HEADER PROTEIN BINDING/IMMUNE SYSTEM 05-MAR-24 8YKT TITLE FAB AND SEB COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: ENTEROTOXIN TYPE B; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: SEB; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: FAB HEAVY CHAIN; COMPND 8 CHAIN: H; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: FAB LIGHT CHAIN; COMPND 12 CHAIN: L; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS; SOURCE 3 ORGANISM_TAXID: 1280; SOURCE 4 GENE: ENTB; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_COMMON: HUMAN; SOURCE 10 ORGANISM_TAXID: 9606; SOURCE 11 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 12 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 14 MOL_ID: 3; SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 16 ORGANISM_COMMON: HUMAN; SOURCE 17 ORGANISM_TAXID: 9606; SOURCE 18 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 19 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 20 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS FAB, SEB, COMPLEX, PROTEIN BINDING/IMMUNE SYSTEM, PROTEIN BINDING- KEYWDS 2 IMMUNE SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR H.ZENG,H.Y.FAN REVDAT 1 12-MAR-25 8YKT 0 JRNL AUTH H.Y.FAN,H.ZENG JRNL TITL STRUCTURE OF STAPHYLOCOCCAL ENTEROTOXIN B MUTANT IN COMPLEX JRNL TITL 2 WITH A NEUTRALIZATION ANTIBODY FAB FRAGMENT JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.04 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) : 2.04 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.06 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 55943 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.197 REMARK 3 R VALUE (WORKING SET) : 0.195 REMARK 3 FREE R VALUE : 0.230 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.140 REMARK 3 FREE R VALUE TEST SET COUNT : 2878 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 38.0600 - 5.6200 0.99 2578 153 0.1820 0.2171 REMARK 3 2 5.6200 - 4.4700 1.00 2562 141 0.1479 0.1622 REMARK 3 3 4.4600 - 3.9000 1.00 2527 152 0.1409 0.1757 REMARK 3 4 3.9000 - 3.5400 1.00 2572 102 0.1681 0.2121 REMARK 3 5 3.5400 - 3.2900 1.00 2531 148 0.1767 0.2065 REMARK 3 6 3.2900 - 3.1000 1.00 2526 128 0.2020 0.2733 REMARK 3 7 3.1000 - 2.9400 1.00 2509 141 0.2078 0.2471 REMARK 3 8 2.9400 - 2.8100 1.00 2517 153 0.2129 0.2344 REMARK 3 9 2.8100 - 2.7100 1.00 2517 134 0.2166 0.2651 REMARK 3 10 2.7100 - 2.6100 1.00 2556 134 0.2239 0.2398 REMARK 3 11 2.6100 - 2.5300 1.00 2548 115 0.2364 0.2545 REMARK 3 12 2.5300 - 2.4600 1.00 2512 144 0.2322 0.3098 REMARK 3 13 2.4600 - 2.3900 1.00 2474 151 0.2433 0.2935 REMARK 3 14 2.3900 - 2.3400 1.00 2517 156 0.2533 0.2554 REMARK 3 15 2.3400 - 2.2800 1.00 2520 152 0.2492 0.3072 REMARK 3 16 2.2800 - 2.2300 1.00 2499 131 0.2494 0.2562 REMARK 3 17 2.2300 - 2.1900 1.00 2537 132 0.2614 0.3017 REMARK 3 18 2.1900 - 2.1500 1.00 2482 127 0.2633 0.3335 REMARK 3 19 2.1500 - 2.1100 1.00 2583 105 0.2746 0.3324 REMARK 3 20 2.1100 - 2.0700 1.00 2495 135 0.2915 0.2868 REMARK 3 21 2.0700 - 2.0400 1.00 2503 144 0.3090 0.3297 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) : 0.250 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.380 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 : 0.002 5287 REMARK 3 ANGLE : 0.572 7185 REMARK 3 CHIRALITY : 0.045 790 REMARK 3 PLANARITY : 0.004 924 REMARK 3 DIHEDRAL : 5.487 720 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 9 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 3 THROUGH 48 ) REMARK 3 ORIGIN FOR THE GROUP (A): 21.9891 0.1585 9.2517 REMARK 3 T TENSOR REMARK 3 T11: 0.4410 T22: 0.4378 REMARK 3 T33: 0.4355 T12: 0.1046 REMARK 3 T13: -0.1048 T23: -0.0418 REMARK 3 L TENSOR REMARK 3 L11: 1.5673 L22: 2.8131 REMARK 3 L33: 1.7638 L12: 0.5804 REMARK 3 L13: 0.8777 L23: 0.9961 REMARK 3 S TENSOR REMARK 3 S11: -0.1659 S12: -0.0585 S13: 0.3260 REMARK 3 S21: -0.1750 S22: -0.1435 S23: 0.6834 REMARK 3 S31: -0.3285 S32: -0.4014 S33: 0.2683 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 49 THROUGH 63 ) REMARK 3 ORIGIN FOR THE GROUP (A): 9.8634 -12.9884 6.9822 REMARK 3 T TENSOR REMARK 3 T11: 0.7842 T22: 0.9661 REMARK 3 T33: 1.0510 T12: -0.0216 REMARK 3 T13: -0.2231 T23: -0.0116 REMARK 3 L TENSOR REMARK 3 L11: 1.4847 L22: 2.1905 REMARK 3 L33: 0.6299 L12: 0.6345 REMARK 3 L13: 0.2145 L23: 0.8347 REMARK 3 S TENSOR REMARK 3 S11: 0.1540 S12: -1.1744 S13: -0.2135 REMARK 3 S21: 1.2452 S22: -0.5233 S23: 0.0923 REMARK 3 S31: -0.4546 S32: -0.9208 S33: 0.3232 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 64 THROUGH 130 ) REMARK 3 ORIGIN FOR THE GROUP (A): 17.0176 -8.3814 -0.0985 REMARK 3 T TENSOR REMARK 3 T11: 0.6126 T22: 0.4674 REMARK 3 T33: 0.5051 T12: 0.0786 REMARK 3 T13: -0.1829 T23: -0.0797 REMARK 3 L TENSOR REMARK 3 L11: 4.2006 L22: 5.4698 REMARK 3 L33: 4.6083 L12: 0.4997 REMARK 3 L13: 1.3740 L23: 0.0297 REMARK 3 S TENSOR REMARK 3 S11: -0.0091 S12: -0.0681 S13: 0.3084 REMARK 3 S21: -0.3818 S22: -0.1851 S23: 0.8614 REMARK 3 S31: -0.5738 S32: -0.5473 S33: 0.2195 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 131 THROUGH 238 ) REMARK 3 ORIGIN FOR THE GROUP (A): 31.9936 -3.2277 11.1794 REMARK 3 T TENSOR REMARK 3 T11: 0.3179 T22: 0.2950 REMARK 3 T33: 0.2047 T12: 0.0170 REMARK 3 T13: -0.0272 T23: -0.0070 REMARK 3 L TENSOR REMARK 3 L11: 3.3002 L22: 4.0733 REMARK 3 L33: 3.0133 L12: 0.3072 REMARK 3 L13: 1.5994 L23: 0.6271 REMARK 3 S TENSOR REMARK 3 S11: -0.0599 S12: 0.0480 S13: 0.1113 REMARK 3 S21: -0.1845 S22: -0.0889 S23: 0.1257 REMARK 3 S31: -0.2916 S32: -0.1196 S33: 0.0947 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 2 THROUGH 99 ) REMARK 3 ORIGIN FOR THE GROUP (A): 50.4809 -26.8771 27.7163 REMARK 3 T TENSOR REMARK 3 T11: 0.2949 T22: 0.2818 REMARK 3 T33: 0.2729 T12: 0.0290 REMARK 3 T13: 0.0181 T23: -0.0429 REMARK 3 L TENSOR REMARK 3 L11: 2.6647 L22: 2.3983 REMARK 3 L33: 3.1546 L12: -0.8156 REMARK 3 L13: 1.2461 L23: -0.3917 REMARK 3 S TENSOR REMARK 3 S11: 0.1002 S12: 0.1195 S13: -0.2923 REMARK 3 S21: -0.1202 S22: 0.0429 S23: 0.0936 REMARK 3 S31: 0.2765 S32: 0.1218 S33: -0.1074 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 100 THROUGH 146 ) REMARK 3 ORIGIN FOR THE GROUP (A): 61.0867 -21.3350 40.3963 REMARK 3 T TENSOR REMARK 3 T11: 0.3066 T22: 0.2591 REMARK 3 T33: 0.2478 T12: 0.0024 REMARK 3 T13: 0.0195 T23: -0.0368 REMARK 3 L TENSOR REMARK 3 L11: 3.1805 L22: 0.9798 REMARK 3 L33: 2.7159 L12: -1.4842 REMARK 3 L13: 2.5475 L23: -1.4550 REMARK 3 S TENSOR REMARK 3 S11: -0.1552 S12: 0.0721 S13: 0.1082 REMARK 3 S21: -0.0097 S22: 0.0324 S23: -0.1308 REMARK 3 S31: -0.1367 S32: 0.1423 S33: -0.0332 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 147 THROUGH 227 ) REMARK 3 ORIGIN FOR THE GROUP (A): 75.4468 -26.8749 60.4817 REMARK 3 T TENSOR REMARK 3 T11: 0.1900 T22: 0.2266 REMARK 3 T33: 0.3060 T12: 0.0126 REMARK 3 T13: 0.0168 T23: 0.0013 REMARK 3 L TENSOR REMARK 3 L11: 1.8491 L22: 4.6142 REMARK 3 L33: 4.4040 L12: -0.8285 REMARK 3 L13: 0.2233 L23: -0.3223 REMARK 3 S TENSOR REMARK 3 S11: -0.0307 S12: -0.0582 S13: -0.0913 REMARK 3 S21: 0.1021 S22: -0.0167 S23: 0.1877 REMARK 3 S31: -0.1944 S32: 0.0822 S33: 0.0343 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 2 THROUGH 111 ) REMARK 3 ORIGIN FOR THE GROUP (A): 51.5469 -4.9818 35.1524 REMARK 3 T TENSOR REMARK 3 T11: 0.2263 T22: 0.2300 REMARK 3 T33: 0.2386 T12: -0.0218 REMARK 3 T13: -0.0010 T23: 0.0206 REMARK 3 L TENSOR REMARK 3 L11: 1.5812 L22: 1.8320 REMARK 3 L33: 4.7867 L12: -0.1965 REMARK 3 L13: 0.1727 L23: 1.6569 REMARK 3 S TENSOR REMARK 3 S11: -0.0673 S12: 0.1292 S13: 0.0567 REMARK 3 S21: -0.1253 S22: 0.0197 S23: -0.0099 REMARK 3 S31: -0.2324 S32: 0.1076 S33: 0.0546 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 112 THROUGH 214 ) REMARK 3 ORIGIN FOR THE GROUP (A): 78.6373 -13.9667 49.6283 REMARK 3 T TENSOR REMARK 3 T11: 0.2527 T22: 0.2436 REMARK 3 T33: 0.2851 T12: -0.0115 REMARK 3 T13: 0.0261 T23: 0.0119 REMARK 3 L TENSOR REMARK 3 L11: 3.2558 L22: 3.6858 REMARK 3 L33: 1.5598 L12: -1.7281 REMARK 3 L13: -0.2676 L23: 0.1152 REMARK 3 S TENSOR REMARK 3 S11: 0.0323 S12: 0.1810 S13: -0.0576 REMARK 3 S21: -0.3256 S22: -0.1199 S23: -0.3291 REMARK 3 S31: 0.1053 S32: 0.1167 S33: 0.0816 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 8YKT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 08-MAR-24. REMARK 100 THE DEPOSITION ID IS D_1300045216. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 26-OCT-23 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRF REMARK 200 BEAMLINE : BL02U1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 S 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2 REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55954 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.040 REMARK 200 RESOLUTION RANGE LOW (A) : 38.330 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 6.800 REMARK 200 R MERGE (I) : 0.15500 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 10.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.04 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.09 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : 7.00 REMARK 200 R MERGE FOR SHELL (I) : 1.40500 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 (%): 57.94 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M LITHUM SULFATE, 0.1M SODIUM REMARK 280 ACETATE PH5.5, 10%PEG1000, 10% PEG8000, VAPOR DIFFUSION, SITTING REMARK 280 DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 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+1/2,Y+1/2,Z REMARK 290 4555 -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 53.12500 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.66000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 53.12500 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 36.66000 REMARK 290 SMTRY3 4 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 GLU A 2 REMARK 465 SER A 97 REMARK 465 LYS A 98 REMARK 465 LYS A 99 REMARK 465 THR A 100 REMARK 465 ASN A 101 REMARK 465 ASP A 102 REMARK 465 ILE A 103 REMARK 465 ASN A 104 REMARK 465 SER A 105 REMARK 465 HIS A 106 REMARK 465 GLN A 107 REMARK 465 THR A 108 REMARK 465 ASP A 109 REMARK 465 LYS A 110 REMARK 465 LYS A 239 REMARK 465 LYS A 240 REMARK 465 ASP H 1 REMARK 465 CYS H 228 REMARK 465 ASP H 229 REMARK 465 LYS H 230 REMARK 465 THR H 231 REMARK 465 HIS H 232 REMARK 465 ASP L 1 REMARK 465 GLU L 215 REMARK 465 CYS L 216 REMARK 465 SER L 217 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O HOH H 443 O HOH H 451 1.82 REMARK 500 O HOH L 448 O HOH L 451 1.95 REMARK 500 OD1 ASP A 225 O HOH A 301 2.00 REMARK 500 O HOH H 345 O HOH H 388 2.03 REMARK 500 O HOH L 415 O HOH L 440 2.04 REMARK 500 O HOH H 368 O HOH H 403 2.06 REMARK 500 O HOH L 485 O HOH L 486 2.07 REMARK 500 O HOH H 425 O HOH H 448 2.09 REMARK 500 O HOH H 414 O HOH L 440 2.10 REMARK 500 N GLY H 116 O HOH H 301 2.11 REMARK 500 O HOH L 420 O HOH L 456 2.12 REMARK 500 OD1 ASN A 143 ND2 ASN L 33 2.12 REMARK 500 ND2 ASN L 26 O HOH L 301 2.16 REMARK 500 O LEU A 127 O HOH A 302 2.17 REMARK 500 OD1 ASN L 26 O HOH L 302 2.17 REMARK 500 O HOH A 304 O HOH A 317 2.18 REMARK 500 O HOH H 409 O HOH H 436 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH L 405 O HOH L 443 2656 2.04 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 TYR A 92 -70.68 -57.16 REMARK 500 GLN A 93 129.90 -173.10 REMARK 500 CYS A 94 -55.06 -122.08 REMARK 500 ALA A 95 -48.97 149.43 REMARK 500 ASP H 156 64.31 62.09 REMARK 500 THR L 53 -19.37 71.94 REMARK 500 LYS L 54 -11.90 -143.73 REMARK 500 ASP L 156 -101.29 55.85 REMARK 500 ASN L 175 -2.75 70.36 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH L 485 DISTANCE = 6.75 ANGSTROMS REMARK 525 HOH L 486 DISTANCE = 8.44 ANGSTROMS DBREF 8YKT A 2 240 UNP P01552 ETXB_STAAU 28 266 DBREF 8YKT H 1 232 PDB 8YKT 8YKT 1 232 DBREF 8YKT L 1 217 PDB 8YKT 8YKT 1 217 SEQADV 8YKT ARG A 46 UNP P01552 LEU 72 CONFLICT SEQADV 8YKT ALA A 90 UNP P01552 TYR 116 CONFLICT SEQADV 8YKT ALA A 95 UNP P01552 TYR 121 CONFLICT SEQRES 1 A 239 GLU SER GLN PRO ASP PRO LYS PRO ASP GLU LEU HIS LYS SEQRES 2 A 239 SER SER LYS PHE THR GLY LEU MET GLU ASN MET LYS VAL SEQRES 3 A 239 LEU TYR ASP ASP ASN HIS VAL SER ALA ILE ASN VAL LYS SEQRES 4 A 239 SER ILE ASP GLN PHE ARG TYR PHE ASP LEU ILE TYR SER SEQRES 5 A 239 ILE LYS ASP THR LYS LEU GLY ASN TYR ASP ASN VAL ARG SEQRES 6 A 239 VAL GLU PHE LYS ASN LYS ASP LEU ALA ASP LYS TYR LYS SEQRES 7 A 239 ASP LYS TYR VAL ASP VAL PHE GLY ALA ASN ALA TYR TYR SEQRES 8 A 239 GLN CYS ALA PHE SER LYS LYS THR ASN ASP ILE ASN SER SEQRES 9 A 239 HIS GLN THR ASP LYS ARG LYS THR CYS MET TYR GLY GLY SEQRES 10 A 239 VAL THR GLU HIS ASN GLY ASN GLN LEU ASP LYS TYR ARG SEQRES 11 A 239 SER ILE THR VAL ARG VAL PHE GLU ASP GLY LYS ASN LEU SEQRES 12 A 239 LEU SER PHE ASP VAL GLN THR ASN LYS LYS LYS VAL THR SEQRES 13 A 239 ALA GLN GLU LEU ASP TYR LEU THR ARG HIS TYR LEU VAL SEQRES 14 A 239 LYS ASN LYS LYS LEU TYR GLU PHE ASN ASN SER PRO TYR SEQRES 15 A 239 GLU THR GLY TYR ILE LYS PHE ILE GLU ASN GLU ASN SER SEQRES 16 A 239 PHE TRP TYR ASP MET MET PRO ALA PRO GLY ASP LYS PHE SEQRES 17 A 239 ASP GLN SER LYS TYR LEU MET MET TYR ASN ASP ASN LYS SEQRES 18 A 239 MET VAL ASP SER LYS ASP VAL LYS ILE GLU VAL TYR LEU SEQRES 19 A 239 THR THR LYS LYS LYS SEQRES 1 H 232 ASP GLU VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL SEQRES 2 H 232 GLN PRO GLY LYS SER LEU ARG LEU SER CYS ALA ALA SER SEQRES 3 H 232 GLY PHE THR PHE SER ASN TYR GLY MET HIS TRP VAL ARG SEQRES 4 H 232 GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA VAL ILE SEQRES 5 H 232 SER TYR ASP GLY SER ASP LYS PHE TYR ALA ASP SER VAL SEQRES 6 H 232 LYS GLY ARG PHE THR VAL SER ARG ASP THR SER LYS ASN SEQRES 7 H 232 THR LEU PHE LEU GLN MET ASN SER LEU ILE PRO GLU ASP SEQRES 8 H 232 THR ALA VAL TYR TYR CYS ALA LYS ASP PRO TYR PRO SER SEQRES 9 H 232 GLN ARG ALA PRO TRP ASN TRP VAL ASP PRO ARG GLY GLN SEQRES 10 H 232 GLY THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY SEQRES 11 H 232 PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SEQRES 12 H 232 SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP SEQRES 13 H 232 TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SEQRES 14 H 232 ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 15 H 232 GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR SEQRES 16 H 232 VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS SEQRES 17 H 232 ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS SEQRES 18 H 232 ARG VAL GLU PRO LYS SER CYS ASP LYS THR HIS SEQRES 1 L 217 ASP GLN SER VAL LEU THR GLN PRO PRO SER VAL SER ALA SEQRES 2 L 217 ALA PRO GLY GLN LYS VAL THR ILE SER CYS SER GLY ASN SEQRES 3 L 217 SER SER ASN ILE GLY GLN ASN HIS VAL SER TRP TYR GLN SEQRES 4 L 217 GLN VAL PRO GLY LYS ALA PRO LYS VAL LEU ILE TYR ASP SEQRES 5 L 217 THR LYS GLU ARG PRO SER GLY ILE PRO ASP ARG PHE SER SEQRES 6 L 217 GLY SER ARG SER GLY THR SER VAL THR LEU GLY ILE THR SEQRES 7 L 217 GLY LEU GLN THR GLY ASP GLU ALA ASP TYR TYR CYS GLY SEQRES 8 L 217 THR TRP ASP SER ARG LEU SER ALA VAL VAL PHE GLY GLY SEQRES 9 L 217 GLY THR LYS LEU THR VAL LEU GLY GLN PRO LYS ALA ALA SEQRES 10 L 217 PRO SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU SEQRES 11 L 217 GLN ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP SEQRES 12 L 217 PHE TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SEQRES 13 L 217 SER SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SEQRES 14 L 217 SER LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR SEQRES 15 L 217 LEU SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER SEQRES 16 L 217 TYR SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU SEQRES 17 L 217 LYS THR VAL ALA PRO THR GLU CYS SER FORMUL 4 HOH *419(H2 O) HELIX 1 AA1 LYS A 14 PHE A 18 5 5 HELIX 2 AA2 MET A 22 VAL A 27 1 6 HELIX 3 AA3 LEU A 28 ASP A 30 5 3 HELIX 4 AA4 ASN A 71 LYS A 79 1 9 HELIX 5 AA5 ALA A 158 LYS A 174 1 17 HELIX 6 AA6 ASP A 210 MET A 216 1 7 HELIX 7 AA7 MET A 217 ASN A 219 5 3 HELIX 8 AA8 THR H 29 TYR H 33 5 5 HELIX 9 AA9 ILE H 88 THR H 92 5 5 HELIX 10 AB1 SER H 168 ALA H 170 5 3 HELIX 11 AB2 SER H 199 LEU H 201 5 3 HELIX 12 AB3 LYS H 213 ASN H 216 5 4 HELIX 13 AB4 GLN L 81 GLU L 85 5 5 HELIX 14 AB5 SER L 126 ALA L 132 1 7 HELIX 15 AB6 THR L 186 HIS L 193 1 8 SHEET 1 AA1 3 VAL A 34 VAL A 39 0 SHEET 2 AA1 3 VAL A 83 GLY A 87 -1 O VAL A 83 N VAL A 39 SHEET 3 AA1 3 VAL A 119 GLU A 121 -1 O THR A 120 N ASP A 84 SHEET 1 AA2 3 ASP A 49 TYR A 52 0 SHEET 2 AA2 3 ASN A 64 GLU A 68 -1 O VAL A 67 N LEU A 50 SHEET 3 AA2 3 LYS A 112 TYR A 116 1 O MET A 115 N GLU A 68 SHEET 1 AA3 6 SER A 196 ASP A 200 0 SHEET 2 AA3 6 TYR A 183 ILE A 191 -1 N PHE A 190 O PHE A 197 SHEET 3 AA3 6 LYS A 230 THR A 237 -1 O GLU A 232 N LYS A 189 SHEET 4 AA3 6 GLN A 126 GLU A 139 1 N PHE A 138 O VAL A 233 SHEET 5 AA3 6 LYS A 142 LYS A 153 -1 O PHE A 147 N VAL A 135 SHEET 6 AA3 6 GLN H 105 ARG H 106 -1 O ARG H 106 N SER A 146 SHEET 1 AA4 2 LYS A 155 THR A 157 0 SHEET 2 AA4 2 MET A 223 ASP A 225 -1 O VAL A 224 N VAL A 156 SHEET 1 AA5 4 GLN H 4 SER H 8 0 SHEET 2 AA5 4 LEU H 19 SER H 26 -1 O SER H 22 N SER H 8 SHEET 3 AA5 4 THR H 79 MET H 84 -1 O MET H 84 N LEU H 19 SHEET 4 AA5 4 PHE H 69 ASP H 74 -1 N THR H 70 O GLN H 83 SHEET 1 AA6 6 VAL H 12 VAL H 13 0 SHEET 2 AA6 6 THR H 119 VAL H 123 1 O THR H 122 N VAL H 13 SHEET 3 AA6 6 ALA H 93 LYS H 99 -1 N TYR H 95 O THR H 119 SHEET 4 AA6 6 MET H 35 GLN H 40 -1 N VAL H 38 O TYR H 96 SHEET 5 AA6 6 LEU H 46 ILE H 52 -1 O VAL H 49 N TRP H 37 SHEET 6 AA6 6 LYS H 59 TYR H 61 -1 O PHE H 60 N VAL H 51 SHEET 1 AA7 4 VAL H 12 VAL H 13 0 SHEET 2 AA7 4 THR H 119 VAL H 123 1 O THR H 122 N VAL H 13 SHEET 3 AA7 4 ALA H 93 LYS H 99 -1 N TYR H 95 O THR H 119 SHEET 4 AA7 4 ASP H 113 PRO H 114 -1 O ASP H 113 N LYS H 99 SHEET 1 AA8 4 SER H 132 LEU H 136 0 SHEET 2 AA8 4 THR H 147 TYR H 157 -1 O GLY H 151 N LEU H 136 SHEET 3 AA8 4 TYR H 188 PRO H 197 -1 O LEU H 190 N VAL H 154 SHEET 4 AA8 4 VAL H 175 THR H 177 -1 N HIS H 176 O VAL H 193 SHEET 1 AA9 4 SER H 132 LEU H 136 0 SHEET 2 AA9 4 THR H 147 TYR H 157 -1 O GLY H 151 N LEU H 136 SHEET 3 AA9 4 TYR H 188 PRO H 197 -1 O LEU H 190 N VAL H 154 SHEET 4 AA9 4 VAL H 181 LEU H 182 -1 N VAL H 181 O SER H 189 SHEET 1 AB1 3 THR H 163 TRP H 166 0 SHEET 2 AB1 3 TYR H 206 HIS H 212 -1 O ASN H 209 N SER H 165 SHEET 3 AB1 3 THR H 217 VAL H 223 -1 O THR H 217 N HIS H 212 SHEET 1 AB2 5 SER L 10 ALA L 13 0 SHEET 2 AB2 5 THR L 106 VAL L 110 1 O LYS L 107 N VAL L 11 SHEET 3 AB2 5 ALA L 86 ASP L 94 -1 N ALA L 86 O LEU L 108 SHEET 4 AB2 5 SER L 36 GLN L 40 -1 N TYR L 38 O TYR L 89 SHEET 5 AB2 5 LYS L 47 ILE L 50 -1 O LEU L 49 N TRP L 37 SHEET 1 AB3 4 SER L 10 ALA L 13 0 SHEET 2 AB3 4 THR L 106 VAL L 110 1 O LYS L 107 N VAL L 11 SHEET 3 AB3 4 ALA L 86 ASP L 94 -1 N ALA L 86 O LEU L 108 SHEET 4 AB3 4 ALA L 99 PHE L 102 -1 O VAL L 101 N THR L 92 SHEET 1 AB4 3 VAL L 19 SER L 24 0 SHEET 2 AB4 3 SER L 72 ILE L 77 -1 O VAL L 73 N CYS L 23 SHEET 3 AB4 3 PHE L 64 SER L 69 -1 N SER L 69 O SER L 72 SHEET 1 AB5 4 SER L 119 PHE L 123 0 SHEET 2 AB5 4 ALA L 135 PHE L 144 -1 O LEU L 140 N THR L 121 SHEET 3 AB5 4 TYR L 177 LEU L 185 -1 O ALA L 179 N ILE L 141 SHEET 4 AB5 4 VAL L 164 THR L 166 -1 N GLU L 165 O TYR L 182 SHEET 1 AB6 4 SER L 119 PHE L 123 0 SHEET 2 AB6 4 ALA L 135 PHE L 144 -1 O LEU L 140 N THR L 121 SHEET 3 AB6 4 TYR L 177 LEU L 185 -1 O ALA L 179 N ILE L 141 SHEET 4 AB6 4 SER L 170 LYS L 171 -1 N SER L 170 O ALA L 178 SHEET 1 AB7 4 SER L 158 VAL L 160 0 SHEET 2 AB7 4 THR L 150 ALA L 155 -1 N ALA L 155 O SER L 158 SHEET 3 AB7 4 TYR L 196 HIS L 202 -1 O THR L 201 N THR L 150 SHEET 4 AB7 4 SER L 205 VAL L 211 -1 O SER L 205 N HIS L 202 SSBOND 1 CYS A 94 CYS A 114 1555 1555 2.03 SSBOND 2 CYS H 23 CYS H 97 1555 1555 2.04 SSBOND 3 CYS H 152 CYS H 208 1555 1555 2.03 SSBOND 4 CYS L 23 CYS L 90 1555 1555 2.04 SSBOND 5 CYS L 139 CYS L 198 1555 1555 2.03 CISPEP 1 ALA H 107 PRO H 108 0 5.61 CISPEP 2 PHE H 158 PRO H 159 0 -3.97 CISPEP 3 GLU H 160 PRO H 161 0 -0.74 CISPEP 4 TYR L 145 PRO L 146 0 1.33 CRYST1 106.250 73.320 114.220 90.00 91.66 90.00 C 1 2 1 4 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 0.009412 0.000000 0.000273 0.00000 SCALE2 0.000000 0.013639 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008759 0.00000