HEADER DNA BINDING PROTEIN 26-DEC-22 8C3K TITLE PAAR2 N-TERMINAL DOMIN IN COMPLEX WITH NANOBODY 33 COMPND MOL_ID: 1; COMPND 2 MOLECULE: PHAGE REPRESSOR PROTEIN CI; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: NANOBODY 33; COMPND 7 CHAIN: B; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI O157:H7; SOURCE 3 ORGANISM_TAXID: 83334; SOURCE 4 GENE: ECS_2279; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 9 ORGANISM_TAXID: 9844; SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 11 EXPRESSION_SYSTEM_TAXID: 469008 KEYWDS CI REPRESSOR, DNA BINDING, HTH MOTIF, HELIX-TURN-HELIX, NANOBODY KEYWDS 2 COMPLEX, NANOBODY, DNA BINDING PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR R.LORIS,M.PROLIC-KALINSEK REVDAT 1 10-JAN-24 8C3K 0 JRNL AUTH M.PROLIK-KALINSEK,A.VOLKOV,R.LORIS JRNL TITL PAAR2, THE CI EQUIVALENT IN ESCHERICHIA COLI O157:H7 CRYPTIC JRNL TITL 2 PROPHAGE CP-933P JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.75 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.11.1_2575 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) : 1.75 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.57 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.338 REMARK 3 COMPLETENESS FOR RANGE (%) : 86.0 REMARK 3 NUMBER OF REFLECTIONS : 16137 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.206 REMARK 3 R VALUE (WORKING SET) : 0.203 REMARK 3 FREE R VALUE : 0.233 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.002 REMARK 3 FREE R VALUE TEST SET COUNT : 1614 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 33.5715 - 4.0038 1.00 1498 173 0.1653 0.2010 REMARK 3 2 4.0038 - 3.1787 1.00 1432 162 0.1801 0.2115 REMARK 3 3 3.1787 - 2.7771 1.00 1421 157 0.2207 0.2200 REMARK 3 4 2.7771 - 2.5233 1.00 1406 152 0.2316 0.2593 REMARK 3 5 2.5233 - 2.3425 1.00 1409 158 0.2369 0.2803 REMARK 3 6 2.3425 - 2.2044 1.00 1413 151 0.2335 0.2692 REMARK 3 7 2.2044 - 2.0940 1.00 1373 150 0.2475 0.2912 REMARK 3 8 2.0940 - 2.0029 1.00 1399 157 0.2726 0.2913 REMARK 3 9 2.0029 - 1.9258 0.87 1217 130 0.2737 0.2977 REMARK 3 10 1.9258 - 1.8593 0.61 835 98 0.2760 0.3114 REMARK 3 11 1.8593 - 1.8012 0.48 647 76 0.2946 0.3486 REMARK 3 12 1.8012 - 1.7497 0.34 473 50 0.2983 0.3984 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) : 0.224 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.415 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 34.00 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.82 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 : 0.006 1365 REMARK 3 ANGLE : 0.787 1863 REMARK 3 CHIRALITY : 0.047 203 REMARK 3 PLANARITY : 0.004 239 REMARK 3 DIHEDRAL : 11.284 822 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 12 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 4 THROUGH 16 ) REMARK 3 ORIGIN FOR THE GROUP (A): -21.9907 27.2708 -3.0734 REMARK 3 T TENSOR REMARK 3 T11: 0.6803 T22: 0.6469 REMARK 3 T33: 0.3494 T12: -0.1194 REMARK 3 T13: -0.0502 T23: 0.1191 REMARK 3 L TENSOR REMARK 3 L11: 1.4083 L22: 5.4070 REMARK 3 L33: 5.3925 L12: -1.0012 REMARK 3 L13: -0.5727 L23: -0.8551 REMARK 3 S TENSOR REMARK 3 S11: 0.0344 S12: 0.8664 S13: 0.3642 REMARK 3 S21: -1.3197 S22: 0.2894 S23: 0.5536 REMARK 3 S31: -0.5568 S32: -0.3218 S33: -0.3222 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 17 THROUGH 39 ) REMARK 3 ORIGIN FOR THE GROUP (A): -19.7026 18.5390 -6.9808 REMARK 3 T TENSOR REMARK 3 T11: 0.9242 T22: 0.8798 REMARK 3 T33: 0.4351 T12: -0.0343 REMARK 3 T13: -0.0463 T23: -0.1214 REMARK 3 L TENSOR REMARK 3 L11: 4.8211 L22: 3.3431 REMARK 3 L33: 2.1793 L12: -1.7580 REMARK 3 L13: -1.8350 L23: -1.0675 REMARK 3 S TENSOR REMARK 3 S11: 0.1245 S12: 1.4768 S13: -0.8059 REMARK 3 S21: -0.8880 S22: -0.3222 S23: 0.6396 REMARK 3 S31: 0.5685 S32: 0.0924 S33: 0.2189 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 40 THROUGH 63 ) REMARK 3 ORIGIN FOR THE GROUP (A): -25.4327 23.9053 3.2257 REMARK 3 T TENSOR REMARK 3 T11: 0.4542 T22: 0.5039 REMARK 3 T33: 0.3748 T12: -0.0797 REMARK 3 T13: -0.0881 T23: 0.0683 REMARK 3 L TENSOR REMARK 3 L11: 4.7716 L22: 4.3944 REMARK 3 L33: 3.3530 L12: 0.2131 REMARK 3 L13: -0.1001 L23: 0.7515 REMARK 3 S TENSOR REMARK 3 S11: -0.0807 S12: 0.3093 S13: 0.2912 REMARK 3 S21: -0.6747 S22: 0.1750 S23: 0.8070 REMARK 3 S31: 0.2229 S32: -0.5259 S33: -0.0844 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.8287 21.0565 16.9469 REMARK 3 T TENSOR REMARK 3 T11: 0.2359 T22: 0.5114 REMARK 3 T33: 0.4243 T12: 0.1164 REMARK 3 T13: 0.1061 T23: 0.0618 REMARK 3 L TENSOR REMARK 3 L11: 3.8450 L22: 0.8806 REMARK 3 L33: 2.1380 L12: 1.1574 REMARK 3 L13: -0.8122 L23: 0.8850 REMARK 3 S TENSOR REMARK 3 S11: 0.0276 S12: 0.6068 S13: -0.6614 REMARK 3 S21: -0.1566 S22: -0.0713 S23: -0.4196 REMARK 3 S31: 0.3193 S32: 0.6733 S33: 0.0473 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 18 THROUGH 30 ) REMARK 3 ORIGIN FOR THE GROUP (A): -10.8062 15.2674 16.7913 REMARK 3 T TENSOR REMARK 3 T11: 0.3161 T22: 0.3424 REMARK 3 T33: 0.4038 T12: 0.0661 REMARK 3 T13: 0.0954 T23: 0.0669 REMARK 3 L TENSOR REMARK 3 L11: 2.0905 L22: 2.7836 REMARK 3 L33: 4.4823 L12: -0.6999 REMARK 3 L13: -1.3826 L23: 0.7077 REMARK 3 S TENSOR REMARK 3 S11: -0.1859 S12: -0.4187 S13: -0.8017 REMARK 3 S21: -0.0487 S22: 0.0143 S23: -0.1179 REMARK 3 S31: 0.7892 S32: 0.5038 S33: 0.1140 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 31 THROUGH 39 ) REMARK 3 ORIGIN FOR THE GROUP (A): -10.0740 22.1330 9.3457 REMARK 3 T TENSOR REMARK 3 T11: 0.3380 T22: 0.4323 REMARK 3 T33: 0.3773 T12: 0.0372 REMARK 3 T13: 0.1427 T23: 0.0484 REMARK 3 L TENSOR REMARK 3 L11: 2.1111 L22: 6.7660 REMARK 3 L33: 4.3235 L12: 3.6240 REMARK 3 L13: -0.1820 L23: -1.4114 REMARK 3 S TENSOR REMARK 3 S11: 0.1955 S12: 0.5693 S13: 0.7054 REMARK 3 S21: -0.2794 S22: -0.0254 S23: 0.4988 REMARK 3 S31: -0.0223 S32: 0.6417 S33: 0.1151 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 40 THROUGH 59 ) REMARK 3 ORIGIN FOR THE GROUP (A): -8.5309 21.1784 4.7937 REMARK 3 T TENSOR REMARK 3 T11: 0.4989 T22: 0.5609 REMARK 3 T33: 0.3069 T12: 0.0650 REMARK 3 T13: 0.0957 T23: 0.0317 REMARK 3 L TENSOR REMARK 3 L11: 5.3052 L22: 4.3516 REMARK 3 L33: 5.6262 L12: -1.1693 REMARK 3 L13: 0.7446 L23: 1.0478 REMARK 3 S TENSOR REMARK 3 S11: -0.1658 S12: 1.0413 S13: -0.1870 REMARK 3 S21: -0.5797 S22: -0.1764 S23: 0.2626 REMARK 3 S31: -0.2164 S32: 0.5362 S33: 0.3316 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 60 THROUGH 66 ) REMARK 3 ORIGIN FOR THE GROUP (A): 0.5654 19.0165 -0.1632 REMARK 3 T TENSOR REMARK 3 T11: 0.5701 T22: 1.2775 REMARK 3 T33: 0.3187 T12: 0.1786 REMARK 3 T13: 0.4321 T23: 0.0442 REMARK 3 L TENSOR REMARK 3 L11: 1.1336 L22: 1.7779 REMARK 3 L33: 6.1186 L12: 1.4099 REMARK 3 L13: 0.2426 L23: 0.3634 REMARK 3 S TENSOR REMARK 3 S11: 0.1181 S12: 0.7621 S13: -0.2213 REMARK 3 S21: -0.2805 S22: 0.9879 S23: -0.2385 REMARK 3 S31: 0.2349 S32: 0.6912 S33: 1.9511 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 67 THROUGH 76 ) REMARK 3 ORIGIN FOR THE GROUP (A): -9.0429 10.7021 11.6165 REMARK 3 T TENSOR REMARK 3 T11: 0.5056 T22: 0.4316 REMARK 3 T33: 0.5811 T12: 0.0850 REMARK 3 T13: 0.0895 T23: -0.0707 REMARK 3 L TENSOR REMARK 3 L11: 9.2153 L22: 6.7133 REMARK 3 L33: 9.2345 L12: 2.1490 REMARK 3 L13: -3.9741 L23: -2.9990 REMARK 3 S TENSOR REMARK 3 S11: -0.1065 S12: 0.9417 S13: -1.0037 REMARK 3 S21: -0.0689 S22: 0.2479 S23: 0.0506 REMARK 3 S31: 1.0160 S32: 0.0540 S33: -0.1419 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 77 THROUGH 90 ) REMARK 3 ORIGIN FOR THE GROUP (A): 1.9805 18.1159 9.2654 REMARK 3 T TENSOR REMARK 3 T11: 0.3565 T22: 0.9560 REMARK 3 T33: 0.5724 T12: 0.0506 REMARK 3 T13: 0.3239 T23: -0.0817 REMARK 3 L TENSOR REMARK 3 L11: 3.8356 L22: 2.5665 REMARK 3 L33: 0.9206 L12: 0.8784 REMARK 3 L13: -1.1736 L23: -0.4813 REMARK 3 S TENSOR REMARK 3 S11: -0.0637 S12: 0.6129 S13: -0.1413 REMARK 3 S21: -0.3328 S22: 0.3826 S23: -0.8960 REMARK 3 S31: 0.3489 S32: 1.5610 S33: 0.2869 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 91 THROUGH 104 ) REMARK 3 ORIGIN FOR THE GROUP (A): -10.8877 25.7367 14.0609 REMARK 3 T TENSOR REMARK 3 T11: 0.2661 T22: 0.3463 REMARK 3 T33: 0.3233 T12: 0.0030 REMARK 3 T13: 0.0565 T23: 0.0830 REMARK 3 L TENSOR REMARK 3 L11: 3.1652 L22: 2.3745 REMARK 3 L33: 2.2317 L12: 0.4894 REMARK 3 L13: 1.3234 L23: 0.9648 REMARK 3 S TENSOR REMARK 3 S11: -0.1101 S12: 0.6390 S13: 0.1649 REMARK 3 S21: -0.1274 S22: 0.0945 S23: -0.1143 REMARK 3 S31: -0.1057 S32: 0.3331 S33: 0.0537 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 105 THROUGH 111 ) REMARK 3 ORIGIN FOR THE GROUP (A): 6.5696 25.4179 14.2773 REMARK 3 T TENSOR REMARK 3 T11: 0.0703 T22: 1.0567 REMARK 3 T33: 0.5087 T12: -0.1075 REMARK 3 T13: 0.2767 T23: 0.0570 REMARK 3 L TENSOR REMARK 3 L11: 0.9089 L22: 1.7799 REMARK 3 L33: 0.1180 L12: 1.2795 REMARK 3 L13: -0.3371 L23: -0.4635 REMARK 3 S TENSOR REMARK 3 S11: -0.1023 S12: 0.9726 S13: -0.2037 REMARK 3 S21: -0.5414 S22: 0.1105 S23: -0.6223 REMARK 3 S31: -0.6875 S32: 1.3377 S33: -0.1425 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 8C3K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-DEC-22. REMARK 100 THE DEPOSITION ID IS D_1292127699. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 27-MAY-21 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 : SOLEIL REMARK 200 BEAMLINE : PROXIMA 1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.978565 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18742 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750 REMARK 200 RESOLUTION RANGE LOW (A) : 44.700 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 200 DATA REDUNDANCY : 19.80 REMARK 200 R MERGE (I) : 0.05400 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 23.9800 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 3.54300 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.850 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 (%): 41.41 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.02 M SODIUM/POTASSIUM PHOSPHATE, 20% REMARK 280 PEG 3350, VAPOR DIFFUSION, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+2/3 REMARK 290 3555 -X+Y,-X,Z+1/3 REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z+1/3 REMARK 290 6555 -X,-X+Y,-Z+2/3 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 46.47133 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 23.23567 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 23.23567 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 46.47133 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: 1270 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 8220 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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 MET A 1 REMARK 465 GLN A 2 REMARK 465 LYS A 3 REMARK 465 GLN A 64 REMARK 465 PRO A 65 REMARK 465 GLY A 66 REMARK 465 SER A 67 REMARK 465 SER A 68 REMARK 465 HIS A 69 REMARK 465 HIS A 70 REMARK 465 HIS A 71 REMARK 465 HIS A 72 REMARK 465 HIS A 73 REMARK 465 HIS A 74 REMARK 465 HIS B 112 REMARK 465 HIS B 113 REMARK 465 HIS B 114 REMARK 465 HIS B 115 REMARK 465 HIS B 116 REMARK 465 HIS B 117 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 A 4 CG CD CE NZ REMARK 470 GLU A 5 CD OE1 OE2 REMARK 470 ARG A 8 CD NE CZ NH1 NH2 REMARK 470 LYS A 12 NZ REMARK 470 LYS A 16 CD CE NZ REMARK 470 LYS A 23 CG CD CE NZ REMARK 470 LYS A 25 CE NZ REMARK 470 GLU A 40 OE1 OE2 REMARK 470 LYS A 41 CD CE NZ REMARK 470 ARG A 45 NE CZ NH1 NH2 REMARK 470 THR A 49 OG1 REMARK 470 GLU A 54 OE1 OE2 REMARK 470 GLU A 63 CA C O CB CG CD OE1 REMARK 470 GLU A 63 OE2 REMARK 470 GLN B 1 CD OE1 NE2 REMARK 470 GLN B 13 CG CD OE1 NE2 REMARK 470 GLU B 42 CG CD OE1 OE2 REMARK 470 LYS B 43 CG CD CE NZ REMARK 470 SER B 73 OG REMARK 470 LYS B 86 NZ REMARK 470 GLU B 88 CG CD OE1 OE2 REMARK 470 SER B 111 O OG 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 B 43 130.14 67.30 REMARK 500 ARG B 45 65.38 60.33 REMARK 500 SER B 62 -22.99 -178.92 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 7NKV RELATED DB: PDB REMARK 900 7NKV IS THE NMR STRUCTURE OF PAAR2 N-TERMINAL DOMAIN DBREF 8C3K A 1 66 UNP Q8XAD6 Q8XAD6_ECO57 1 66 DBREF 8C3K B 1 117 PDB 8C3K 8C3K 1 117 SEQADV 8C3K SER A 67 UNP Q8XAD6 EXPRESSION TAG SEQADV 8C3K SER A 68 UNP Q8XAD6 EXPRESSION TAG SEQADV 8C3K HIS A 69 UNP Q8XAD6 EXPRESSION TAG SEQADV 8C3K HIS A 70 UNP Q8XAD6 EXPRESSION TAG SEQADV 8C3K HIS A 71 UNP Q8XAD6 EXPRESSION TAG SEQADV 8C3K HIS A 72 UNP Q8XAD6 EXPRESSION TAG SEQADV 8C3K HIS A 73 UNP Q8XAD6 EXPRESSION TAG SEQADV 8C3K HIS A 74 UNP Q8XAD6 EXPRESSION TAG SEQRES 1 A 74 MET GLN LYS LYS GLU ILE ARG ARG LEU ARG LEU LYS GLU SEQRES 2 A 74 TRP PHE LYS ASP LYS THR LEU PRO PRO LYS GLU LYS SER SEQRES 3 A 74 TYR LEU SER GLN LEU MET SER GLY ARG ALA SER PHE GLY SEQRES 4 A 74 GLU LYS ALA ALA ARG ARG ILE GLU GLN THR TYR GLY MET SEQRES 5 A 74 PRO GLU GLY TYR LEU ASP ALA GLU TYR ALA GLU GLN PRO SEQRES 6 A 74 GLY SER SER HIS HIS HIS HIS HIS HIS SEQRES 1 B 117 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 B 117 SER GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 B 117 SER ILE PHE ARG THR THR GLY MET ASN TRP TYR ARG GLN SEQRES 4 B 117 THR PRO GLU LYS GLN ARG GLU TRP VAL ALA LEU ILE THR SEQRES 5 B 117 SER HIS GLY THR THR SER TYR ALA ALA SER VAL GLU GLY SEQRES 6 B 117 ARG PHE THR ILE SER ARG ASP SER ALA GLY THR THR VAL SEQRES 7 B 117 TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP ALA GLY SEQRES 8 B 117 VAL TYR TYR CYS THR THR ARG GLY TYR TRP GLY GLN GLY SEQRES 9 B 117 THR GLN VAL THR VAL SER SER HIS HIS HIS HIS HIS HIS FORMUL 3 HOH *68(H2 O) HELIX 1 AA1 LYS A 4 LYS A 16 1 13 HELIX 2 AA2 PRO A 21 SER A 33 1 13 HELIX 3 AA3 GLY A 39 GLY A 51 1 13 HELIX 4 AA4 GLY A 55 ALA A 59 5 5 HELIX 5 AA5 GLY B 26 THR B 31 5 6 HELIX 6 AA6 LYS B 86 ALA B 90 5 5 SHEET 1 AA1 4 LEU B 4 SER B 7 0 SHEET 2 AA1 4 LEU B 18 ALA B 24 -1 O SER B 21 N SER B 7 SHEET 3 AA1 4 THR B 77 MET B 82 -1 O MET B 82 N LEU B 18 SHEET 4 AA1 4 PHE B 67 ARG B 71 -1 N THR B 68 O GLN B 81 SHEET 1 AA2 6 GLY B 10 GLN B 13 0 SHEET 2 AA2 6 THR B 105 SER B 110 1 O THR B 108 N GLY B 10 SHEET 3 AA2 6 GLY B 91 THR B 97 -1 N TYR B 93 O THR B 105 SHEET 4 AA2 6 MET B 34 GLN B 39 -1 N TYR B 37 O TYR B 94 SHEET 5 AA2 6 GLU B 46 ILE B 51 -1 O GLU B 46 N ARG B 38 SHEET 6 AA2 6 THR B 57 TYR B 59 -1 O SER B 58 N LEU B 50 SHEET 1 AA3 4 GLY B 10 GLN B 13 0 SHEET 2 AA3 4 THR B 105 SER B 110 1 O THR B 108 N GLY B 10 SHEET 3 AA3 4 GLY B 91 THR B 97 -1 N TYR B 93 O THR B 105 SHEET 4 AA3 4 TYR B 100 TRP B 101 -1 O TYR B 100 N THR B 97 SSBOND 1 CYS B 22 CYS B 95 1555 1555 2.06 CRYST1 67.143 67.143 69.707 90.00 90.00 120.00 P 32 2 1 6 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.014894 0.008599 0.000000 0.00000 SCALE2 0.000000 0.017198 0.000000 0.00000 SCALE3 0.000000 0.000000 0.014346 0.00000