HEADER IMMUNE SYSTEM 31-MAR-24 8YWQ TITLE CRYSTAL STRUCTURE OF THE FAB FRAGMENT OF THE ANTI-IL-6 ANTIBODY I9H IN TITLE 2 COMPLEX WITH A DOMAIN-SWAPPED IL-6 DIMER COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEAVY CHAIN OF THE FAB FRAGMENT OF ANTI-IL-6 ANTIBODY I9H; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: LIGHT CHAIN OF THE FAB FRAGMENT OF ANTI-IL-6 ANTIBODY I9H; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: INTERLEUKIN-6; COMPND 11 CHAIN: A; COMPND 12 SYNONYM: IL-6,B-CELL STIMULATORY FACTOR 2,BSF-2,CTL DIFFERENTIATION COMPND 13 FACTOR,CDF,HYBRIDOMA GROWTH FACTOR,INTERFERON BETA-2,IFN-BETA-2; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: CHO-IL69HUM; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_TAXID: 9606; SOURCE 10 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 12 EXPRESSION_SYSTEM_STRAIN: CHO-IL69HUM; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 15 ORGANISM_COMMON: HUMAN; SOURCE 16 ORGANISM_TAXID: 9606; SOURCE 17 GENE: IL6, IFNB2; SOURCE 18 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 20 EXPRESSION_SYSTEM_CELL_LINE: HEK293 KEYWDS INTERLEUKIN, DIMER, SWAP, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR S.BUKHDRUKER,A.YUDENKO,E.MARIN,A.REMEEVA,S.RODIN,A.BURTSEVA,A.PETROV, AUTHOR 2 A.ISCHENKO,V.BORSHCHEVSKIY REVDAT 1 06-NOV-24 8YWQ 0 JRNL AUTH A.YUDENKO,S.BUKHDRUKER,P.SHISHKIN,S.RODIN,A.BURTSEVA, JRNL AUTH 2 A.PETROV,N.PIGAREVA,A.SOKOLOV,E.ZINOVEV,I.ELISEEV,A.REMEEVA, JRNL AUTH 3 E.MARIN,A.MISHIN,V.GODELIY,I.GUSHCHIN,A.ISCHENKO, JRNL AUTH 4 V.BORSHCHEVSKIY JRNL TITL STRUCTURAL BASIS OF SIGNALING COMPLEX INHIBITION BY IL-6 JRNL TITL 2 DOMAIN-SWAPPED DIMERS JRNL REF STRUCTURE 2025 JRNL REFN ISSN 0969-2126 REMARK 2 REMARK 2 RESOLUTION. 2.51 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) : 2.51 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.97 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 58.2 REMARK 3 NUMBER OF REFLECTIONS : 14833 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.243 REMARK 3 R VALUE (WORKING SET) : 0.239 REMARK 3 FREE R VALUE : 0.277 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.950 REMARK 3 FREE R VALUE TEST SET COUNT : 1476 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 40.9700 - 5.5800 0.99 2203 243 0.2038 0.2381 REMARK 3 2 5.5800 - 4.4300 1.00 2116 232 0.2063 0.2386 REMARK 3 3 4.4300 - 3.8700 1.00 2090 237 0.2247 0.2877 REMARK 3 4 3.8700 - 3.5200 0.99 2052 229 0.2739 0.3021 REMARK 3 5 3.5200 - 3.2600 0.93 1941 216 0.3451 0.3881 REMARK 3 6 3.2600 - 3.0700 0.58 1195 126 0.3786 0.4378 REMARK 3 7 3.0700 - 2.9200 0.35 732 78 0.3807 0.3713 REMARK 3 8 2.9200 - 2.7900 0.23 474 46 0.3986 0.3445 REMARK 3 9 2.7900 - 2.6800 0.15 300 37 0.4927 0.4928 REMARK 3 10 2.6800 - 2.5900 0.09 188 25 0.4848 0.5314 REMARK 3 11 2.5900 - 2.5100 0.03 66 7 0.4784 0.5819 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) : 0.327 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 40.830 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 89.68 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 89.35 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 4358 REMARK 3 ANGLE : 0.508 5964 REMARK 3 CHIRALITY : 0.040 709 REMARK 3 PLANARITY : 0.004 762 REMARK 3 DIHEDRAL : 11.430 1488 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: (CHAIN 'H' AND RESID 1 THROUGH 225) REMARK 3 ORIGIN FOR THE GROUP (A): -26.3534 -20.6667 29.7319 REMARK 3 T TENSOR REMARK 3 T11: 0.3635 T22: 0.1574 REMARK 3 T33: 0.2589 T12: -0.1537 REMARK 3 T13: -0.2869 T23: -0.2307 REMARK 3 L TENSOR REMARK 3 L11: 1.0620 L22: 1.0998 REMARK 3 L33: 2.1950 L12: 0.4877 REMARK 3 L13: 0.5883 L23: 0.9417 REMARK 3 S TENSOR REMARK 3 S11: 0.3843 S12: 0.5497 S13: -0.4035 REMARK 3 S21: -0.3528 S22: 0.3864 S23: -0.3168 REMARK 3 S31: -0.0514 S32: 0.1890 S33: 2.1003 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (CHAIN 'L' AND RESID 1 THROUGH 213) REMARK 3 ORIGIN FOR THE GROUP (A): -43.5810 -19.8401 36.7377 REMARK 3 T TENSOR REMARK 3 T11: 0.4496 T22: 0.8685 REMARK 3 T33: 0.4601 T12: -0.0567 REMARK 3 T13: -0.0921 T23: 0.0094 REMARK 3 L TENSOR REMARK 3 L11: 0.8176 L22: 1.0322 REMARK 3 L33: 0.3676 L12: 0.1619 REMARK 3 L13: 0.0483 L23: 0.0769 REMARK 3 S TENSOR REMARK 3 S11: 0.1738 S12: -0.3202 S13: -0.1666 REMARK 3 S21: -0.0256 S22: -0.1405 S23: 0.1430 REMARK 3 S31: -0.0376 S32: -0.8560 S33: 0.0000 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: (CHAIN 'A' AND RESID 19 THROUGH 184) REMARK 3 ORIGIN FOR THE GROUP (A): -1.8224 -1.2169 63.1008 REMARK 3 T TENSOR REMARK 3 T11: 0.3377 T22: 0.2135 REMARK 3 T33: 0.3666 T12: 0.0490 REMARK 3 T13: -0.0090 T23: -0.0356 REMARK 3 L TENSOR REMARK 3 L11: 1.4855 L22: 0.7485 REMARK 3 L33: 2.0593 L12: 0.2363 REMARK 3 L13: 0.4847 L23: -0.1544 REMARK 3 S TENSOR REMARK 3 S11: 0.4872 S12: 0.1818 S13: -0.2037 REMARK 3 S21: 0.2434 S22: 0.2008 S23: 0.0050 REMARK 3 S31: 0.1711 S32: -0.1159 S33: 0.9071 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 8YWQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-APR-24. REMARK 100 THE DEPOSITION ID IS D_1300046428. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 19-NOV-19 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 10.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SLS REMARK 200 BEAMLINE : X06SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.850 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS 20190315 REMARK 200 DATA SCALING SOFTWARE : STARANISO 2.3.15 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14890 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.510 REMARK 200 RESOLUTION RANGE LOW (A) : 40.970 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 91.7 REMARK 200 DATA REDUNDANCY : 13.00 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.51 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.82 REMARK 200 COMPLETENESS FOR SHELL (%) : 69.3 REMARK 200 DATA REDUNDANCY IN SHELL : 12.30 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.700 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: 1ALU,8YWP REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 53.28 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 40% V/V 2-METHYL-2,4-PENTANEDIOL, 100 REMARK 280 MM CAPS (SEED STOCK CRYSTALLIZATION CONDITIONS: 14-16% PEG 8000, REMARK 280 100 MM MAGNESIUM ACETATE, 100 MM MES PH 6.5), PH 10.5, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -X,Y,-Z 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 REMARK 290 7555 -X+1/2,Y+1/2,-Z 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 0.00000 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 0.00000 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 63.31050 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 75.93750 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 63.31050 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 75.93750 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 63.31050 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 75.93750 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 63.31050 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 75.93750 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: HEXAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, A REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000 REMARK 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 MG MG A 501 LIES ON A SPECIAL POSITION. REMARK 375 HOH A 602 LIES ON A SPECIAL POSITION. REMARK 375 HOH A 603 LIES ON A SPECIAL POSITION. 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 SER H 138 REMARK 465 SER H 139 REMARK 465 LYS H 140 REMARK 465 SER H 141 REMARK 465 THR H 142 REMARK 465 SER H 143 REMARK 465 GLY H 144 REMARK 465 SER H 226 REMARK 465 CYS H 227 REMARK 465 ASP H 228 REMARK 465 LYS H 229 REMARK 465 THR H 230 REMARK 465 HIS H 231 REMARK 465 CYS L 214 REMARK 465 ALA A 0 REMARK 465 PRO A 1 REMARK 465 VAL A 2 REMARK 465 PRO A 3 REMARK 465 PRO A 4 REMARK 465 GLY A 5 REMARK 465 GLU A 6 REMARK 465 ASP A 7 REMARK 465 SER A 8 REMARK 465 LYS A 9 REMARK 465 ASP A 10 REMARK 465 VAL A 11 REMARK 465 ALA A 12 REMARK 465 ALA A 13 REMARK 465 PRO A 14 REMARK 465 HIS A 15 REMARK 465 ARG A 16 REMARK 465 GLN A 17 REMARK 465 PRO A 18 REMARK 465 GLU A 42 REMARK 465 THR A 43 REMARK 465 CYS A 44 REMARK 465 ASN A 45 REMARK 465 LYS A 46 REMARK 465 SER A 47 REMARK 465 ASN A 48 REMARK 465 MET A 49 REMARK 465 CYS A 50 REMARK 465 GLU A 51 REMARK 465 SER A 52 REMARK 465 SER A 53 REMARK 465 LYS A 54 REMARK 465 GLU A 55 REMARK 465 ALA A 56 REMARK 465 LEU A 57 REMARK 465 ALA A 58 REMARK 465 LEU A 133 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 LYS H 13 CG CD CE NZ REMARK 470 GLN H 16 CD OE1 NE2 REMARK 470 LYS H 45 CE NZ REMARK 470 LYS H 66 CD CE NZ REMARK 470 LYS H 77 CG CD CE NZ REMARK 470 ASN H 86 CG OD1 ND2 REMARK 470 GLN H 116 CG CD OE1 NE2 REMARK 470 LEU H 200 CG CD1 CD2 REMARK 470 THR H 202 OG1 CG2 REMARK 470 GLN H 203 CG CD OE1 NE2 REMARK 470 LYS H 212 CG CD CE NZ REMARK 470 LYS H 217 CD CE NZ REMARK 470 LYS H 221 CG CD CE NZ REMARK 470 GLU H 223 CG CD OE1 OE2 REMARK 470 LYS H 225 CG CD CE NZ REMARK 470 ASP L 1 CG OD1 OD2 REMARK 470 LYS L 24 CG CD CE NZ REMARK 470 LYS L 42 CD CE NZ REMARK 470 LYS L 45 CG CD CE NZ REMARK 470 ARG L 93 CG CD NE CZ NH1 NH2 REMARK 470 LYS L 103 CG CD CE NZ REMARK 470 GLU L 105 CG CD OE1 OE2 REMARK 470 LYS L 107 CG CD CE NZ REMARK 470 PHE L 116 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ASP L 122 CG OD1 OD2 REMARK 470 LYS L 126 CG CD CE NZ REMARK 470 ARG L 142 CG CD NE CZ NH1 NH2 REMARK 470 LYS L 145 CG CD CE NZ REMARK 470 LYS L 149 CD CE NZ REMARK 470 ASN L 152 CG OD1 ND2 REMARK 470 LEU L 154 CG CD1 CD2 REMARK 470 ASN L 158 CG OD1 ND2 REMARK 470 LYS L 169 CG CD CE NZ REMARK 470 LYS L 183 CG CD CE NZ REMARK 470 GLU L 187 CG CD OE1 OE2 REMARK 470 LYS L 188 CG CD CE NZ REMARK 470 LYS L 190 CG CD CE NZ REMARK 470 GLU L 195 CG CD OE1 OE2 REMARK 470 LYS L 207 CD CE NZ REMARK 470 PHE L 209 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG L 211 CG CD NE CZ NH1 NH2 REMARK 470 LEU A 19 CG CD1 CD2 REMARK 470 LYS A 41 CE NZ REMARK 470 GLU A 59 CG CD OE1 OE2 REMARK 470 ASN A 60 CG OD1 ND2 REMARK 470 LYS A 66 CG CD CE NZ REMARK 470 GLU A 69 CG CD OE1 OE2 REMARK 470 GLU A 80 CG CD OE1 OE2 REMARK 470 GLU A 81 CG CD OE1 OE2 REMARK 470 GLU A 99 CG CD OE1 OE2 REMARK 470 LYS A 120 CG CD CE NZ REMARK 470 GLN A 124 CG CD OE1 NE2 REMARK 470 GLN A 127 CG CD OE1 NE2 REMARK 470 LYS A 128 CD CE NZ REMARK 470 LYS A 129 CG CD CE NZ REMARK 470 LYS A 131 CG CD CE NZ REMARK 470 ASN A 132 CG OD1 ND2 REMARK 470 LYS A 150 CG CD CE NZ REMARK 470 GLN A 156 CG CD OE1 NE2 REMARK 470 MET A 161 CG SD CE REMARK 470 ARG A 168 NE CZ NH1 NH2 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 22 CA - CB - SG ANGL. DEV. = 8.4 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 LEU H 50 -69.22 -102.48 REMARK 500 ASP H 91 32.63 -97.51 REMARK 500 ASP H 155 78.15 60.63 REMARK 500 SER L 30 -140.24 57.96 REMARK 500 LEU L 47 -71.77 -111.39 REMARK 500 ALA L 51 -52.54 67.93 REMARK 500 SER L 76 -77.80 -65.20 REMARK 500 LYS L 126 49.66 -74.54 REMARK 500 SER L 127 -140.80 -163.81 REMARK 500 ASN L 138 76.14 57.54 REMARK 500 ASP L 170 12.85 -144.55 REMARK 500 PRO L 204 96.99 -65.50 REMARK 500 THR A 20 -168.71 -108.07 REMARK 500 ALA A 130 -71.89 -69.22 REMARK 500 GLN A 183 33.85 -79.38 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MG A 501 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU A 106 OE2 REMARK 620 2 GLU A 106 OE2 0.0 REMARK 620 N 1 DBREF 8YWQ H 1 231 PDB 8YWQ 8YWQ 1 231 DBREF 8YWQ L 1 214 PDB 8YWQ 8YWQ 1 214 DBREF 8YWQ A 0 184 UNP P05231 IL6_HUMAN 28 212 SEQRES 1 H 231 GLN ILE THR LEU LYS GLU SER GLY PRO ALA LEU VAL LYS SEQRES 2 H 231 PRO THR GLN THR LEU THR LEU THR CYS THR PHE SER GLY SEQRES 3 H 231 PHE SER LEU SER THR SER GLY MET GLY VAL GLY TRP ILE SEQRES 4 H 231 ARG GLN PRO PRO GLY LYS ALA LEU GLU TRP LEU ALA HIS SEQRES 5 H 231 ILE TRP TRP ASP ASP ASP LYS TYR TYR ASN PRO SER LEU SEQRES 6 H 231 LYS SER ARG LEU THR ILE SER LYS ASP THR SER LYS ASN SEQRES 7 H 231 GLN VAL VAL LEU THR MET THR ASN MET ASP PRO VAL ASP SEQRES 8 H 231 THR ALA THR TYR TYR CYS ALA ARG ARG ALA ASN TYR GLY SEQRES 9 H 231 THR SER TYR ASP TYR GLY MET ASP TYR TRP GLY GLN GLY SEQRES 10 H 231 THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SEQRES 11 H 231 SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER SEQRES 12 H 231 GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 13 H 231 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA SEQRES 14 H 231 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15 H 231 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 16 H 231 PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN SEQRES 17 H 231 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS SEQRES 18 H 231 VAL GLU PRO LYS SER CYS ASP LYS THR HIS SEQRES 1 L 214 ASP VAL VAL MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS LYS ALA SER SEQRES 3 L 214 GLN SER VAL SER ASP VAL LEU THR TRP TYR GLN GLN LYS SEQRES 4 L 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR TYR ALA SER SEQRES 5 L 214 ASN ARG TYR THR GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 214 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 214 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN GLY SEQRES 8 L 214 TYR ARG SER PRO TYR THR PHE GLY GLY GLY THR LYS LEU SEQRES 9 L 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 L 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 L 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 L 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 L 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 L 214 PHE ASN ARG GLY GLU CYS SEQRES 1 A 185 ALA PRO VAL PRO PRO GLY GLU ASP SER LYS ASP VAL ALA SEQRES 2 A 185 ALA PRO HIS ARG GLN PRO LEU THR SER SER GLU ARG ILE SEQRES 3 A 185 ASP LYS GLN ILE ARG TYR ILE LEU ASP GLY ILE SER ALA SEQRES 4 A 185 LEU ARG LYS GLU THR CYS ASN LYS SER ASN MET CYS GLU SEQRES 5 A 185 SER SER LYS GLU ALA LEU ALA GLU ASN ASN LEU ASN LEU SEQRES 6 A 185 PRO LYS MET ALA GLU LYS ASP GLY CYS PHE GLN SER GLY SEQRES 7 A 185 PHE ASN GLU GLU THR CYS LEU VAL LYS ILE ILE THR GLY SEQRES 8 A 185 LEU LEU GLU PHE GLU VAL TYR LEU GLU TYR LEU GLN ASN SEQRES 9 A 185 ARG PHE GLU SER SER GLU GLU GLN ALA ARG ALA VAL GLN SEQRES 10 A 185 MET SER THR LYS VAL LEU ILE GLN PHE LEU GLN LYS LYS SEQRES 11 A 185 ALA LYS ASN LEU ASP ALA ILE THR THR PRO ASP PRO THR SEQRES 12 A 185 THR ASN ALA SER LEU LEU THR LYS LEU GLN ALA GLN ASN SEQRES 13 A 185 GLN TRP LEU GLN ASP MET THR THR HIS LEU ILE LEU ARG SEQRES 14 A 185 SER PHE LYS GLU PHE LEU GLN SER SER LEU ARG ALA LEU SEQRES 15 A 185 ARG GLN MET HET MG A 501 1 HETNAM MG MAGNESIUM ION FORMUL 4 MG MG 2+ FORMUL 5 HOH *3(H2 O) HELIX 1 AA1 LEU H 65 SER H 67 5 3 HELIX 2 AA2 ASP H 88 THR H 92 5 5 HELIX 3 AA3 LYS H 212 ASN H 215 5 4 HELIX 4 AA4 GLN L 79 PHE L 83 5 5 HELIX 5 AA5 SER L 121 LYS L 126 1 6 HELIX 6 AA6 LYS L 183 HIS L 189 1 7 HELIX 7 AA7 THR A 20 LYS A 41 1 22 HELIX 8 AA8 ALA A 68 GLY A 72 5 5 HELIX 9 AA9 GLU A 81 LYS A 131 1 51 HELIX 10 AB1 ASP A 140 GLN A 154 1 15 HELIX 11 AB2 ASN A 155 GLN A 183 1 29 SHEET 1 AA1 4 THR H 3 SER H 7 0 SHEET 2 AA1 4 LEU H 18 SER H 25 -1 O THR H 21 N SER H 7 SHEET 3 AA1 4 GLN H 79 MET H 84 -1 O MET H 84 N LEU H 18 SHEET 4 AA1 4 LEU H 69 ASP H 74 -1 N SER H 72 O VAL H 81 SHEET 1 AA2 6 LEU H 11 VAL H 12 0 SHEET 2 AA2 6 THR H 118 VAL H 122 1 O THR H 121 N VAL H 12 SHEET 3 AA2 6 ALA H 93 ARG H 100 -1 N TYR H 95 O THR H 118 SHEET 4 AA2 6 GLY H 35 GLN H 41 -1 N ILE H 39 O TYR H 96 SHEET 5 AA2 6 GLU H 48 TRP H 54 -1 O LEU H 50 N TRP H 38 SHEET 6 AA2 6 TYR H 60 TYR H 61 -1 O TYR H 60 N HIS H 52 SHEET 1 AA3 4 LEU H 11 VAL H 12 0 SHEET 2 AA3 4 THR H 118 VAL H 122 1 O THR H 121 N VAL H 12 SHEET 3 AA3 4 ALA H 93 ARG H 100 -1 N TYR H 95 O THR H 118 SHEET 4 AA3 4 MET H 111 TRP H 114 -1 O TYR H 113 N ARG H 99 SHEET 1 AA4 4 SER H 131 LEU H 135 0 SHEET 2 AA4 4 LEU H 149 TYR H 156 -1 O LEU H 152 N PHE H 133 SHEET 3 AA4 4 TYR H 187 VAL H 193 -1 O LEU H 189 N VAL H 153 SHEET 4 AA4 4 VAL H 174 THR H 176 -1 N HIS H 175 O VAL H 192 SHEET 1 AA5 4 SER H 131 LEU H 135 0 SHEET 2 AA5 4 LEU H 149 TYR H 156 -1 O LEU H 152 N PHE H 133 SHEET 3 AA5 4 TYR H 187 VAL H 193 -1 O LEU H 189 N VAL H 153 SHEET 4 AA5 4 VAL H 180 LEU H 181 -1 N VAL H 180 O SER H 188 SHEET 1 AA6 3 THR H 162 TRP H 165 0 SHEET 2 AA6 3 ILE H 206 HIS H 211 -1 O ASN H 208 N SER H 164 SHEET 3 AA6 3 THR H 216 LYS H 221 -1 O THR H 216 N HIS H 211 SHEET 1 AA7 4 MET L 4 SER L 7 0 SHEET 2 AA7 4 VAL L 19 ALA L 25 -1 O LYS L 24 N THR L 5 SHEET 3 AA7 4 ASP L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AA7 4 PHE L 62 SER L 67 -1 N SER L 65 O THR L 72 SHEET 1 AA8 6 SER L 10 ALA 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 ALA L 84 GLN L 90 -1 N ALA L 84 O LEU L 104 SHEET 4 AA8 6 LEU L 33 GLN L 38 -1 N THR L 34 O GLN L 89 SHEET 5 AA8 6 LYS L 45 TYR L 49 -1 O LYS L 45 N GLN L 37 SHEET 6 AA8 6 ASN L 53 ARG L 54 -1 O ASN L 53 N TYR 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 LEU L 135 N PHE L 116 SHEET 3 AA9 4 TYR L 173 SER L 182 -1 O LEU L 179 N VAL L 132 SHEET 4 AA9 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178 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 THR L 206 ASN L 210 -1 O LYS L 207 N CYS L 194 SSBOND 1 CYS H 22 CYS H 97 1555 1555 2.04 SSBOND 2 CYS H 151 CYS H 207 1555 1555 2.04 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.03 SSBOND 4 CYS L 134 CYS L 194 1555 1555 2.04 SSBOND 5 CYS A 73 CYS A 83 1555 1555 2.03 LINK OE2 GLU A 106 MG MG A 501 1555 1555 2.08 LINK OE2 GLU A 106 MG MG A 501 1555 4557 2.29 CISPEP 1 PHE H 157 PRO H 158 0 -2.26 CISPEP 2 GLU H 159 PRO H 160 0 3.03 CISPEP 3 SER L 7 PRO L 8 0 -0.27 CISPEP 4 SER L 94 PRO L 95 0 0.16 CISPEP 5 TYR L 140 PRO L 141 0 1.96 CRYST1 126.621 151.875 76.053 90.00 90.00 90.00 C 2 2 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 0.007898 0.000000 0.000000 0.00000 SCALE2 0.000000 0.006584 0.000000 0.00000 SCALE3 0.000000 0.000000 0.013149 0.00000