HEADER IMMUNE SYSTEM 12-AUG-24 9D41 TITLE CRYSTAL STRUCTURE OF N-TERMINAL DOMAIN OF BOREALIN (20-88) IN COMPLEX TITLE 2 WITH SYNTHETIC ANTIBODY FRAGMENT COMPND MOL_ID: 1; COMPND 2 MOLECULE: BOREALIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: CELL DIVISION CYCLE-ASSOCIATED PROTEIN 8,DASRA-B,HDASRA-B, COMPND 5 PLURIPOTENT EMBRYONIC STEM CELL-RELATED GENE 3 PROTEIN; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: FAB HEAVY CHAIN; COMPND 9 CHAIN: H; COMPND 10 ENGINEERED: YES; COMPND 11 OTHER_DETAILS: ENGINEERED ELBOW REGION FNQIKG; COMPND 12 MOL_ID: 3; COMPND 13 MOLECULE: FAB LIGHT CHAIN; COMPND 14 CHAIN: L; COMPND 15 ENGINEERED: YES; COMPND 16 OTHER_DETAILS: ENGINEERED CRYSTAL KAPPA REGION SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: CDCA8, PESCRG3; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PHFT2; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 12 ORGANISM_COMMON: HUMAN; SOURCE 13 ORGANISM_TAXID: 9606; SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21(GOLD); SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 18 EXPRESSION_SYSTEM_PLASMID: RH2.2; SOURCE 19 MOL_ID: 3; SOURCE 20 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 21 ORGANISM_COMMON: HUMAN; SOURCE 22 ORGANISM_TAXID: 9606; SOURCE 23 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 24 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 25 EXPRESSION_SYSTEM_STRAIN: BL21(GOLD); SOURCE 26 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 27 EXPRESSION_SYSTEM_PLASMID: RH2.2 KEYWDS BOREALIN, CPC CORE, FAB, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR E.V.FILIPPOVA,J.HOU,S.MUKHERJEE,A.A.KOSSIAKOFF REVDAT 1 20-AUG-25 9D41 0 JRNL AUTH E.V.FILIPPOVA,J.HOU,S.MUKHERJEE,A.A.KOSSIAKOFF JRNL TITL CRYSTAL STRUCTURE OF N-TERMINAL DOMAIN OF BOREALIN (20-88) JRNL TITL 2 IN COMPLEX WITH SYNTHETIC ANTIBODY FRAGMENT JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.84 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0258 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.84 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.06 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8 REMARK 3 NUMBER OF REFLECTIONS : 61029 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.157 REMARK 3 R VALUE (WORKING SET) : 0.155 REMARK 3 FREE R VALUE : 0.197 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 3300 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.84 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.89 REMARK 3 REFLECTION IN BIN (WORKING SET) : 3818 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.50 REMARK 3 BIN R VALUE (WORKING SET) : 0.3420 REMARK 3 BIN FREE R VALUE SET COUNT : 216 REMARK 3 BIN FREE R VALUE : 0.3150 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3803 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 81 REMARK 3 SOLVENT ATOMS : 363 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.59 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.02000 REMARK 3 B22 (A**2) : -0.02000 REMARK 3 B33 (A**2) : 0.06000 REMARK 3 B12 (A**2) : -0.01000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.122 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.098 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.094 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.963 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.979 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.968 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4013 ; 0.011 ; 0.013 REMARK 3 BOND LENGTHS OTHERS (A): 3658 ; 0.001 ; 0.017 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5472 ; 1.625 ; 1.650 REMARK 3 BOND ANGLES OTHERS (DEGREES): 8497 ; 1.448 ; 1.573 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 498 ; 7.507 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 179 ;35.118 ;22.849 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 639 ;14.410 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;17.315 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 524 ; 0.072 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4430 ; 0.008 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 833 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1986 ; 4.693 ; 4.110 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1985 ; 4.717 ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2486 ; 5.522 ; 6.139 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2487 ; 5.521 ; 9.233 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2027 ; 7.162 ; 4.905 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2028 ; 7.160 ; 4.908 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2987 ; 7.785 ; 7.074 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 4410 ; 7.794 ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 4325 ; 7.760 ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): 3943 ; 5.013 ; 3.000 REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 13 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : L 1 L 34 REMARK 3 ORIGIN FOR THE GROUP (A): -17.664 11.181 36.657 REMARK 3 T TENSOR REMARK 3 T11: 0.0244 T22: 0.0546 REMARK 3 T33: 0.0506 T12: 0.0046 REMARK 3 T13: -0.0063 T23: 0.0189 REMARK 3 L TENSOR REMARK 3 L11: 0.2759 L22: 0.1610 REMARK 3 L33: 0.1664 L12: 0.1198 REMARK 3 L13: -0.1325 L23: -0.0342 REMARK 3 S TENSOR REMARK 3 S11: -0.0164 S12: -0.0560 S13: -0.0989 REMARK 3 S21: -0.0156 S22: 0.0069 S23: -0.0509 REMARK 3 S31: 0.0378 S32: 0.0138 S33: 0.0094 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : L 35 L 46 REMARK 3 ORIGIN FOR THE GROUP (A): -22.077 24.740 33.115 REMARK 3 T TENSOR REMARK 3 T11: 0.0357 T22: 0.0468 REMARK 3 T33: 0.0029 T12: 0.0006 REMARK 3 T13: -0.0036 T23: -0.0013 REMARK 3 L TENSOR REMARK 3 L11: 0.8896 L22: 1.5704 REMARK 3 L33: 1.3062 L12: 0.6124 REMARK 3 L13: -0.6825 L23: -0.2425 REMARK 3 S TENSOR REMARK 3 S11: -0.0172 S12: 0.0352 S13: 0.0362 REMARK 3 S21: -0.0519 S22: 0.0361 S23: 0.0613 REMARK 3 S31: -0.0631 S32: -0.0605 S33: -0.0189 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : L 47 L 100 REMARK 3 ORIGIN FOR THE GROUP (A): -20.802 17.898 40.510 REMARK 3 T TENSOR REMARK 3 T11: 0.0389 T22: 0.0521 REMARK 3 T33: 0.0058 T12: -0.0007 REMARK 3 T13: -0.0056 T23: 0.0019 REMARK 3 L TENSOR REMARK 3 L11: 0.5510 L22: 0.0884 REMARK 3 L33: 0.0166 L12: 0.1221 REMARK 3 L13: -0.0732 L23: -0.0177 REMARK 3 S TENSOR REMARK 3 S11: 0.0117 S12: -0.0571 S13: -0.0217 REMARK 3 S21: 0.0308 S22: -0.0121 S23: -0.0095 REMARK 3 S31: 0.0102 S32: 0.0025 S33: 0.0004 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : L 101 L 107 REMARK 3 ORIGIN FOR THE GROUP (A): -24.098 14.880 26.934 REMARK 3 T TENSOR REMARK 3 T11: 0.0932 T22: 0.0895 REMARK 3 T33: 0.0956 T12: -0.0128 REMARK 3 T13: 0.0680 T23: -0.0122 REMARK 3 L TENSOR REMARK 3 L11: 0.8740 L22: 0.8981 REMARK 3 L33: 0.7002 L12: 0.8549 REMARK 3 L13: 0.7645 L23: 0.7900 REMARK 3 S TENSOR REMARK 3 S11: -0.0542 S12: 0.0606 S13: -0.0988 REMARK 3 S21: -0.0027 S22: 0.0785 S23: -0.0278 REMARK 3 S31: -0.0145 S32: 0.0433 S33: -0.0243 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : L 108 L 125 REMARK 3 ORIGIN FOR THE GROUP (A): -27.126 15.153 3.917 REMARK 3 T TENSOR REMARK 3 T11: 0.0704 T22: 0.0486 REMARK 3 T33: 0.0082 T12: -0.0318 REMARK 3 T13: 0.0131 T23: -0.0041 REMARK 3 L TENSOR REMARK 3 L11: 0.2100 L22: 0.1072 REMARK 3 L33: 0.6214 L12: -0.0469 REMARK 3 L13: -0.0576 L23: 0.2265 REMARK 3 S TENSOR REMARK 3 S11: -0.0356 S12: 0.0300 S13: -0.0155 REMARK 3 S21: 0.0095 S22: -0.0031 S23: 0.0121 REMARK 3 S31: 0.0977 S32: -0.0657 S33: 0.0387 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : L 126 L 181 REMARK 3 ORIGIN FOR THE GROUP (A): -20.472 14.441 5.309 REMARK 3 T TENSOR REMARK 3 T11: 0.0440 T22: 0.0328 REMARK 3 T33: 0.0024 T12: -0.0083 REMARK 3 T13: -0.0025 T23: -0.0001 REMARK 3 L TENSOR REMARK 3 L11: 0.4873 L22: 0.1132 REMARK 3 L33: 0.4740 L12: -0.1863 REMARK 3 L13: -0.2992 L23: 0.1030 REMARK 3 S TENSOR REMARK 3 S11: 0.0099 S12: -0.0028 S13: 0.0092 REMARK 3 S21: 0.0078 S22: -0.0060 S23: 0.0044 REMARK 3 S31: 0.0031 S32: -0.0014 S33: -0.0040 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : L 182 L 213 REMARK 3 ORIGIN FOR THE GROUP (A): -18.321 10.971 -6.251 REMARK 3 T TENSOR REMARK 3 T11: 0.0515 T22: 0.0488 REMARK 3 T33: 0.0210 T12: -0.0092 REMARK 3 T13: -0.0053 T23: -0.0052 REMARK 3 L TENSOR REMARK 3 L11: 0.4683 L22: 0.4396 REMARK 3 L33: 0.6369 L12: 0.1656 REMARK 3 L13: -0.2542 L23: -0.1081 REMARK 3 S TENSOR REMARK 3 S11: 0.0412 S12: 0.0870 S13: -0.0226 REMARK 3 S21: -0.0473 S22: 0.0208 S23: 0.0151 REMARK 3 S31: 0.0395 S32: -0.0236 S33: -0.0620 REMARK 3 REMARK 3 TLS GROUP : 8 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : H 4 H 10 REMARK 3 ORIGIN FOR THE GROUP (A): -17.788 39.860 38.359 REMARK 3 T TENSOR REMARK 3 T11: 0.0289 T22: 0.0609 REMARK 3 T33: 0.0400 T12: 0.0113 REMARK 3 T13: -0.0106 T23: 0.0014 REMARK 3 L TENSOR REMARK 3 L11: 4.3453 L22: 0.4907 REMARK 3 L33: 5.7294 L12: 1.4549 REMARK 3 L13: -2.7860 L23: -0.8345 REMARK 3 S TENSOR REMARK 3 S11: 0.1118 S12: 0.0451 S13: 0.3263 REMARK 3 S21: 0.0305 S22: 0.0078 S23: 0.1148 REMARK 3 S31: -0.1323 S32: -0.2550 S33: -0.1196 REMARK 3 REMARK 3 TLS GROUP : 9 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : H 11 H 67 REMARK 3 ORIGIN FOR THE GROUP (A): -6.292 33.169 35.170 REMARK 3 T TENSOR REMARK 3 T11: 0.0362 T22: 0.0453 REMARK 3 T33: 0.0157 T12: -0.0011 REMARK 3 T13: -0.0055 T23: -0.0064 REMARK 3 L TENSOR REMARK 3 L11: 0.2225 L22: 0.1292 REMARK 3 L33: 0.4870 L12: 0.1159 REMARK 3 L13: 0.1003 L23: -0.0172 REMARK 3 S TENSOR REMARK 3 S11: -0.0113 S12: -0.0299 S13: 0.0168 REMARK 3 S21: 0.0019 S22: 0.0102 S23: -0.0133 REMARK 3 S31: 0.0420 S32: 0.0131 S33: 0.0011 REMARK 3 REMARK 3 TLS GROUP : 10 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : H 68 H 89 REMARK 3 ORIGIN FOR THE GROUP (A): -1.468 37.654 35.086 REMARK 3 T TENSOR REMARK 3 T11: 0.0379 T22: 0.0559 REMARK 3 T33: 0.0046 T12: -0.0045 REMARK 3 T13: -0.0042 T23: 0.0073 REMARK 3 L TENSOR REMARK 3 L11: 0.2071 L22: 0.0533 REMARK 3 L33: 0.6672 L12: 0.0617 REMARK 3 L13: 0.0063 L23: 0.0854 REMARK 3 S TENSOR REMARK 3 S11: -0.0199 S12: -0.0001 S13: 0.0052 REMARK 3 S21: 0.0124 S22: -0.0163 S23: -0.0019 REMARK 3 S31: 0.0207 S32: 0.0176 S33: 0.0362 REMARK 3 REMARK 3 TLS GROUP : 11 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : H 90 H 138 REMARK 3 ORIGIN FOR THE GROUP (A): -11.985 29.999 27.941 REMARK 3 T TENSOR REMARK 3 T11: 0.0322 T22: 0.0348 REMARK 3 T33: 0.0093 T12: -0.0033 REMARK 3 T13: -0.0045 T23: 0.0024 REMARK 3 L TENSOR REMARK 3 L11: 0.1246 L22: 0.0834 REMARK 3 L33: 0.2474 L12: 0.0399 REMARK 3 L13: 0.0272 L23: 0.1391 REMARK 3 S TENSOR REMARK 3 S11: -0.0127 S12: -0.0266 S13: 0.0030 REMARK 3 S21: -0.0169 S22: 0.0063 S23: 0.0046 REMARK 3 S31: -0.0265 S32: 0.0173 S33: 0.0064 REMARK 3 REMARK 3 TLS GROUP : 12 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : H 139 H 210 REMARK 3 ORIGIN FOR THE GROUP (A): -24.516 27.168 3.753 REMARK 3 T TENSOR REMARK 3 T11: 0.0494 T22: 0.0497 REMARK 3 T33: 0.0143 T12: -0.0025 REMARK 3 T13: 0.0031 T23: -0.0053 REMARK 3 L TENSOR REMARK 3 L11: 0.0560 L22: 0.5246 REMARK 3 L33: 0.1160 L12: 0.1576 REMARK 3 L13: 0.0120 L23: -0.0471 REMARK 3 S TENSOR REMARK 3 S11: 0.0021 S12: -0.0129 S13: 0.0224 REMARK 3 S21: 0.0347 S22: -0.0305 S23: 0.0453 REMARK 3 S31: 0.0111 S32: -0.0116 S33: 0.0284 REMARK 3 REMARK 3 TLS GROUP : 13 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : H 211 H 215 REMARK 3 ORIGIN FOR THE GROUP (A): -21.393 35.134 0.548 REMARK 3 T TENSOR REMARK 3 T11: 0.0504 T22: 0.0463 REMARK 3 T33: 0.0256 T12: -0.0084 REMARK 3 T13: -0.0077 T23: -0.0059 REMARK 3 L TENSOR REMARK 3 L11: 2.3812 L22: 2.0650 REMARK 3 L33: 1.6662 L12: 1.5430 REMARK 3 L13: 1.8711 L23: 1.0812 REMARK 3 S TENSOR REMARK 3 S11: -0.0496 S12: 0.0399 S13: -0.0385 REMARK 3 S21: -0.0378 S22: 0.0334 S23: 0.0146 REMARK 3 S31: -0.1147 S32: 0.0177 S33: 0.0162 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 9D41 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-AUG-24. REMARK 100 THE DEPOSITION ID IS D_1000287234. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 26-MAY-24 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 : NSLS-II REMARK 200 BEAMLINE : 17-ID-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.920105 REMARK 200 MONOCHROMATOR : A DOUBLE CRYSTAL SI(111) REMARK 200 OPTICS : MIRRORS 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 : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 65038 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.840 REMARK 200 RESOLUTION RANGE LOW (A) : 34.060 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 11.90 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.84 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.87 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL 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 (%): 64.07 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.42 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M CAPS, 40 % V/V MPD, PH 10.5, REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K 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 162.08600 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 81.04300 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 81.04300 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 162.08600 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 7760 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 24220 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -113.0 KCAL/MOL 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 LYS A 20 REMARK 465 LEU A 21 REMARK 465 ALA A 22 REMARK 465 SER A 23 REMARK 465 PHE A 24 REMARK 465 LYS A 80 REMARK 465 GLN A 81 REMARK 465 ALA A 82 REMARK 465 LEU A 83 REMARK 465 GLU A 84 REMARK 465 GLU A 85 REMARK 465 ALA A 86 REMARK 465 ALA A 87 REMARK 465 THR A 88 REMARK 465 GLU H -2 REMARK 465 ILE H -1 REMARK 465 SER H 0 REMARK 465 CYS H 216 REMARK 465 ASP H 217 REMARK 465 LYS H 218 REMARK 465 THR H 219 REMARK 465 HIS H 220 REMARK 465 THR H 221 REMARK 465 CYS L 214 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 ALA H 88 164.82 178.56 REMARK 500 SER L 30 -132.31 51.07 REMARK 500 ALA L 51 -38.92 78.04 REMARK 500 SER L 52 -0.23 -141.51 REMARK 500 ALA L 84 -177.09 179.02 REMARK 500 ASN L 138 62.33 60.34 REMARK 500 REMARK 500 REMARK: NULL DBREF 9D41 A 20 88 UNP Q53HL2 BOREA_HUMAN 20 88 DBREF 9D41 H -2 221 PDB 9D41 9D41 -2 221 DBREF 9D41 L 0 214 PDB 9D41 9D41 0 214 SEQRES 1 A 69 LYS LEU ALA SER PHE LEU LYS ASP PHE ASP ARG GLU VAL SEQRES 2 A 69 GLU ILE ARG ILE LYS GLN ILE GLU SER ASP ARG GLN ASN SEQRES 3 A 69 LEU LEU LYS GLU VAL ASP ASN LEU TYR ASN ILE GLU ILE SEQRES 4 A 69 LEU ARG LEU PRO LYS ALA LEU ARG GLU MET ASN TRP LEU SEQRES 5 A 69 ASP TYR PHE ALA LEU GLY GLY ASN LYS GLN ALA LEU GLU SEQRES 6 A 69 GLU ALA ALA THR SEQRES 1 H 233 GLU ILE SER GLU VAL GLN LEU VAL GLU SER GLY GLY GLY SEQRES 2 H 233 LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA SEQRES 3 H 233 ALA SER GLY PHE ASN PHE SER TYR SER SER ILE HIS TRP SEQRES 4 H 233 VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA SEQRES 5 H 233 SER ILE TYR PRO TYR SER GLY SER THR TYR TYR ALA ASP SEQRES 6 H 233 SER VAL LYS GLY ARG PHE THR ILE SER ALA ASP THR SER SEQRES 7 H 233 LYS ASN THR ALA TYR LEU GLN MET ASN SER LEU ARG ALA SEQRES 8 H 233 GLU ASP THR ALA VAL TYR TYR CYS ALA ARG LYS GLN VAL SEQRES 9 H 233 SER GLY TRP TRP TRP TYR TYR GLY PHE ASP TYR TRP GLY SEQRES 10 H 233 GLN GLY THR LEU VAL THR VAL PHE ASN GLN ILE LYS GLY SEQRES 11 H 233 PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SEQRES 12 H 233 SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP SEQRES 13 H 233 TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SEQRES 14 H 233 ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 15 H 233 GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR SEQRES 16 H 233 VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS SEQRES 17 H 233 ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS SEQRES 18 H 233 LYS VAL GLU PRO LYS SER CYS ASP LYS THR HIS THR SEQRES 1 L 213 SER ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER SEQRES 2 L 213 ALA SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SEQRES 3 L 213 SER GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN SEQRES 4 L 213 LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SEQRES 5 L 213 SER SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SEQRES 6 L 213 SER ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER SEQRES 7 L 213 LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SEQRES 8 L 213 SER TYR TRP TRP PRO ILE THR PHE GLY GLN GLY THR LYS SEQRES 9 L 213 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 L 213 ILE PHE PRO PRO SER ASP SER GLN LEU LYS SER GLY THR SEQRES 11 L 213 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 L 213 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 L 213 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 L 213 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 L 213 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 L 213 GLU VAL THR GLN GLY THR THR SER VAL THR LYS SER PHE SEQRES 17 L 213 ASN ARG GLY GLU CYS HET MPD A 101 8 HET MPD A 102 8 HET CL H 301 1 HET MPD H 302 8 HET MPD H 303 8 HET MPD H 304 8 HET MPD H 305 8 HET MPD L 301 8 HET MPD L 302 8 HET MPD L 303 8 HET MPD L 304 8 HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL HETNAM CL CHLORIDE ION FORMUL 4 MPD 10(C6 H14 O2) FORMUL 6 CL CL 1- FORMUL 15 HOH *363(H2 O) HELIX 1 AA1 LEU A 25 ARG A 66 1 42 HELIX 2 AA2 ASN A 69 LEU A 76 1 8 HELIX 3 AA3 ASN H 28 SER H 30 5 3 HELIX 4 AA4 THR H 73 LYS H 75 5 3 HELIX 5 AA5 ARG H 83 THR H 87 5 5 HELIX 6 AA6 SER H 156 ALA H 158 5 3 HELIX 7 AA7 SER H 187 LEU H 189 5 3 HELIX 8 AA8 LYS H 201 ASN H 204 5 4 HELIX 9 AA9 GLN L 79 PHE L 83 5 5 HELIX 10 AB1 SER L 121 SER L 127 1 7 HELIX 11 AB2 LYS L 183 HIS L 189 1 7 SHEET 1 AA1 4 GLN H 3 SER H 7 0 SHEET 2 AA1 4 LEU H 18 SER H 25 -1 O ALA H 23 N VAL H 5 SHEET 3 AA1 4 THR H 77 MET H 82 -1 O LEU H 80 N LEU H 20 SHEET 4 AA1 4 PHE H 67 ASP H 72 -1 N THR H 68 O GLN H 81 SHEET 1 AA2 6 GLY H 10 VAL H 12 0 SHEET 2 AA2 6 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA2 6 ALA H 88 GLN H 96 -1 N ALA H 88 O VAL H 109 SHEET 4 AA2 6 SER H 32 GLN H 39 -1 N VAL H 37 O TYR H 91 SHEET 5 AA2 6 GLU H 46 ILE H 51 -1 O VAL H 48 N TRP H 36 SHEET 6 AA2 6 THR H 58 TYR H 59 -1 O TYR H 58A N SER H 50 SHEET 1 AA3 4 GLY H 10 VAL H 12 0 SHEET 2 AA3 4 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA3 4 ALA H 88 GLN H 96 -1 N ALA H 88 O VAL H 109 SHEET 4 AA3 4 PHE H 100F TRP H 103 -1 O TYR H 102 N ARG H 94 SHEET 1 AA4 4 SER H 120 LEU H 124 0 SHEET 2 AA4 4 THR H 135 TYR H 145 -1 O LYS H 143 N SER H 120 SHEET 3 AA4 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142 SHEET 4 AA4 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AA5 4 THR H 131 SER H 132 0 SHEET 2 AA5 4 THR H 135 TYR H 145 -1 O THR H 135 N SER H 132 SHEET 3 AA5 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142 SHEET 4 AA5 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AA6 3 THR H 151 TRP H 154 0 SHEET 2 AA6 3 ILE H 195 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 AA6 3 THR H 205 LYS H 210 -1 O VAL H 207 N VAL H 198 SHEET 1 AA7 4 MET L 4 SER L 7 0 SHEET 2 AA7 4 VAL L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AA7 4 ASP L 70 ILE L 75 -1 O ILE L 75 N VAL L 19 SHEET 4 AA7 4 PHE L 62 SER L 67 -1 N SER L 67 O ASP L 70 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 VAL L 104 SHEET 4 AA8 6 VAL L 33 GLN L 38 -1 N GLN L 38 O THR L 85 SHEET 5 AA8 6 LYS L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AA8 6 SER L 53 LEU L 54 -1 O SER L 53 N TYR L 49 SHEET 1 AA9 4 SER L 10 ALA L 13 0 SHEET 2 AA9 4 THR L 102 ILE L 106 1 O GLU L 105 N LEU L 11 SHEET 3 AA9 4 ALA L 84 GLN L 90 -1 N ALA L 84 O VAL L 104 SHEET 4 AA9 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AB1 4 SER L 114 PHE L 118 0 SHEET 2 AB1 4 THR L 129 PHE L 139 -1 O LEU L 135 N PHE L 116 SHEET 3 AB1 4 TYR L 173 SER L 182 -1 O LEU L 175 N LEU L 136 SHEET 4 AB1 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178 SHEET 1 AB2 4 ALA L 153 LEU L 154 0 SHEET 2 AB2 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AB2 4 VAL L 191 GLN L 200 -1 O GLU L 195 N GLN L 147 SHEET 4 AB2 4 THR L 203 ASN L 210 -1 O VAL L 205 N VAL L 196 SSBOND 1 CYS H 22 CYS H 92 1555 1555 1.93 SSBOND 2 CYS H 140 CYS H 196 1555 1555 2.08 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.18 SSBOND 4 CYS L 134 CYS L 194 1555 1555 2.01 CISPEP 1 PHE H 146 PRO H 147 0 -12.32 CISPEP 2 GLU H 148 PRO H 149 0 -0.22 CISPEP 3 GLU H 148 PRO H 149 0 -7.95 CISPEP 4 SER L 7 PRO L 8 0 -6.81 CISPEP 5 TRP L 94 PRO L 95 0 -5.95 CISPEP 6 TYR L 140 PRO L 141 0 -0.19 CRYST1 72.432 72.432 243.129 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 0.013806 0.007971 0.000000 0.00000 SCALE2 0.000000 0.015942 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004113 0.00000