HEADER IMMUNE SYSTEM 07-DEC-23 8RDA TITLE CRYSTAL STRUCTURE OF HAEMOPHILUS INFLUENZAE TYPE B (HIB) DP2 TITLE 2 OLIGOSACCHARIDE BOUND TO FAB CA4 COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB CA4 H CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: FAB CA4 L CHAIN; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES 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 ANTIGEN, ANTIBODY, CARBOHYDRATE, HAEMOPHILUS INFLUENZAE TYPE B, HIB, KEYWDS 2 IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR F.NONNE,L.DELLO IACONO JRNL AUTH F.NONNE,L.D.IACONO,S.BERTUZZI,L.UNIONE,D.PROIETTI,N.NORAIS, JRNL AUTH 2 I.MARGARIT,R.ADAMO,J.JIMENEZ-BARBERO,F.CARBONI,M.R.ROMANO JRNL TITL A MULTIDISCIPLINARY STRUCTURAL APPROACH TO THE JRNL TITL 2 IDENTIFICATION OF THE HAEMOPHILUS INFLUENZAE TYPE B CAPSULAR JRNL TITL 3 POLYSACCHARIDE PROTECTIVE EPITOPE JRNL REF ACS CENT.SCI. 2024 JRNL REFN ESSN 2374-7951 JRNL DOI 10.1021/ACSCENTSCI.3C01515 REMARK 2 REMARK 2 RESOLUTION. 2.29 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.15.2_3472 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) : 2.29 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 51.50 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 3 NUMBER OF REFLECTIONS : 26531 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.228 REMARK 3 R VALUE (WORKING SET) : 0.226 REMARK 3 FREE R VALUE : 0.270 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.870 REMARK 3 FREE R VALUE TEST SET COUNT : 1293 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 51.5000 - 4.7600 1.00 2955 163 0.1909 0.2288 REMARK 3 2 4.7600 - 3.7800 1.00 2848 139 0.1822 0.2202 REMARK 3 3 3.7800 - 3.3000 1.00 2798 158 0.2147 0.2754 REMARK 3 4 3.3000 - 3.0000 1.00 2802 156 0.2408 0.2888 REMARK 3 5 3.0000 - 2.7800 1.00 2796 128 0.2587 0.2888 REMARK 3 6 2.7800 - 2.6200 1.00 2778 146 0.2675 0.3282 REMARK 3 7 2.6200 - 2.4900 1.00 2799 131 0.2823 0.3320 REMARK 3 8 2.4900 - 2.3800 1.00 2797 125 0.3153 0.3733 REMARK 3 9 2.3800 - 2.2900 0.96 2665 147 0.3540 0.3800 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) : 0.354 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.027 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 39.22 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.09 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 3433 REMARK 3 ANGLE : 0.619 4684 REMARK 3 CHIRALITY : 0.046 541 REMARK 3 PLANARITY : 0.004 592 REMARK 3 DIHEDRAL : 9.099 2091 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 9 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 83 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.5756 14.5420 -24.4598 REMARK 3 T TENSOR REMARK 3 T11: 0.4548 T22: 0.3004 REMARK 3 T33: 0.2926 T12: -0.0329 REMARK 3 T13: 0.0231 T23: -0.0005 REMARK 3 L TENSOR REMARK 3 L11: 1.2994 L22: 0.3735 REMARK 3 L33: 1.0552 L12: 0.2576 REMARK 3 L13: -0.4482 L23: -0.6240 REMARK 3 S TENSOR REMARK 3 S11: 0.0167 S12: -0.0037 S13: -0.0099 REMARK 3 S21: -0.2463 S22: -0.0650 S23: 0.0174 REMARK 3 S31: -0.1181 S32: -0.0636 S33: 0.0000 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 84 THROUGH 119 ) REMARK 3 ORIGIN FOR THE GROUP (A): -5.3569 15.2596 -19.3193 REMARK 3 T TENSOR REMARK 3 T11: 0.4800 T22: 0.3392 REMARK 3 T33: 0.3412 T12: 0.0075 REMARK 3 T13: 0.0457 T23: -0.0359 REMARK 3 L TENSOR REMARK 3 L11: 0.2290 L22: 0.2260 REMARK 3 L33: 0.5423 L12: -0.0352 REMARK 3 L13: 0.0713 L23: -0.3581 REMARK 3 S TENSOR REMARK 3 S11: 0.0481 S12: -0.0856 S13: 0.0480 REMARK 3 S21: 0.2635 S22: -0.0895 S23: 0.0186 REMARK 3 S31: -0.2509 S32: 0.0429 S33: -0.0003 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 120 THROUGH 144 ) REMARK 3 ORIGIN FOR THE GROUP (A): 11.5821 15.8154 7.7008 REMARK 3 T TENSOR REMARK 3 T11: 0.3737 T22: 0.5197 REMARK 3 T33: 0.4612 T12: -0.0465 REMARK 3 T13: 0.0110 T23: 0.0417 REMARK 3 L TENSOR REMARK 3 L11: 0.1352 L22: 0.6520 REMARK 3 L33: 0.3619 L12: -0.1295 REMARK 3 L13: 0.0735 L23: 0.3531 REMARK 3 S TENSOR REMARK 3 S11: 0.0009 S12: -0.1037 S13: 0.0391 REMARK 3 S21: 0.4394 S22: 0.0437 S23: 0.1212 REMARK 3 S31: -0.6306 S32: 0.2436 S33: 0.0000 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 145 THROUGH 200 ) REMARK 3 ORIGIN FOR THE GROUP (A): 6.8736 11.4054 8.0531 REMARK 3 T TENSOR REMARK 3 T11: 0.4083 T22: 0.3547 REMARK 3 T33: 0.4066 T12: -0.0064 REMARK 3 T13: -0.0176 T23: 0.0316 REMARK 3 L TENSOR REMARK 3 L11: 0.7842 L22: 0.0238 REMARK 3 L33: 0.2970 L12: 0.1232 REMARK 3 L13: 0.1099 L23: 0.0668 REMARK 3 S TENSOR REMARK 3 S11: -0.0845 S12: 0.0517 S13: -0.0729 REMARK 3 S21: -0.1847 S22: 0.0156 S23: -0.0439 REMARK 3 S31: 0.0985 S32: 0.0458 S33: 0.0000 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 201 THROUGH 224 ) REMARK 3 ORIGIN FOR THE GROUP (A): 14.3872 5.7407 7.1526 REMARK 3 T TENSOR REMARK 3 T11: 0.4327 T22: 0.5593 REMARK 3 T33: 0.5446 T12: 0.0018 REMARK 3 T13: -0.0120 T23: -0.0035 REMARK 3 L TENSOR REMARK 3 L11: 0.1193 L22: 0.1376 REMARK 3 L33: 0.1327 L12: -0.1209 REMARK 3 L13: -0.1231 L23: 0.1011 REMARK 3 S TENSOR REMARK 3 S11: 0.0055 S12: 0.1813 S13: -0.1951 REMARK 3 S21: -0.0635 S22: -0.0131 S23: -0.2942 REMARK 3 S31: 0.4085 S32: 0.3157 S33: 0.0004 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 2 THROUGH 91 ) REMARK 3 ORIGIN FOR THE GROUP (A): -21.4590 13.7722 -9.1405 REMARK 3 T TENSOR REMARK 3 T11: 0.3384 T22: 0.3760 REMARK 3 T33: 0.4227 T12: 0.0086 REMARK 3 T13: -0.0253 T23: -0.0044 REMARK 3 L TENSOR REMARK 3 L11: 0.9537 L22: 0.4865 REMARK 3 L33: 1.1094 L12: 0.0984 REMARK 3 L13: -0.4853 L23: 0.4431 REMARK 3 S TENSOR REMARK 3 S11: 0.0913 S12: -0.1329 S13: -0.1057 REMARK 3 S21: -0.0183 S22: -0.1044 S23: 0.1081 REMARK 3 S31: 0.0534 S32: -0.1211 S33: 0.0000 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 92 THROUGH 103 ) REMARK 3 ORIGIN FOR THE GROUP (A): -16.0841 22.0216 -19.4182 REMARK 3 T TENSOR REMARK 3 T11: 0.5055 T22: 0.3534 REMARK 3 T33: 0.3675 T12: 0.1167 REMARK 3 T13: -0.0601 T23: 0.0061 REMARK 3 L TENSOR REMARK 3 L11: 0.9161 L22: 0.4089 REMARK 3 L33: 1.6151 L12: 0.3142 REMARK 3 L13: -1.1343 L23: -0.1329 REMARK 3 S TENSOR REMARK 3 S11: 0.4267 S12: 0.0691 S13: 0.1129 REMARK 3 S21: -0.3748 S22: -0.2915 S23: -0.2305 REMARK 3 S31: -0.3759 S32: 0.2922 S33: 0.1404 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 104 THROUGH 130 ) REMARK 3 ORIGIN FOR THE GROUP (A): 0.3084 15.5964 14.6037 REMARK 3 T TENSOR REMARK 3 T11: 0.3266 T22: 0.4183 REMARK 3 T33: 0.4178 T12: -0.0190 REMARK 3 T13: -0.0158 T23: -0.0284 REMARK 3 L TENSOR REMARK 3 L11: 0.1059 L22: 0.0183 REMARK 3 L33: 0.7406 L12: -0.0098 REMARK 3 L13: 0.2473 L23: -0.1211 REMARK 3 S TENSOR REMARK 3 S11: 0.0883 S12: -0.1060 S13: -0.1456 REMARK 3 S21: 0.0915 S22: -0.0523 S23: -0.0836 REMARK 3 S31: -0.0964 S32: 0.0194 S33: 0.0001 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 131 THROUGH 216 ) REMARK 3 ORIGIN FOR THE GROUP (A): 1.1472 21.2234 18.7716 REMARK 3 T TENSOR REMARK 3 T11: 0.3866 T22: 0.3867 REMARK 3 T33: 0.3651 T12: -0.0886 REMARK 3 T13: 0.0250 T23: 0.0024 REMARK 3 L TENSOR REMARK 3 L11: 0.8747 L22: 0.6951 REMARK 3 L33: 0.8551 L12: -0.7130 REMARK 3 L13: 0.4237 L23: -0.5679 REMARK 3 S TENSOR REMARK 3 S11: 0.0643 S12: -0.0174 S13: 0.1410 REMARK 3 S21: 0.3462 S22: -0.0877 S23: 0.0523 REMARK 3 S31: -0.2911 S32: -0.0567 S33: 0.0010 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 8RDA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE. REMARK 100 THE DEPOSITION ID IS D_1292135209. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 19-SEP-19 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I03 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.976 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DIALS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26582 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.290 REMARK 200 RESOLUTION RANGE LOW (A) : 51.500 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 200 DATA REDUNDANCY : 7.800 REMARK 200 R MERGE (I) : 0.16200 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 7.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.29 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.33 REMARK 200 COMPLETENESS FOR SHELL (%) : 93.4 REMARK 200 DATA REDUNDANCY IN SHELL : 4.60 REMARK 200 R MERGE FOR SHELL (I) : 1.16400 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.100 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 (%): 59.45 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.03 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.01M ZINC SULFATE HEPTAHYDRATE, 0.1M REMARK 280 MES PH 6.5, 25% W/V PEG 500 MME, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 293K 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 72.54800 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 72.54800 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 30.33250 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 65.79400 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 30.33250 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 65.79400 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 72.54800 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 30.33250 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 65.79400 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 72.54800 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 30.33250 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 65.79400 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3710 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19390 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 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 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 HOH H 452 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 LYS H 139 REMARK 465 SER H 140 REMARK 465 SER H 225 REMARK 465 CYS H 226 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 224 CG CD CE NZ REMARK 470 LYS L 171 CG CD CE NZ REMARK 470 GLU L 189 CG CD OE1 OE2 REMARK 470 LYS L 190 CG CD CE NZ REMARK 470 GLU L 215 CG CD OE1 OE2 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 LYS H 43 -169.71 -114.33 REMARK 500 VAL H 48 -62.72 -98.22 REMARK 500 THR H 108 -110.79 -132.66 REMARK 500 SER H 137 -151.40 -101.92 REMARK 500 ASP H 154 79.74 60.30 REMARK 500 THR L 52 -47.58 68.63 REMARK 500 ALA L 69 -99.24 57.87 REMARK 500 TYR L 92 23.95 -141.87 REMARK 500 PRO L 97 95.94 -50.77 REMARK 500 LYS L 171 -61.84 -90.07 REMARK 500 GLU L 215 -95.55 -116.62 REMARK 500 REMARK 500 REMARK: NULL DBREF 8RDA H 1 226 PDB 8RDA 8RDA 1 226 DBREF 8RDA L 1 216 PDB 8RDA 8RDA 1 216 SEQRES 1 H 226 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL THR SEQRES 2 H 226 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 226 PHE THR PHE ASN THR TYR SER MET ASN TRP VAL ARG GLN SEQRES 4 H 226 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER SER ILE SER SEQRES 5 H 226 ARG SER SER ASP TYR ILE TYR TYR ALA ASP SER VAL LYS SEQRES 6 H 226 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SER SEQRES 7 H 226 VAL TYR LEU GLN MET THR SER LEU ARG ASP GLU ASP THR SEQRES 8 H 226 ALA VAL TYR TYR CYS ALA ARG ASP PRO GLY GLY MET PRO SEQRES 9 H 226 THR THR VAL THR THR TRP LEU TYR TRP GLY GLN GLY THR SEQRES 10 H 226 LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER SEQRES 11 H 226 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY SEQRES 12 H 226 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE SEQRES 13 H 226 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU SEQRES 14 H 226 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SEQRES 15 H 226 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SEQRES 16 H 226 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL SEQRES 17 H 226 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL SEQRES 18 H 226 GLU PRO LYS SER CYS SEQRES 1 L 216 GLU ILE VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 L 216 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 L 216 GLN SER VAL THR SER ASN TYR LEU ALA TRP TYR GLN GLN SEQRES 4 L 216 LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR ASP THR SEQRES 5 L 216 SER ARG ARG ALA THR GLY ILE PRO ASP ARG PHE SER GLY SEQRES 6 L 216 SER GLY SER ALA THR ASP PHE THR LEU THR ILE SER ARG SEQRES 7 L 216 LEU GLU PRO ASP ASP PHE ALA ILE TYR TYR CYS GLN GLN SEQRES 8 L 216 TYR GLY SER SER PRO PRO VAL THR PHE GLY HIS GLY THR SEQRES 9 L 216 LYS VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL SEQRES 10 L 216 PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY SEQRES 11 L 216 THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO SEQRES 12 L 216 ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU SEQRES 13 L 216 GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SEQRES 14 L 216 SER LYS ASP SER THR TYR SER LEU SER SER THR LEU THR SEQRES 15 L 216 LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA SEQRES 16 L 216 CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR SEQRES 17 L 216 LYS SER PHE ASN ARG GLY GLU CYS HET H1A H 301 45 HET ZN L 301 1 HET EDO L 302 4 HETNAM ZN ZINC ION HETNAM EDO 1,2-ETHANEDIOL HETSYN EDO ETHYLENE GLYCOL FORMUL 3 H1A FORMUL 4 ZN ZN 2+ FORMUL 5 EDO C2 H6 O2 FORMUL 6 HOH *114(H2 O) HELIX 1 AA1 THR H 28 TYR H 32 5 5 HELIX 2 AA2 ARG H 87 THR H 91 5 5 HELIX 3 AA3 SER H 166 ALA H 168 5 3 HELIX 4 AA4 SER H 197 THR H 201 5 5 HELIX 5 AA5 LYS H 211 ASN H 214 5 4 HELIX 6 AA6 VAL L 29 ASN L 32 5 4 HELIX 7 AA7 GLU L 80 PHE L 84 5 5 HELIX 8 AA8 SER L 123 LYS L 128 1 6 HELIX 9 AA9 LYS L 185 GLU L 189 1 5 SHEET 1 AA1 4 GLN H 3 SER H 7 0 SHEET 2 AA1 4 LEU H 18 SER H 25 -1 O SER H 21 N SER H 7 SHEET 3 AA1 4 SER H 78 MET H 83 -1 O MET H 83 N LEU H 18 SHEET 4 AA1 4 PHE H 68 ASP H 73 -1 N SER H 71 O TYR H 80 SHEET 1 AA2 6 LEU H 11 VAL H 12 0 SHEET 2 AA2 6 THR H 117 VAL H 121 1 O THR H 120 N VAL H 12 SHEET 3 AA2 6 ALA H 92 ARG H 98 -1 N TYR H 94 O THR H 117 SHEET 4 AA2 6 MET H 34 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AA2 6 LEU H 45 ILE H 51 -1 O SER H 49 N TRP H 36 SHEET 6 AA2 6 ILE H 58 TYR H 60 -1 O TYR H 59 N SER H 50 SHEET 1 AA3 4 LEU H 11 VAL H 12 0 SHEET 2 AA3 4 THR H 117 VAL H 121 1 O THR H 120 N VAL H 12 SHEET 3 AA3 4 ALA H 92 ARG H 98 -1 N TYR H 94 O THR H 117 SHEET 4 AA3 4 TYR H 112 TRP H 113 -1 O TYR H 112 N ARG H 98 SHEET 1 AA4 4 SER H 130 LEU H 134 0 SHEET 2 AA4 4 THR H 145 TYR H 155 -1 O LEU H 151 N PHE H 132 SHEET 3 AA4 4 TYR H 186 PRO H 195 -1 O VAL H 194 N ALA H 146 SHEET 4 AA4 4 VAL H 173 THR H 175 -1 N HIS H 174 O VAL H 191 SHEET 1 AA5 4 SER H 130 LEU H 134 0 SHEET 2 AA5 4 THR H 145 TYR H 155 -1 O LEU H 151 N PHE H 132 SHEET 3 AA5 4 TYR H 186 PRO H 195 -1 O VAL H 194 N ALA H 146 SHEET 4 AA5 4 VAL H 179 LEU H 180 -1 N VAL H 179 O SER H 187 SHEET 1 AA6 3 THR H 161 TRP H 164 0 SHEET 2 AA6 3 TYR H 204 HIS H 210 -1 O ASN H 207 N SER H 163 SHEET 3 AA6 3 THR H 215 VAL H 221 -1 O VAL H 217 N VAL H 208 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 ASP L 71 ILE L 76 -1 O LEU L 74 N LEU L 21 SHEET 4 AA7 4 PHE L 63 SER L 68 -1 N SER L 64 O THR L 75 SHEET 1 AA8 6 THR L 10 LEU L 13 0 SHEET 2 AA8 6 THR L 104 ILE L 108 1 O GLU L 107 N LEU L 11 SHEET 3 AA8 6 ALA L 85 GLN L 91 -1 N ALA L 85 O VAL L 106 SHEET 4 AA8 6 LEU L 34 GLN L 39 -1 N ALA L 35 O GLN L 90 SHEET 5 AA8 6 ARG L 46 TYR L 50 -1 O ARG L 46 N GLN L 38 SHEET 6 AA8 6 ARG L 54 ARG L 55 -1 O ARG L 54 N TYR L 50 SHEET 1 AA9 4 THR L 10 LEU L 13 0 SHEET 2 AA9 4 THR L 104 ILE L 108 1 O GLU L 107 N LEU L 11 SHEET 3 AA9 4 ALA L 85 GLN L 91 -1 N ALA L 85 O VAL L 106 SHEET 4 AA9 4 THR L 99 PHE L 100 -1 O THR L 99 N GLN L 91 SHEET 1 AB1 4 SER L 116 PHE L 120 0 SHEET 2 AB1 4 THR L 131 PHE L 141 -1 O VAL L 135 N PHE L 120 SHEET 3 AB1 4 TYR L 175 SER L 184 -1 O LEU L 177 N LEU L 138 SHEET 4 AB1 4 SER L 161 VAL L 165 -1 N SER L 164 O SER L 178 SHEET 1 AB2 4 ALA L 155 LEU L 156 0 SHEET 2 AB2 4 LYS L 147 VAL L 152 -1 N VAL L 152 O ALA L 155 SHEET 3 AB2 4 VAL L 193 THR L 199 -1 O GLU L 197 N GLN L 149 SHEET 4 AB2 4 VAL L 207 ASN L 212 -1 O LYS L 209 N CYS L 196 SSBOND 1 CYS H 22 CYS H 96 1555 1555 2.03 SSBOND 2 CYS H 150 CYS H 206 1555 1555 2.05 SSBOND 3 CYS L 23 CYS L 89 1555 1555 2.04 SSBOND 4 CYS L 136 CYS L 196 1555 1555 2.03 CISPEP 1 PHE H 156 PRO H 157 0 -2.05 CISPEP 2 GLU H 158 PRO H 159 0 -1.60 CISPEP 3 SER L 7 PRO L 8 0 -2.47 CISPEP 4 TYR L 142 PRO L 143 0 4.68 CRYST1 60.665 131.588 145.096 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 0.016484 0.000000 0.000000 0.00000 SCALE2 0.000000 0.007599 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006892 0.00000