.2670 S12: 0.1688 S13: -0.1555 REMARK 3 S21: 0.2595 S22: 0.0119 S23: 0.3181 REMARK 3 S31: -0.3012 S32: 0.6996 S33: 0.2740 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 151 THROUGH 163 ) REMARK 3 ORIGIN FOR THE GROUP (A): 25.3110 22.5193 -12.3670 REMARK 3 T TENSOR REMARK 3 T11: 0.5559 T22: 0.6140 REMARK 3 T33: 0.5622 T12: -0.2285 REMARK 3 T13: -0.0305 T23: 0.0232 REMARK 3 L TENSOR REMARK 3 L11: 0.6817 L22: 6.7470 REMARK 3 L33: 3.2306 L12: 1.6716 REMARK 3 L13: 0.8231 L23: 0.9227 REMARK 3 S TENSOR REMARK 3 S11: 0.2045 S12: -0.4531 S13: 0.0384 REMARK 3 S21: -0.2981 S22: -0.1719 S23: -0.9712 REMARK 3 S31: -1.1371 S32: 0.7473 S33: -0.0201 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 164 THROUGH 214 ) REMARK 3 ORIGIN FOR THE GROUP (A): 29.6578 21.2976 -19.7421 REMARK 3 T TENSOR REMARK 3 T11: 0.5717 T22: 0.6338 REMARK 3 T33: 0.2931 T12: -0.1749 REMARK 3 T13: 0.0709 T23: 0.0514 REMARK 3 L TENSOR REMARK 3 L11: 6.8195 L22: 8.4629 REMARK 3 L33: 2.0230 L12: -3.0920 REMARK 3 L13: 0.1987 L23: 0.1653 REMARK 3 S TENSOR REMARK 3 S11: -0.2121 S12: 0.2127 S13: 0.5227 REMARK 3 S21: -0.5295 S22: 0.0928 S23: -0.5449 REMARK 3 S31: -0.5078 S32: 0.6799 S33: 0.1176 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 8GBX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-MAR-23. REMARK 100 THE DEPOSITION ID IS D_1000272565. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 17-OCT-15 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-D REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.03320 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17633 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700 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 : 6.900 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.25000 REMARK 200 FOR THE DATA SET : 7.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.75 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.6 REMARK 200 DATA REDUNDANCY IN SHELL : 4.00 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 1.55000 REMARK 200 FOR SHELL : 1.000 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER 2.8.3 REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 60.48 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.11 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 10% GLYCEROL, 0.1 M MES, 5% PEG 1000, REMARK 280 30% PEG 600, PH 6, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE REMARK 280 293.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 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 -X,Y,-Z+1/2 REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 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 52.27650 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 52.27650 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 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 45.81050 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 65.55050 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 45.81050 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 65.55050 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 52.27650 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 45.81050 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 65.55050 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 52.27650 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 45.81050 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 65.55050 REMARK 290 SMTRY3 8 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: 4100 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 21260 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L 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 ASP H 217 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 H 15 -3.81 86.35 REMARK 500 TYR H 31A 36.69 -97.20 REMARK 500 ASP H 144 66.86 60.91 REMARK 500 ASP L 50 -132.04 54.19 REMARK 500 ALA L 84 -156.16 -166.03 REMARK 500 ASN L 138 83.78 56.79 REMARK 500 LYS L 169 -77.66 -89.84 REMARK 500 LYS L 190 -54.81 -127.76 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 8GBV RELATED DB: PDB REMARK 900 RELATED ID: 8GBW RELATED DB: PDB REMARK 900 RELATED ID: 8GBY RELATED DB: PDB REMARK 900 RELATED ID: 8GBZ RELATED DB: PDB REMARK 900 RELATED ID: 8GC0 RELATED DB: PDB REMARK 900 RELATED ID: 8GC1 RELATED DB: PDB DBREF 8GBX H 1 217 PDB 8GBX 8GBX 1 217 DBREF 8GBX L -1 214 PDB 8GBX 8GBX -1 214 SEQRES 1 H 243 GLN VAL GLN LEU GLN GLN TRP GLY ALA GLY LEU LEU LYS SEQRES 2 H 243 PRO SER GLU THR LEU SER VAL THR CYS ALA ILE TYR GLY SEQRES 3 H 243 ASP SER LEU SER ASP TYR SER TRP LYS TRP GLY VAL SER SEQRES 4 H 243 ARG ASP ASP TYR TYR TRP THR TRP ILE ARG GLN SER PRO SEQRES 5 H 243 GLY LYS ARG LEU GLU TRP ILE GLY GLU ILE ASN ARG GLY SEQRES 6 H 243 GLY ASN THR LYS TYR ASN PRO SER LEU SER SER ARG VAL SEQRES 7 H 243 LYS MET SER ILE ASP ALA SER LYS ASN GLN PHE SER LEU SEQRES 8 H 243 ARG MET ARG SER VAL THR ASP THR ASP THR GLY ILE TYR SEQRES 9 H 243 TYR CYS ALA ARG GLY ARG ARG SER ARG GLN TRP ILE GLY SEQRES 10 H 243 ASP LEU PRO PRO GLY ASN GLN GLY LEU ASP VAL TRP GLY SEQRES 11 H 243 GLN GLY THR THR VAL ILE VAL SER SER ALA SER THR LYS SEQRES 12 H 243 GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER SEQRES 13 H 243 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS SEQRES 14 H 243 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 15 H 243 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 16 H 243 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL SEQRES 17 H 243 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE SEQRES 18 H 243 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP SEQRES 19 H 243 LYS ARG VAL GLU PRO LYS SER CYS ASP SEQRES 1 L 218 VAL HIS GLU ILE VAL LEU THR GLN SER PRO VAL THR LEU SEQRES 2 L 218 SER LEU SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG SEQRES 3 L 218 ALA SER GLN SER VAL SER SER SER TYR LEU ALA TRP TYR SEQRES 4 L 218 GLN HIS LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE SER SEQRES 5 L 218 ASP VAL TYR ARG ARG ALA SER GLY VAL PRO ASP ARG PHE SEQRES 6 L 218 SER GLY SER GLY SER GLY THR GLU PHE THR LEU THR ILE SEQRES 7 L 218 SER ARG LEU GLU PRO GLU ASP PHE ALA ILE TYR TYR CYS SEQRES 8 L 218 GLN GLN TYR GLY SER SER PRO PRO TYR THR PHE GLY GLN SEQRES 9 L 218 GLY THR LYS VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SEQRES 10 L 218 SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SEQRES 11 L 218 SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE SEQRES 12 L 218 TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN SEQRES 13 L 218 ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU SEQRES 14 L 218 GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER THR SEQRES 15 L 218 LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL SEQRES 16 L 218 TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO SEQRES 17 L 218 VAL THR LYS SER PHE ASN ARG GLY GLU CYS FORMUL 3 HOH *4(H2 O) HELIX 1 AA1 THR H 83 THR H 87 5 5 HELIX 2 AA2 SER H 127 LYS H 129 5 3 HELIX 3 AA3 SER H 156 ALA H 158 5 3 HELIX 4 AA4 SER H 187 THR H 191 5 5 HELIX 5 AA5 SER L 29 SER L 31 5 3 HELIX 6 AA6 GLU L 79 PHE L 83 5 5 HELIX 7 AA7 SER L 121 LYS L 126 1 6 HELIX 8 AA8 LYS L 183 LYS L 188 1 6 SHEET 1 AA1 4 GLN H 3 GLN H 5 0 SHEET 2 AA1 4 LEU H 18 TYR H 25 -1 O ALA H 23 N GLN H 5 SHEET 3 AA1 4 GLN H 77 MET H 82 -1 O MET H 82 N LEU H 18 SHEET 4 AA1 4 VAL H 67 ASP H 72 -1 N ASP H 72 O GLN H 77 SHEET 1 AA2 6 GLY H 10 LEU H 12 0 SHEET 2 AA2 6 THR H 107 VAL H 111 1 O THR H 108 N GLY H 10 SHEET 3 AA2 6 GLY H 88 ARG H 96 -1 N TYR H 90 O THR H 107 SHEET 4 AA2 6 TYR H 32 GLN H 39 -1 N TYR H 33 O GLY H 95 SHEET 5 AA2 6 GLU H 46 ASN H 52 -1 O GLU H 46 N ARG H 38 SHEET 6 AA2 6 THR H 57 TYR H 59 -1 O LYS H 58 N GLU H 50 SHEET 1 AA3 4 GLY H 10 LEU H 12 0 SHEET 2 AA3 4 THR H 107 VAL H 111 1 O THR H 108 N GLY H 10 SHEET 3 AA3 4 GLY H 88 ARG H 96 -1 N TYR H 90 O THR H 107 SHEET 4 AA3 4 GLY H 100K TRP H 103 -1 O VAL H 102 N ARG H 94 SHEET 1 AA4 4 SER H 120 LEU H 124 0 SHEET 2 AA4 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AA4 4 TYR H 176 PRO H 185 -1 O TYR H 176 N TYR H 145 SHEET 4 AA4 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AA5 4 THR H 131 SER H 132 0 SHEET 2 AA5 4 THR H 135 TYR H 145 -1 O THR H 135 N SER H 132 SHEET 3 AA5 4 TYR H 176 PRO H 185 -1 O TYR H 176 N TYR H 145 SHEET 4 AA5 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AA6 3 THR H 151 TRP H 154 0 SHEET 2 AA6 3 ILE H 195 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 AA6 3 THR H 205 ARG H 210 -1 O THR H 205 N HIS H 200 SHEET 1 AA7 4 LEU L 4 SER L 7 0 SHEET 2 AA7 4 ALA L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AA7 4 GLU L 70 ILE L 75 -1 O ILE L 75 N ALA L 19 SHEET 4 AA7 4 PHE L 62 GLY L 66 -1 N SER L 65 O THR L 72 SHEET 1 AA8 6 THR L 10 LEU L 13 0 SHEET 2 AA8 6 THR L 102 ILE L 106 1 O GLU L 105 N LEU L 11 SHEET 3 AA8 6 ILE L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AA8 6 LEU L 33 HIS L 38 -1 N ALA L 34 O GLN L 89 SHEET 5 AA8 6 ARG L 45 SER L 49 -1 O ARG L 45 N GLN L 37 SHEET 6 AA8 6 ARG L 53 ARG L 54 -1 O ARG L 53 N SER L 49 SHEET 1 AA9 4 SER L 114 PHE L 118 0 SHEET 2 AA9 4 THR L 129 PHE L 139 -1 O VAL L 133 N PHE L 118 SHEET 3 AA9 4 TYR L 173 SER L 182 -1 O LEU L 175 N LEU L 136 SHEET 4 AA9 4 SER L 159 VAL L 163 -1 N SER L 162 O SER L 176 SHEET 1 AB1 4 ALA L 153 LEU L 154 0 SHEET 2 AB1 4 ALA L 144 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AB1 4 VAL L 191 HIS L 198 -1 O GLU L 195 N GLN L 147 SHEET 4 AB1 4 VAL L 205 ASN L 210 -1 O PHE L 209 N TYR L 192 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.04 SSBOND 2 CYS H 140 CYS H 196 1555 1555 2.04 SSBOND 3 CYS H 216 CYS L 214 1555 1555 2.04 SSBOND 4 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 5 CYS L 134 CYS L 194 1555 1555 2.03 CISPEP 1 PHE H 146 PRO H 147 0 -4.08 CISPEP 2 GLU H 148 PRO H 149 0 -4.31 CISPEP 3 SER L 7 PRO L 8 0 -3.37 CISPEP 4 PRO L 95 PRO L 95A 0 -0.49 CISPEP 5 TYR L 140 PRO L 141 0 0.36 CRYST1 91.621 131.101 104.553 90.00 90.00 90.00 C 2 2 21 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 0.010915 0.000000 0.000000 0.00000 SCALE2 0.000000 0.007628 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009565 0.00000