HEADER VIRAL PROTEIN 06-MAY-20 6YZ7 TITLE H11-D4, SARS-COV-2 RBD, CR3022 TERNARY COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: SPIKE GLYCOPROTEIN; COMPND 3 CHAIN: A, E; COMPND 4 SYNONYM: S GLYCOPROTEIN,E2,PEPLOMER PROTEIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: ANTIBODY CR3022; COMPND 8 CHAIN: B, H; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: ANTIBODY LIGHT CHAIN; COMPND 12 CHAIN: C, L; COMPND 13 ENGINEERED: YES; COMPND 14 MOL_ID: 4; COMPND 15 MOLECULE: NANOBODY; COMPND 16 CHAIN: D, F; COMPND 17 ENGINEERED: YES; COMPND 18 OTHER_DETAILS: HIS TAG SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS SOURCE 3 2; SOURCE 4 ORGANISM_COMMON: 2019-NCOV; SOURCE 5 ORGANISM_TAXID: 2697049; SOURCE 6 GENE: S, 2; SOURCE 7 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 8 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 9 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 10 EXPRESSION_SYSTEM_CELL_LINE: HEK293S GNTI-; SOURCE 11 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-3022; SOURCE 12 MOL_ID: 2; SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 14 ORGANISM_COMMON: HUMAN; SOURCE 15 ORGANISM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 17 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 18 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 19 EXPRESSION_SYSTEM_CELL_LINE: HEK293T; SOURCE 20 MOL_ID: 3; SOURCE 21 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 22 ORGANISM_COMMON: HUMAN; SOURCE 23 ORGANISM_TAXID: 9606; SOURCE 24 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 25 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 26 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 27 MOL_ID: 4; SOURCE 28 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 29 ORGANISM_COMMON: LLAMA; SOURCE 30 ORGANISM_TAXID: 9844; SOURCE 31 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 32 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS ANTIBODY, NANOBODY COMPLEX, RBD, VIRAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR J.H.NAISMITH,J.REN,D.ZHOU,Y.ZHAO,D.I.STUART JRNL AUTH J.H.NAISMITH JRNL TITL STRUCTURAL CHARACTERISATION OF A NANOBODY DERIVED FROM A JRNL TITL 2 NAIVE LIBRARY THAT NEUTRALISES SARS-COV-2 JRNL REF TO BE PUBLISHED 2020 JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.30 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 : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 128.19 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 96.3 REMARK 3 NUMBER OF REFLECTIONS : 40954 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) : 0.238 REMARK 3 FREE R VALUE : 0.269 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.735 REMARK 3 FREE R VALUE TEST SET COUNT : 1939 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) : 3.30 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.39 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1472 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 49.71 REMARK 3 BIN R VALUE (WORKING SET) : 0.4150 REMARK 3 BIN FREE R VALUE SET COUNT : 66 REMARK 3 BIN FREE R VALUE : 0.3790 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 11686 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 28 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 144.1 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -1.97000 REMARK 3 B22 (A**2) : -1.97000 REMARK 3 B33 (A**2) : 3.94000 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): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.500 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.571 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 94.993 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.935 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.930 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 12028 ; 0.004 ; 0.013 REMARK 3 BOND LENGTHS OTHERS (A): 10650 ; 0.001 ; 0.017 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 16366 ; 1.390 ; 1.649 REMARK 3 BOND ANGLES OTHERS (DEGREES): 24822 ; 1.126 ; 1.574 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1504 ; 7.668 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 558 ;33.684 ;22.796 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1886 ;17.533 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 52 ;14.960 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1560 ; 0.049 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 13512 ; 0.004 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 2568 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1894 ; 0.206 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 62 ; 0.237 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5567 ; 0.169 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 237 ; 0.164 ; 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): 6045 ; 1.678 ; 9.809 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 6044 ; 1.679 ; 9.808 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7540 ; 2.879 ;14.712 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 7541 ; 2.879 ;14.713 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5982 ; 1.600 ; 9.993 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 5983 ; 1.600 ; 9.994 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 8826 ; 2.857 ;14.928 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 8827 ; 2.857 ;14.929 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 : 4 REMARK 3 REMARK 3 NCS GROUP NUMBER : 1 REMARK 3 CHAIN NAMES : Chains A E REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 2 REMARK 3 CHAIN NAMES : Chains B H REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 3 REMARK 3 CHAIN NAMES : Chains C L REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 4 REMARK 3 CHAIN NAMES : Chains D F REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 28 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 : A 334 A 398 REMARK 3 ORIGIN FOR THE GROUP (A): -55.3770 -30.5620 42.1650 REMARK 3 T TENSOR REMARK 3 T11: 0.4631 T22: 0.9313 REMARK 3 T33: 0.7458 T12: 0.2067 REMARK 3 T13: 0.1472 T23: 0.0554 REMARK 3 L TENSOR REMARK 3 L11: 7.3659 L22: 6.6534 REMARK 3 L33: 4.7085 L12: -2.6568 REMARK 3 L13: -4.4313 L23: 3.0509 REMARK 3 S TENSOR REMARK 3 S11: 0.1805 S12: -0.3527 S13: 1.6956 REMARK 3 S21: -0.8589 S22: 0.3432 S23: -0.5248 REMARK 3 S31: -0.6016 S32: -0.3872 S33: -0.5238 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 : A 399 A 493 REMARK 3 ORIGIN FOR THE GROUP (A): -60.4080 -42.2160 59.5660 REMARK 3 T TENSOR REMARK 3 T11: 0.5946 T22: 1.1689 REMARK 3 T33: 0.3966 T12: 0.1167 REMARK 3 T13: 0.1039 T23: 0.0617 REMARK 3 L TENSOR REMARK 3 L11: 3.5821 L22: 3.7845 REMARK 3 L33: 4.4103 L12: 0.9232 REMARK 3 L13: -2.6271 L23: 0.3642 REMARK 3 S TENSOR REMARK 3 S11: -0.1016 S12: -1.0358 S13: -0.1034 REMARK 3 S21: 1.0771 S22: 0.2374 S23: -0.1497 REMARK 3 S31: 0.6998 S32: -0.0586 S33: -0.1358 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 : A 494 A 528 REMARK 3 ORIGIN FOR THE GROUP (A): -54.2670 -34.4780 47.6050 REMARK 3 T TENSOR REMARK 3 T11: 0.2106 T22: 0.8388 REMARK 3 T33: 0.4238 T12: 0.1083 REMARK 3 T13: 0.2430 T23: -0.0669 REMARK 3 L TENSOR REMARK 3 L11: 6.5974 L22: 5.7711 REMARK 3 L33: 10.3103 L12: -0.4703 REMARK 3 L13: 4.9164 L23: -1.0515 REMARK 3 S TENSOR REMARK 3 S11: 0.2222 S12: 0.0143 S13: 0.8048 REMARK 3 S21: -0.2827 S22: -0.3062 S23: -0.1503 REMARK 3 S31: -0.0172 S32: 0.0335 S33: 0.0840 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 : B 0 B 143 REMARK 3 ORIGIN FOR THE GROUP (A): -35.9670 -55.0050 28.1100 REMARK 3 T TENSOR REMARK 3 T11: 0.2356 T22: 0.3703 REMARK 3 T33: 0.2196 T12: -0.0382 REMARK 3 T13: -0.1112 T23: 0.0795 REMARK 3 L TENSOR REMARK 3 L11: 2.7805 L22: 2.8859 REMARK 3 L33: 5.0671 L12: -0.6427 REMARK 3 L13: -2.0569 L23: 1.8810 REMARK 3 S TENSOR REMARK 3 S11: -0.0843 S12: -0.3390 S13: -0.3405 REMARK 3 S21: 0.0482 S22: 0.4072 S23: 0.2592 REMARK 3 S31: 0.5864 S32: 0.1540 S33: -0.3229 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 : B 144 B 219 REMARK 3 ORIGIN FOR THE GROUP (A): -21.3260 -62.3100 3.8940 REMARK 3 T TENSOR REMARK 3 T11: 1.0624 T22: 0.4927 REMARK 3 T33: 0.5663 T12: 0.0089 REMARK 3 T13: -0.2575 T23: -0.2275 REMARK 3 L TENSOR REMARK 3 L11: 4.8000 L22: 4.5180 REMARK 3 L33: 5.4693 L12: 0.1641 REMARK 3 L13: -0.2146 L23: -1.6880 REMARK 3 S TENSOR REMARK 3 S11: -0.4964 S12: -0.2188 S13: 0.4779 REMARK 3 S21: -0.1836 S22: -0.0324 S23: -0.5064 REMARK 3 S31: -0.4729 S32: 0.5245 S33: 0.5288 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 : C 1 C 113 REMARK 3 ORIGIN FOR THE GROUP (A): -54.4660 -49.4690 16.8770 REMARK 3 T TENSOR REMARK 3 T11: 0.1903 T22: 0.4044 REMARK 3 T33: 0.3306 T12: -0.0710 REMARK 3 T13: -0.1512 T23: 0.0478 REMARK 3 L TENSOR REMARK 3 L11: 3.3937 L22: 5.2558 REMARK 3 L33: 8.6397 L12: -1.1327 REMARK 3 L13: -0.8560 L23: 0.1408 REMARK 3 S TENSOR REMARK 3 S11: 0.3145 S12: 0.0610 S13: -0.5631 REMARK 3 S21: -0.4611 S22: -0.0364 S23: 0.9338 REMARK 3 S31: 0.0898 S32: -0.8631 S33: -0.2780 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 : C 114 C 219 REMARK 3 ORIGIN FOR THE GROUP (A): -32.2900 -71.2750 -5.2190 REMARK 3 T TENSOR REMARK 3 T11: 0.7983 T22: 0.3851 REMARK 3 T33: 0.3180 T12: -0.1589 REMARK 3 T13: -0.0858 T23: -0.2053 REMARK 3 L TENSOR REMARK 3 L11: 3.6834 L22: 8.8523 REMARK 3 L33: 3.9715 L12: -3.9389 REMARK 3 L13: 0.0460 L23: 1.0055 REMARK 3 S TENSOR REMARK 3 S11: -0.0797 S12: -0.1292 S13: -0.1720 REMARK 3 S21: -0.4094 S22: 0.0450 S23: -0.3587 REMARK 3 S31: 0.0797 S32: -0.0509 S33: 0.0347 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 : D 1 D 42 REMARK 3 ORIGIN FOR THE GROUP (A): -60.1950 -27.2090 88.5180 REMARK 3 T TENSOR REMARK 3 T11: 2.6458 T22: 2.9929 REMARK 3 T33: 1.2371 T12: -0.3482 REMARK 3 T13: 0.0915 T23: -0.4970 REMARK 3 L TENSOR REMARK 3 L11: 1.5746 L22: 4.0038 REMARK 3 L33: 0.8572 L12: -2.4941 REMARK 3 L13: -1.1441 L23: 1.8430 REMARK 3 S TENSOR REMARK 3 S11: -0.4197 S12: -0.1082 S13: -0.0806 REMARK 3 S21: 0.9266 S22: 0.0308 S23: 0.2628 REMARK 3 S31: 0.5461 S32: -0.1624 S33: 0.3889 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 : D 43 D 103 REMARK 3 ORIGIN FOR THE GROUP (A): -62.5460 -34.8320 88.1220 REMARK 3 T TENSOR REMARK 3 T11: 2.5035 T22: 2.9429 REMARK 3 T33: 1.1242 T12: -0.0195 REMARK 3 T13: 0.2266 T23: -0.4292 REMARK 3 L TENSOR REMARK 3 L11: 1.0142 L22: 0.3498 REMARK 3 L33: 0.5202 L12: 0.5009 REMARK 3 L13: 0.6158 L23: 0.1893 REMARK 3 S TENSOR REMARK 3 S11: 0.5110 S12: -0.7812 S13: 0.5297 REMARK 3 S21: 0.7008 S22: -0.5872 S23: 0.3174 REMARK 3 S31: -0.0245 S32: -0.2516 S33: 0.0762 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 : D 104 D 128 REMARK 3 ORIGIN FOR THE GROUP (A): -56.7230 -34.5680 87.2280 REMARK 3 T TENSOR REMARK 3 T11: 2.0234 T22: 2.1143 REMARK 3 T33: 0.7944 T12: -0.1349 REMARK 3 T13: 0.1048 T23: -0.1330 REMARK 3 L TENSOR REMARK 3 L11: 1.4054 L22: 2.0189 REMARK 3 L33: 0.0658 L12: 0.8449 REMARK 3 L13: -0.1904 L23: -0.3175 REMARK 3 S TENSOR REMARK 3 S11: 0.3227 S12: -0.1790 S13: 0.3625 REMARK 3 S21: 0.2958 S22: -0.2347 S23: 0.4205 REMARK 3 S31: -0.2141 S32: 0.0647 S33: -0.0880 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 : EE 334 EE 386 REMARK 3 ORIGIN FOR THE GROUP (A): -46.6100 -22.8480 2.4000 REMARK 3 T TENSOR REMARK 3 T11: 0.3292 T22: 0.3256 REMARK 3 T33: 0.3974 T12: 0.1961 REMARK 3 T13: 0.0743 T23: 0.1293 REMARK 3 L TENSOR REMARK 3 L11: 2.0964 L22: 6.6741 REMARK 3 L33: 7.9488 L12: -0.3363 REMARK 3 L13: 0.8500 L23: -1.4968 REMARK 3 S TENSOR REMARK 3 S11: 0.4019 S12: -0.1540 S13: -0.3645 REMARK 3 S21: 0.0206 S22: -0.0904 S23: 1.2801 REMARK 3 S31: -0.6056 S32: -0.6456 S33: -0.3115 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 : EE 387 EE 423 REMARK 3 ORIGIN FOR THE GROUP (A): -36.1950 -19.9770 -1.1030 REMARK 3 T TENSOR REMARK 3 T11: 0.2733 T22: 0.2509 REMARK 3 T33: 0.2271 T12: 0.1162 REMARK 3 T13: 0.0828 T23: 0.0185 REMARK 3 L TENSOR REMARK 3 L11: 4.2888 L22: 6.0627 REMARK 3 L33: 8.1297 L12: 0.4570 REMARK 3 L13: 0.9881 L23: 0.3154 REMARK 3 S TENSOR REMARK 3 S11: -0.0780 S12: -0.1960 S13: -0.2323 REMARK 3 S21: -0.0264 S22: 0.3723 S23: -0.0029 REMARK 3 S31: 0.2347 S32: 0.5514 S33: -0.2943 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 : EE 424 EE 515 REMARK 3 ORIGIN FOR THE GROUP (A): -34.9760 -17.4400 -12.9780 REMARK 3 T TENSOR REMARK 3 T11: 0.4506 T22: 0.3837 REMARK 3 T33: 0.0263 T12: 0.0289 REMARK 3 T13: 0.0780 T23: -0.0299 REMARK 3 L TENSOR REMARK 3 L11: 2.6087 L22: 3.9155 REMARK 3 L33: 5.5265 L12: 0.1828 REMARK 3 L13: -0.1091 L23: -2.3449 REMARK 3 S TENSOR REMARK 3 S11: 0.0102 S12: 0.2476 S13: -0.0933 REMARK 3 S21: -0.4895 S22: 0.2590 S23: 0.0212 REMARK 3 S31: -0.5938 S32: 0.5329 S33: -0.2691 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 : EE 516 EE 528 REMARK 3 ORIGIN FOR THE GROUP (A): -48.0370 -14.2760 15.5540 REMARK 3 T TENSOR REMARK 3 T11: 1.0633 T22: 0.9298 REMARK 3 T33: 0.9123 T12: 0.1367 REMARK 3 T13: 0.2143 T23: -0.1111 REMARK 3 L TENSOR REMARK 3 L11: 4.9019 L22: 8.4776 REMARK 3 L33: 13.3374 L12: -5.4758 REMARK 3 L13: 7.5365 L23: -10.0419 REMARK 3 S TENSOR REMARK 3 S11: -0.4790 S12: -0.9285 S13: 0.4616 REMARK 3 S21: 0.3924 S22: 0.3693 S23: 0.7057 REMARK 3 S31: 0.1901 S32: -0.8893 S33: 0.1097 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 : F 1 F 67 REMARK 3 ORIGIN FOR THE GROUP (A): -39.2730 -13.4190 -41.6480 REMARK 3 T TENSOR REMARK 3 T11: 0.5324 T22: 0.3326 REMARK 3 T33: 0.3196 T12: 0.0706 REMARK 3 T13: 0.0312 T23: 0.0357 REMARK 3 L TENSOR REMARK 3 L11: 4.2686 L22: 2.6393 REMARK 3 L33: 9.1706 L12: -0.9124 REMARK 3 L13: 0.0010 L23: 1.1319 REMARK 3 S TENSOR REMARK 3 S11: 0.0604 S12: -0.2508 S13: -0.3141 REMARK 3 S21: 0.0407 S22: 0.1145 S23: 0.4671 REMARK 3 S31: -0.4515 S32: -0.3597 S33: -0.1749 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 : F 68 F 128 REMARK 3 ORIGIN FOR THE GROUP (A): -38.2750 -13.5710 -41.1650 REMARK 3 T TENSOR REMARK 3 T11: 0.4776 T22: 0.3789 REMARK 3 T33: 0.2466 T12: 0.1206 REMARK 3 T13: 0.0700 T23: -0.0397 REMARK 3 L TENSOR REMARK 3 L11: 1.4734 L22: 3.1358 REMARK 3 L33: 10.1624 L12: -0.1329 REMARK 3 L13: 1.2640 L23: 0.8990 REMARK 3 S TENSOR REMARK 3 S11: 0.1378 S12: -0.1427 S13: -0.1111 REMARK 3 S21: -0.0738 S22: 0.0305 S23: 0.2805 REMARK 3 S31: -0.6603 S32: 0.0394 S33: -0.1683 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 : H 0 H 129 REMARK 3 ORIGIN FOR THE GROUP (A): -22.8100 -40.4530 16.8470 REMARK 3 T TENSOR REMARK 3 T11: 0.2476 T22: 0.2960 REMARK 3 T33: 0.0637 T12: 0.0343 REMARK 3 T13: 0.0468 T23: -0.0560 REMARK 3 L TENSOR REMARK 3 L11: 2.9787 L22: 3.8086 REMARK 3 L33: 4.4577 L12: -0.8579 REMARK 3 L13: 2.0651 L23: -2.9297 REMARK 3 S TENSOR REMARK 3 S11: 0.6177 S12: 0.0563 S13: -0.0042 REMARK 3 S21: -0.3061 S22: -0.4770 S23: -0.1607 REMARK 3 S31: 0.2232 S32: 0.4146 S33: -0.1407 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 : H 130 H 219 REMARK 3 ORIGIN FOR THE GROUP (A): -16.1870 -54.2900 45.2530 REMARK 3 T TENSOR REMARK 3 T11: 0.5251 T22: 0.9176 REMARK 3 T33: 0.5202 T12: -0.3069 REMARK 3 T13: -0.2098 T23: 0.2721 REMARK 3 L TENSOR REMARK 3 L11: 3.6002 L22: 3.5959 REMARK 3 L33: 6.1543 L12: -2.2155 REMARK 3 L13: 0.7137 L23: -0.6495 REMARK 3 S TENSOR REMARK 3 S11: 0.4697 S12: -0.8352 S13: -0.8912 REMARK 3 S21: 0.2945 S22: 0.0310 S23: 0.4851 REMARK 3 S31: 0.6584 S32: -0.4535 S33: -0.5007 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 : L 1 L 114 REMARK 3 ORIGIN FOR THE GROUP (A): -28.0290 -22.5260 30.2390 REMARK 3 T TENSOR REMARK 3 T11: 0.3051 T22: 0.3366 REMARK 3 T33: 0.1354 T12: -0.0521 REMARK 3 T13: 0.0793 T23: -0.1360 REMARK 3 L TENSOR REMARK 3 L11: 5.0720 L22: 4.1141 REMARK 3 L33: 6.8563 L12: -1.2448 REMARK 3 L13: 0.9174 L23: -1.7829 REMARK 3 S TENSOR REMARK 3 S11: 0.0089 S12: -0.4313 S13: 0.6287 REMARK 3 S21: 0.3993 S22: 0.0257 S23: -0.3094 REMARK 3 S31: -0.8755 S32: -0.2193 S33: -0.0346 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 : L 115 L 219 REMARK 3 ORIGIN FOR THE GROUP (A): -6.3220 -44.1130 52.7160 REMARK 3 T TENSOR REMARK 3 T11: 0.3336 T22: 0.8456 REMARK 3 T33: 0.1468 T12: -0.3074 REMARK 3 T13: -0.0433 T23: 0.2187 REMARK 3 L TENSOR REMARK 3 L11: 8.7459 L22: 6.7445 REMARK 3 L33: 4.1406 L12: -4.3604 REMARK 3 L13: 3.5194 L23: -1.1786 REMARK 3 S TENSOR REMARK 3 S11: 0.3969 S12: -1.0501 S13: -0.5119 REMARK 3 S21: 0.0148 S22: -0.1924 S23: -0.4298 REMARK 3 S31: -0.0925 S32: -0.3568 S33: -0.2045 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 : A 334 A 528 REMARK 3 ORIGIN FOR THE GROUP (A): -57.6380 -36.9750 51.6600 REMARK 3 T TENSOR REMARK 3 T11: 0.2855 T22: 0.8624 REMARK 3 T33: 0.3317 T12: 0.1148 REMARK 3 T13: 0.1049 T23: 0.0182 REMARK 3 L TENSOR REMARK 3 L11: 4.7078 L22: 4.0650 REMARK 3 L33: 4.0617 L12: 0.3466 REMARK 3 L13: -2.3920 L23: 1.0891 REMARK 3 S TENSOR REMARK 3 S11: 0.1268 S12: -0.5662 S13: 0.5436 REMARK 3 S21: 0.2249 S22: 0.1237 S23: -0.0942 REMARK 3 S31: 0.1270 S32: -0.2138 S33: -0.2504 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 : B 0 B 219 REMARK 3 ORIGIN FOR THE GROUP (A): -30.7650 -57.6080 19.5410 REMARK 3 T TENSOR REMARK 3 T11: 0.3675 T22: 0.3769 REMARK 3 T33: 0.2610 T12: -0.0690 REMARK 3 T13: -0.1564 T23: -0.0110 REMARK 3 L TENSOR REMARK 3 L11: 1.7108 L22: 2.1849 REMARK 3 L33: 3.8773 L12: -0.6951 REMARK 3 L13: -1.7744 L23: 1.0097 REMARK 3 S TENSOR REMARK 3 S11: -0.0257 S12: -0.0629 S13: -0.2108 REMARK 3 S21: -0.3620 S22: 0.3609 S23: 0.0548 REMARK 3 S31: 0.5117 S32: 0.2721 S33: -0.3353 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 : C 1 C 219 REMARK 3 ORIGIN FOR THE GROUP (A): -43.7780 -59.9820 6.2380 REMARK 3 T TENSOR REMARK 3 T11: 0.4513 T22: 0.4469 REMARK 3 T33: 0.4392 T12: -0.1425 REMARK 3 T13: -0.2283 T23: -0.0298 REMARK 3 L TENSOR REMARK 3 L11: 1.1542 L22: 4.1209 REMARK 3 L33: 3.5770 L12: -1.3410 REMARK 3 L13: -1.7021 L23: 2.0552 REMARK 3 S TENSOR REMARK 3 S11: 0.1349 S12: 0.1066 S13: -0.2961 REMARK 3 S21: -0.6863 S22: -0.0170 S23: 0.4178 REMARK 3 S31: 0.0837 S32: -0.3604 S33: -0.1179 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 : D 1 D 128 REMARK 3 ORIGIN FOR THE GROUP (A): -60.7060 -32.4480 88.0380 REMARK 3 T TENSOR REMARK 3 T11: 2.0844 T22: 2.4586 REMARK 3 T33: 0.9956 T12: -0.1756 REMARK 3 T13: 0.1618 T23: -0.3516 REMARK 3 L TENSOR REMARK 3 L11: 0.0566 L22: 0.0703 REMARK 3 L33: 0.0012 L12: 0.0455 REMARK 3 L13: -0.0057 L23: -0.0004 REMARK 3 S TENSOR REMARK 3 S11: 0.2280 S12: -0.2058 S13: 0.1683 REMARK 3 S21: 0.3428 S22: -0.1965 S23: 0.0112 REMARK 3 S31: 0.0024 S32: 0.0283 S33: -0.0316 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 : EE 334 EE 528 REMARK 3 ORIGIN FOR THE GROUP (A): -39.1790 -19.1930 -4.7330 REMARK 3 T TENSOR REMARK 3 T11: 0.2926 T22: 0.2681 REMARK 3 T33: 0.1165 T12: 0.1196 REMARK 3 T13: 0.0510 T23: 0.0147 REMARK 3 L TENSOR REMARK 3 L11: 2.2998 L22: 4.3479 REMARK 3 L33: 4.3510 L12: 0.6710 REMARK 3 L13: 0.6093 L23: -1.1858 REMARK 3 S TENSOR REMARK 3 S11: 0.0313 S12: -0.0765 S13: -0.1351 REMARK 3 S21: -0.0980 S22: 0.2405 S23: 0.3480 REMARK 3 S31: -0.5283 S32: 0.0845 S33: -0.2718 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 : F 1 F 128 REMARK 3 ORIGIN FOR THE GROUP (A): -38.8290 -13.4640 -41.3800 REMARK 3 T TENSOR REMARK 3 T11: 0.4215 T22: 0.2279 REMARK 3 T33: 0.2249 T12: 0.0809 REMARK 3 T13: 0.0489 T23: -0.0113 REMARK 3 L TENSOR REMARK 3 L11: 2.8021 L22: 1.9016 REMARK 3 L33: 9.3262 L12: -0.8709 REMARK 3 L13: 0.6770 L23: 0.5956 REMARK 3 S TENSOR REMARK 3 S11: 0.0465 S12: -0.1719 S13: -0.2281 REMARK 3 S21: 0.0000 S22: 0.1547 S23: 0.4082 REMARK 3 S31: -0.5881 S32: -0.2245 S33: -0.2012 REMARK 3 REMARK 3 TLS GROUP : 27 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : H 0 H 219 REMARK 3 ORIGIN FOR THE GROUP (A): -20.2180 -45.8580 27.8960 REMARK 3 T TENSOR REMARK 3 T11: 0.2533 T22: 0.3833 REMARK 3 T33: 0.1665 T12: -0.1243 REMARK 3 T13: -0.0507 T23: 0.0356 REMARK 3 L TENSOR REMARK 3 L11: 2.8475 L22: 2.4235 REMARK 3 L33: 3.9703 L12: -1.0990 REMARK 3 L13: 2.0925 L23: -1.8220 REMARK 3 S TENSOR REMARK 3 S11: 0.5415 S12: -0.4402 S13: -0.4394 REMARK 3 S21: 0.0189 S22: -0.2055 S23: -0.0275 REMARK 3 S31: 0.3040 S32: 0.1328 S33: -0.3360 REMARK 3 REMARK 3 TLS GROUP : 28 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : L 1 L 219 REMARK 3 ORIGIN FOR THE GROUP (A): -17.7300 -32.7620 40.9010 REMARK 3 T TENSOR REMARK 3 T11: 0.2938 T22: 0.4824 REMARK 3 T33: 0.0794 T12: -0.2047 REMARK 3 T13: 0.0419 T23: -0.0501 REMARK 3 L TENSOR REMARK 3 L11: 5.2998 L22: 2.2289 REMARK 3 L33: 4.0605 L12: -2.1719 REMARK 3 L13: 3.0614 L23: -2.3104 REMARK 3 S TENSOR REMARK 3 S11: -0.0055 S12: -0.8523 S13: 0.0684 REMARK 3 S21: 0.3194 S22: -0.0243 S23: -0.1608 REMARK 3 S31: -0.4402 S32: -0.2494 S33: 0.0298 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.10 REMARK 3 ION PROBE RADIUS : 1.00 REMARK 3 SHRINKAGE RADIUS : 1.00 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THEIR REMARK 3 RIDING POSITIONS REMARK 4 REMARK 4 6YZ7 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_1292108594. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 20-APR-20 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 : I03 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.978 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40954 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.290 REMARK 200 RESOLUTION RANGE LOW (A) : 128.187 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0 REMARK 200 DATA REDUNDANCY : 78.00 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 4.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.29 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.35 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: NULL REMARK 200 STARTING MODEL: 6YLA REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 68.59 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.92 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: THE BEST CRYSTALS WERE GROWN IN REMARK 280 CONDITION CONTAINING 0.1 M SODIUM CITRATE TRIBASIC DIHYDRATE, PH REMARK 280 5.0, 10% (W/V) POLYETHYLENE GLYCOL 6000., VAPOR DIFFUSION, REMARK 280 TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -Y,X,Z+1/4 REMARK 290 4555 Y,-X,Z+3/4 REMARK 290 5555 -X,Y,-Z REMARK 290 6555 X,-Y,-Z+1/2 REMARK 290 7555 Y,X,-Z+3/4 REMARK 290 8555 -Y,-X,-Z+1/4 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 114.65600 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 57.32800 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 171.98400 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 0.00000 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 114.65600 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 171.98400 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 57.32800 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, 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 PRO A 330 REMARK 465 ASN A 331 REMARK 465 ILE A 332 REMARK 465 THR A 333 REMARK 465 LYS A 529 REMARK 465 SER A 530 REMARK 465 THR A 531 REMARK 465 ASN A 532 REMARK 465 LYS A 533 REMARK 465 HIS A 534 REMARK 465 HIS A 535 REMARK 465 HIS A 536 REMARK 465 HIS A 537 REMARK 465 HIS A 538 REMARK 465 HIS A 539 REMARK 465 LYS B 133 REMARK 465 SER B 134 REMARK 465 THR B 135 REMARK 465 SER B 136 REMARK 465 CYS B 220 REMARK 465 ASP B 221 REMARK 465 LYS B 222 REMARK 465 HIS B 223 REMARK 465 HIS B 224 REMARK 465 HIS B 225 REMARK 465 HIS B 226 REMARK 465 HIS B 227 REMARK 465 HIS B 228 REMARK 465 CYS C 220 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 LYS E 529 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 LYS F 128 REMARK 465 HIS F 129 REMARK 465 HIS F 130 REMARK 465 HIS F 131 REMARK 465 HIS F 132 REMARK 465 HIS F 133 REMARK 465 HIS F 134 REMARK 465 LYS H 133 REMARK 465 SER H 134 REMARK 465 THR H 135 REMARK 465 SER H 136 REMARK 465 CYS H 220 REMARK 465 ASP H 221 REMARK 465 LYS H 222 REMARK 465 HIS H 223 REMARK 465 HIS H 224 REMARK 465 HIS H 225 REMARK 465 HIS H 226 REMARK 465 HIS H 227 REMARK 465 HIS H 228 REMARK 465 CYS L 220 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 OH TYR D 60 N ILE D 70 1.68 REMARK 500 OH TYR F 60 N ILE F 70 1.69 REMARK 500 OH TYR F 60 CA THR F 69 1.94 REMARK 500 OH TYR D 60 CA THR D 69 1.94 REMARK 500 OH TYR D 60 C THR D 69 2.02 REMARK 500 OH TYR F 60 C THR F 69 2.02 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 VAL A 341 -60.26 -123.99 REMARK 500 PHE A 377 64.67 -119.60 REMARK 500 ASP A 389 38.98 -151.57 REMARK 500 ALA A 411 144.28 -175.92 REMARK 500 ASN A 422 -64.04 -129.23 REMARK 500 ASP A 428 44.67 -92.02 REMARK 500 SER A 438 39.14 -140.02 REMARK 500 ARG A 457 140.13 -177.30 REMARK 500 ASN A 481 49.82 -105.23 REMARK 500 PHE A 486 109.84 -57.58 REMARK 500 LEU A 518 -152.31 -81.99 REMARK 500 THR A 523 23.52 -154.24 REMARK 500 PRO A 527 -82.26 -65.03 REMARK 500 PRO B 41 106.17 -45.38 REMARK 500 PHE B 64 -27.84 -143.55 REMARK 500 GLN B 65 -71.87 -15.58 REMARK 500 SER B 85 124.14 -172.53 REMARK 500 ALA B 92 174.71 177.92 REMARK 500 SER B 160 -16.66 86.96 REMARK 500 ALA B 162 52.18 -95.63 REMARK 500 LEU B 163 84.46 -171.46 REMARK 500 SER B 165 80.82 -53.93 REMARK 500 THR B 195 -73.07 -137.98 REMARK 500 ASN C 35 72.68 -39.82 REMARK 500 TRP C 56 50.74 26.51 REMARK 500 ALA C 57 -26.16 76.85 REMARK 500 SER C 58 -23.43 -148.32 REMARK 500 ILE C 81 75.27 -110.16 REMARK 500 ALA C 86 -73.37 -34.98 REMARK 500 ALA C 90 179.27 175.25 REMARK 500 ASN C 144 91.87 51.63 REMARK 500 GLU C 149 91.23 -62.76 REMARK 500 ASN C 158 53.32 38.71 REMARK 500 SER C 162 108.09 -165.65 REMARK 500 SER C 208 -74.47 -45.16 REMARK 500 ARG D 27 82.81 -65.73 REMARK 500 ARG D 67 -57.01 -125.97 REMARK 500 ALA D 110 -64.73 -98.46 REMARK 500 SER D 126 -148.14 -121.69 REMARK 500 VAL E 341 -60.03 -124.59 REMARK 500 SER E 373 58.88 -93.58 REMARK 500 PHE E 377 65.34 -119.18 REMARK 500 ASP E 389 40.01 -151.68 REMARK 500 ALA E 411 144.47 -176.88 REMARK 500 ASN E 422 -64.66 -128.81 REMARK 500 ASP E 428 48.27 -92.55 REMARK 500 SER E 438 39.53 -140.35 REMARK 500 ARG E 457 141.24 -178.88 REMARK 500 ASN E 481 49.19 -105.00 REMARK 500 LEU E 518 -149.25 -81.43 REMARK 500 REMARK 500 THIS ENTRY HAS 82 RAMACHANDRAN OUTLIERS. 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 GLY B 98 GLY B 99 149.23 REMARK 500 REMARK 500 REMARK: NULL DBREF 6YZ7 A 330 532 UNP P0DTC2 SPIKE_SARS2 330 532 DBREF 6YZ7 B 0 228 PDB 6YZ7 6YZ7 0 228 DBREF 6YZ7 C 1 220 PDB 6YZ7 6YZ7 1 220 DBREF 6YZ7 D 1 134 PDB 6YZ7 6YZ7 1 134 DBREF 6YZ7 E 330 532 UNP P0DTC2 SPIKE_SARS2 330 532 DBREF 6YZ7 F 1 134 PDB 6YZ7 6YZ7 1 134 DBREF 6YZ7 H 0 228 PDB 6YZ7 6YZ7 0 228 DBREF 6YZ7 L 1 220 PDB 6YZ7 6YZ7 1 220 SEQADV 6YZ7 LYS A 533 UNP P0DTC2 EXPRESSION TAG SEQADV 6YZ7 HIS A 534 UNP P0DTC2 EXPRESSION TAG SEQADV 6YZ7 HIS A 535 UNP P0DTC2 EXPRESSION TAG SEQADV 6YZ7 HIS A 536 UNP P0DTC2 EXPRESSION TAG SEQADV 6YZ7 HIS A 537 UNP P0DTC2 EXPRESSION TAG SEQADV 6YZ7 HIS A 538 UNP P0DTC2 EXPRESSION TAG SEQADV 6YZ7 HIS A 539 UNP P0DTC2 EXPRESSION TAG SEQADV 6YZ7 LYS E 533 UNP P0DTC2 EXPRESSION TAG SEQADV 6YZ7 HIS E 534 UNP P0DTC2 EXPRESSION TAG SEQADV 6YZ7 HIS E 535 UNP P0DTC2 EXPRESSION TAG SEQADV 6YZ7 HIS E 536 UNP P0DTC2 EXPRESSION TAG SEQADV 6YZ7 HIS E 537 UNP P0DTC2 EXPRESSION TAG SEQADV 6YZ7 HIS E 538 UNP P0DTC2 EXPRESSION TAG SEQADV 6YZ7 HIS E 539 UNP P0DTC2 EXPRESSION TAG SEQRES 1 A 210 PRO ASN ILE THR ASN LEU CYS PRO PHE GLY GLU VAL PHE SEQRES 2 A 210 ASN ALA THR ARG PHE ALA SER VAL TYR ALA TRP ASN ARG SEQRES 3 A 210 LYS ARG ILE SER ASN CYS VAL ALA ASP TYR SER VAL LEU SEQRES 4 A 210 TYR ASN SER ALA SER PHE SER THR PHE LYS CYS TYR GLY SEQRES 5 A 210 VAL SER PRO THR LYS LEU ASN ASP LEU CYS PHE THR ASN SEQRES 6 A 210 VAL TYR ALA ASP SER PHE VAL ILE ARG GLY ASP GLU VAL SEQRES 7 A 210 ARG GLN ILE ALA PRO GLY GLN THR GLY LYS ILE ALA ASP SEQRES 8 A 210 TYR ASN TYR LYS LEU PRO ASP ASP PHE THR GLY CYS VAL SEQRES 9 A 210 ILE ALA TRP ASN SER ASN ASN LEU ASP SER LYS VAL GLY SEQRES 10 A 210 GLY ASN TYR ASN TYR LEU TYR ARG LEU PHE ARG LYS SER SEQRES 11 A 210 ASN LEU LYS PRO PHE GLU ARG ASP ILE SER THR GLU ILE SEQRES 12 A 210 TYR GLN ALA GLY SER THR PRO CYS ASN GLY VAL GLU GLY SEQRES 13 A 210 PHE ASN CYS TYR PHE PRO LEU GLN SER TYR GLY PHE GLN SEQRES 14 A 210 PRO THR ASN GLY VAL GLY TYR GLN PRO TYR ARG VAL VAL SEQRES 15 A 210 VAL LEU SER PHE GLU LEU LEU HIS ALA PRO ALA THR VAL SEQRES 16 A 210 CYS GLY PRO LYS LYS SER THR ASN LYS HIS HIS HIS HIS SEQRES 17 A 210 HIS HIS SEQRES 1 B 229 THR GLN MET GLN LEU VAL GLN SER GLY THR GLU VAL LYS SEQRES 2 B 229 LYS PRO GLY GLU SER LEU LYS ILE SER CYS LYS GLY SER SEQRES 3 B 229 GLY TYR GLY PHE ILE THR TYR TRP ILE GLY TRP VAL ARG SEQRES 4 B 229 GLN MET PRO GLY LYS GLY LEU GLU TRP MET GLY ILE ILE SEQRES 5 B 229 TYR PRO GLY ASP SER GLU THR ARG TYR SER PRO SER PHE SEQRES 6 B 229 GLN GLY GLN VAL THR ILE SER ALA ASP LYS SER ILE ASN SEQRES 7 B 229 THR ALA TYR LEU GLN TRP SER SER LEU LYS ALA SER ASP SEQRES 8 B 229 THR ALA ILE TYR TYR CYS ALA GLY GLY SER GLY ILE SER SEQRES 9 B 229 THR PRO MET ASP VAL TRP GLY GLN GLY THR THR VAL THR SEQRES 10 B 229 VAL ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 11 B 229 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU SEQRES 12 B 229 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR SEQRES 13 B 229 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS SEQRES 14 B 229 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER SEQRES 15 B 229 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY SEQRES 16 B 229 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER SEQRES 17 B 229 ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 18 B 229 ASP LYS HIS HIS HIS HIS HIS HIS SEQRES 1 C 220 ASP ILE GLN LEU THR GLN SER PRO ASP SER LEU ALA VAL SEQRES 2 C 220 SER LEU GLY GLU ARG ALA THR ILE ASN CYS LYS SER SER SEQRES 3 C 220 GLN SER VAL LEU TYR SER SER ILE ASN LYS ASN TYR LEU SEQRES 4 C 220 ALA TRP TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU SEQRES 5 C 220 LEU ILE TYR TRP ALA SER THR ARG GLU SER GLY VAL PRO SEQRES 6 C 220 ASP ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR SEQRES 7 C 220 LEU THR ILE SER SER LEU GLN ALA GLU ASP VAL ALA VAL SEQRES 8 C 220 TYR TYR CYS GLN GLN TYR TYR SER THR PRO TYR THR PHE SEQRES 9 C 220 GLY GLN GLY THR LYS VAL GLU ILE LYS ARG THR VAL ALA SEQRES 10 C 220 ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN SEQRES 11 C 220 LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN SEQRES 12 C 220 ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL SEQRES 13 C 220 ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL SEQRES 14 C 220 THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SEQRES 15 C 220 SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS SEQRES 16 C 220 LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SEQRES 17 C 220 SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 D 134 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU MET GLN SEQRES 2 D 134 ALA GLY GLY SER LEU ARG LEU SER CYS ALA VAL SER GLY SEQRES 3 D 134 ARG THR PHE SER THR ALA ALA MET GLY TRP PHE ARG GLN SEQRES 4 D 134 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA ILE ARG SEQRES 5 D 134 TRP SER GLY GLY SER ALA TYR TYR ALA ASP SER VAL LYS SEQRES 6 D 134 GLY ARG PHE THR ILE SER ARG ASP LYS ALA LYS ASN THR SEQRES 7 D 134 VAL TYR LEU GLN MET ASN SER LEU LYS TYR GLU ASP THR SEQRES 8 D 134 ALA VAL TYR TYR CYS ALA ARG THR GLU ASN VAL ARG SER SEQRES 9 D 134 LEU LEU SER ASP TYR ALA THR TRP PRO TYR ASP TYR TRP SEQRES 10 D 134 GLY GLN GLY THR GLN VAL THR VAL SER SER LYS HIS HIS SEQRES 11 D 134 HIS HIS HIS HIS SEQRES 1 E 210 PRO ASN ILE THR ASN LEU CYS PRO PHE GLY GLU VAL PHE SEQRES 2 E 210 ASN ALA THR ARG PHE ALA SER VAL TYR ALA TRP ASN ARG SEQRES 3 E 210 LYS ARG ILE SER ASN CYS VAL ALA ASP TYR SER VAL LEU SEQRES 4 E 210 TYR ASN SER ALA SER PHE SER THR PHE LYS CYS TYR GLY SEQRES 5 E 210 VAL SER PRO THR LYS LEU ASN ASP LEU CYS PHE THR ASN SEQRES 6 E 210 VAL TYR ALA ASP SER PHE VAL ILE ARG GLY ASP GLU VAL SEQRES 7 E 210 ARG GLN ILE ALA PRO GLY GLN THR GLY LYS ILE ALA ASP SEQRES 8 E 210 TYR ASN TYR LYS LEU PRO ASP ASP PHE THR GLY CYS VAL SEQRES 9 E 210 ILE ALA TRP ASN SER ASN ASN LEU ASP SER LYS VAL GLY SEQRES 10 E 210 GLY ASN TYR ASN TYR LEU TYR ARG LEU PHE ARG LYS SER SEQRES 11 E 210 ASN LEU LYS PRO PHE GLU ARG ASP ILE SER THR GLU ILE SEQRES 12 E 210 TYR GLN ALA GLY SER THR PRO CYS ASN GLY VAL GLU GLY SEQRES 13 E 210 PHE ASN CYS TYR PHE PRO LEU GLN SER TYR GLY PHE GLN SEQRES 14 E 210 PRO THR ASN GLY VAL GLY TYR GLN PRO TYR ARG VAL VAL SEQRES 15 E 210 VAL LEU SER PHE GLU LEU LEU HIS ALA PRO ALA THR VAL SEQRES 16 E 210 CYS GLY PRO LYS LYS SER THR ASN LYS HIS HIS HIS HIS SEQRES 17 E 210 HIS HIS SEQRES 1 F 134 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU MET GLN SEQRES 2 F 134 ALA GLY GLY SER LEU ARG LEU SER CYS ALA VAL SER GLY SEQRES 3 F 134 ARG THR PHE SER THR ALA ALA MET GLY TRP PHE ARG GLN SEQRES 4 F 134 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA ILE ARG SEQRES 5 F 134 TRP SER GLY GLY SER ALA TYR TYR ALA ASP SER VAL LYS SEQRES 6 F 134 GLY ARG PHE THR ILE SER ARG ASP LYS ALA LYS ASN THR SEQRES 7 F 134 VAL TYR LEU GLN MET ASN SER LEU LYS TYR GLU ASP THR SEQRES 8 F 134 ALA VAL TYR TYR CYS ALA ARG THR GLU ASN VAL ARG SER SEQRES 9 F 134 LEU LEU SER ASP TYR ALA THR TRP PRO TYR ASP TYR TRP SEQRES 10 F 134 GLY GLN GLY THR GLN VAL THR VAL SER SER LYS HIS HIS SEQRES 11 F 134 HIS HIS HIS HIS SEQRES 1 H 229 THR GLN MET GLN LEU VAL GLN SER GLY THR GLU VAL LYS SEQRES 2 H 229 LYS PRO GLY GLU SER LEU LYS ILE SER CYS LYS GLY SER SEQRES 3 H 229 GLY TYR GLY PHE ILE THR TYR TRP ILE GLY TRP VAL ARG SEQRES 4 H 229 GLN MET PRO GLY LYS GLY LEU GLU TRP MET GLY ILE ILE SEQRES 5 H 229 TYR PRO GLY ASP SER GLU THR ARG TYR SER PRO SER PHE SEQRES 6 H 229 GLN GLY GLN VAL THR ILE SER ALA ASP LYS SER ILE ASN SEQRES 7 H 229 THR ALA TYR LEU GLN TRP SER SER LEU LYS ALA SER ASP SEQRES 8 H 229 THR ALA ILE TYR TYR CYS ALA GLY GLY SER GLY ILE SER SEQRES 9 H 229 THR PRO MET ASP VAL TRP GLY GLN GLY THR THR VAL THR SEQRES 10 H 229 VAL ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 11 H 229 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU SEQRES 12 H 229 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR SEQRES 13 H 229 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS SEQRES 14 H 229 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER SEQRES 15 H 229 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY SEQRES 16 H 229 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER SEQRES 17 H 229 ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 18 H 229 ASP LYS HIS HIS HIS HIS HIS HIS SEQRES 1 L 220 ASP ILE GLN LEU THR GLN SER PRO ASP SER LEU ALA VAL SEQRES 2 L 220 SER LEU GLY GLU ARG ALA THR ILE ASN CYS LYS SER SER SEQRES 3 L 220 GLN SER VAL LEU TYR SER SER ILE ASN LYS ASN TYR LEU SEQRES 4 L 220 ALA TRP TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU SEQRES 5 L 220 LEU ILE TYR TRP ALA SER THR ARG GLU SER GLY VAL PRO SEQRES 6 L 220 ASP ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR SEQRES 7 L 220 LEU THR ILE SER SER LEU GLN ALA GLU ASP VAL ALA VAL SEQRES 8 L 220 TYR TYR CYS GLN GLN TYR TYR SER THR PRO TYR THR PHE SEQRES 9 L 220 GLY GLN GLY THR LYS VAL GLU ILE LYS ARG THR VAL ALA SEQRES 10 L 220 ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN SEQRES 11 L 220 LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN SEQRES 12 L 220 ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL SEQRES 13 L 220 ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL SEQRES 14 L 220 THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SEQRES 15 L 220 SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS SEQRES 16 L 220 LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SEQRES 17 L 220 SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS HET NAG A 601 14 HET NAG E 601 14 HETNAM NAG N-ACETYL-D-GLUCOSAMINE FORMUL 9 NAG 2(C8 H15 N O6) HELIX 1 AA1 PHE A 338 ASN A 343 1 6 HELIX 2 AA2 SER A 349 TRP A 353 5 5 HELIX 3 AA3 TYR A 365 ASN A 370 1 6 HELIX 4 AA4 LYS A 386 LEU A 390 5 5 HELIX 5 AA5 ASP A 405 ILE A 410 5 6 HELIX 6 AA6 GLY A 416 ASN A 422 1 7 HELIX 7 AA7 SER A 438 SER A 443 1 6 HELIX 8 AA8 GLY A 502 TYR A 505 5 4 HELIX 9 AA9 GLY B 28 ILE B 30 5 3 HELIX 10 AB1 LYS B 74 ILE B 76 5 3 HELIX 11 AB2 SER B 160 ALA B 162 5 3 HELIX 12 AB3 SER B 191 LEU B 193 5 3 HELIX 13 AB4 GLN C 85 VAL C 89 5 5 HELIX 14 AB5 SER C 127 GLY C 134 1 8 HELIX 15 AB6 LYS C 189 GLU C 193 1 5 HELIX 16 AB7 ARG D 27 THR D 31 5 5 HELIX 17 AB8 LYS D 87 THR D 91 5 5 HELIX 18 AB9 LEU D 105 ALA D 110 5 6 HELIX 19 AC1 PHE E 338 ASN E 343 1 6 HELIX 20 AC2 SER E 349 TRP E 353 5 5 HELIX 21 AC3 TYR E 365 ASN E 370 1 6 HELIX 22 AC4 LYS E 386 LEU E 390 5 5 HELIX 23 AC5 ASP E 405 ILE E 410 5 6 HELIX 24 AC6 GLY E 416 ASN E 422 1 7 HELIX 25 AC7 SER E 438 SER E 443 1 6 HELIX 26 AC8 GLY E 502 TYR E 505 5 4 HELIX 27 AC9 ARG F 27 THR F 31 5 5 HELIX 28 AD1 LYS F 87 THR F 91 5 5 HELIX 29 AD2 SER F 107 TRP F 112 1 6 HELIX 30 AD3 GLY H 28 ILE H 30 5 3 HELIX 31 AD4 LYS H 74 ILE H 76 5 3 HELIX 32 AD5 SER H 160 ALA H 162 5 3 HELIX 33 AD6 SER H 191 LEU H 193 5 3 HELIX 34 AD7 GLN L 85 VAL L 89 5 5 HELIX 35 AD8 SER L 127 GLY L 134 1 8 HELIX 36 AD9 LYS L 189 GLU L 193 1 5 SHEET 1 AA1 5 ASN A 354 ILE A 358 0 SHEET 2 AA1 5 ASN A 394 ARG A 403 -1 O VAL A 395 N ILE A 358 SHEET 3 AA1 5 PRO A 507 GLU A 516 -1 O VAL A 510 N PHE A 400 SHEET 4 AA1 5 GLY A 431 ASN A 437 -1 N ILE A 434 O VAL A 511 SHEET 5 AA1 5 THR A 376 TYR A 380 -1 N TYR A 380 O GLY A 431 SHEET 1 AA2 2 LEU A 452 ARG A 454 0 SHEET 2 AA2 2 LEU A 492 SER A 494 -1 O GLN A 493 N TYR A 453 SHEET 1 AA3 2 TYR A 473 GLN A 474 0 SHEET 2 AA3 2 CYS A 488 TYR A 489 -1 O TYR A 489 N TYR A 473 SHEET 1 AA4 4 MET B 2 GLN B 6 0 SHEET 2 AA4 4 LEU B 18 GLY B 26 -1 O LYS B 23 N VAL B 5 SHEET 3 AA4 4 THR B 78 TRP B 83 -1 O ALA B 79 N CYS B 22 SHEET 4 AA4 4 VAL B 68 ASP B 73 -1 N SER B 71 O TYR B 80 SHEET 1 AA5 6 GLU B 10 LYS B 12 0 SHEET 2 AA5 6 THR B 113 VAL B 117 1 O THR B 116 N GLU B 10 SHEET 3 AA5 6 ALA B 92 SER B 100 -1 N TYR B 94 O THR B 113 SHEET 4 AA5 6 TYR B 32 GLN B 39 -1 N TRP B 33 O GLY B 99 SHEET 5 AA5 6 LEU B 45 TYR B 52 -1 O GLU B 46 N ARG B 38 SHEET 6 AA5 6 GLU B 57 TYR B 60 -1 O ARG B 59 N ILE B 50 SHEET 1 AA6 4 GLU B 10 LYS B 12 0 SHEET 2 AA6 4 THR B 113 VAL B 117 1 O THR B 116 N GLU B 10 SHEET 3 AA6 4 ALA B 92 SER B 100 -1 N TYR B 94 O THR B 113 SHEET 4 AA6 4 VAL B 108 TRP B 109 -1 O VAL B 108 N GLY B 98 SHEET 1 AA7 4 SER B 124 LEU B 128 0 SHEET 2 AA7 4 THR B 139 TYR B 149 -1 O LEU B 145 N PHE B 126 SHEET 3 AA7 4 TYR B 180 PRO B 189 -1 O SER B 184 N CYS B 144 SHEET 4 AA7 4 VAL B 167 THR B 169 -1 N HIS B 168 O VAL B 185 SHEET 1 AA8 4 SER B 124 LEU B 128 0 SHEET 2 AA8 4 THR B 139 TYR B 149 -1 O LEU B 145 N PHE B 126 SHEET 3 AA8 4 TYR B 180 PRO B 189 -1 O SER B 184 N CYS B 144 SHEET 4 AA8 4 VAL B 173 LEU B 174 -1 N VAL B 173 O SER B 181 SHEET 1 AA9 3 VAL B 154 TRP B 158 0 SHEET 2 AA9 3 TYR B 198 HIS B 204 -1 O ASN B 201 N SER B 157 SHEET 3 AA9 3 THR B 209 VAL B 215 -1 O VAL B 211 N VAL B 202 SHEET 1 AB1 4 LEU C 4 SER C 7 0 SHEET 2 AB1 4 THR C 20 SER C 25 -1 O LYS C 24 N THR C 5 SHEET 3 AB1 4 ASP C 76 ILE C 81 -1 O PHE C 77 N CYS C 23 SHEET 4 AB1 4 PHE C 68 SER C 73 -1 N SER C 69 O THR C 80 SHEET 1 AB2 6 SER C 10 SER C 14 0 SHEET 2 AB2 6 THR C 108 LYS C 113 1 O GLU C 111 N LEU C 11 SHEET 3 AB2 6 ALA C 90 GLN C 96 -1 N ALA C 90 O VAL C 110 SHEET 4 AB2 6 LEU C 39 GLN C 44 -1 N TYR C 42 O TYR C 93 SHEET 5 AB2 6 LYS C 51 TYR C 55 -1 O LYS C 51 N GLN C 43 SHEET 6 AB2 6 THR C 59 ARG C 60 -1 O THR C 59 N TYR C 55 SHEET 1 AB3 4 SER C 10 SER C 14 0 SHEET 2 AB3 4 THR C 108 LYS C 113 1 O GLU C 111 N LEU C 11 SHEET 3 AB3 4 ALA C 90 GLN C 96 -1 N ALA C 90 O VAL C 110 SHEET 4 AB3 4 THR C 103 PHE C 104 -1 O THR C 103 N GLN C 96 SHEET 1 AB4 2 LEU C 30 TYR C 31 0 SHEET 2 AB4 2 LYS C 36 ASN C 37 -1 O LYS C 36 N TYR C 31 SHEET 1 AB5 4 SER C 120 PHE C 124 0 SHEET 2 AB5 4 THR C 135 PHE C 145 -1 O LEU C 141 N PHE C 122 SHEET 3 AB5 4 TYR C 179 SER C 188 -1 O LEU C 185 N VAL C 138 SHEET 4 AB5 4 SER C 165 VAL C 169 -1 N SER C 168 O SER C 182 SHEET 1 AB6 4 LEU C 160 GLN C 161 0 SHEET 2 AB6 4 ALA C 150 VAL C 156 -1 N TRP C 154 O GLN C 161 SHEET 3 AB6 4 VAL C 197 HIS C 204 -1 O GLU C 201 N GLN C 153 SHEET 4 AB6 4 VAL C 211 ASN C 216 -1 O VAL C 211 N VAL C 202 SHEET 1 AB7 4 GLN D 3 VAL D 5 0 SHEET 2 AB7 4 SER D 17 SER D 25 -1 O ALA D 23 N VAL D 5 SHEET 3 AB7 4 THR D 78 ASN D 84 -1 O VAL D 79 N CYS D 22 SHEET 4 AB7 4 PHE D 68 ASP D 73 -1 N SER D 71 O TYR D 80 SHEET 1 AB8 5 LEU D 11 GLN D 13 0 SHEET 2 AB8 5 THR D 121 SER D 126 1 O SER D 126 N MET D 12 SHEET 3 AB8 5 ALA D 92 THR D 99 -1 N TYR D 94 O THR D 121 SHEET 4 AB8 5 ALA D 33 GLN D 39 -1 N PHE D 37 O TYR D 95 SHEET 5 AB8 5 GLU D 46 ARG D 52 -1 O ALA D 49 N TRP D 36 SHEET 1 AB9 4 LEU D 11 GLN D 13 0 SHEET 2 AB9 4 THR D 121 SER D 126 1 O SER D 126 N MET D 12 SHEET 3 AB9 4 ALA D 92 THR D 99 -1 N TYR D 94 O THR D 121 SHEET 4 AB9 4 TYR D 116 TRP D 117 -1 O TYR D 116 N ARG D 98 SHEET 1 AC1 5 ASN E 354 ILE E 358 0 SHEET 2 AC1 5 ASN E 394 ARG E 403 -1 O VAL E 395 N ILE E 358 SHEET 3 AC1 5 PRO E 507 GLU E 516 -1 O TYR E 508 N ILE E 402 SHEET 4 AC1 5 GLY E 431 ASN E 437 -1 N ILE E 434 O VAL E 511 SHEET 5 AC1 5 THR E 376 TYR E 380 -1 N TYR E 380 O GLY E 431 SHEET 1 AC2 2 LEU E 452 ARG E 454 0 SHEET 2 AC2 2 LEU E 492 SER E 494 -1 O GLN E 493 N TYR E 453 SHEET 1 AC3 2 TYR E 473 GLN E 474 0 SHEET 2 AC3 2 CYS E 488 TYR E 489 -1 O TYR E 489 N TYR E 473 SHEET 1 AC4 4 GLN F 3 VAL F 5 0 SHEET 2 AC4 4 SER F 17 SER F 25 -1 O ALA F 23 N VAL F 5 SHEET 3 AC4 4 THR F 78 ASN F 84 -1 O VAL F 79 N CYS F 22 SHEET 4 AC4 4 PHE F 68 ASP F 73 -1 N SER F 71 O TYR F 80 SHEET 1 AC5 5 LEU F 11 GLN F 13 0 SHEET 2 AC5 5 THR F 121 SER F 126 1 O THR F 124 N MET F 12 SHEET 3 AC5 5 ALA F 92 THR F 99 -1 N TYR F 94 O THR F 121 SHEET 4 AC5 5 ALA F 33 GLN F 39 -1 N PHE F 37 O TYR F 95 SHEET 5 AC5 5 GLU F 46 ARG F 52 -1 O ALA F 49 N TRP F 36 SHEET 1 AC6 4 LEU F 11 GLN F 13 0 SHEET 2 AC6 4 THR F 121 SER F 126 1 O THR F 124 N MET F 12 SHEET 3 AC6 4 ALA F 92 THR F 99 -1 N TYR F 94 O THR F 121 SHEET 4 AC6 4 TYR F 116 TRP F 117 -1 O TYR F 116 N ARG F 98 SHEET 1 AC7 4 MET H 2 GLN H 6 0 SHEET 2 AC7 4 LEU H 18 GLY H 26 -1 O LYS H 23 N VAL H 5 SHEET 3 AC7 4 THR H 78 TRP H 83 -1 O ALA H 79 N CYS H 22 SHEET 4 AC7 4 VAL H 68 ASP H 73 -1 N SER H 71 O TYR H 80 SHEET 1 AC8 6 GLU H 10 LYS H 12 0 SHEET 2 AC8 6 THR H 113 VAL H 117 1 O THR H 116 N GLU H 10 SHEET 3 AC8 6 ALA H 92 SER H 100 -1 N TYR H 94 O THR H 113 SHEET 4 AC8 6 TYR H 32 GLN H 39 -1 N TRP H 33 O GLY H 99 SHEET 5 AC8 6 LEU H 45 TYR H 52 -1 O GLU H 46 N ARG H 38 SHEET 6 AC8 6 GLU H 57 TYR H 60 -1 O ARG H 59 N ILE H 50 SHEET 1 AC9 4 GLU H 10 LYS H 12 0 SHEET 2 AC9 4 THR H 113 VAL H 117 1 O THR H 116 N GLU H 10 SHEET 3 AC9 4 ALA H 92 SER H 100 -1 N TYR H 94 O THR H 113 SHEET 4 AC9 4 VAL H 108 TRP H 109 -1 O VAL H 108 N GLY H 98 SHEET 1 AD1 4 SER H 124 LEU H 128 0 SHEET 2 AD1 4 THR H 139 TYR H 149 -1 O LEU H 145 N PHE H 126 SHEET 3 AD1 4 TYR H 180 PRO H 189 -1 O SER H 184 N CYS H 144 SHEET 4 AD1 4 VAL H 167 THR H 169 -1 N HIS H 168 O VAL H 185 SHEET 1 AD2 4 SER H 124 LEU H 128 0 SHEET 2 AD2 4 THR H 139 TYR H 149 -1 O LEU H 145 N PHE H 126 SHEET 3 AD2 4 TYR H 180 PRO H 189 -1 O SER H 184 N CYS H 144 SHEET 4 AD2 4 VAL H 173 LEU H 174 -1 N VAL H 173 O SER H 181 SHEET 1 AD3 3 VAL H 154 TRP H 158 0 SHEET 2 AD3 3 TYR H 198 HIS H 204 -1 O ASN H 201 N SER H 157 SHEET 3 AD3 3 THR H 209 VAL H 215 -1 O LYS H 213 N CYS H 200 SHEET 1 AD4 4 LEU L 4 SER L 7 0 SHEET 2 AD4 4 THR L 20 SER L 25 -1 O LYS L 24 N THR L 5 SHEET 3 AD4 4 ASP L 76 ILE L 81 -1 O PHE L 77 N CYS L 23 SHEET 4 AD4 4 PHE L 68 SER L 73 -1 N SER L 69 O THR L 80 SHEET 1 AD5 6 SER L 10 SER L 14 0 SHEET 2 AD5 6 THR L 108 LYS L 113 1 O GLU L 111 N LEU L 11 SHEET 3 AD5 6 ALA L 90 GLN L 96 -1 N ALA L 90 O VAL L 110 SHEET 4 AD5 6 LEU L 39 GLN L 44 -1 N TYR L 42 O TYR L 93 SHEET 5 AD5 6 LYS L 51 TYR L 55 -1 O LYS L 51 N GLN L 43 SHEET 6 AD5 6 THR L 59 ARG L 60 -1 O THR L 59 N TYR L 55 SHEET 1 AD6 4 SER L 10 SER L 14 0 SHEET 2 AD6 4 THR L 108 LYS L 113 1 O GLU L 111 N LEU L 11 SHEET 3 AD6 4 ALA L 90 GLN L 96 -1 N ALA L 90 O VAL L 110 SHEET 4 AD6 4 THR L 103 PHE L 104 -1 O THR L 103 N GLN L 96 SHEET 1 AD7 2 LEU L 30 TYR L 31 0 SHEET 2 AD7 2 LYS L 36 ASN L 37 -1 O LYS L 36 N TYR L 31 SHEET 1 AD8 4 SER L 120 PHE L 124 0 SHEET 2 AD8 4 THR L 135 PHE L 145 -1 O LEU L 141 N PHE L 122 SHEET 3 AD8 4 TYR L 179 SER L 188 -1 O LEU L 185 N VAL L 138 SHEET 4 AD8 4 SER L 165 VAL L 169 -1 N SER L 168 O SER L 182 SHEET 1 AD9 4 LEU L 160 GLN L 161 0 SHEET 2 AD9 4 ALA L 150 VAL L 156 -1 N TRP L 154 O GLN L 161 SHEET 3 AD9 4 VAL L 197 HIS L 204 -1 O GLU L 201 N GLN L 153 SHEET 4 AD9 4 VAL L 211 ASN L 216 -1 O VAL L 211 N VAL L 202 SSBOND 1 CYS A 336 CYS A 361 1555 1555 2.05 SSBOND 2 CYS A 379 CYS A 432 1555 1555 2.04 SSBOND 3 CYS A 391 CYS A 525 1555 1555 2.04 SSBOND 4 CYS A 480 CYS A 488 1555 1555 2.04 SSBOND 5 CYS B 22 CYS B 96 1555 1555 2.05 SSBOND 6 CYS B 144 CYS B 200 1555 1555 2.04 SSBOND 7 CYS C 23 CYS C 94 1555 1555 2.06 SSBOND 8 CYS C 140 CYS C 200 1555 1555 2.03 SSBOND 9 CYS D 22 CYS D 96 1555 1555 2.04 SSBOND 10 CYS E 336 CYS E 361 1555 1555 2.05 SSBOND 11 CYS E 379 CYS E 432 1555 1555 2.04 SSBOND 12 CYS E 391 CYS E 525 1555 1555 2.03 SSBOND 13 CYS E 480 CYS E 488 1555 1555 1.99 SSBOND 14 CYS F 22 CYS F 96 1555 1555 2.04 SSBOND 15 CYS H 22 CYS H 96 1555 1555 2.06 SSBOND 16 CYS H 144 CYS H 200 1555 1555 2.05 SSBOND 17 CYS L 23 CYS L 94 1555 1555 2.05 SSBOND 18 CYS L 140 CYS L 200 1555 1555 2.03 LINK ND2 ASN A 343 C1 NAG A 601 1555 1555 1.44 LINK ND2 ASN E 343 C1 NAG E 601 1555 1555 1.43 CISPEP 1 PHE B 150 PRO B 151 0 -12.47 CISPEP 2 GLU B 152 PRO B 153 0 -4.66 CISPEP 3 SER C 7 PRO C 8 0 1.17 CISPEP 4 THR C 100 PRO C 101 0 -1.20 CISPEP 5 TYR C 146 PRO C 147 0 6.87 CISPEP 6 PHE H 150 PRO H 151 0 -11.55 CISPEP 7 GLU H 152 PRO H 153 0 5.15 CISPEP 8 SER L 7 PRO L 8 0 1.56 CISPEP 9 THR L 100 PRO L 101 0 1.33 CISPEP 10 TYR L 146 PRO L 147 0 6.65 CRYST1 154.598 154.598 229.312 90.00 90.00 90.00 P 41 2 2 16 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 0.006468 0.000000 0.000000 0.00000 SCALE2 0.000000 0.006468 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004361 0.00000