HEADER VIRAL PROTEIN 28-APR-23 8OWT TITLE SARS-COV-2 SPIKE RBD WITH A8 AND H3 NANOBODIES BOUND COMPND MOL_ID: 1; COMPND 2 MOLECULE: NANOBODY A8; COMPND 3 CHAIN: AAA, DDD; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: SPIKE PROTEIN S1; COMPND 7 CHAIN: BBB, EEE; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: NANOBODY H3; COMPND 11 CHAIN: CCC, FFF; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 3 ORGANISM_TAXID: 9844; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS SOURCE 8 2; SOURCE 9 ORGANISM_TAXID: 2697049; SOURCE 10 GENE: S, 2; SOURCE 11 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 15 ORGANISM_TAXID: 9844; SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS NANOBODY, COMPLEX, RECEPTOR BINDING DOMAIN, SARS-COV-2, VIRAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR H.MIKOLAJEK,J.H.NAISMITH,R.J.OWENS JRNL AUTH K.A.S.CORNISH,H.MIKOLAJEK,J.H.NAISMITH,R.J.OWENS JRNL TITL TRIMERIC NANOBODIES POTENTLY NEUTRALIZE OMICRON VARIANTS OF JRNL TITL 2 SARS-COV-2 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.37 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0267 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.37 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 58.78 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 42863 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.213 REMARK 3 FREE R VALUE : 0.249 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.797 REMARK 3 FREE R VALUE TEST SET COUNT : 2056 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.37 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.43 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2982 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0 REMARK 3 BIN R VALUE (WORKING SET) : 0.3460 REMARK 3 BIN FREE R VALUE SET COUNT : 139 REMARK 3 BIN FREE R VALUE : 0.3520 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6960 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 40 REMARK 3 SOLVENT ATOMS : 172 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 54.72 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.24600 REMARK 3 B22 (A**2) : 0.21800 REMARK 3 B33 (A**2) : 0.02700 REMARK 3 B12 (A**2) : 0.00000 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): 0.396 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.252 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.248 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 22.968 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.924 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7220 ; 0.003 ; 0.012 REMARK 3 BOND LENGTHS OTHERS (A): 6477 ; 0.001 ; 0.018 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9817 ; 1.241 ; 1.651 REMARK 3 BOND ANGLES OTHERS (DEGREES): 14848 ; 1.119 ; 1.583 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 895 ; 6.771 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 390 ;29.027 ;21.538 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1076 ;13.613 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 49 ;14.816 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 901 ; 0.042 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8396 ; 0.003 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1898 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1037 ; 0.174 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 121 ; 0.188 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3375 ; 0.166 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 209 ; 0.121 ; 0.200 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): 3574 ; 1.142 ; 2.656 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3573 ; 1.142 ; 2.656 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4459 ; 1.850 ; 3.982 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 4460 ; 1.850 ; 3.983 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3646 ; 1.382 ; 2.779 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3644 ; 1.335 ; 2.776 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5354 ; 2.249 ; 4.117 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 5355 ; 2.249 ; 4.119 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL 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 : 3 REMARK 3 REMARK 3 NCS GROUP NUMBER : 1 REMARK 3 CHAIN NAMES : AAA DDD REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 AA 3 AA 125 NULL REMARK 3 1 DD 3 DD 125 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 2 REMARK 3 CHAIN NAMES : BBB EEE REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 2 BB 334 BB 528 NULL REMARK 3 2 EE 334 EE 528 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 3 REMARK 3 CHAIN NAMES : CCC FFF REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 3 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 3 CC 4 CC 127 NULL REMARK 3 3 FF 4 FF 127 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 26 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 : NULL NULL NULL NULL REMARK 3 ORIGIN FOR THE GROUP (A): 3.0930 13.1920 -33.6730 REMARK 3 T TENSOR REMARK 3 T11: 0.4031 T22: 0.6262 REMARK 3 T33: 0.1324 T12: -0.0228 REMARK 3 T13: -0.0920 T23: -0.0821 REMARK 3 L TENSOR REMARK 3 L11: 10.3768 L22: 4.2166 REMARK 3 L33: 1.2954 L12: -3.5336 REMARK 3 L13: 1.6316 L23: -0.9063 REMARK 3 S TENSOR REMARK 3 S11: 0.4403 S12: 0.3433 S13: 0.2223 REMARK 3 S21: -0.8751 S22: -0.3838 S23: 0.2028 REMARK 3 S31: 0.0234 S32: -0.1643 S33: -0.0565 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 : NULL NULL NULL NULL REMARK 3 ORIGIN FOR THE GROUP (A): 7.4160 14.3220 -24.8650 REMARK 3 T TENSOR REMARK 3 T11: 0.2106 T22: 0.6694 REMARK 3 T33: 0.1890 T12: -0.0235 REMARK 3 T13: -0.0727 T23: -0.0293 REMARK 3 L TENSOR REMARK 3 L11: 4.3846 L22: 1.5767 REMARK 3 L33: 5.5010 L12: -0.8697 REMARK 3 L13: -2.1479 L23: 0.6639 REMARK 3 S TENSOR REMARK 3 S11: 0.1071 S12: 0.7120 S13: 0.5677 REMARK 3 S21: -0.3463 S22: -0.3077 S23: -0.0596 REMARK 3 S31: -0.8702 S32: -0.0009 S33: 0.2006 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 : NULL NULL NULL NULL REMARK 3 ORIGIN FOR THE GROUP (A): -0.5280 11.5630 -21.9590 REMARK 3 T TENSOR REMARK 3 T11: 0.0884 T22: 0.6038 REMARK 3 T33: 0.2032 T12: -0.0153 REMARK 3 T13: -0.0457 T23: -0.0794 REMARK 3 L TENSOR REMARK 3 L11: 3.5881 L22: 4.7815 REMARK 3 L33: 6.5224 L12: -1.6121 REMARK 3 L13: -0.2633 L23: -0.1408 REMARK 3 S TENSOR REMARK 3 S11: -0.1799 S12: 0.2657 S13: 0.2184 REMARK 3 S21: -0.1988 S22: 0.0384 S23: 0.3887 REMARK 3 S31: -0.5675 S32: -0.6422 S33: 0.1415 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 : NULL NULL NULL NULL REMARK 3 ORIGIN FOR THE GROUP (A): 7.5200 17.0660 -23.4790 REMARK 3 T TENSOR REMARK 3 T11: 0.3323 T22: 0.6388 REMARK 3 T33: 0.1849 T12: -0.0866 REMARK 3 T13: -0.1253 T23: -0.0049 REMARK 3 L TENSOR REMARK 3 L11: 3.4055 L22: 4.7648 REMARK 3 L33: 2.1861 L12: -1.1644 REMARK 3 L13: -1.3647 L23: -1.8088 REMARK 3 S TENSOR REMARK 3 S11: 0.2180 S12: 0.4992 S13: 0.3455 REMARK 3 S21: -0.5546 S22: -0.0636 S23: 0.1707 REMARK 3 S31: -0.1630 S32: 0.0260 S33: -0.1544 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 : NULL NULL NULL NULL REMARK 3 ORIGIN FOR THE GROUP (A): 12.9840 12.4060 8.6520 REMARK 3 T TENSOR REMARK 3 T11: 0.4297 T22: 0.6045 REMARK 3 T33: 0.0996 T12: -0.0238 REMARK 3 T13: 0.0666 T23: -0.0569 REMARK 3 L TENSOR REMARK 3 L11: 4.6888 L22: 7.8944 REMARK 3 L33: 2.1728 L12: 3.8656 REMARK 3 L13: -0.8225 L23: -3.0867 REMARK 3 S TENSOR REMARK 3 S11: 0.0582 S12: -0.2232 S13: -0.2912 REMARK 3 S21: 0.8693 S22: 0.0854 S23: 0.1265 REMARK 3 S31: 0.0428 S32: -0.2412 S33: -0.1435 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 : NULL NULL NULL NULL REMARK 3 ORIGIN FOR THE GROUP (A): 12.4940 5.0320 -0.3730 REMARK 3 T TENSOR REMARK 3 T11: 0.1355 T22: 0.7139 REMARK 3 T33: 0.1197 T12: -0.0612 REMARK 3 T13: 0.0142 T23: 0.0053 REMARK 3 L TENSOR REMARK 3 L11: 0.9711 L22: 1.3400 REMARK 3 L33: 1.2155 L12: 0.8621 REMARK 3 L13: -0.0532 L23: -0.1633 REMARK 3 S TENSOR REMARK 3 S11: 0.0345 S12: -0.0955 S13: -0.1658 REMARK 3 S21: 0.0645 S22: -0.0454 S23: -0.0285 REMARK 3 S31: 0.3772 S32: -0.2685 S33: 0.0109 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 : NULL NULL NULL NULL REMARK 3 ORIGIN FOR THE GROUP (A): 21.3370 21.2920 -8.9020 REMARK 3 T TENSOR REMARK 3 T11: 0.1551 T22: 0.4505 REMARK 3 T33: 0.1470 T12: -0.0295 REMARK 3 T13: 0.0842 T23: 0.0021 REMARK 3 L TENSOR REMARK 3 L11: 5.8475 L22: 1.8008 REMARK 3 L33: 5.6952 L12: -1.6622 REMARK 3 L13: 1.3469 L23: 1.3284 REMARK 3 S TENSOR REMARK 3 S11: -0.0061 S12: 0.4175 S13: 0.3143 REMARK 3 S21: -0.3462 S22: -0.0231 S23: -0.0682 REMARK 3 S31: -0.4401 S32: 0.1604 S33: 0.0292 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 : NULL NULL NULL NULL REMARK 3 ORIGIN FOR THE GROUP (A): 21.7200 25.0690 0.3210 REMARK 3 T TENSOR REMARK 3 T11: 0.0024 T22: 0.4841 REMARK 3 T33: 0.0151 T12: 0.0088 REMARK 3 T13: -0.0029 T23: -0.0009 REMARK 3 L TENSOR REMARK 3 L11: 1.1415 L22: 3.0995 REMARK 3 L33: 0.9168 L12: 1.5968 REMARK 3 L13: 0.2981 L23: 0.7161 REMARK 3 S TENSOR REMARK 3 S11: -0.0059 S12: 0.0152 S13: -0.0293 REMARK 3 S21: 0.0327 S22: -0.0280 S23: -0.1227 REMARK 3 S31: 0.0226 S32: -0.0114 S33: 0.0340 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 : NULL NULL NULL NULL REMARK 3 ORIGIN FOR THE GROUP (A): 13.0170 -5.8560 7.5610 REMARK 3 T TENSOR REMARK 3 T11: 0.4195 T22: 0.4838 REMARK 3 T33: 0.3713 T12: -0.0963 REMARK 3 T13: 0.0062 T23: 0.0943 REMARK 3 L TENSOR REMARK 3 L11: 4.9563 L22: 7.8792 REMARK 3 L33: 4.5692 L12: -5.1462 REMARK 3 L13: -3.2043 L23: 0.8133 REMARK 3 S TENSOR REMARK 3 S11: -0.3641 S12: 0.2287 S13: -0.3110 REMARK 3 S21: 0.0148 S22: 0.2341 S23: 0.3594 REMARK 3 S31: 0.5950 S32: -0.6543 S33: 0.1300 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 : NULL NULL NULL NULL REMARK 3 ORIGIN FOR THE GROUP (A): 9.6220 44.5920 19.7330 REMARK 3 T TENSOR REMARK 3 T11: 0.2221 T22: 0.5341 REMARK 3 T33: 0.7405 T12: -0.0023 REMARK 3 T13: -0.0854 T23: 0.1846 REMARK 3 L TENSOR REMARK 3 L11: 15.8281 L22: 15.0739 REMARK 3 L33: 14.2693 L12: 8.5180 REMARK 3 L13: 7.1729 L23: 0.5277 REMARK 3 S TENSOR REMARK 3 S11: -0.4938 S12: -0.4432 S13: -0.8216 REMARK 3 S21: -0.7074 S22: 0.2057 S23: 0.9354 REMARK 3 S31: -0.4257 S32: -0.1852 S33: 0.2881 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 : NULL NULL NULL NULL REMARK 3 ORIGIN FOR THE GROUP (A): 18.9230 52.8030 16.8600 REMARK 3 T TENSOR REMARK 3 T11: 0.2269 T22: 0.4747 REMARK 3 T33: 0.2117 T12: 0.0045 REMARK 3 T13: -0.0566 T23: -0.0116 REMARK 3 L TENSOR REMARK 3 L11: 5.1255 L22: 6.1746 REMARK 3 L33: 4.0689 L12: 0.6378 REMARK 3 L13: 0.0361 L23: 0.7487 REMARK 3 S TENSOR REMARK 3 S11: -0.0458 S12: 0.0474 S13: 0.9351 REMARK 3 S21: 0.3338 S22: -0.0269 S23: -0.2867 REMARK 3 S31: -0.8674 S32: -0.0322 S33: 0.0728 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 : NULL NULL NULL NULL REMARK 3 ORIGIN FOR THE GROUP (A): 25.3270 49.7370 14.2960 REMARK 3 T TENSOR REMARK 3 T11: 0.0867 T22: 0.4688 REMARK 3 T33: 0.1519 T12: -0.0529 REMARK 3 T13: -0.0352 T23: 0.0048 REMARK 3 L TENSOR REMARK 3 L11: 5.2579 L22: 2.7024 REMARK 3 L33: 3.1773 L12: -1.7277 REMARK 3 L13: -0.3629 L23: 1.0516 REMARK 3 S TENSOR REMARK 3 S11: -0.0487 S12: 0.1686 S13: 0.8499 REMARK 3 S21: 0.0293 S22: -0.0312 S23: -0.3366 REMARK 3 S31: -0.4414 S32: 0.2561 S33: 0.0800 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 : NULL NULL NULL NULL REMARK 3 ORIGIN FOR THE GROUP (A): 16.8810 50.1310 9.3680 REMARK 3 T TENSOR REMARK 3 T11: 0.0776 T22: 0.4507 REMARK 3 T33: 0.1479 T12: -0.0186 REMARK 3 T13: -0.0006 T23: 0.0355 REMARK 3 L TENSOR REMARK 3 L11: 3.4580 L22: 4.9226 REMARK 3 L33: 4.3562 L12: -0.5644 REMARK 3 L13: -0.8612 L23: 0.9031 REMARK 3 S TENSOR REMARK 3 S11: 0.0514 S12: 0.1123 S13: 0.5976 REMARK 3 S21: 0.1210 S22: -0.1080 S23: 0.3300 REMARK 3 S31: -0.5215 S32: -0.2152 S33: 0.0565 REMARK 3 REMARK 3 TLS GROUP : 14 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : NULL NULL NULL NULL REMARK 3 ORIGIN FOR THE GROUP (A): 14.0880 15.7910 63.0020 REMARK 3 T TENSOR REMARK 3 T11: 0.4261 T22: 0.4478 REMARK 3 T33: 0.3544 T12: 0.0262 REMARK 3 T13: -0.0271 T23: -0.0284 REMARK 3 L TENSOR REMARK 3 L11: 3.2710 L22: 13.1459 REMARK 3 L33: 4.0023 L12: -5.2532 REMARK 3 L13: -3.5589 L23: 6.0371 REMARK 3 S TENSOR REMARK 3 S11: -0.1463 S12: -0.1420 S13: -0.0450 REMARK 3 S21: 0.6538 S22: 0.0304 S23: 0.2322 REMARK 3 S31: 0.0016 S32: 0.0434 S33: 0.1158 REMARK 3 REMARK 3 TLS GROUP : 15 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : NULL NULL NULL NULL REMARK 3 ORIGIN FOR THE GROUP (A): 15.4300 12.9140 54.3410 REMARK 3 T TENSOR REMARK 3 T11: 0.3358 T22: 0.4519 REMARK 3 T33: 0.3377 T12: -0.0459 REMARK 3 T13: -0.0743 T23: -0.0394 REMARK 3 L TENSOR REMARK 3 L11: 6.8600 L22: 3.0953 REMARK 3 L33: 4.2472 L12: -1.7888 REMARK 3 L13: -0.6046 L23: -1.0840 REMARK 3 S TENSOR REMARK 3 S11: -0.0241 S12: -0.3774 S13: 0.7566 REMARK 3 S21: 0.4811 S22: -0.1110 S23: 0.3169 REMARK 3 S31: -0.7690 S32: -0.3605 S33: 0.1352 REMARK 3 REMARK 3 TLS GROUP : 16 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : NULL NULL NULL NULL REMARK 3 ORIGIN FOR THE GROUP (A): 16.5460 19.8270 51.1060 REMARK 3 T TENSOR REMARK 3 T11: 0.5271 T22: 0.5171 REMARK 3 T33: 0.4394 T12: -0.0373 REMARK 3 T13: -0.1290 T23: 0.0279 REMARK 3 L TENSOR REMARK 3 L11: 4.0524 L22: 6.0980 REMARK 3 L33: 4.2943 L12: -1.3769 REMARK 3 L13: -0.6588 L23: 0.5301 REMARK 3 S TENSOR REMARK 3 S11: 0.0899 S12: -0.0820 S13: 0.7973 REMARK 3 S21: 0.3780 S22: -0.1006 S23: 0.3904 REMARK 3 S31: -0.9328 S32: -0.2229 S33: 0.0107 REMARK 3 REMARK 3 TLS GROUP : 17 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : NULL NULL NULL NULL REMARK 3 ORIGIN FOR THE GROUP (A): 10.3710 13.5470 52.6400 REMARK 3 T TENSOR REMARK 3 T11: 0.3530 T22: 0.5447 REMARK 3 T33: 0.3626 T12: 0.0210 REMARK 3 T13: -0.0490 T23: -0.0458 REMARK 3 L TENSOR REMARK 3 L11: 2.5568 L22: 4.2159 REMARK 3 L33: 4.7804 L12: -0.3144 REMARK 3 L13: -1.9514 L23: 0.6184 REMARK 3 S TENSOR REMARK 3 S11: 0.0326 S12: -0.2278 S13: 0.5474 REMARK 3 S21: 0.6894 S22: -0.1047 S23: 0.6068 REMARK 3 S31: -0.7076 S32: -0.2072 S33: 0.0720 REMARK 3 REMARK 3 TLS GROUP : 18 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : NULL NULL NULL NULL REMARK 3 ORIGIN FOR THE GROUP (A): 18.4880 8.2590 26.2670 REMARK 3 T TENSOR REMARK 3 T11: 0.2600 T22: 0.8127 REMARK 3 T33: 0.3041 T12: -0.0405 REMARK 3 T13: -0.0575 T23: 0.2861 REMARK 3 L TENSOR REMARK 3 L11: 3.7065 L22: 0.6689 REMARK 3 L33: 1.4630 L12: -0.2536 REMARK 3 L13: 0.2961 L23: 0.8842 REMARK 3 S TENSOR REMARK 3 S11: -0.0440 S12: 0.8086 S13: 0.6484 REMARK 3 S21: -0.1590 S22: 0.0009 S23: -0.1632 REMARK 3 S31: -0.3873 S32: 0.2709 S33: 0.0431 REMARK 3 REMARK 3 TLS GROUP : 19 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : NULL NULL NULL NULL REMARK 3 ORIGIN FOR THE GROUP (A): 16.3510 3.5940 29.6940 REMARK 3 T TENSOR REMARK 3 T11: 0.1822 T22: 0.3048 REMARK 3 T33: 0.1082 T12: -0.0104 REMARK 3 T13: -0.0700 T23: 0.0904 REMARK 3 L TENSOR REMARK 3 L11: 8.4717 L22: 2.6252 REMARK 3 L33: 1.8482 L12: -1.2705 REMARK 3 L13: -0.8714 L23: 0.4523 REMARK 3 S TENSOR REMARK 3 S11: -0.0359 S12: 0.2643 S13: 0.0443 REMARK 3 S21: -0.0854 S22: -0.1222 S23: 0.0027 REMARK 3 S31: -0.0779 S32: 0.0632 S33: 0.1580 REMARK 3 REMARK 3 TLS GROUP : 20 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : NULL NULL NULL NULL REMARK 3 ORIGIN FOR THE GROUP (A): 4.6450 1.6240 31.1980 REMARK 3 T TENSOR REMARK 3 T11: 0.0949 T22: 0.4728 REMARK 3 T33: 0.0141 T12: 0.0540 REMARK 3 T13: 0.0044 T23: 0.0396 REMARK 3 L TENSOR REMARK 3 L11: 5.1137 L22: 2.9737 REMARK 3 L33: 3.1557 L12: -0.1061 REMARK 3 L13: 1.7608 L23: 0.0487 REMARK 3 S TENSOR REMARK 3 S11: -0.1164 S12: 0.0586 S13: 0.1406 REMARK 3 S21: 0.1474 S22: -0.0201 S23: -0.0985 REMARK 3 S31: -0.0353 S32: -0.0254 S33: 0.1365 REMARK 3 REMARK 3 TLS GROUP : 21 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : NULL NULL NULL NULL REMARK 3 ORIGIN FOR THE GROUP (A): -5.1790 -8.1250 25.8170 REMARK 3 T TENSOR REMARK 3 T11: 0.1859 T22: 0.4612 REMARK 3 T33: 0.1248 T12: 0.0932 REMARK 3 T13: 0.0439 T23: 0.0256 REMARK 3 L TENSOR REMARK 3 L11: 5.6837 L22: 0.9922 REMARK 3 L33: 2.3796 L12: 2.3130 REMARK 3 L13: 2.0639 L23: 0.5794 REMARK 3 S TENSOR REMARK 3 S11: -0.1314 S12: 0.0678 S13: -0.4867 REMARK 3 S21: -0.0944 S22: 0.0411 S23: -0.2221 REMARK 3 S31: 0.2012 S32: 0.1044 S33: 0.0903 REMARK 3 REMARK 3 TLS GROUP : 22 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : NULL NULL NULL NULL REMARK 3 ORIGIN FOR THE GROUP (A): 17.8500 6.0140 28.0760 REMARK 3 T TENSOR REMARK 3 T11: 0.2435 T22: 0.4935 REMARK 3 T33: 0.1401 T12: -0.0162 REMARK 3 T13: -0.0545 T23: 0.1388 REMARK 3 L TENSOR REMARK 3 L11: 9.6263 L22: 2.1964 REMARK 3 L33: 1.0883 L12: -2.2615 REMARK 3 L13: -0.7640 L23: 1.1532 REMARK 3 S TENSOR REMARK 3 S11: -0.1978 S12: 0.2472 S13: 0.5146 REMARK 3 S21: -0.0062 S22: 0.1325 S23: -0.2069 REMARK 3 S31: -0.0778 S32: 0.2679 S33: 0.0653 REMARK 3 REMARK 3 TLS GROUP : 23 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : NULL NULL NULL NULL REMARK 3 ORIGIN FOR THE GROUP (A): -18.8500 12.3140 9.8250 REMARK 3 T TENSOR REMARK 3 T11: 0.4217 T22: 0.4454 REMARK 3 T33: 0.2999 T12: 0.1234 REMARK 3 T13: 0.0107 T23: -0.0324 REMARK 3 L TENSOR REMARK 3 L11: 20.3654 L22: 1.8173 REMARK 3 L33: 7.6107 L12: 4.8554 REMARK 3 L13: 9.2133 L23: 1.0069 REMARK 3 S TENSOR REMARK 3 S11: -0.5599 S12: 0.2940 S13: 0.6895 REMARK 3 S21: -0.0293 S22: 0.1710 S23: 0.0410 REMARK 3 S31: -0.7494 S32: 0.1497 S33: 0.3888 REMARK 3 REMARK 3 TLS GROUP : 24 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : NULL NULL NULL NULL REMARK 3 ORIGIN FOR THE GROUP (A): -26.4550 2.3360 13.2570 REMARK 3 T TENSOR REMARK 3 T11: 0.0867 T22: 0.5623 REMARK 3 T33: 0.1130 T12: 0.0296 REMARK 3 T13: 0.0329 T23: 0.0032 REMARK 3 L TENSOR REMARK 3 L11: 5.5798 L22: 3.1578 REMARK 3 L33: 3.7430 L12: 1.0361 REMARK 3 L13: 0.6525 L23: -0.4614 REMARK 3 S TENSOR REMARK 3 S11: -0.0064 S12: 0.1104 S13: 0.1217 REMARK 3 S21: 0.1023 S22: -0.0363 S23: 0.5668 REMARK 3 S31: -0.0374 S32: -0.6009 S33: 0.0427 REMARK 3 REMARK 3 TLS GROUP : 25 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : NULL NULL NULL NULL REMARK 3 ORIGIN FOR THE GROUP (A): -21.8160 -3.8150 15.2860 REMARK 3 T TENSOR REMARK 3 T11: 0.0567 T22: 0.4711 REMARK 3 T33: 0.0916 T12: 0.0005 REMARK 3 T13: 0.0465 T23: -0.0085 REMARK 3 L TENSOR REMARK 3 L11: 3.8722 L22: 2.1428 REMARK 3 L33: 3.7409 L12: 0.0311 REMARK 3 L13: 0.0649 L23: -0.3558 REMARK 3 S TENSOR REMARK 3 S11: -0.0120 S12: 0.2093 S13: -0.1460 REMARK 3 S21: 0.1218 S22: -0.0238 S23: 0.2848 REMARK 3 S31: 0.3303 S32: -0.3792 S33: 0.0359 REMARK 3 REMARK 3 TLS GROUP : 26 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : NULL NULL NULL NULL REMARK 3 ORIGIN FOR THE GROUP (A): -25.1890 3.5640 20.1560 REMARK 3 T TENSOR REMARK 3 T11: 0.1225 T22: 0.5174 REMARK 3 T33: 0.1406 T12: 0.0049 REMARK 3 T13: 0.0489 T23: 0.0022 REMARK 3 L TENSOR REMARK 3 L11: 4.4003 L22: 1.6064 REMARK 3 L33: 2.5181 L12: -0.6457 REMARK 3 L13: 1.7216 L23: -0.1281 REMARK 3 S TENSOR REMARK 3 S11: -0.0817 S12: 0.1180 S13: 0.0309 REMARK 3 S21: 0.1411 S22: 0.0211 S23: 0.4513 REMARK 3 S31: -0.0244 S32: -0.3408 S33: 0.0606 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK BULK SOLVENT REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.00 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 THEIR REMARK 3 RIDING POSITIONS REMARK 4 REMARK 4 8OWT 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_1292129660. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 27-MAR-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 : DIAMOND REMARK 200 BEAMLINE : I04 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 XE 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2 REMARK 200 DATA SCALING SOFTWARE : DIALS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57917 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.140 REMARK 200 RESOLUTION RANGE LOW (A) : 58.780 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 13.70 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.14 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18 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 (%): 49.32 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NACL, POTASSIUM CITRATE PH 4.2, PEG REMARK 280 8000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 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 45.30450 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 58.79150 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.59850 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 58.79150 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 45.30450 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 48.59850 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: HEXAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 7520 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 40400 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: AAA, BBB, CCC, DDD, EEE, FFF 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 SER A 126 REMARK 465 SER A 127 REMARK 465 LYS A 128 REMARK 465 HIS A 129 REMARK 465 HIS A 130 REMARK 465 HIS A 131 REMARK 465 HIS A 132 REMARK 465 HIS A 133 REMARK 465 HIS A 134 REMARK 465 PRO B 330 REMARK 465 SER B 530 REMARK 465 THR B 531 REMARK 465 ASN B 532 REMARK 465 LYS B 533 REMARK 465 HIS B 534 REMARK 465 HIS B 535 REMARK 465 HIS B 536 REMARK 465 HIS B 537 REMARK 465 HIS B 538 REMARK 465 HIS B 539 REMARK 465 MET C 1 REMARK 465 ALA C 2 REMARK 465 GLN C 3 REMARK 465 SER C 129 REMARK 465 LYS C 130 REMARK 465 HIS C 131 REMARK 465 HIS C 132 REMARK 465 HIS C 133 REMARK 465 HIS C 134 REMARK 465 HIS C 135 REMARK 465 HIS C 136 REMARK 465 SER D 126 REMARK 465 SER D 127 REMARK 465 LYS D 128 REMARK 465 HIS D 129 REMARK 465 HIS D 130 REMARK 465 HIS D 131 REMARK 465 HIS D 132 REMARK 465 HIS D 133 REMARK 465 HIS D 134 REMARK 465 PRO E 330 REMARK 465 ASN E 331 REMARK 465 ILE E 332 REMARK 465 THR E 333 REMARK 465 SER E 530 REMARK 465 THR E 531 REMARK 465 ASN E 532 REMARK 465 LYS E 533 REMARK 465 HIS E 534 REMARK 465 HIS E 535 REMARK 465 HIS E 536 REMARK 465 HIS E 537 REMARK 465 HIS E 538 REMARK 465 HIS E 539 REMARK 465 MET F 1 REMARK 465 ALA F 2 REMARK 465 LYS F 130 REMARK 465 HIS F 131 REMARK 465 HIS F 132 REMARK 465 HIS F 133 REMARK 465 HIS F 134 REMARK 465 HIS F 135 REMARK 465 HIS F 136 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 THRAA 30 66.55 37.42 REMARK 500 ASNBB 334 170.45 78.70 REMARK 500 ALABB 352 45.32 -106.15 REMARK 500 LEUBB 368 -60.74 -91.44 REMARK 500 ASNBB 422 -62.34 -124.67 REMARK 500 THRDD 30 66.20 36.39 REMARK 500 ALAEE 352 44.75 -105.82 REMARK 500 LEUEE 368 -61.33 -90.55 REMARK 500 ASNEE 422 -61.20 -123.76 REMARK 500 HISEE 519 73.13 -68.68 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 SERBB 494 TYRBB 495 150.00 REMARK 500 REMARK 500 REMARK: NULL DBREF 8OWTAA 3 134 PDB 8OWT 8OWT 3 134 DBREF 8OWTBB 330 532 UNP P0DTC2 SPIKE_SARS2 330 532 DBREF 8OWTCC 1 136 PDB 8OWT 8OWT 1 136 DBREF 8OWTDD 3 134 PDB 8OWT 8OWT 3 134 DBREF 8OWTEE 330 532 UNP P0DTC2 SPIKE_SARS2 330 532 DBREF 8OWTFF 1 136 PDB 8OWT 8OWT 1 136 SEQADV 8OWT LYSBB 533 UNP P0DTC2 EXPRESSION TAG SEQADV 8OWT HISBB 534 UNP P0DTC2 EXPRESSION TAG SEQADV 8OWT HISBB 535 UNP P0DTC2 EXPRESSION TAG SEQADV 8OWT HISBB 536 UNP P0DTC2 EXPRESSION TAG SEQADV 8OWT HISBB 537 UNP P0DTC2 EXPRESSION TAG SEQADV 8OWT HISBB 538 UNP P0DTC2 EXPRESSION TAG SEQADV 8OWT HISBB 539 UNP P0DTC2 EXPRESSION TAG SEQADV 8OWT LYSEE 533 UNP P0DTC2 EXPRESSION TAG SEQADV 8OWT HISEE 534 UNP P0DTC2 EXPRESSION TAG SEQADV 8OWT HISEE 535 UNP P0DTC2 EXPRESSION TAG SEQADV 8OWT HISEE 536 UNP P0DTC2 EXPRESSION TAG SEQADV 8OWT HISEE 537 UNP P0DTC2 EXPRESSION TAG SEQADV 8OWT HISEE 538 UNP P0DTC2 EXPRESSION TAG SEQADV 8OWT HISEE 539 UNP P0DTC2 EXPRESSION TAG SEQRES 1AA 132 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2AA 132 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3AA 132 GLY THR PHE SER THR ALA ALA MET GLY TRP PHE ARG GLN SEQRES 4AA 132 ALA PRO GLY GLU GLU ARG GLU CYS VAL ALA SER ILE GLY SEQRES 5AA 132 TRP ARG GLY VAL ARG THR TRP TYR ALA ASP SER VAL LYS SEQRES 6AA 132 GLY ARG PHE THR ILE SER ARG ASP ASN PRO GLN ASN THR SEQRES 7AA 132 VAL TYR LEU GLN MET ASN ASN LEU LYS SER GLY ASP THR SEQRES 8AA 132 ALA VAL TYR TYR CYS ALA ALA SER VAL GLY ASN TYR GLY SEQRES 9AA 132 LEU PRO TRP ALA HIS PHE GLU TYR ASP PHE TRP GLY GLN SEQRES 10AA 132 GLY ILE GLN VAL THR VAL SER SER LYS HIS HIS HIS HIS SEQRES 11AA 132 HIS HIS SEQRES 1BB 210 PRO ASN ILE THR ASN LEU CYS PRO PHE GLY GLU VAL PHE SEQRES 2BB 210 ASN ALA THR ARG PHE ALA SER VAL TYR ALA TRP ASN ARG SEQRES 3BB 210 LYS ARG ILE SER ASN CYS VAL ALA ASP TYR SER VAL LEU SEQRES 4BB 210 TYR ASN SER ALA SER PHE SER THR PHE LYS CYS TYR GLY SEQRES 5BB 210 VAL SER PRO THR LYS LEU ASN ASP LEU CYS PHE THR ASN SEQRES 6BB 210 VAL TYR ALA ASP SER PHE VAL ILE ARG GLY ASP GLU VAL SEQRES 7BB 210 ARG GLN ILE ALA PRO GLY GLN THR GLY LYS ILE ALA ASP SEQRES 8BB 210 TYR ASN TYR LYS LEU PRO ASP ASP PHE THR GLY CYS VAL SEQRES 9BB 210 ILE ALA TRP ASN SER ASN ASN LEU ASP SER LYS VAL GLY SEQRES 10BB 210 GLY ASN TYR ASN TYR LEU TYR ARG LEU PHE ARG LYS SER SEQRES 11BB 210 ASN LEU LYS PRO PHE GLU ARG ASP ILE SER THR GLU ILE SEQRES 12BB 210 TYR GLN ALA GLY SER THR PRO CYS ASN GLY VAL GLU GLY SEQRES 13BB 210 PHE ASN CYS TYR PHE PRO LEU GLN SER TYR GLY PHE GLN SEQRES 14BB 210 PRO THR ASN GLY VAL GLY TYR GLN PRO TYR ARG VAL VAL SEQRES 15BB 210 VAL LEU SER PHE GLU LEU LEU HIS ALA PRO ALA THR VAL SEQRES 16BB 210 CYS GLY PRO LYS LYS SER THR ASN LYS HIS HIS HIS HIS SEQRES 17BB 210 HIS HIS SEQRES 1CC 136 MET ALA GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU SEQRES 2CC 136 VAL LYS THR GLY GLY SER LEU ARG LEU SER CYS ALA ALA SEQRES 3CC 136 SER GLY ARG THR PHE SER THR TYR SER MET GLY TRP PHE SEQRES 4CC 136 ARG GLN ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA GLY SEQRES 5CC 136 MET ARG TRP THR GLY SER SER THR PHE TYR SER ASP SER SEQRES 6CC 136 VAL LYS GLY ARG PHE THR VAL SER ARG ASN ASN ALA LYS SEQRES 7CC 136 ASP THR VAL TYR LEU HIS MET ASN SER LEU LYS PRO GLU SEQRES 8CC 136 ASP THR ALA VAL TYR TYR CYS ALA ILE THR THR ILE VAL SEQRES 9CC 136 ARG ALA TYR TYR THR GLU TYR THR GLU ALA ASP PHE GLY SEQRES 10CC 136 SER TRP GLY GLN GLY THR GLN VAL THR VAL SER SER LYS SEQRES 11CC 136 HIS HIS HIS HIS HIS HIS SEQRES 1DD 132 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2DD 132 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3DD 132 GLY THR PHE SER THR ALA ALA MET GLY TRP PHE ARG GLN SEQRES 4DD 132 ALA PRO GLY GLU GLU ARG GLU CYS VAL ALA SER ILE GLY SEQRES 5DD 132 TRP ARG GLY VAL ARG THR TRP TYR ALA ASP SER VAL LYS SEQRES 6DD 132 GLY ARG PHE THR ILE SER ARG ASP ASN PRO GLN ASN THR SEQRES 7DD 132 VAL TYR LEU GLN MET ASN ASN LEU LYS SER GLY ASP THR SEQRES 8DD 132 ALA VAL TYR TYR CYS ALA ALA SER VAL GLY ASN TYR GLY SEQRES 9DD 132 LEU PRO TRP ALA HIS PHE GLU TYR ASP PHE TRP GLY GLN SEQRES 10DD 132 GLY ILE GLN VAL THR VAL SER SER LYS HIS HIS HIS HIS SEQRES 11DD 132 HIS HIS SEQRES 1EE 210 PRO ASN ILE THR ASN LEU CYS PRO PHE GLY GLU VAL PHE SEQRES 2EE 210 ASN ALA THR ARG PHE ALA SER VAL TYR ALA TRP ASN ARG SEQRES 3EE 210 LYS ARG ILE SER ASN CYS VAL ALA ASP TYR SER VAL LEU SEQRES 4EE 210 TYR ASN SER ALA SER PHE SER THR PHE LYS CYS TYR GLY SEQRES 5EE 210 VAL SER PRO THR LYS LEU ASN ASP LEU CYS PHE THR ASN SEQRES 6EE 210 VAL TYR ALA ASP SER PHE VAL ILE ARG GLY ASP GLU VAL SEQRES 7EE 210 ARG GLN ILE ALA PRO GLY GLN THR GLY LYS ILE ALA ASP SEQRES 8EE 210 TYR ASN TYR LYS LEU PRO ASP ASP PHE THR GLY CYS VAL SEQRES 9EE 210 ILE ALA TRP ASN SER ASN ASN LEU ASP SER LYS VAL GLY SEQRES 10EE 210 GLY ASN TYR ASN TYR LEU TYR ARG LEU PHE ARG LYS SER SEQRES 11EE 210 ASN LEU LYS PRO PHE GLU ARG ASP ILE SER THR GLU ILE SEQRES 12EE 210 TYR GLN ALA GLY SER THR PRO CYS ASN GLY VAL GLU GLY SEQRES 13EE 210 PHE ASN CYS TYR PHE PRO LEU GLN SER TYR GLY PHE GLN SEQRES 14EE 210 PRO THR ASN GLY VAL GLY TYR GLN PRO TYR ARG VAL VAL SEQRES 15EE 210 VAL LEU SER PHE GLU LEU LEU HIS ALA PRO ALA THR VAL SEQRES 16EE 210 CYS GLY PRO LYS LYS SER THR ASN LYS HIS HIS HIS HIS SEQRES 17EE 210 HIS HIS SEQRES 1FF 136 MET ALA GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU SEQRES 2FF 136 VAL LYS THR GLY GLY SER LEU ARG LEU SER CYS ALA ALA SEQRES 3FF 136 SER GLY ARG THR PHE SER THR TYR SER MET GLY TRP PHE SEQRES 4FF 136 ARG GLN ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA GLY SEQRES 5FF 136 MET ARG TRP THR GLY SER SER THR PHE TYR SER ASP SER SEQRES 6FF 136 VAL LYS GLY ARG PHE THR VAL SER ARG ASN ASN ALA LYS SEQRES 7FF 136 ASP THR VAL TYR LEU HIS MET ASN SER LEU LYS PRO GLU SEQRES 8FF 136 ASP THR ALA VAL TYR TYR CYS ALA ILE THR THR ILE VAL SEQRES 9FF 136 ARG ALA TYR TYR THR GLU TYR THR GLU ALA ASP PHE GLY SEQRES 10FF 136 SER TRP GLY GLN GLY THR GLN VAL THR VAL SER SER LYS SEQRES 11FF 136 HIS HIS HIS HIS HIS HIS HET NAG BB 601 14 HET NAG EE 601 14 HET MES EE 602 12 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID FORMUL 7 NAG 2(C8 H15 N O6) FORMUL 9 MES C6 H13 N O4 S FORMUL 10 HOH *172(H2 O) HELIX 1 AA1 THRAA 30 ALAAA 34 5 5 HELIX 2 AA2 ASPAA 64 LYSAA 67 5 4 HELIX 3 AA3 ASNAA 76 GLNAA 78 5 3 HELIX 4 AA4 LYSAA 89 THRAA 93 5 5 HELIX 5 AA5 ALAAA 110 TYRAA 114 5 5 HELIX 6 AA6 PROBB 337 ASNBB 343 1 7 HELIX 7 AA7 SERBB 349 TRPBB 353 5 5 HELIX 8 AA8 TYRBB 365 ASNBB 370 1 6 HELIX 9 AA9 SERBB 383 ASPBB 389 5 7 HELIX 10 AB1 ASPBB 405 ILEBB 410 5 6 HELIX 11 AB2 GLYBB 416 ASNBB 422 1 7 HELIX 12 AB3 SERBB 438 SERBB 443 1 6 HELIX 13 AB4 GLYBB 502 TYRBB 505 5 4 HELIX 14 AB5 ARGCC 29 TYRCC 34 1 6 HELIX 15 AB6 LYSCC 89 THRCC 93 5 5 HELIX 16 AB7 TYRCC 107 TYRCC 111 5 5 HELIX 17 AB8 THRCC 112 PHECC 116 5 5 HELIX 18 AB9 THRDD 30 ALADD 34 5 5 HELIX 19 AC1 ASPDD 64 LYSDD 67 5 4 HELIX 20 AC2 ASNDD 76 GLNDD 78 5 3 HELIX 21 AC3 LYSDD 89 THRDD 93 5 5 HELIX 22 AC4 ALADD 110 TYRDD 114 5 5 HELIX 23 AC5 PROEE 337 ASNEE 343 1 7 HELIX 24 AC6 SEREE 349 TRPEE 353 5 5 HELIX 25 AC7 TYREE 365 ASNEE 370 1 6 HELIX 26 AC8 SEREE 383 ASPEE 389 5 7 HELIX 27 AC9 ASPEE 405 ILEEE 410 5 6 HELIX 28 AD1 GLYEE 416 ASNEE 422 1 7 HELIX 29 AD2 SEREE 438 SEREE 443 1 6 HELIX 30 AD3 GLYEE 502 TYREE 505 5 4 HELIX 31 AD4 ARGFF 29 TYRFF 34 1 6 HELIX 32 AD5 LYSFF 89 THRFF 93 5 5 HELIX 33 AD6 TYRFF 107 TYRFF 111 5 5 HELIX 34 AD7 THRFF 112 PHEFF 116 5 5 SHEET 1 AA1 4 GLNAA 5 SERAA 9 0 SHEET 2 AA1 4 LEUAA 20 SERAA 27 -1 O ALAAA 25 N VALAA 7 SHEET 3 AA1 4 THRAA 80 METAA 85 -1 O LEUAA 83 N LEUAA 22 SHEET 4 AA1 4 PHEAA 70 ASPAA 75 -1 N SERAA 73 O TYRAA 82 SHEET 1 AA2 6 GLYAA 12 LEUAA 13 0 SHEET 2 AA2 6 ILEAA 121 THRAA 124 1 O GLNAA 122 N GLYAA 12 SHEET 3 AA2 6 ALAAA 94 SERAA 101 -1 N TYRAA 96 O ILEAA 121 SHEET 4 AA2 6 ALAAA 35 GLNAA 41 -1 N PHEAA 39 O TYRAA 97 SHEET 5 AA2 6 GLUAA 48 ILEAA 53 -1 O ALAAA 51 N TRPAA 38 SHEET 6 AA2 6 THRAA 60 TYRAA 62 -1 O TRPAA 61 N SERAA 52 SHEET 1 AA3 4 GLYAA 12 LEUAA 13 0 SHEET 2 AA3 4 ILEAA 121 THRAA 124 1 O GLNAA 122 N GLYAA 12 SHEET 3 AA3 4 ALAAA 94 SERAA 101 -1 N TYRAA 96 O ILEAA 121 SHEET 4 AA3 4 PHEAA 116 TRPAA 117 -1 O PHEAA 116 N ALAAA 100 SHEET 1 AA4 5 ASNBB 354 ILEBB 358 0 SHEET 2 AA4 5 ASNBB 394 ARGBB 403 -1 O VALBB 395 N ILEBB 358 SHEET 3 AA4 5 PROBB 507 GLUBB 516 -1 O TYRBB 508 N ILEBB 402 SHEET 4 AA4 5 GLYBB 431 ASNBB 437 -1 N ILEBB 434 O VALBB 511 SHEET 5 AA4 5 THRBB 376 TYRBB 380 -1 N LYSBB 378 O VALBB 433 SHEET 1 AA5 3 CYSBB 361 VALBB 362 0 SHEET 2 AA5 3 VALBB 524 CYSBB 525 1 O CYSBB 525 N CYSBB 361 SHEET 3 AA5 3 CYSBB 391 PHEBB 392 -1 N PHEBB 392 O VALBB 524 SHEET 1 AA6 2 LEUBB 452 ARGBB 454 0 SHEET 2 AA6 2 LEUBB 492 SERBB 494 -1 O GLNBB 493 N TYRBB 453 SHEET 1 AA7 2 TYRBB 473 GLNBB 474 0 SHEET 2 AA7 2 CYSBB 488 TYRBB 489 -1 O TYRBB 489 N TYRBB 473 SHEET 1 AA8 4 VALCC 7 SERCC 9 0 SHEET 2 AA8 4 LEUCC 20 ALACC 25 -1 O SERCC 23 N SERCC 9 SHEET 3 AA8 4 THRCC 80 METCC 85 -1 O METCC 85 N LEUCC 20 SHEET 4 AA8 4 PHECC 70 ARGCC 74 -1 N THRCC 71 O HISCC 84 SHEET 1 AA9 6 GLYCC 12 VALCC 14 0 SHEET 2 AA9 6 THRCC 123 VALCC 127 1 O GLNCC 124 N GLYCC 12 SHEET 3 AA9 6 ALACC 94 ILECC 100 -1 N TYRCC 96 O THRCC 123 SHEET 4 AA9 6 METCC 36 GLNCC 41 -1 N PHECC 39 O TYRCC 97 SHEET 5 AA9 6 GLUCC 48 METCC 53 -1 O ALACC 51 N TRPCC 38 SHEET 6 AA9 6 THRCC 60 TYRCC 62 -1 O PHECC 61 N GLYCC 52 SHEET 1 AB1 4 GLNDD 5 SERDD 9 0 SHEET 2 AB1 4 LEUDD 20 SERDD 27 -1 O ALADD 25 N VALDD 7 SHEET 3 AB1 4 THRDD 80 METDD 85 -1 O LEUDD 83 N LEUDD 22 SHEET 4 AB1 4 PHEDD 70 ASPDD 75 -1 N SERDD 73 O TYRDD 82 SHEET 1 AB2 6 GLYDD 12 LEUDD 13 0 SHEET 2 AB2 6 ILEDD 121 THRDD 124 1 O GLNDD 122 N GLYDD 12 SHEET 3 AB2 6 ALADD 94 SERDD 101 -1 N TYRDD 96 O ILEDD 121 SHEET 4 AB2 6 ALADD 35 GLNDD 41 -1 N PHEDD 39 O TYRDD 97 SHEET 5 AB2 6 GLUDD 48 ILEDD 53 -1 O ALADD 51 N TRPDD 38 SHEET 6 AB2 6 THRDD 60 TYRDD 62 -1 O TRPDD 61 N SERDD 52 SHEET 1 AB3 4 GLYDD 12 LEUDD 13 0 SHEET 2 AB3 4 ILEDD 121 THRDD 124 1 O GLNDD 122 N GLYDD 12 SHEET 3 AB3 4 ALADD 94 SERDD 101 -1 N TYRDD 96 O ILEDD 121 SHEET 4 AB3 4 PHEDD 116 TRPDD 117 -1 O PHEDD 116 N ALADD 100 SHEET 1 AB4 5 ASNEE 354 ILEEE 358 0 SHEET 2 AB4 5 ASNEE 394 ARGEE 403 -1 O VALEE 395 N ILEEE 358 SHEET 3 AB4 5 PROEE 507 GLUEE 516 -1 O TYREE 508 N ILEEE 402 SHEET 4 AB4 5 GLYEE 431 ASNEE 437 -1 N ILEEE 434 O VALEE 511 SHEET 5 AB4 5 THREE 376 TYREE 380 -1 N LYSEE 378 O VALEE 433 SHEET 1 AB5 3 CYSEE 361 VALEE 362 0 SHEET 2 AB5 3 VALEE 524 CYSEE 525 1 O CYSEE 525 N CYSEE 361 SHEET 3 AB5 3 CYSEE 391 PHEEE 392 -1 N PHEEE 392 O VALEE 524 SHEET 1 AB6 2 LEUEE 452 ARGEE 454 0 SHEET 2 AB6 2 LEUEE 492 SEREE 494 -1 O GLNEE 493 N TYREE 453 SHEET 1 AB7 2 TYREE 473 GLNEE 474 0 SHEET 2 AB7 2 CYSEE 488 TYREE 489 -1 O TYREE 489 N TYREE 473 SHEET 1 AB8 4 VALFF 7 SERFF 9 0 SHEET 2 AB8 4 LEUFF 20 ALAFF 25 -1 O SERFF 23 N SERFF 9 SHEET 3 AB8 4 THRFF 80 METFF 85 -1 O METFF 85 N LEUFF 20 SHEET 4 AB8 4 PHEFF 70 ARGFF 74 -1 N THRFF 71 O HISFF 84 SHEET 1 AB9 6 GLYFF 12 LYSFF 15 0 SHEET 2 AB9 6 THRFF 123 SERFF 128 1 O GLNFF 124 N GLYFF 12 SHEET 3 AB9 6 ALAFF 94 ILEFF 100 -1 N TYRFF 96 O THRFF 123 SHEET 4 AB9 6 METFF 36 GLNFF 41 -1 N PHEFF 39 O TYRFF 97 SHEET 5 AB9 6 GLUFF 48 METFF 53 -1 O ALAFF 51 N TRPFF 38 SHEET 6 AB9 6 THRFF 60 TYRFF 62 -1 O PHEFF 61 N GLYFF 52 SSBOND 1 CYSAA 24 CYSAA 98 1555 1555 2.05 SSBOND 2 CYSBB 336 CYSBB 361 1555 1555 2.04 SSBOND 3 CYSBB 379 CYSBB 432 1555 1555 2.08 SSBOND 4 CYSBB 391 CYSBB 525 1555 1555 2.05 SSBOND 5 CYSBB 480 CYSBB 488 1555 1555 2.05 SSBOND 6 CYSCC 24 CYSCC 98 1555 1555 2.06 SSBOND 7 CYSDD 24 CYSDD 98 1555 1555 2.04 SSBOND 8 CYSEE 336 CYSEE 361 1555 1555 2.04 SSBOND 9 CYSEE 379 CYSEE 432 1555 1555 2.06 SSBOND 10 CYSEE 391 CYSEE 525 1555 1555 2.04 SSBOND 11 CYSEE 480 CYSEE 488 1555 1555 2.06 SSBOND 12 CYSFF 24 CYSFF 98 1555 1555 2.06 LINK ND2 ASNBB 343 C1 NAGBB 601 1555 1555 1.43 LINK ND2 ASNEE 343 C1 NAGEE 601 1555 1555 1.45 CRYST1 90.609 97.197 117.583 90.00 90.00 90.00 P 21 21 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 0.011036 0.000000 0.000000 0.00000 SCALE2 0.000000 0.010288 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008505 0.00000