HEADER ALLERGEN/IMMUNE SYSTEM 11-MAR-25 9NPG TITLE X-RAY CRYSTAL STRUCTURE OF RECOMBINANT CAN F 1-C100S IN COMPLEX WITH TITLE 2 HUMAN IGE MAB 12F3 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: IGE 12F3 FAB HEAVY CHAIN; COMPND 3 CHAIN: A, D, G, K; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: IGE 12F3 FAB LIGHT CHAIN; COMPND 7 CHAIN: B, E, H, J; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: MAJOR ALLERGEN CAN F 1; COMPND 11 CHAIN: C, F, L, I; COMPND 12 SYNONYM: ALLERGEN DOG 1; COMPND 13 ENGINEERED: YES; COMPND 14 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: CANIS LUPUS FAMILIARIS; SOURCE 17 ORGANISM_COMMON: DOG; SOURCE 18 ORGANISM_TAXID: 9615; SOURCE 19 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 20 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS CAN F 1-IGE, DOG ALLERGEN, ALLERGEN-ANTIBODY COMPLEX, HUMAN ANTIBODY, KEYWDS 2 IGE-CAN F 1 COMPLEX, ALLERGEN-ANTIBODY INTERACTION, ALLERGEN, KEYWDS 3 ALLERGEN-IMMUNE SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR K.KHATRI,A.BALL,S.A.SMITH,M.D.CHAMPAN,A.POMES,M.CHRUSZCZ REVDAT 1 27-AUG-25 9NPG 0 JRNL AUTH K.KHATRI,A.BALL,J.GLESNER,C.LINN,L.D.VAILES,S.WUNSCHMANN, JRNL AUTH 2 S.A.GABEL,J.ZHANG,R.S.PEEBLES JR.,T.BOROWSKI,G.A.MUELLER, JRNL AUTH 3 M.D.CHAPMAN,S.A.SMITH,A.POMES,M.CHRUSZCZ JRNL TITL HUMAN IGE MONOCLONAL ANTIBODIES DEFINE TWO UNUSUAL EPITOPES JRNL TITL 2 TRAPPING DOG ALLERGEN CAN F 1 IN DIFFERENT CONFORMATIONS. JRNL REF PROTEIN SCI. V. 34 70269 2025 JRNL REFN ESSN 1469-896X JRNL PMID 40828364 JRNL DOI 10.1002/PRO.70269 REMARK 2 REMARK 2 RESOLUTION. 3.12 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0425 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.12 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.67 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 44368 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.205 REMARK 3 R VALUE (WORKING SET) : 0.203 REMARK 3 FREE R VALUE : 0.245 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900 REMARK 3 FREE R VALUE TEST SET COUNT : 2298 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) : 3.12 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.20 REMARK 3 REFLECTION IN BIN (WORKING SET) : 3266 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.94 REMARK 3 BIN R VALUE (WORKING SET) : 0.2900 REMARK 3 BIN FREE R VALUE SET COUNT : 148 REMARK 3 BIN FREE R VALUE : 0.3140 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 17418 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 96 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 83.62 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.26000 REMARK 3 B22 (A**2) : -2.06000 REMARK 3 B33 (A**2) : 0.02000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 1.71000 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): 0.488 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.425 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 53.438 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.902 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.877 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 17796 ; 0.005 ; 0.012 REMARK 3 BOND LENGTHS OTHERS (A): 16375 ; 0.001 ; 0.016 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 24227 ; 1.291 ; 1.814 REMARK 3 BOND ANGLES OTHERS (DEGREES): 37853 ; 0.455 ; 1.732 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2294 ; 6.495 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 80 ;10.191 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2825 ;13.904 ;10.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2772 ; 0.060 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 20934 ; 0.004 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 3914 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 9224 ; 1.338 ; 2.255 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 9224 ; 1.337 ; 2.255 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11502 ; 2.375 ; 4.046 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 11503 ; 2.375 ; 4.046 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 8572 ; 1.286 ; 2.307 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 8573 ; 1.286 ; 2.307 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 12726 ; 2.251 ; 4.199 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 69233 ; 5.383 ;26.640 REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 69221 ; 5.380 ;26.640 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 : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 36 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 1 A 32 REMARK 3 ORIGIN FOR THE GROUP (A): -11.156 54.032 16.957 REMARK 3 T TENSOR REMARK 3 T11: 0.2307 T22: 0.6849 REMARK 3 T33: 0.3586 T12: -0.0102 REMARK 3 T13: -0.1605 T23: -0.1022 REMARK 3 L TENSOR REMARK 3 L11: 0.8354 L22: 5.1915 REMARK 3 L33: 4.2593 L12: -0.0259 REMARK 3 L13: 1.1879 L23: 0.7869 REMARK 3 S TENSOR REMARK 3 S11: -0.2677 S12: 0.0662 S13: -0.0667 REMARK 3 S21: -0.7313 S22: 0.3331 S23: 0.4767 REMARK 3 S31: -0.4653 S32: -0.3360 S33: -0.0653 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 33 A 126 REMARK 3 ORIGIN FOR THE GROUP (A): -4.447 54.026 22.181 REMARK 3 T TENSOR REMARK 3 T11: 0.1755 T22: 0.4618 REMARK 3 T33: 0.2402 T12: -0.0116 REMARK 3 T13: -0.1177 T23: -0.0620 REMARK 3 L TENSOR REMARK 3 L11: 0.5719 L22: 3.0819 REMARK 3 L33: 2.0657 L12: 1.0193 REMARK 3 L13: 0.3570 L23: 2.1385 REMARK 3 S TENSOR REMARK 3 S11: 0.0229 S12: -0.0486 S13: -0.0113 REMARK 3 S21: 0.0405 S22: -0.0017 S23: -0.0570 REMARK 3 S31: 0.0707 S32: -0.0814 S33: -0.0212 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 127 A 224 REMARK 3 ORIGIN FOR THE GROUP (A): -24.079 28.149 39.464 REMARK 3 T TENSOR REMARK 3 T11: 0.0377 T22: 0.3552 REMARK 3 T33: 0.3102 T12: -0.0538 REMARK 3 T13: -0.0593 T23: -0.0665 REMARK 3 L TENSOR REMARK 3 L11: 1.1669 L22: 1.0638 REMARK 3 L33: 9.0616 L12: -0.6282 REMARK 3 L13: -0.5228 L23: 0.0673 REMARK 3 S TENSOR REMARK 3 S11: -0.0374 S12: -0.0515 S13: -0.1979 REMARK 3 S21: -0.0407 S22: 0.1025 S23: 0.1913 REMARK 3 S31: 0.0086 S32: -0.5556 S33: -0.0651 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 1 B 142 REMARK 3 ORIGIN FOR THE GROUP (A): -7.065 51.990 43.021 REMARK 3 T TENSOR REMARK 3 T11: 0.2976 T22: 0.5222 REMARK 3 T33: 0.1305 T12: -0.0793 REMARK 3 T13: -0.1397 T23: -0.0799 REMARK 3 L TENSOR REMARK 3 L11: 0.6955 L22: 2.3926 REMARK 3 L33: 0.4476 L12: 0.5566 REMARK 3 L13: -0.5036 L23: -0.7716 REMARK 3 S TENSOR REMARK 3 S11: 0.1833 S12: -0.1469 S13: 0.0581 REMARK 3 S21: 0.2585 S22: -0.1307 S23: 0.0571 REMARK 3 S31: -0.1279 S32: 0.1734 S33: -0.0526 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 143 B 148 REMARK 3 ORIGIN FOR THE GROUP (A): -4.668 34.274 49.137 REMARK 3 T TENSOR REMARK 3 T11: 0.5429 T22: 0.7780 REMARK 3 T33: 0.1088 T12: -0.3062 REMARK 3 T13: -0.1725 T23: -0.0411 REMARK 3 L TENSOR REMARK 3 L11: 25.1555 L22: 31.3894 REMARK 3 L33: 9.9382 L12: -12.8415 REMARK 3 L13: 4.5589 L23: 8.2044 REMARK 3 S TENSOR REMARK 3 S11: 0.1161 S12: 0.5562 S13: -0.4357 REMARK 3 S21: 1.8499 S22: -0.3062 S23: -0.0445 REMARK 3 S31: -0.4787 S32: 1.5133 S33: 0.1901 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 : B 149 B 213 REMARK 3 ORIGIN FOR THE GROUP (A): -7.920 24.307 46.913 REMARK 3 T TENSOR REMARK 3 T11: 0.2388 T22: 0.5409 REMARK 3 T33: 0.2293 T12: 0.1865 REMARK 3 T13: -0.1614 T23: -0.0511 REMARK 3 L TENSOR REMARK 3 L11: 0.8825 L22: 8.9755 REMARK 3 L33: 11.4542 L12: -2.1073 REMARK 3 L13: -2.8903 L23: 4.3303 REMARK 3 S TENSOR REMARK 3 S11: -0.3123 S12: -0.2817 S13: 0.0640 REMARK 3 S21: 0.4407 S22: 0.4019 S23: -0.2885 REMARK 3 S31: 1.2325 S32: 1.4543 S33: -0.0897 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 11 C 31 REMARK 3 ORIGIN FOR THE GROUP (A): 8.613 85.574 30.772 REMARK 3 T TENSOR REMARK 3 T11: 0.2448 T22: 0.3063 REMARK 3 T33: 0.2517 T12: -0.0475 REMARK 3 T13: -0.0093 T23: -0.1004 REMARK 3 L TENSOR REMARK 3 L11: 12.0191 L22: 8.8098 REMARK 3 L33: 8.1489 L12: 8.2280 REMARK 3 L13: -3.1755 L23: -6.1074 REMARK 3 S TENSOR REMARK 3 S11: 0.6503 S12: -0.4971 S13: 0.8962 REMARK 3 S21: 0.8872 S22: -0.5388 S23: 0.5491 REMARK 3 S31: -0.8773 S32: 1.1257 S33: -0.1115 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 : C 32 C 62 REMARK 3 ORIGIN FOR THE GROUP (A): 4.711 88.666 37.017 REMARK 3 T TENSOR REMARK 3 T11: 0.2788 T22: 0.2880 REMARK 3 T33: 0.2699 T12: -0.0485 REMARK 3 T13: -0.1063 T23: -0.0291 REMARK 3 L TENSOR REMARK 3 L11: 13.5993 L22: 9.8445 REMARK 3 L33: 4.1903 L12: 7.9855 REMARK 3 L13: -2.3695 L23: 3.0176 REMARK 3 S TENSOR REMARK 3 S11: 0.4928 S12: -0.0774 S13: 0.8280 REMARK 3 S21: 0.8259 S22: -0.0711 S23: 0.1631 REMARK 3 S31: 0.3327 S32: 0.0018 S33: -0.4217 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 : C 63 C 153 REMARK 3 ORIGIN FOR THE GROUP (A): 7.716 84.934 24.995 REMARK 3 T TENSOR REMARK 3 T11: 0.0596 T22: 0.3557 REMARK 3 T33: 0.1915 T12: -0.0394 REMARK 3 T13: -0.0922 T23: -0.0312 REMARK 3 L TENSOR REMARK 3 L11: 2.2198 L22: 3.8712 REMARK 3 L33: 2.8713 L12: 0.2991 REMARK 3 L13: 0.7508 L23: -1.0556 REMARK 3 S TENSOR REMARK 3 S11: 0.0002 S12: 0.2706 S13: 0.0755 REMARK 3 S21: 0.0607 S22: -0.0316 S23: -0.2720 REMARK 3 S31: -0.0059 S32: 0.1415 S33: 0.0314 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 1 D 30 REMARK 3 ORIGIN FOR THE GROUP (A): -53.500 5.669 23.436 REMARK 3 T TENSOR REMARK 3 T11: 0.1715 T22: 0.3749 REMARK 3 T33: 0.2792 T12: -0.0067 REMARK 3 T13: 0.1092 T23: -0.0628 REMARK 3 L TENSOR REMARK 3 L11: 1.5589 L22: 16.9446 REMARK 3 L33: 3.5995 L12: 2.7815 REMARK 3 L13: 1.1518 L23: 3.5445 REMARK 3 S TENSOR REMARK 3 S11: -0.0718 S12: 0.0975 S13: -0.1980 REMARK 3 S21: 1.2928 S22: 0.1216 S23: 0.5636 REMARK 3 S31: 0.1215 S32: -0.5462 S33: -0.0499 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 : D 31 D 126 REMARK 3 ORIGIN FOR THE GROUP (A): -44.508 4.559 22.028 REMARK 3 T TENSOR REMARK 3 T11: 0.2256 T22: 0.3654 REMARK 3 T33: 0.2807 T12: 0.0152 REMARK 3 T13: -0.1359 T23: -0.0290 REMARK 3 L TENSOR REMARK 3 L11: 1.3156 L22: 3.7217 REMARK 3 L33: 2.2185 L12: -1.6049 REMARK 3 L13: -0.9797 L23: 1.2196 REMARK 3 S TENSOR REMARK 3 S11: 0.0197 S12: 0.0178 S13: 0.0526 REMARK 3 S21: 0.4516 S22: -0.1798 S23: -0.0021 REMARK 3 S31: -0.0170 S32: -0.0576 S33: 0.1601 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 : D 127 D 225 REMARK 3 ORIGIN FOR THE GROUP (A): -54.409 31.440 -2.469 REMARK 3 T TENSOR REMARK 3 T11: 0.1551 T22: 0.3742 REMARK 3 T33: 0.4945 T12: -0.0074 REMARK 3 T13: -0.0668 T23: -0.0479 REMARK 3 L TENSOR REMARK 3 L11: 3.9647 L22: 2.8350 REMARK 3 L33: 5.8792 L12: -1.7413 REMARK 3 L13: -2.1899 L23: 0.5285 REMARK 3 S TENSOR REMARK 3 S11: -0.0522 S12: 0.3101 S13: 0.2487 REMARK 3 S21: 0.2984 S22: -0.0041 S23: 0.5251 REMARK 3 S31: 0.1420 S32: -0.4099 S33: 0.0563 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 : E 1 E 69 REMARK 3 ORIGIN FOR THE GROUP (A): -35.981 -1.428 4.167 REMARK 3 T TENSOR REMARK 3 T11: 0.1788 T22: 0.2899 REMARK 3 T33: 0.2056 T12: 0.0081 REMARK 3 T13: -0.1366 T23: -0.0376 REMARK 3 L TENSOR REMARK 3 L11: 0.3113 L22: 3.2024 REMARK 3 L33: 3.3241 L12: 0.1194 REMARK 3 L13: -0.5614 L23: -0.6336 REMARK 3 S TENSOR REMARK 3 S11: -0.0726 S12: 0.1511 S13: 0.0049 REMARK 3 S21: -0.2074 S22: 0.0207 S23: -0.2373 REMARK 3 S31: 0.1858 S32: 0.0285 S33: 0.0519 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 : E 70 E 187 REMARK 3 ORIGIN FOR THE GROUP (A): -38.587 22.028 -0.599 REMARK 3 T TENSOR REMARK 3 T11: 0.0569 T22: 0.3815 REMARK 3 T33: 0.3125 T12: 0.0288 REMARK 3 T13: -0.1146 T23: -0.0319 REMARK 3 L TENSOR REMARK 3 L11: 0.0994 L22: 4.5428 REMARK 3 L33: 0.6220 L12: -0.6300 REMARK 3 L13: 0.2374 L23: -1.6310 REMARK 3 S TENSOR REMARK 3 S11: 0.0037 S12: 0.0267 S13: 0.0101 REMARK 3 S21: 0.1047 S22: -0.0156 S23: -0.1873 REMARK 3 S31: -0.0062 S32: -0.0538 S33: 0.0119 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 : E 188 E 212 REMARK 3 ORIGIN FOR THE GROUP (A): -34.969 40.163 -7.461 REMARK 3 T TENSOR REMARK 3 T11: 0.0602 T22: 0.3612 REMARK 3 T33: 0.3450 T12: -0.0001 REMARK 3 T13: -0.1039 T23: -0.0091 REMARK 3 L TENSOR REMARK 3 L11: 3.5391 L22: 19.9481 REMARK 3 L33: 3.5730 L12: -6.9427 REMARK 3 L13: -2.8114 L23: 8.3464 REMARK 3 S TENSOR REMARK 3 S11: 0.0472 S12: -0.1734 S13: 0.3317 REMARK 3 S21: -0.1324 S22: 0.2606 S23: -0.5723 REMARK 3 S31: -0.0275 S32: 0.2419 S33: -0.3078 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 12 F 56 REMARK 3 ORIGIN FOR THE GROUP (A): -32.137 -27.749 15.344 REMARK 3 T TENSOR REMARK 3 T11: 0.2988 T22: 0.2487 REMARK 3 T33: 0.3634 T12: 0.0107 REMARK 3 T13: -0.0671 T23: -0.0274 REMARK 3 L TENSOR REMARK 3 L11: 2.1785 L22: 4.3965 REMARK 3 L33: 7.2018 L12: -2.6690 REMARK 3 L13: 1.9236 L23: -3.4556 REMARK 3 S TENSOR REMARK 3 S11: 0.1310 S12: 0.0312 S13: -0.2447 REMARK 3 S21: -0.3390 S22: 0.1160 S23: -0.1453 REMARK 3 S31: 0.0963 S32: 0.0713 S33: -0.2470 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 : F 57 F 88 REMARK 3 ORIGIN FOR THE GROUP (A): -40.400 -30.719 18.619 REMARK 3 T TENSOR REMARK 3 T11: 0.4469 T22: 0.2587 REMARK 3 T33: 0.1551 T12: 0.0696 REMARK 3 T13: -0.0631 T23: 0.0336 REMARK 3 L TENSOR REMARK 3 L11: 8.4727 L22: 1.4502 REMARK 3 L33: 2.4051 L12: 1.8067 REMARK 3 L13: -2.5729 L23: 0.3010 REMARK 3 S TENSOR REMARK 3 S11: -0.2328 S12: -0.1918 S13: -0.2140 REMARK 3 S21: 0.0858 S22: -0.0072 S23: 0.0605 REMARK 3 S31: 0.7054 S32: 0.1812 S33: 0.2400 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 : F 89 F 153 REMARK 3 ORIGIN FOR THE GROUP (A): -29.851 -25.604 25.704 REMARK 3 T TENSOR REMARK 3 T11: 0.2188 T22: 0.3683 REMARK 3 T33: 0.2615 T12: 0.0735 REMARK 3 T13: -0.1712 T23: 0.0341 REMARK 3 L TENSOR REMARK 3 L11: 0.8829 L22: 2.2984 REMARK 3 L33: 3.1329 L12: 0.9912 REMARK 3 L13: 0.0493 L23: -0.3372 REMARK 3 S TENSOR REMARK 3 S11: 0.1204 S12: -0.3046 S13: -0.1337 REMARK 3 S21: 0.2669 S22: -0.1459 S23: -0.5007 REMARK 3 S31: 0.0415 S32: 0.2103 S33: 0.0255 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 : G 1 G 127 REMARK 3 ORIGIN FOR THE GROUP (A): -6.559 -0.220 21.540 REMARK 3 T TENSOR REMARK 3 T11: 0.1286 T22: 0.4499 REMARK 3 T33: 0.2923 T12: 0.0593 REMARK 3 T13: -0.1518 T23: -0.0890 REMARK 3 L TENSOR REMARK 3 L11: 0.4988 L22: 3.7865 REMARK 3 L33: 1.9276 L12: -1.3713 REMARK 3 L13: -0.0522 L23: 0.3049 REMARK 3 S TENSOR REMARK 3 S11: -0.1312 S12: -0.1015 S13: 0.0579 REMARK 3 S21: 0.3742 S22: 0.3032 S23: -0.2022 REMARK 3 S31: -0.1284 S32: 0.1236 S33: -0.1720 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 : G 128 G 144 REMARK 3 ORIGIN FOR THE GROUP (A): -10.966 31.912 -6.124 REMARK 3 T TENSOR REMARK 3 T11: 0.5451 T22: 0.4725 REMARK 3 T33: 0.5972 T12: 0.3444 REMARK 3 T13: 0.0692 T23: 0.0618 REMARK 3 L TENSOR REMARK 3 L11: 0.9550 L22: 11.6867 REMARK 3 L33: 4.6903 L12: 1.6718 REMARK 3 L13: 1.5069 L23: 0.3223 REMARK 3 S TENSOR REMARK 3 S11: 0.1831 S12: 0.1671 S13: 0.0413 REMARK 3 S21: 0.1908 S22: -0.0430 S23: -0.5629 REMARK 3 S31: -0.6681 S32: -0.2418 S33: -0.1401 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 : G 145 G 224 REMARK 3 ORIGIN FOR THE GROUP (A): -15.284 25.687 -2.648 REMARK 3 T TENSOR REMARK 3 T11: 0.0795 T22: 0.4696 REMARK 3 T33: 0.3210 T12: -0.0128 REMARK 3 T13: -0.0939 T23: -0.0683 REMARK 3 L TENSOR REMARK 3 L11: 1.8899 L22: 1.2986 REMARK 3 L33: 3.9614 L12: -0.7693 REMARK 3 L13: -1.1968 L23: -0.0633 REMARK 3 S TENSOR REMARK 3 S11: -0.0352 S12: 0.2753 S13: 0.0594 REMARK 3 S21: 0.0940 S22: -0.1435 S23: 0.2681 REMARK 3 S31: -0.0357 S32: -0.4928 S33: 0.1788 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 : H 1 H 30 REMARK 3 ORIGIN FOR THE GROUP (A): 9.702 -3.288 2.591 REMARK 3 T TENSOR REMARK 3 T11: 0.1305 T22: 0.3086 REMARK 3 T33: 0.5275 T12: 0.0246 REMARK 3 T13: 0.0130 T23: 0.0198 REMARK 3 L TENSOR REMARK 3 L11: 2.1070 L22: 1.8529 REMARK 3 L33: 10.3780 L12: -1.0108 REMARK 3 L13: -1.0662 L23: -0.1445 REMARK 3 S TENSOR REMARK 3 S11: 0.1680 S12: -0.0956 S13: 0.3749 REMARK 3 S21: -0.3224 S22: -0.1657 S23: -0.7612 REMARK 3 S31: 0.2281 S32: 0.2708 S33: -0.0023 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 : H 31 H 108 REMARK 3 ORIGIN FOR THE GROUP (A): 1.071 -6.758 3.582 REMARK 3 T TENSOR REMARK 3 T11: 0.0443 T22: 0.4154 REMARK 3 T33: 0.2836 T12: 0.0243 REMARK 3 T13: -0.0703 T23: -0.1184 REMARK 3 L TENSOR REMARK 3 L11: 1.6853 L22: 3.8501 REMARK 3 L33: 3.3658 L12: -2.1076 REMARK 3 L13: 1.8716 L23: -2.6661 REMARK 3 S TENSOR REMARK 3 S11: 0.0788 S12: -0.0325 S13: 0.1673 REMARK 3 S21: -0.1971 S22: 0.0134 S23: -0.2428 REMARK 3 S31: 0.1205 S32: 0.0463 S33: -0.0922 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 : H 109 H 214 REMARK 3 ORIGIN FOR THE GROUP (A): 1.343 28.409 -3.869 REMARK 3 T TENSOR REMARK 3 T11: 0.0340 T22: 0.4623 REMARK 3 T33: 0.2048 T12: -0.0082 REMARK 3 T13: -0.0742 T23: 0.0181 REMARK 3 L TENSOR REMARK 3 L11: 1.3776 L22: 6.7888 REMARK 3 L33: 5.1864 L12: -0.9412 REMARK 3 L13: -0.2808 L23: 4.0558 REMARK 3 S TENSOR REMARK 3 S11: 0.0409 S12: -0.1499 S13: 0.0653 REMARK 3 S21: -0.1040 S22: -0.0069 S23: -0.2512 REMARK 3 S31: -0.0978 S32: 0.2758 S33: -0.0340 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 : I 12 I 60 REMARK 3 ORIGIN FOR THE GROUP (A): 10.534 -33.634 14.771 REMARK 3 T TENSOR REMARK 3 T11: 0.3473 T22: 0.2759 REMARK 3 T33: 0.3460 T12: 0.0712 REMARK 3 T13: -0.0990 T23: -0.1124 REMARK 3 L TENSOR REMARK 3 L11: 5.1937 L22: 1.9111 REMARK 3 L33: 7.1726 L12: -1.0857 REMARK 3 L13: 3.4070 L23: -1.2162 REMARK 3 S TENSOR REMARK 3 S11: 0.1136 S12: 0.3338 S13: -0.2922 REMARK 3 S21: -0.3871 S22: 0.2111 S23: -0.4127 REMARK 3 S31: 0.8972 S32: 0.5543 S33: -0.3247 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 : I 61 I 74 REMARK 3 ORIGIN FOR THE GROUP (A): -0.113 -33.927 15.720 REMARK 3 T TENSOR REMARK 3 T11: 0.2802 T22: 0.3146 REMARK 3 T33: 0.1757 T12: 0.0049 REMARK 3 T13: -0.2025 T23: -0.0168 REMARK 3 L TENSOR REMARK 3 L11: 18.6138 L22: 11.2794 REMARK 3 L33: 11.2925 L12: -10.4308 REMARK 3 L13: -10.8443 L23: 2.7872 REMARK 3 S TENSOR REMARK 3 S11: -0.3011 S12: -0.1612 S13: 0.6904 REMARK 3 S21: -0.3560 S22: 0.8224 S23: -0.1314 REMARK 3 S31: 0.6723 S32: 0.2148 S33: -0.5213 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 : I 75 I 153 REMARK 3 ORIGIN FOR THE GROUP (A): 9.218 -31.017 24.542 REMARK 3 T TENSOR REMARK 3 T11: 0.2443 T22: 0.4745 REMARK 3 T33: 0.1956 T12: 0.1923 REMARK 3 T13: -0.1936 T23: -0.1338 REMARK 3 L TENSOR REMARK 3 L11: 2.0392 L22: 3.4746 REMARK 3 L33: 2.7584 L12: 0.3871 REMARK 3 L13: 0.1589 L23: -2.9166 REMARK 3 S TENSOR REMARK 3 S11: -0.1700 S12: -0.0417 S13: -0.0857 REMARK 3 S21: 0.2275 S22: 0.0757 S23: -0.3369 REMARK 3 S31: -0.0376 S32: 0.0668 S33: 0.0943 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 : J 1 J 35 REMARK 3 ORIGIN FOR THE GROUP (A): -39.043 64.775 43.313 REMARK 3 T TENSOR REMARK 3 T11: 0.2684 T22: 0.5504 REMARK 3 T33: 0.2653 T12: 0.0640 REMARK 3 T13: -0.2423 T23: 0.0599 REMARK 3 L TENSOR REMARK 3 L11: 7.5923 L22: 3.4890 REMARK 3 L33: 4.7482 L12: 2.4147 REMARK 3 L13: -5.4311 L23: -2.4628 REMARK 3 S TENSOR REMARK 3 S11: 0.3649 S12: -0.4412 S13: -0.3909 REMARK 3 S21: 0.2745 S22: -0.6954 S23: -0.4953 REMARK 3 S31: -0.2645 S32: 0.8245 S33: 0.3305 REMARK 3 REMARK 3 TLS GROUP : 29 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : J 36 J 122 REMARK 3 ORIGIN FOR THE GROUP (A): -48.216 61.760 42.129 REMARK 3 T TENSOR REMARK 3 T11: 0.3236 T22: 0.3872 REMARK 3 T33: 0.1796 T12: 0.0431 REMARK 3 T13: -0.1647 T23: -0.0470 REMARK 3 L TENSOR REMARK 3 L11: 0.4050 L22: 4.1213 REMARK 3 L33: 0.6416 L12: 0.8766 REMARK 3 L13: -0.2715 L23: -1.5923 REMARK 3 S TENSOR REMARK 3 S11: -0.1313 S12: 0.0073 S13: -0.0181 REMARK 3 S21: 0.1733 S22: 0.0553 S23: -0.1202 REMARK 3 S31: -0.1364 S32: -0.0564 S33: 0.0760 REMARK 3 REMARK 3 TLS GROUP : 30 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : J 123 J 213 REMARK 3 ORIGIN FOR THE GROUP (A): -50.515 30.524 47.304 REMARK 3 T TENSOR REMARK 3 T11: 0.0374 T22: 0.3418 REMARK 3 T33: 0.2231 T12: -0.0263 REMARK 3 T13: -0.0797 T23: 0.0108 REMARK 3 L TENSOR REMARK 3 L11: 0.8736 L22: 6.3507 REMARK 3 L33: 2.9986 L12: -1.5531 REMARK 3 L13: -0.7367 L23: 1.5313 REMARK 3 S TENSOR REMARK 3 S11: -0.0733 S12: 0.1229 S13: 0.0120 REMARK 3 S21: 0.2074 S22: -0.0789 S23: -0.1855 REMARK 3 S31: 0.0801 S32: 0.0275 S33: 0.1522 REMARK 3 REMARK 3 TLS GROUP : 31 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : K 1 K 127 REMARK 3 ORIGIN FOR THE GROUP (A): -45.797 61.032 20.330 REMARK 3 T TENSOR REMARK 3 T11: 0.3004 T22: 0.3391 REMARK 3 T33: 0.1865 T12: -0.0289 REMARK 3 T13: -0.0713 T23: -0.0373 REMARK 3 L TENSOR REMARK 3 L11: 0.7266 L22: 2.1019 REMARK 3 L33: 0.9457 L12: 0.4479 REMARK 3 L13: 0.2913 L23: -0.1242 REMARK 3 S TENSOR REMARK 3 S11: 0.0275 S12: 0.0854 S13: -0.0537 REMARK 3 S21: -0.2659 S22: -0.1380 S23: -0.3102 REMARK 3 S31: 0.1911 S32: 0.0632 S33: 0.1105 REMARK 3 REMARK 3 TLS GROUP : 32 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : K 128 K 148 REMARK 3 ORIGIN FOR THE GROUP (A): -63.901 29.582 44.548 REMARK 3 T TENSOR REMARK 3 T11: 0.0454 T22: 0.5910 REMARK 3 T33: 0.2450 T12: -0.0337 REMARK 3 T13: -0.0741 T23: -0.0349 REMARK 3 L TENSOR REMARK 3 L11: 4.3991 L22: 3.7761 REMARK 3 L33: 23.9067 L12: 0.7980 REMARK 3 L13: -6.6660 L23: 2.9291 REMARK 3 S TENSOR REMARK 3 S11: -0.0431 S12: 0.2166 S13: -0.4359 REMARK 3 S21: -0.0420 S22: -0.3557 S23: 0.2937 REMARK 3 S31: 0.5118 S32: -2.5504 S33: 0.3988 REMARK 3 REMARK 3 TLS GROUP : 33 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : K 149 K 225 REMARK 3 ORIGIN FOR THE GROUP (A): -64.428 35.515 37.797 REMARK 3 T TENSOR REMARK 3 T11: 0.2420 T22: 0.4770 REMARK 3 T33: 0.3359 T12: 0.1597 REMARK 3 T13: -0.1792 T23: -0.1323 REMARK 3 L TENSOR REMARK 3 L11: 0.4326 L22: 2.7843 REMARK 3 L33: 11.0251 L12: 0.4202 REMARK 3 L13: -0.6155 L23: 1.5446 REMARK 3 S TENSOR REMARK 3 S11: -0.0789 S12: -0.0927 S13: -0.1477 REMARK 3 S21: -0.7172 S22: -0.1941 S23: 0.3265 REMARK 3 S31: -0.7079 S32: -1.1302 S33: 0.2730 REMARK 3 REMARK 3 TLS GROUP : 34 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : L 11 L 42 REMARK 3 ORIGIN FOR THE GROUP (A): -33.560 92.578 32.474 REMARK 3 T TENSOR REMARK 3 T11: 0.5876 T22: 0.4756 REMARK 3 T33: 0.3709 T12: -0.1332 REMARK 3 T13: -0.4475 T23: -0.0012 REMARK 3 L TENSOR REMARK 3 L11: 6.6344 L22: 6.8962 REMARK 3 L33: 2.1808 L12: 2.6781 REMARK 3 L13: -2.4506 L23: 0.0155 REMARK 3 S TENSOR REMARK 3 S11: -0.0087 S12: -0.6906 S13: 0.1578 REMARK 3 S21: 1.1009 S22: -0.0963 S23: -0.9547 REMARK 3 S31: -0.2099 S32: 0.4093 S33: 0.1050 REMARK 3 REMARK 3 TLS GROUP : 35 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : L 43 L 66 REMARK 3 ORIGIN FOR THE GROUP (A): -38.387 97.451 35.638 REMARK 3 T TENSOR REMARK 3 T11: 0.5052 T22: 0.1908 REMARK 3 T33: 0.1524 T12: -0.1475 REMARK 3 T13: -0.0387 T23: -0.0434 REMARK 3 L TENSOR REMARK 3 L11: 22.8168 L22: 3.8996 REMARK 3 L33: 5.0626 L12: 4.6130 REMARK 3 L13: 5.4167 L23: 3.3931 REMARK 3 S TENSOR REMARK 3 S11: 0.1725 S12: -0.5802 S13: 0.7893 REMARK 3 S21: 0.5140 S22: -0.3593 S23: 0.2501 REMARK 3 S31: -0.4219 S32: 0.0260 S33: 0.1867 REMARK 3 REMARK 3 TLS GROUP : 36 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : L 67 L 153 REMARK 3 ORIGIN FOR THE GROUP (A): -33.230 91.819 23.699 REMARK 3 T TENSOR REMARK 3 T11: 0.2487 T22: 0.3804 REMARK 3 T33: 0.2627 T12: -0.1215 REMARK 3 T13: -0.1864 T23: 0.0079 REMARK 3 L TENSOR REMARK 3 L11: 1.7438 L22: 2.8008 REMARK 3 L33: 3.9246 L12: -0.7414 REMARK 3 L13: 0.2811 L23: -1.4331 REMARK 3 S TENSOR REMARK 3 S11: 0.1363 S12: 0.1151 S13: -0.0259 REMARK 3 S21: 0.2419 S22: -0.1466 S23: -0.4104 REMARK 3 S31: -0.5543 S32: 0.6303 S33: 0.0103 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 9NPG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAR-25. REMARK 100 THE DEPOSITION ID IS D_1000293865. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 29-NOV-23 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 4.2 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : NSLS-II REMARK 200 BEAMLINE : 17-ID-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.979 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 S 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46837 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.120 REMARK 200 RESOLUTION RANGE LOW (A) : 40.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 7.000 REMARK 200 R MERGE (I) : 0.25700 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 7.4700 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.12 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.17 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 6.60 REMARK 200 R MERGE FOR SHELL (I) : 0.74900 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.970 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 53.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M NACL, 0.1 M SODIUM CITRATE REMARK 280 TRIBASIC DIHYDRATE PH 4.2, 20% W/V PEG 8,000 CONDITIONS, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 277.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 95.57800 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5650 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 25400 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5620 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 26310 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F 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: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5670 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 25640 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, I 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: 4 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5690 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 25830 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, J, L REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 LYS A 138 REMARK 465 SER A 139 REMARK 465 THR A 140 REMARK 465 SER A 141 REMARK 465 CYS A 225 REMARK 465 HIS A 226 REMARK 465 HIS A 227 REMARK 465 HIS A 228 REMARK 465 HIS A 229 REMARK 465 HIS A 230 REMARK 465 HIS A 231 REMARK 465 GLU B 214 REMARK 465 CYS B 215 REMARK 465 ASP C 9 REMARK 465 THR C 10 REMARK 465 GLY C 154 REMARK 465 GLY C 155 REMARK 465 GLN C 156 REMARK 465 LYS D 138 REMARK 465 SER D 139 REMARK 465 THR D 140 REMARK 465 SER D 141 REMARK 465 HIS D 231 REMARK 465 GLY E 213 REMARK 465 GLU E 214 REMARK 465 CYS E 215 REMARK 465 ASP F 9 REMARK 465 THR F 10 REMARK 465 VAL F 11 REMARK 465 GLY F 154 REMARK 465 GLY F 155 REMARK 465 GLN F 156 REMARK 465 LYS G 138 REMARK 465 SER G 139 REMARK 465 THR G 140 REMARK 465 SER G 141 REMARK 465 CYS G 225 REMARK 465 HIS G 226 REMARK 465 HIS G 227 REMARK 465 HIS G 228 REMARK 465 HIS G 229 REMARK 465 HIS G 230 REMARK 465 HIS G 231 REMARK 465 CYS H 215 REMARK 465 LYS K 138 REMARK 465 SER K 139 REMARK 465 THR K 140 REMARK 465 SER K 141 REMARK 465 HIS K 226 REMARK 465 HIS K 227 REMARK 465 HIS K 228 REMARK 465 HIS K 229 REMARK 465 HIS K 230 REMARK 465 HIS K 231 REMARK 465 GLU J 214 REMARK 465 CYS J 215 REMARK 465 ASP L 9 REMARK 465 THR L 10 REMARK 465 GLY L 154 REMARK 465 GLY L 155 REMARK 465 GLN L 156 REMARK 465 ASP I 9 REMARK 465 THR I 10 REMARK 465 VAL I 11 REMARK 465 GLY I 154 REMARK 465 GLY I 155 REMARK 465 GLN I 156 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLN A 1 CG CD OE1 NE2 REMARK 470 ARG A 31 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 63 CG CD CE NZ REMARK 470 LYS A 219 CG CD CE NZ REMARK 470 LYS A 223 CG CD CE NZ REMARK 470 ARG B 24 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 127 CG CD CE NZ REMARK 470 LYS B 146 CG CD CE NZ REMARK 470 LYS B 170 CG CD CE NZ REMARK 470 LYS B 191 CG CD CE NZ REMARK 470 GLU C 30 CG CD OE1 OE2 REMARK 470 LYS C 31 CG CD CE NZ REMARK 470 LYS C 44 CG CD CE NZ REMARK 470 ARG C 107 CG CD NE CZ NH1 NH2 REMARK 470 GLN D 1 CG CD OE1 NE2 REMARK 470 LYS D 13 CG CD CE NZ REMARK 470 SER D 122 OG REMARK 470 LYS D 223 CG CD CE NZ REMARK 470 HIS D 226 CG ND1 CD2 CE1 NE2 REMARK 470 HIS D 227 CG ND1 CD2 CE1 NE2 REMARK 470 HIS D 228 CG ND1 CD2 CE1 NE2 REMARK 470 HIS D 229 CG ND1 CD2 CE1 NE2 REMARK 470 LYS E 170 CG CD CE NZ REMARK 470 LYS E 191 CG CD CE NZ REMARK 470 GLU F 30 CG CD OE1 OE2 REMARK 470 LYS F 31 CG CD CE NZ REMARK 470 LYS F 69 CG CD CE NZ REMARK 470 GLU F 72 CG CD OE1 OE2 REMARK 470 GLN F 140 CG CD OE1 NE2 REMARK 470 LYS G 210 CG CD CE NZ REMARK 470 LYS G 223 CG CD CE NZ REMARK 470 GLU H 214 CG CD OE1 OE2 REMARK 470 GLN K 3 CG CD OE1 NE2 REMARK 470 LYS K 23 CG CD CE NZ REMARK 470 GLU K 89 CG CD OE1 OE2 REMARK 470 LYS K 126 CG CD CE NZ REMARK 470 LEU K 184 CG CD1 CD2 REMARK 470 LYS K 223 CG CD CE NZ REMARK 470 LYS J 191 CG CD CE NZ REMARK 470 GLU L 30 CG CD OE1 OE2 REMARK 470 LYS L 31 CG CD CE NZ REMARK 470 LYS L 44 CG CD CE NZ REMARK 470 ARG L 107 CG CD NE CZ NH1 NH2 REMARK 470 ASP L 118 CG OD1 OD2 REMARK 470 GLU L 120 CG CD OE1 OE2 REMARK 470 LYS I 31 CG CD CE NZ REMARK 470 LYS I 44 CG CD CE NZ REMARK 470 GLU I 72 CG CD OE1 OE2 REMARK 470 GLN I 82 CG CD OE1 NE2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 PRO A 158 N - CA - CB ANGL. DEV. = -7.0 DEGREES REMARK 500 PRO D 158 N - CA - CB ANGL. DEV. = -7.4 DEGREES REMARK 500 PRO G 158 N - CA - CB ANGL. DEV. = -7.5 DEGREES REMARK 500 PRO K 158 N - CA - CB ANGL. DEV. = -7.4 DEGREES 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 CYS A 22 87.25 -157.31 REMARK 500 PHE A 29 42.84 -108.09 REMARK 500 GLN A 43 -165.40 -121.16 REMARK 500 SER A 121 147.81 -174.15 REMARK 500 ASP A 153 69.09 63.85 REMARK 500 GLU B 27 -166.89 -118.08 REMARK 500 SER B 31 41.31 37.34 REMARK 500 ALA B 51 -42.05 72.39 REMARK 500 PRO B 59 150.01 -49.39 REMARK 500 ALA B 84 -172.76 -171.65 REMARK 500 LEU B 97 50.84 -113.40 REMARK 500 ASN B 139 74.38 59.05 REMARK 500 CYS D 22 86.68 -156.86 REMARK 500 THR D 28 -164.35 -101.37 REMARK 500 PHE D 29 51.96 -153.16 REMARK 500 ASP D 153 69.84 66.13 REMARK 500 HIS D 228 -6.50 -141.46 REMARK 500 GLU E 27 -168.92 -118.49 REMARK 500 ALA E 51 -43.67 73.46 REMARK 500 ALA E 84 -175.38 -171.97 REMARK 500 ASN E 139 78.06 52.39 REMARK 500 GLU E 144 108.89 -56.80 REMARK 500 HIS F 105 53.00 38.31 REMARK 500 ASN F 139 134.85 -34.76 REMARK 500 CYS G 22 85.81 -155.52 REMARK 500 THR G 28 -168.16 -123.54 REMARK 500 SER G 121 147.51 -173.30 REMARK 500 ASP G 153 68.03 65.97 REMARK 500 GLU H 27 -161.36 -120.39 REMARK 500 SER H 30 -144.75 51.31 REMARK 500 SER H 31 53.42 -95.37 REMARK 500 ALA H 51 -44.06 76.65 REMARK 500 ALA H 84 -172.72 -170.47 REMARK 500 LEU H 97 53.11 -119.20 REMARK 500 ASN H 139 73.54 62.21 REMARK 500 GLU H 144 105.90 -53.72 REMARK 500 LEU H 182 -165.09 -119.96 REMARK 500 CYS K 22 86.80 -156.14 REMARK 500 GLN K 43 -169.54 -111.52 REMARK 500 ALA K 92 -179.78 -172.66 REMARK 500 ASP K 153 78.10 62.02 REMARK 500 SER J 30 -144.98 57.92 REMARK 500 SER J 31 52.63 -97.92 REMARK 500 ALA J 51 -43.89 74.02 REMARK 500 ALA J 84 -174.50 -171.98 REMARK 500 LEU J 97 50.92 -113.02 REMARK 500 ASN J 139 73.47 59.94 REMARK 500 GLU J 144 108.89 -52.54 REMARK 500 ASN L 139 46.86 -85.34 REMARK 500 ASN I 139 39.44 -84.86 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 SER D 136 SER D 137 148.55 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG A 57 0.08 SIDE CHAIN REMARK 500 ARG B 18 0.11 SIDE CHAIN REMARK 500 ARG B 61 0.10 SIDE CHAIN REMARK 500 ARG E 18 0.11 SIDE CHAIN REMARK 500 ARG E 61 0.09 SIDE CHAIN REMARK 500 ARG F 93 0.09 SIDE CHAIN REMARK 500 ARG H 18 0.08 SIDE CHAIN REMARK 500 ARG H 143 0.13 SIDE CHAIN REMARK 500 ARG K 67 0.09 SIDE CHAIN REMARK 500 ARG J 61 0.08 SIDE CHAIN REMARK 500 ARG I 107 0.11 SIDE CHAIN REMARK 500 ARG I 134 0.09 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH D 309 DISTANCE = 6.31 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 8VQF RELATED DB: PDB REMARK 900 RELATED ID: 8VQG RELATED DB: PDB DBREF 9NPG A 1 231 PDB 9NPG 9NPG 1 231 DBREF 9NPG B 1 215 PDB 9NPG 9NPG 1 215 DBREF 9NPG C 9 156 UNP O18873 ALL1_CANLF 27 174 DBREF 9NPG D 1 231 PDB 9NPG 9NPG 1 231 DBREF 9NPG E 1 215 PDB 9NPG 9NPG 1 215 DBREF 9NPG F 9 156 UNP O18873 ALL1_CANLF 27 174 DBREF 9NPG G 1 231 PDB 9NPG 9NPG 1 231 DBREF 9NPG H 1 215 PDB 9NPG 9NPG 1 215 DBREF 9NPG K 1 231 PDB 9NPG 9NPG 1 231 DBREF 9NPG J 1 215 PDB 9NPG 9NPG 1 215 DBREF 9NPG L 9 156 UNP O18873 ALL1_CANLF 27 174 DBREF 9NPG I 9 156 UNP O18873 ALL1_CANLF 27 174 SEQADV 9NPG SER C 100 UNP O18873 CYS 118 ENGINEERED MUTATION SEQADV 9NPG SER F 100 UNP O18873 CYS 118 ENGINEERED MUTATION SEQADV 9NPG SER L 100 UNP O18873 CYS 118 ENGINEERED MUTATION SEQADV 9NPG SER I 100 UNP O18873 CYS 118 ENGINEERED MUTATION SEQRES 1 A 231 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL GLN LYS SEQRES 2 A 231 PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 A 231 GLY THR PHE SER ARG TYR PRO LEU ILE TRP VAL ARG GLN SEQRES 4 A 231 THR PRO GLY GLN GLY LEU GLU TRP MET GLY GLY ILE PHE SEQRES 5 A 231 PRO VAL ILE GLY ARG THR ASN TYR ALA GLU LYS PHE GLN SEQRES 6 A 231 GLY ARG VAL THR ILE THR ALA ASP GLU SER THR SER THR SEQRES 7 A 231 ALA TYR MET GLU LEU ASN SER LEU THR SER GLU ASP THR SEQRES 8 A 231 ALA VAL TYR TYR CYS ALA ARG LEU ASP THR TYR GLU ILE SEQRES 9 A 231 LEU GLY TYR GLY THR ASP VAL TRP GLY GLN GLY THR THR SEQRES 10 A 231 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 A 231 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 A 231 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 A 231 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 A 231 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 A 231 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 A 231 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 A 231 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU SEQRES 18 A 231 PRO LYS SER CYS HIS HIS HIS HIS HIS HIS SEQRES 1 B 215 GLU ILE VAL LEU THR GLN SER PRO ALA THR LEU SER LEU SEQRES 2 B 215 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 B 215 GLU SER VAL SER SER SER VAL ALA TRP TYR GLN GLN LYS SEQRES 4 B 215 PHE GLY GLN ALA PRO ARG LEU LEU ILE TYR ASP ALA SER SEQRES 5 B 215 ASN ARG ALA THR GLY ILE PRO ALA ARG PHE SER GLY SER SEQRES 6 B 215 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 B 215 GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN LEU ARG SEQRES 8 B 215 SER ASN TRP PRO PRO LEU THR PHE GLY GLY GLY THR LYS SEQRES 9 B 215 VAL GLN ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 B 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 B 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 B 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 B 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 B 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 B 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 B 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 B 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 C 148 ASP THR VAL ALA VAL SER GLY LYS TRP TYR LEU LYS ALA SEQRES 2 C 148 MET THR ALA ASP GLN GLU VAL PRO GLU LYS PRO ASP SER SEQRES 3 C 148 VAL THR PRO MET ILE LEU LYS ALA GLN LYS GLY GLY ASN SEQRES 4 C 148 LEU GLU ALA LYS ILE THR MET LEU THR ASN GLY GLN CYS SEQRES 5 C 148 GLN ASN ILE THR VAL VAL LEU HIS LYS THR SER GLU PRO SEQRES 6 C 148 GLY LYS TYR THR ALA TYR GLU GLY GLN ARG VAL VAL PHE SEQRES 7 C 148 ILE GLN PRO SER PRO VAL ARG ASP HIS TYR ILE LEU TYR SEQRES 8 C 148 SER GLU GLY GLU LEU HIS GLY ARG GLN ILE ARG MET ALA SEQRES 9 C 148 LYS LEU LEU GLY ARG ASP PRO GLU GLN SER GLN GLU ALA SEQRES 10 C 148 LEU GLU ASP PHE ARG GLU PHE SER ARG ALA LYS GLY LEU SEQRES 11 C 148 ASN GLN GLU ILE LEU GLU LEU ALA GLN SER GLU THR CYS SEQRES 12 C 148 SER PRO GLY GLY GLN SEQRES 1 D 231 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL GLN LYS SEQRES 2 D 231 PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 D 231 GLY THR PHE SER ARG TYR PRO LEU ILE TRP VAL ARG GLN SEQRES 4 D 231 THR PRO GLY GLN GLY LEU GLU TRP MET GLY GLY ILE PHE SEQRES 5 D 231 PRO VAL ILE GLY ARG THR ASN TYR ALA GLU LYS PHE GLN SEQRES 6 D 231 GLY ARG VAL THR ILE THR ALA ASP GLU SER THR SER THR SEQRES 7 D 231 ALA TYR MET GLU LEU ASN SER LEU THR SER GLU ASP THR SEQRES 8 D 231 ALA VAL TYR TYR CYS ALA ARG LEU ASP THR TYR GLU ILE SEQRES 9 D 231 LEU GLY TYR GLY THR ASP VAL TRP GLY GLN GLY THR THR SEQRES 10 D 231 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 D 231 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 D 231 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 D 231 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 D 231 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 D 231 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 D 231 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 D 231 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU SEQRES 18 D 231 PRO LYS SER CYS HIS HIS HIS HIS HIS HIS SEQRES 1 E 215 GLU ILE VAL LEU THR GLN SER PRO ALA THR LEU SER LEU SEQRES 2 E 215 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 E 215 GLU SER VAL SER SER SER VAL ALA TRP TYR GLN GLN LYS SEQRES 4 E 215 PHE GLY GLN ALA PRO ARG LEU LEU ILE TYR ASP ALA SER SEQRES 5 E 215 ASN ARG ALA THR GLY ILE PRO ALA ARG PHE SER GLY SER SEQRES 6 E 215 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 E 215 GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN LEU ARG SEQRES 8 E 215 SER ASN TRP PRO PRO LEU THR PHE GLY GLY GLY THR LYS SEQRES 9 E 215 VAL GLN ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 E 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 E 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 E 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 E 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 E 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 E 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 E 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 E 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 F 148 ASP THR VAL ALA VAL SER GLY LYS TRP TYR LEU LYS ALA SEQRES 2 F 148 MET THR ALA ASP GLN GLU VAL PRO GLU LYS PRO ASP SER SEQRES 3 F 148 VAL THR PRO MET ILE LEU LYS ALA GLN LYS GLY GLY ASN SEQRES 4 F 148 LEU GLU ALA LYS ILE THR MET LEU THR ASN GLY GLN CYS SEQRES 5 F 148 GLN ASN ILE THR VAL VAL LEU HIS LYS THR SER GLU PRO SEQRES 6 F 148 GLY LYS TYR THR ALA TYR GLU GLY GLN ARG VAL VAL PHE SEQRES 7 F 148 ILE GLN PRO SER PRO VAL ARG ASP HIS TYR ILE LEU TYR SEQRES 8 F 148 SER GLU GLY GLU LEU HIS GLY ARG GLN ILE ARG MET ALA SEQRES 9 F 148 LYS LEU LEU GLY ARG ASP PRO GLU GLN SER GLN GLU ALA SEQRES 10 F 148 LEU GLU ASP PHE ARG GLU PHE SER ARG ALA LYS GLY LEU SEQRES 11 F 148 ASN GLN GLU ILE LEU GLU LEU ALA GLN SER GLU THR CYS SEQRES 12 F 148 SER PRO GLY GLY GLN SEQRES 1 G 231 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL GLN LYS SEQRES 2 G 231 PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 G 231 GLY THR PHE SER ARG TYR PRO LEU ILE TRP VAL ARG GLN SEQRES 4 G 231 THR PRO GLY GLN GLY LEU GLU TRP MET GLY GLY ILE PHE SEQRES 5 G 231 PRO VAL ILE GLY ARG THR ASN TYR ALA GLU LYS PHE GLN SEQRES 6 G 231 GLY ARG VAL THR ILE THR ALA ASP GLU SER THR SER THR SEQRES 7 G 231 ALA TYR MET GLU LEU ASN SER LEU THR SER GLU ASP THR SEQRES 8 G 231 ALA VAL TYR TYR CYS ALA ARG LEU ASP THR TYR GLU ILE SEQRES 9 G 231 LEU GLY TYR GLY THR ASP VAL TRP GLY GLN GLY THR THR SEQRES 10 G 231 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 G 231 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 G 231 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 G 231 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 G 231 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 G 231 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 G 231 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 G 231 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU SEQRES 18 G 231 PRO LYS SER CYS HIS HIS HIS HIS HIS HIS SEQRES 1 H 215 GLU ILE VAL LEU THR GLN SER PRO ALA THR LEU SER LEU SEQRES 2 H 215 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 H 215 GLU SER VAL SER SER SER VAL ALA TRP TYR GLN GLN LYS SEQRES 4 H 215 PHE GLY GLN ALA PRO ARG LEU LEU ILE TYR ASP ALA SER SEQRES 5 H 215 ASN ARG ALA THR GLY ILE PRO ALA ARG PHE SER GLY SER SEQRES 6 H 215 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 H 215 GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN LEU ARG SEQRES 8 H 215 SER ASN TRP PRO PRO LEU THR PHE GLY GLY GLY THR LYS SEQRES 9 H 215 VAL GLN ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 H 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 H 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 H 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 H 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 H 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 H 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 H 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 H 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 K 231 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL GLN LYS SEQRES 2 K 231 PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 K 231 GLY THR PHE SER ARG TYR PRO LEU ILE TRP VAL ARG GLN SEQRES 4 K 231 THR PRO GLY GLN GLY LEU GLU TRP MET GLY GLY ILE PHE SEQRES 5 K 231 PRO VAL ILE GLY ARG THR ASN TYR ALA GLU LYS PHE GLN SEQRES 6 K 231 GLY ARG VAL THR ILE THR ALA ASP GLU SER THR SER THR SEQRES 7 K 231 ALA TYR MET GLU LEU ASN SER LEU THR SER GLU ASP THR SEQRES 8 K 231 ALA VAL TYR TYR CYS ALA ARG LEU ASP THR TYR GLU ILE SEQRES 9 K 231 LEU GLY TYR GLY THR ASP VAL TRP GLY GLN GLY THR THR SEQRES 10 K 231 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 K 231 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 K 231 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 K 231 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 K 231 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 K 231 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 K 231 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 K 231 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU SEQRES 18 K 231 PRO LYS SER CYS HIS HIS HIS HIS HIS HIS SEQRES 1 J 215 GLU ILE VAL LEU THR GLN SER PRO ALA THR LEU SER LEU SEQRES 2 J 215 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 J 215 GLU SER VAL SER SER SER VAL ALA TRP TYR GLN GLN LYS SEQRES 4 J 215 PHE GLY GLN ALA PRO ARG LEU LEU ILE TYR ASP ALA SER SEQRES 5 J 215 ASN ARG ALA THR GLY ILE PRO ALA ARG PHE SER GLY SER SEQRES 6 J 215 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 J 215 GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN LEU ARG SEQRES 8 J 215 SER ASN TRP PRO PRO LEU THR PHE GLY GLY GLY THR LYS SEQRES 9 J 215 VAL GLN ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 J 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 J 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 J 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 J 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 J 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 J 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 J 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 J 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 L 148 ASP THR VAL ALA VAL SER GLY LYS TRP TYR LEU LYS ALA SEQRES 2 L 148 MET THR ALA ASP GLN GLU VAL PRO GLU LYS PRO ASP SER SEQRES 3 L 148 VAL THR PRO MET ILE LEU LYS ALA GLN LYS GLY GLY ASN SEQRES 4 L 148 LEU GLU ALA LYS ILE THR MET LEU THR ASN GLY GLN CYS SEQRES 5 L 148 GLN ASN ILE THR VAL VAL LEU HIS LYS THR SER GLU PRO SEQRES 6 L 148 GLY LYS TYR THR ALA TYR GLU GLY GLN ARG VAL VAL PHE SEQRES 7 L 148 ILE GLN PRO SER PRO VAL ARG ASP HIS TYR ILE LEU TYR SEQRES 8 L 148 SER GLU GLY GLU LEU HIS GLY ARG GLN ILE ARG MET ALA SEQRES 9 L 148 LYS LEU LEU GLY ARG ASP PRO GLU GLN SER GLN GLU ALA SEQRES 10 L 148 LEU GLU ASP PHE ARG GLU PHE SER ARG ALA LYS GLY LEU SEQRES 11 L 148 ASN GLN GLU ILE LEU GLU LEU ALA GLN SER GLU THR CYS SEQRES 12 L 148 SER PRO GLY GLY GLN SEQRES 1 I 148 ASP THR VAL ALA VAL SER GLY LYS TRP TYR LEU LYS ALA SEQRES 2 I 148 MET THR ALA ASP GLN GLU VAL PRO GLU LYS PRO ASP SER SEQRES 3 I 148 VAL THR PRO MET ILE LEU LYS ALA GLN LYS GLY GLY ASN SEQRES 4 I 148 LEU GLU ALA LYS ILE THR MET LEU THR ASN GLY GLN CYS SEQRES 5 I 148 GLN ASN ILE THR VAL VAL LEU HIS LYS THR SER GLU PRO SEQRES 6 I 148 GLY LYS TYR THR ALA TYR GLU GLY GLN ARG VAL VAL PHE SEQRES 7 I 148 ILE GLN PRO SER PRO VAL ARG ASP HIS TYR ILE LEU TYR SEQRES 8 I 148 SER GLU GLY GLU LEU HIS GLY ARG GLN ILE ARG MET ALA SEQRES 9 I 148 LYS LEU LEU GLY ARG ASP PRO GLU GLN SER GLN GLU ALA SEQRES 10 I 148 LEU GLU ASP PHE ARG GLU PHE SER ARG ALA LYS GLY LEU SEQRES 11 I 148 ASN GLN GLU ILE LEU GLU LEU ALA GLN SER GLU THR CYS SEQRES 12 I 148 SER PRO GLY GLY GLN FORMUL 13 HOH *96(H2 O) HELIX 1 AA1 THR A 87 THR A 91 5 5 HELIX 2 AA2 SER A 165 ALA A 167 5 3 HELIX 3 AA3 SER A 196 GLY A 199 5 4 HELIX 4 AA4 LYS A 210 ASN A 213 5 4 HELIX 5 AA5 GLU B 79 PHE B 83 5 5 HELIX 6 AA6 SER B 122 LYS B 127 1 6 HELIX 7 AA7 LYS B 184 LYS B 189 1 6 HELIX 8 AA8 LYS C 44 GLY C 46 5 3 HELIX 9 AA9 SER C 122 GLY C 137 1 16 HELIX 10 AB1 THR D 87 THR D 91 5 5 HELIX 11 AB2 SER D 165 ALA D 167 5 3 HELIX 12 AB3 SER D 196 GLY D 199 5 4 HELIX 13 AB4 LYS D 210 ASN D 213 5 4 HELIX 14 AB5 GLU E 79 PHE E 83 5 5 HELIX 15 AB6 SER E 122 LYS E 127 1 6 HELIX 16 AB7 LYS E 184 LYS E 189 1 6 HELIX 17 AB8 LYS F 44 GLY F 46 5 3 HELIX 18 AB9 SER F 122 GLY F 137 1 16 HELIX 19 AC1 THR G 87 THR G 91 5 5 HELIX 20 AC2 SER G 165 ALA G 167 5 3 HELIX 21 AC3 SER G 196 GLY G 199 5 4 HELIX 22 AC4 LYS G 210 ASN G 213 5 4 HELIX 23 AC5 GLU H 79 PHE H 83 5 5 HELIX 24 AC6 GLN H 125 SER H 128 5 4 HELIX 25 AC7 LYS H 184 LYS H 189 1 6 HELIX 26 AC8 THR K 87 THR K 91 5 5 HELIX 27 AC9 SER K 165 ALA K 167 5 3 HELIX 28 AD1 SER K 196 GLY K 199 5 4 HELIX 29 AD2 LYS K 210 ASN K 213 5 4 HELIX 30 AD3 GLU J 79 PHE J 83 5 5 HELIX 31 AD4 SER J 122 LYS J 127 1 6 HELIX 32 AD5 LYS J 184 LYS J 189 1 6 HELIX 33 AD6 LYS L 44 GLY L 46 5 3 HELIX 34 AD7 SER L 122 GLY L 137 1 16 HELIX 35 AD8 LYS I 44 GLY I 46 5 3 HELIX 36 AD9 SER I 122 GLY I 137 1 16 SHEET 1 AA1 4 GLN A 3 GLN A 6 0 SHEET 2 AA1 4 VAL A 18 SER A 25 -1 O SER A 25 N GLN A 3 SHEET 3 AA1 4 THR A 78 LEU A 83 -1 O MET A 81 N VAL A 20 SHEET 4 AA1 4 VAL A 68 ASP A 73 -1 N ASP A 73 O THR A 78 SHEET 1 AA2 6 GLU A 10 GLN A 12 0 SHEET 2 AA2 6 THR A 116 VAL A 120 1 O THR A 119 N GLU A 10 SHEET 3 AA2 6 ALA A 92 ARG A 98 -1 N TYR A 94 O THR A 116 SHEET 4 AA2 6 LEU A 34 GLN A 39 -1 N VAL A 37 O TYR A 95 SHEET 5 AA2 6 GLU A 46 PHE A 52 -1 O GLU A 46 N ARG A 38 SHEET 6 AA2 6 ARG A 57 TYR A 60 -1 O ASN A 59 N GLY A 50 SHEET 1 AA3 4 GLU A 10 GLN A 12 0 SHEET 2 AA3 4 THR A 116 VAL A 120 1 O THR A 119 N GLU A 10 SHEET 3 AA3 4 ALA A 92 ARG A 98 -1 N TYR A 94 O THR A 116 SHEET 4 AA3 4 VAL A 111 TRP A 112 -1 O VAL A 111 N ARG A 98 SHEET 1 AA4 4 SER A 129 LEU A 133 0 SHEET 2 AA4 4 THR A 144 TYR A 154 -1 O LEU A 150 N PHE A 131 SHEET 3 AA4 4 TYR A 185 PRO A 194 -1 O TYR A 185 N TYR A 154 SHEET 4 AA4 4 VAL A 172 THR A 174 -1 N HIS A 173 O VAL A 190 SHEET 1 AA5 4 SER A 129 LEU A 133 0 SHEET 2 AA5 4 THR A 144 TYR A 154 -1 O LEU A 150 N PHE A 131 SHEET 3 AA5 4 TYR A 185 PRO A 194 -1 O TYR A 185 N TYR A 154 SHEET 4 AA5 4 VAL A 178 LEU A 179 -1 N VAL A 178 O SER A 186 SHEET 1 AA6 3 THR A 160 TRP A 163 0 SHEET 2 AA6 3 TYR A 203 HIS A 209 -1 O ASN A 206 N SER A 162 SHEET 3 AA6 3 THR A 214 VAL A 220 -1 O VAL A 216 N VAL A 207 SHEET 1 AA7 3 LEU B 4 THR B 5 0 SHEET 2 AA7 3 ALA B 19 VAL B 29 -1 O ARG B 24 N THR B 5 SHEET 3 AA7 3 PHE B 62 ILE B 75 -1 O GLY B 68 N VAL B 29 SHEET 1 AA8 6 THR B 10 LEU B 13 0 SHEET 2 AA8 6 THR B 103 ILE B 107 1 O GLN B 106 N LEU B 11 SHEET 3 AA8 6 VAL B 85 LEU B 90 -1 N TYR B 86 O THR B 103 SHEET 4 AA8 6 VAL B 33 GLN B 38 -1 N TYR B 36 O TYR B 87 SHEET 5 AA8 6 ARG B 45 TYR B 49 -1 O LEU B 47 N TRP B 35 SHEET 6 AA8 6 ASN B 53 ARG B 54 -1 O ASN B 53 N TYR B 49 SHEET 1 AA9 4 SER B 115 PHE B 119 0 SHEET 2 AA9 4 THR B 130 PHE B 140 -1 O LEU B 136 N PHE B 117 SHEET 3 AA9 4 TYR B 174 SER B 183 -1 O LEU B 176 N LEU B 137 SHEET 4 AA9 4 SER B 160 VAL B 164 -1 N SER B 163 O SER B 177 SHEET 1 AB1 4 ALA B 154 LEU B 155 0 SHEET 2 AB1 4 ALA B 145 VAL B 151 -1 N VAL B 151 O ALA B 154 SHEET 3 AB1 4 VAL B 192 HIS B 199 -1 O GLU B 196 N GLN B 148 SHEET 4 AB1 4 VAL B 206 ASN B 211 -1 O VAL B 206 N VAL B 197 SHEET 1 AB2 6 LEU C 143 GLU C 144 0 SHEET 2 AB2 6 SER C 14 ALA C 24 -1 N MET C 22 O LEU C 143 SHEET 3 AB2 6 MET C 38 ALA C 42 -1 O MET C 38 N TRP C 17 SHEET 4 AB2 6 LEU C 48 THR C 56 -1 O GLU C 49 N LYS C 41 SHEET 5 AB2 6 SER C 34 VAL C 35 -1 N SER C 34 O LEU C 55 SHEET 6 AB2 6 ALA C 146 GLN C 147 1 O ALA C 146 N VAL C 35 SHEET 1 AB310 LEU C 143 GLU C 144 0 SHEET 2 AB310 SER C 14 ALA C 24 -1 N MET C 22 O LEU C 143 SHEET 3 AB310 ARG C 107 GLY C 116 -1 O GLY C 116 N TYR C 18 SHEET 4 AB310 HIS C 95 LEU C 104 -1 N SER C 100 O MET C 111 SHEET 5 AB310 ARG C 83 PRO C 89 -1 N PHE C 86 O TYR C 99 SHEET 6 AB310 LYS C 75 ALA C 78 -1 N TYR C 76 O VAL C 85 SHEET 7 AB310 GLN C 59 LYS C 69 -1 N HIS C 68 O THR C 77 SHEET 8 AB310 LEU C 48 THR C 56 -1 N LEU C 48 O LEU C 67 SHEET 9 AB310 SER C 34 VAL C 35 -1 N SER C 34 O LEU C 55 SHEET 10 AB310 ALA C 146 GLN C 147 1 O ALA C 146 N VAL C 35 SHEET 1 AB4 4 LEU D 4 GLN D 6 0 SHEET 2 AB4 4 VAL D 18 ALA D 24 -1 O LYS D 23 N VAL D 5 SHEET 3 AB4 4 THR D 78 LEU D 83 -1 O MET D 81 N VAL D 20 SHEET 4 AB4 4 VAL D 68 ASP D 73 -1 N ASP D 73 O THR D 78 SHEET 1 AB5 6 GLU D 10 GLN D 12 0 SHEET 2 AB5 6 THR D 116 VAL D 120 1 O THR D 117 N GLU D 10 SHEET 3 AB5 6 ALA D 92 ARG D 98 -1 N TYR D 94 O THR D 116 SHEET 4 AB5 6 LEU D 34 GLN D 39 -1 N VAL D 37 O TYR D 95 SHEET 5 AB5 6 GLU D 46 PHE D 52 -1 O GLU D 46 N ARG D 38 SHEET 6 AB5 6 ARG D 57 TYR D 60 -1 O ASN D 59 N GLY D 50 SHEET 1 AB6 4 GLU D 10 GLN D 12 0 SHEET 2 AB6 4 THR D 116 VAL D 120 1 O THR D 117 N GLU D 10 SHEET 3 AB6 4 ALA D 92 ARG D 98 -1 N TYR D 94 O THR D 116 SHEET 4 AB6 4 VAL D 111 TRP D 112 -1 O VAL D 111 N ARG D 98 SHEET 1 AB7 4 SER D 129 LEU D 133 0 SHEET 2 AB7 4 THR D 144 TYR D 154 -1 O LEU D 150 N PHE D 131 SHEET 3 AB7 4 TYR D 185 PRO D 194 -1 O TYR D 185 N TYR D 154 SHEET 4 AB7 4 VAL D 172 THR D 174 -1 N HIS D 173 O VAL D 190 SHEET 1 AB8 4 SER D 129 LEU D 133 0 SHEET 2 AB8 4 THR D 144 TYR D 154 -1 O LEU D 150 N PHE D 131 SHEET 3 AB8 4 TYR D 185 PRO D 194 -1 O TYR D 185 N TYR D 154 SHEET 4 AB8 4 VAL D 178 LEU D 179 -1 N VAL D 178 O SER D 186 SHEET 1 AB9 3 THR D 160 TRP D 163 0 SHEET 2 AB9 3 ILE D 204 HIS D 209 -1 O ASN D 206 N SER D 162 SHEET 3 AB9 3 THR D 214 LYS D 219 -1 O VAL D 216 N VAL D 207 SHEET 1 AC1 3 LEU E 4 THR E 5 0 SHEET 2 AC1 3 ALA E 19 VAL E 29 -1 O ARG E 24 N THR E 5 SHEET 3 AC1 3 PHE E 62 ILE E 75 -1 O LEU E 73 N LEU E 21 SHEET 1 AC2 6 THR E 10 LEU E 13 0 SHEET 2 AC2 6 THR E 103 ILE E 107 1 O LYS E 104 N LEU E 11 SHEET 3 AC2 6 VAL E 85 LEU E 90 -1 N TYR E 86 O THR E 103 SHEET 4 AC2 6 VAL E 33 GLN E 38 -1 N TYR E 36 O TYR E 87 SHEET 5 AC2 6 ARG E 45 TYR E 49 -1 O LEU E 47 N TRP E 35 SHEET 6 AC2 6 ASN E 53 ARG E 54 -1 O ASN E 53 N TYR E 49 SHEET 1 AC3 4 SER E 115 PHE E 119 0 SHEET 2 AC3 4 THR E 130 PHE E 140 -1 O LEU E 136 N PHE E 117 SHEET 3 AC3 4 TYR E 174 SER E 183 -1 O LEU E 180 N VAL E 133 SHEET 4 AC3 4 SER E 160 VAL E 164 -1 N GLN E 161 O THR E 179 SHEET 1 AC4 4 ALA E 154 LEU E 155 0 SHEET 2 AC4 4 ALA E 145 VAL E 151 -1 N VAL E 151 O ALA E 154 SHEET 3 AC4 4 VAL E 192 HIS E 199 -1 O GLU E 196 N GLN E 148 SHEET 4 AC4 4 VAL E 206 ASN E 211 -1 O VAL E 206 N VAL E 197 SHEET 1 AC5 6 LEU F 143 GLU F 144 0 SHEET 2 AC5 6 SER F 14 ALA F 24 -1 N MET F 22 O LEU F 143 SHEET 3 AC5 6 MET F 38 ALA F 42 -1 O MET F 38 N TRP F 17 SHEET 4 AC5 6 LEU F 48 THR F 56 -1 O LYS F 51 N ILE F 39 SHEET 5 AC5 6 SER F 34 VAL F 35 -1 N SER F 34 O LEU F 55 SHEET 6 AC5 6 ALA F 146 GLN F 147 1 O ALA F 146 N VAL F 35 SHEET 1 AC610 LEU F 143 GLU F 144 0 SHEET 2 AC610 SER F 14 ALA F 24 -1 N MET F 22 O LEU F 143 SHEET 3 AC610 ARG F 107 GLY F 116 -1 O GLY F 116 N TYR F 18 SHEET 4 AC610 HIS F 95 LEU F 104 -1 N TYR F 96 O LEU F 115 SHEET 5 AC610 ARG F 83 PRO F 89 -1 N GLN F 88 O ILE F 97 SHEET 6 AC610 LYS F 75 ALA F 78 -1 N TYR F 76 O VAL F 85 SHEET 7 AC610 GLN F 59 LYS F 69 -1 N HIS F 68 O THR F 77 SHEET 8 AC610 LEU F 48 THR F 56 -1 N LEU F 48 O LEU F 67 SHEET 9 AC610 SER F 34 VAL F 35 -1 N SER F 34 O LEU F 55 SHEET 10 AC610 ALA F 146 GLN F 147 1 O ALA F 146 N VAL F 35 SHEET 1 AC7 4 LEU G 4 GLN G 6 0 SHEET 2 AC7 4 VAL G 18 ALA G 24 -1 O LYS G 23 N VAL G 5 SHEET 3 AC7 4 THR G 78 LEU G 83 -1 O MET G 81 N VAL G 20 SHEET 4 AC7 4 VAL G 68 ASP G 73 -1 N ASP G 73 O THR G 78 SHEET 1 AC8 6 GLU G 10 GLN G 12 0 SHEET 2 AC8 6 THR G 116 VAL G 120 1 O THR G 117 N GLU G 10 SHEET 3 AC8 6 ALA G 92 ARG G 98 -1 N TYR G 94 O THR G 116 SHEET 4 AC8 6 LEU G 34 GLN G 39 -1 N VAL G 37 O TYR G 95 SHEET 5 AC8 6 GLU G 46 PHE G 52 -1 O GLU G 46 N ARG G 38 SHEET 6 AC8 6 ARG G 57 TYR G 60 -1 O ASN G 59 N GLY G 50 SHEET 1 AC9 4 GLU G 10 GLN G 12 0 SHEET 2 AC9 4 THR G 116 VAL G 120 1 O THR G 117 N GLU G 10 SHEET 3 AC9 4 ALA G 92 ARG G 98 -1 N TYR G 94 O THR G 116 SHEET 4 AC9 4 VAL G 111 TRP G 112 -1 O VAL G 111 N ARG G 98 SHEET 1 AD1 4 SER G 129 LEU G 133 0 SHEET 2 AD1 4 THR G 144 TYR G 154 -1 O LEU G 150 N PHE G 131 SHEET 3 AD1 4 TYR G 185 PRO G 194 -1 O LEU G 187 N VAL G 151 SHEET 4 AD1 4 VAL G 172 THR G 174 -1 N HIS G 173 O VAL G 190 SHEET 1 AD2 4 SER G 129 LEU G 133 0 SHEET 2 AD2 4 THR G 144 TYR G 154 -1 O LEU G 150 N PHE G 131 SHEET 3 AD2 4 TYR G 185 PRO G 194 -1 O LEU G 187 N VAL G 151 SHEET 4 AD2 4 VAL G 178 LEU G 179 -1 N VAL G 178 O SER G 186 SHEET 1 AD3 3 THR G 160 TRP G 163 0 SHEET 2 AD3 3 TYR G 203 HIS G 209 -1 O ASN G 206 N SER G 162 SHEET 3 AD3 3 THR G 214 VAL G 220 -1 O VAL G 216 N VAL G 207 SHEET 1 AD4 4 LEU H 4 THR H 5 0 SHEET 2 AD4 4 ALA H 19 ALA H 25 -1 O ARG H 24 N THR H 5 SHEET 3 AD4 4 ASP H 70 ILE H 75 -1 O LEU H 73 N LEU H 21 SHEET 4 AD4 4 PHE H 62 SER H 67 -1 N SER H 63 O THR H 74 SHEET 1 AD5 6 THR H 10 LEU H 13 0 SHEET 2 AD5 6 THR H 103 ILE H 107 1 O GLN H 106 N LEU H 11 SHEET 3 AD5 6 VAL H 85 LEU H 90 -1 N TYR H 86 O THR H 103 SHEET 4 AD5 6 VAL H 33 GLN H 38 -1 N TYR H 36 O TYR H 87 SHEET 5 AD5 6 ARG H 45 TYR H 49 -1 O LEU H 47 N TRP H 35 SHEET 6 AD5 6 ASN H 53 ARG H 54 -1 O ASN H 53 N TYR H 49 SHEET 1 AD6 4 SER H 115 PHE H 119 0 SHEET 2 AD6 4 THR H 130 PHE H 140 -1 O LEU H 136 N PHE H 117 SHEET 3 AD6 4 TYR H 174 SER H 183 -1 O LEU H 176 N LEU H 137 SHEET 4 AD6 4 SER H 160 VAL H 164 -1 N SER H 163 O SER H 177 SHEET 1 AD7 4 ALA H 154 LEU H 155 0 SHEET 2 AD7 4 ALA H 145 VAL H 151 -1 N VAL H 151 O ALA H 154 SHEET 3 AD7 4 VAL H 192 HIS H 199 -1 O GLU H 196 N GLN H 148 SHEET 4 AD7 4 VAL H 206 ASN H 211 -1 O VAL H 206 N VAL H 197 SHEET 1 AD8 4 GLN K 3 GLN K 6 0 SHEET 2 AD8 4 VAL K 18 SER K 25 -1 O SER K 25 N GLN K 3 SHEET 3 AD8 4 THR K 78 LEU K 83 -1 O MET K 81 N VAL K 20 SHEET 4 AD8 4 VAL K 68 ASP K 73 -1 N ASP K 73 O THR K 78 SHEET 1 AD9 6 GLU K 10 GLN K 12 0 SHEET 2 AD9 6 THR K 116 VAL K 120 1 O THR K 117 N GLU K 10 SHEET 3 AD9 6 ALA K 92 ARG K 98 -1 N TYR K 94 O THR K 116 SHEET 4 AD9 6 LEU K 34 GLN K 39 -1 N VAL K 37 O TYR K 95 SHEET 5 AD9 6 GLU K 46 PHE K 52 -1 O GLU K 46 N ARG K 38 SHEET 6 AD9 6 ARG K 57 TYR K 60 -1 O ASN K 59 N GLY K 50 SHEET 1 AE1 4 GLU K 10 GLN K 12 0 SHEET 2 AE1 4 THR K 116 VAL K 120 1 O THR K 117 N GLU K 10 SHEET 3 AE1 4 ALA K 92 ARG K 98 -1 N TYR K 94 O THR K 116 SHEET 4 AE1 4 VAL K 111 TRP K 112 -1 O VAL K 111 N ARG K 98 SHEET 1 AE2 4 SER K 129 LEU K 133 0 SHEET 2 AE2 4 THR K 144 TYR K 154 -1 O LEU K 150 N PHE K 131 SHEET 3 AE2 4 TYR K 185 PRO K 194 -1 O VAL K 193 N ALA K 145 SHEET 4 AE2 4 VAL K 172 THR K 174 -1 N HIS K 173 O VAL K 190 SHEET 1 AE3 4 SER K 129 LEU K 133 0 SHEET 2 AE3 4 THR K 144 TYR K 154 -1 O LEU K 150 N PHE K 131 SHEET 3 AE3 4 TYR K 185 PRO K 194 -1 O VAL K 193 N ALA K 145 SHEET 4 AE3 4 VAL K 178 LEU K 179 -1 N VAL K 178 O SER K 186 SHEET 1 AE4 3 THR K 160 TRP K 163 0 SHEET 2 AE4 3 TYR K 203 HIS K 209 -1 O ASN K 206 N SER K 162 SHEET 3 AE4 3 THR K 214 VAL K 220 -1 O VAL K 216 N VAL K 207 SHEET 1 AE5 4 LEU J 4 SER J 7 0 SHEET 2 AE5 4 ALA J 19 ALA J 25 -1 O ARG J 24 N THR J 5 SHEET 3 AE5 4 ASP J 70 ILE J 75 -1 O LEU J 73 N LEU J 21 SHEET 4 AE5 4 PHE J 62 SER J 67 -1 N SER J 63 O THR J 74 SHEET 1 AE6 6 THR J 10 LEU J 13 0 SHEET 2 AE6 6 THR J 103 ILE J 107 1 O LYS J 104 N LEU J 11 SHEET 3 AE6 6 VAL J 85 LEU J 90 -1 N TYR J 86 O THR J 103 SHEET 4 AE6 6 VAL J 33 GLN J 38 -1 N TYR J 36 O TYR J 87 SHEET 5 AE6 6 ARG J 45 TYR J 49 -1 O LEU J 47 N TRP J 35 SHEET 6 AE6 6 ASN J 53 ARG J 54 -1 O ASN J 53 N TYR J 49 SHEET 1 AE7 4 SER J 115 PHE J 119 0 SHEET 2 AE7 4 THR J 130 PHE J 140 -1 O LEU J 136 N PHE J 117 SHEET 3 AE7 4 TYR J 174 SER J 183 -1 O LEU J 180 N VAL J 133 SHEET 4 AE7 4 SER J 160 VAL J 164 -1 N SER J 163 O SER J 177 SHEET 1 AE8 4 ALA J 154 LEU J 155 0 SHEET 2 AE8 4 ALA J 145 VAL J 151 -1 N VAL J 151 O ALA J 154 SHEET 3 AE8 4 VAL J 192 HIS J 199 -1 O GLU J 196 N GLN J 148 SHEET 4 AE8 4 VAL J 206 ASN J 211 -1 O VAL J 206 N VAL J 197 SHEET 1 AE9 6 LEU L 143 GLU L 144 0 SHEET 2 AE9 6 SER L 14 ALA L 24 -1 N MET L 22 O LEU L 143 SHEET 3 AE9 6 MET L 38 ALA L 42 -1 O MET L 38 N TRP L 17 SHEET 4 AE9 6 LEU L 48 THR L 56 -1 O LYS L 51 N ILE L 39 SHEET 5 AE9 6 SER L 34 VAL L 35 -1 N SER L 34 O LEU L 55 SHEET 6 AE9 6 ALA L 146 GLN L 147 1 O ALA L 146 N VAL L 35 SHEET 1 AF110 LEU L 143 GLU L 144 0 SHEET 2 AF110 SER L 14 ALA L 24 -1 N MET L 22 O LEU L 143 SHEET 3 AF110 GLN L 108 GLY L 116 -1 O GLY L 116 N TYR L 18 SHEET 4 AF110 HIS L 95 GLU L 103 -1 N TYR L 96 O LEU L 115 SHEET 5 AF110 ARG L 83 PRO L 89 -1 N GLN L 88 O ILE L 97 SHEET 6 AF110 LYS L 75 ALA L 78 -1 N TYR L 76 O VAL L 85 SHEET 7 AF110 GLN L 59 LYS L 69 -1 N HIS L 68 O THR L 77 SHEET 8 AF110 LEU L 48 THR L 56 -1 N LEU L 48 O LEU L 67 SHEET 9 AF110 SER L 34 VAL L 35 -1 N SER L 34 O LEU L 55 SHEET 10 AF110 ALA L 146 GLN L 147 1 O ALA L 146 N VAL L 35 SHEET 1 AF2 6 LEU I 143 GLU I 144 0 SHEET 2 AF2 6 SER I 14 ALA I 24 -1 N MET I 22 O LEU I 143 SHEET 3 AF2 6 MET I 38 ALA I 42 -1 O MET I 38 N TRP I 17 SHEET 4 AF2 6 LEU I 48 THR I 56 -1 O LYS I 51 N ILE I 39 SHEET 5 AF2 6 SER I 34 VAL I 35 -1 N SER I 34 O LEU I 55 SHEET 6 AF2 6 ALA I 146 GLN I 147 1 O ALA I 146 N VAL I 35 SHEET 1 AF310 LEU I 143 GLU I 144 0 SHEET 2 AF310 SER I 14 ALA I 24 -1 N MET I 22 O LEU I 143 SHEET 3 AF310 ARG I 107 GLY I 116 -1 O GLY I 116 N TYR I 18 SHEET 4 AF310 HIS I 95 LEU I 104 -1 N TYR I 96 O LEU I 115 SHEET 5 AF310 ARG I 83 PRO I 89 -1 N VAL I 84 O GLU I 101 SHEET 6 AF310 LYS I 75 ALA I 78 -1 N TYR I 76 O VAL I 85 SHEET 7 AF310 GLN I 59 LYS I 69 -1 N HIS I 68 O THR I 77 SHEET 8 AF310 LEU I 48 THR I 56 -1 N LEU I 48 O LEU I 67 SHEET 9 AF310 SER I 34 VAL I 35 -1 N SER I 34 O LEU I 55 SHEET 10 AF310 ALA I 146 GLN I 147 1 O ALA I 146 N VAL I 35 SSBOND 1 CYS A 22 CYS A 96 1555 1555 2.35 SSBOND 2 CYS A 149 CYS A 205 1555 1555 2.23 SSBOND 3 CYS B 23 CYS B 88 1555 1555 2.10 SSBOND 4 CYS B 135 CYS B 195 1555 1555 1.98 SSBOND 5 CYS C 60 CYS C 151 1555 1555 2.09 SSBOND 6 CYS D 22 CYS D 96 1555 1555 2.37 SSBOND 7 CYS D 149 CYS D 205 1555 1555 2.08 SSBOND 8 CYS E 23 CYS E 88 1555 1555 2.11 SSBOND 9 CYS E 135 CYS E 195 1555 1555 1.98 SSBOND 10 CYS F 60 CYS F 151 1555 1555 2.75 SSBOND 11 CYS G 22 CYS G 96 1555 1555 2.37 SSBOND 12 CYS G 149 CYS G 205 1555 1555 2.07 SSBOND 13 CYS H 23 CYS H 88 1555 1555 2.09 SSBOND 14 CYS H 135 CYS H 195 1555 1555 2.02 SSBOND 15 CYS K 22 CYS K 96 1555 1555 2.36 SSBOND 16 CYS K 149 CYS K 205 1555 1555 2.24 SSBOND 17 CYS J 23 CYS J 88 1555 1555 2.09 SSBOND 18 CYS J 135 CYS J 195 1555 1555 1.88 SSBOND 19 CYS L 60 CYS L 151 1555 1555 2.09 SSBOND 20 CYS I 60 CYS I 151 1555 1555 2.76 CISPEP 1 PHE A 155 PRO A 156 0 -13.65 CISPEP 2 GLU A 157 PRO A 158 0 15.04 CISPEP 3 SER B 7 PRO B 8 0 1.65 CISPEP 4 PRO B 95 PRO B 96 0 -5.80 CISPEP 5 TYR B 141 PRO B 142 0 0.92 CISPEP 6 PHE D 155 PRO D 156 0 -6.08 CISPEP 7 GLU D 157 PRO D 158 0 20.36 CISPEP 8 SER E 7 PRO E 8 0 4.95 CISPEP 9 PRO E 95 PRO E 96 0 -4.63 CISPEP 10 TYR E 141 PRO E 142 0 1.30 CISPEP 11 PHE G 155 PRO G 156 0 -6.48 CISPEP 12 GLU G 157 PRO G 158 0 8.98 CISPEP 13 SER H 7 PRO H 8 0 6.34 CISPEP 14 PRO H 95 PRO H 96 0 -0.80 CISPEP 15 TYR H 141 PRO H 142 0 1.51 CISPEP 16 PHE K 155 PRO K 156 0 -5.88 CISPEP 17 GLU K 157 PRO K 158 0 10.20 CISPEP 18 SER J 7 PRO J 8 0 -7.63 CISPEP 19 PRO J 95 PRO J 96 0 -5.92 CISPEP 20 TYR J 141 PRO J 142 0 1.67 CRYST1 81.407 191.156 88.187 90.00 102.91 90.00 P 1 21 1 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 0.012284 0.000000 0.002815 0.00000 SCALE2 0.000000 0.005231 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011634 0.00000