HEADER IMMUNE SYSTEM 26-JAN-24 8VTE TITLE CO-STRUCTURE OF THE FAB OF THE ANTI-TIGIT VIBOSTOLIMAB ANTIBODY WITH TITLE 2 ITS ANTIGEN COMPND MOL_ID: 1; COMPND 2 MOLECULE: TIRAGOLUMAB ANTIBODY LIGHT CHAIN VARIABLE DOMAINS; COMPND 3 CHAIN: A, C; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: TIRAGOLUMAB ANTIBODY HEAVY CHAIN VARIABLE DOMAINS; COMPND 7 CHAIN: B, D; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: T-CELL IMMUNORECEPTOR WITH IG AND ITIM DOMAINS; COMPND 11 CHAIN: E, F; COMPND 12 SYNONYM: V-SET AND IMMUNOGLOBULIN DOMAIN-CONTAINING PROTEIN 9,V-SET COMPND 13 AND TRANSMEMBRANE DOMAIN-CONTAINING PROTEIN 3; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: EXPICHO; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 11 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 12 ORGANISM_TAXID: 10090; SOURCE 13 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 14 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 16 EXPRESSION_SYSTEM_CELL_LINE: EXPICHO; SOURCE 17 MOL_ID: 3; SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 19 ORGANISM_COMMON: HUMAN; SOURCE 20 ORGANISM_TAXID: 9606; SOURCE 21 GENE: TIGIT, VSIG9, VSTM3; SOURCE 22 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 23 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS ANTIBODY TIGIT IMMUNOTHERAPY, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR T.FISCHMANN,S.BAHMANJAH REVDAT 1 28-MAY-25 8VTE 0 JRNL AUTH T.O.FISCHMANN,D.MALASHOCK,H.WANG,J.GREIN,S.BAHMANJAH,D.BAN, JRNL AUTH 2 E.CHIEN,M.HSIEH,T.MAYHOOD,J.YUAN,M.BEAUMONT,J.BAKER, JRNL AUTH 3 M.A.MCCOY,D.WILSON,S.M.G.WILLIAMS,W.BLUMENSCHEIN, JRNL AUTH 4 L.FAYADAT-DILMAN,W.SEGHEZZI,T.KEENAN,J.-H.HAN JRNL TITL PHARMACOLOGICAL AND STRUCTURAL CHARACTERIZATION OF JRNL TITL 2 VIBOSTOLIMAB, A NOVEL ANTI-HUMAN TIGIT BLOCKING ANTIBODY FOR JRNL TITL 3 CANCER IMMUNOTHERAPY JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.29 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.11.8 REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER, REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN, REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.29 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.21 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 73.5 REMARK 3 NUMBER OF REFLECTIONS : 49801 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) : 0.231 REMARK 3 R VALUE (WORKING SET) : 0.229 REMARK 3 FREE R VALUE : 0.268 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 2483 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.29 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.43 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 9.05 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : NULL REMARK 3 BIN R VALUE (WORKING + TEST SET) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.2845 REMARK 3 BIN FREE R VALUE : 0.3305 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : 32 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 8413 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 425 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 70.97 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.96230 REMARK 3 B22 (A**2) : 0.96230 REMARK 3 B33 (A**2) : -1.92470 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 COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.350 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.456 REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.283 REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL REMARK 3 REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797 REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.921 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.885 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 16803 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 30305 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 4970 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL REMARK 3 GENERAL PLANES : 2648 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 8633 ; 10.000 ; HARMONIC REMARK 3 BAD NON-BONDED CONTACTS : 12 ; 5.000 ; SEMIHARMONIC REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : 1161 ; 5.000 ; SEMIHARMONIC REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL REMARK 3 IDEAL-DIST CONTACT TERM : 12324 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.007 REMARK 3 BOND ANGLES (DEGREES) : 0.99 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.95 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 15.61 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 10 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: { A|1 - A|111 } REMARK 3 ORIGIN FOR THE GROUP (A): 62.9938 -41.8512 -27.7564 REMARK 3 T TENSOR REMARK 3 T11: 0.2291 T22: 0.0312 REMARK 3 T33: 0.0501 T12: -0.1181 REMARK 3 T13: 0.0454 T23: -0.066 REMARK 3 L TENSOR REMARK 3 L11: 7.2651 L22: 3.9674 REMARK 3 L33: 3.2102 L12: 2.2704 REMARK 3 L13: -0.0229 L23: 0.1377 REMARK 3 S TENSOR REMARK 3 S11: -0.0202 S12: -0.0139 S13: 0.3715 REMARK 3 S21: -0.0139 S22: -0.0046 S23: -0.0875 REMARK 3 S31: 0.3715 S32: -0.0875 S33: 0.0247 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: { A|112 - A|219 } REMARK 3 ORIGIN FOR THE GROUP (A): 86.4129 -11.7405 -25.2925 REMARK 3 T TENSOR REMARK 3 T11: 0.0345 T22: 0.0945 REMARK 3 T33: 0.0516 T12: -0.0396 REMARK 3 T13: -0.0823 T23: -0.0264 REMARK 3 L TENSOR REMARK 3 L11: 1.592 L22: 7.4077 REMARK 3 L33: 3.0902 L12: -0.1017 REMARK 3 L13: -0.6199 L23: 1.4688 REMARK 3 S TENSOR REMARK 3 S11: -0.0483 S12: 0.4356 S13: 0.0194 REMARK 3 S21: 0.4356 S22: 0.0885 S23: 0.2224 REMARK 3 S31: 0.0194 S32: 0.2224 S33: -0.0402 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: { B|1 - B|127 } REMARK 3 ORIGIN FOR THE GROUP (A): 47.8976 -25.8734 -31.4472 REMARK 3 T TENSOR REMARK 3 T11: 0.1197 T22: 0.2745 REMARK 3 T33: 0.0756 T12: -0.096 REMARK 3 T13: -0.0073 T23: -0.0873 REMARK 3 L TENSOR REMARK 3 L11: 2.3427 L22: 4.7804 REMARK 3 L33: 1.4514 L12: 0.0997 REMARK 3 L13: -0.1808 L23: 0.5062 REMARK 3 S TENSOR REMARK 3 S11: -0.0297 S12: -0.2042 S13: 0.0661 REMARK 3 S21: -0.2042 S22: -0.2061 S23: -0.604 REMARK 3 S31: 0.0661 S32: -0.604 S33: 0.2358 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: { B|128 - B|227 } REMARK 3 ORIGIN FOR THE GROUP (A): 76.6571 -9.0091 -37.5361 REMARK 3 T TENSOR REMARK 3 T11: 0.1465 T22: 0.0065 REMARK 3 T33: -0.0045 T12: -0.0705 REMARK 3 T13: -0.0713 T23: -0.0213 REMARK 3 L TENSOR REMARK 3 L11: 3.7281 L22: 3.484 REMARK 3 L33: 6.2057 L12: 0.9445 REMARK 3 L13: -1.8088 L23: 0.2119 REMARK 3 S TENSOR REMARK 3 S11: -0.0342 S12: -0.1561 S13: -0.1913 REMARK 3 S21: -0.1561 S22: -0.0138 S23: 0.1367 REMARK 3 S31: -0.1913 S32: 0.1367 S33: 0.048 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: { C|1 - C|111 } REMARK 3 ORIGIN FOR THE GROUP (A): 54.8518 -35.9645 2.6129 REMARK 3 T TENSOR REMARK 3 T11: 0.2301 T22: 0.1657 REMARK 3 T33: 0.0429 T12: -0.2644 REMARK 3 T13: 0.0457 T23: -0.0574 REMARK 3 L TENSOR REMARK 3 L11: 5.6098 L22: 2.9064 REMARK 3 L33: 4.164 L12: -0.2274 REMARK 3 L13: -0.2822 L23: 0.0502 REMARK 3 S TENSOR REMARK 3 S11: -0.1028 S12: 0.0558 S13: 0.2759 REMARK 3 S21: 0.0558 S22: 0.0023 S23: -0.5695 REMARK 3 S31: 0.2759 S32: -0.5695 S33: 0.1006 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: { C|112 - C|217 } REMARK 3 ORIGIN FOR THE GROUP (A): 31.5876 -8.8358 -10.4602 REMARK 3 T TENSOR REMARK 3 T11: -0.0808 T22: 0.4305 REMARK 3 T33: 0.2524 T12: 0.0246 REMARK 3 T13: -0.0153 T23: -0.1315 REMARK 3 L TENSOR REMARK 3 L11: 6.0879 L22: 12.7037 REMARK 3 L33: 5.6135 L12: -0.4155 REMARK 3 L13: 0.3807 L23: -2.6838 REMARK 3 S TENSOR REMARK 3 S11: 0.0927 S12: -1.3219 S13: -0.0359 REMARK 3 S21: -1.3219 S22: 0.2178 S23: -0.8299 REMARK 3 S31: -0.0359 S32: -0.8299 S33: -0.3105 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: { D|1 - D|127 } REMARK 3 ORIGIN FOR THE GROUP (A): 69.7529 -19.7384 0.6629 REMARK 3 T TENSOR REMARK 3 T11: 0.1886 T22: 0.1386 REMARK 3 T33: 0.0922 T12: -0.1239 REMARK 3 T13: 0.0387 T23: -0.0565 REMARK 3 L TENSOR REMARK 3 L11: 1.7243 L22: 2.0517 REMARK 3 L33: 2.4114 L12: -0.3081 REMARK 3 L13: 0.7671 L23: -0.609 REMARK 3 S TENSOR REMARK 3 S11: 0.0294 S12: -0.0123 S13: 0.0696 REMARK 3 S21: -0.0123 S22: -0.0674 S23: -0.1147 REMARK 3 S31: 0.0696 S32: -0.1147 S33: 0.0381 REMARK 3 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: { D|128 - D|227 } REMARK 3 ORIGIN FOR THE GROUP (A): 41.8768 -1.9318 -0.3938 REMARK 3 T TENSOR REMARK 3 T11: 0.1659 T22: 0.2623 REMARK 3 T33: 0.1631 T12: 0.0362 REMARK 3 T13: 0.1166 T23: -0.2316 REMARK 3 L TENSOR REMARK 3 L11: 8.7231 L22: 6.4878 REMARK 3 L33: 5.8134 L12: -0.3058 REMARK 3 L13: -2.0262 L23: -0.2688 REMARK 3 S TENSOR REMARK 3 S11: 0.1292 S12: 0.8357 S13: -0.154 REMARK 3 S21: 0.8357 S22: 0.0421 S23: -1.0099 REMARK 3 S31: -0.154 S32: -1.0099 S33: -0.1714 REMARK 3 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: { E|* } REMARK 3 ORIGIN FOR THE GROUP (A): 28.4355 -45.0558 -26.2091 REMARK 3 T TENSOR REMARK 3 T11: -0.1614 T22: -0.0581 REMARK 3 T33: 0.3458 T12: -0.3129 REMARK 3 T13: 0.2023 T23: -0.2147 REMARK 3 L TENSOR REMARK 3 L11: 14.4761 L22: 7.7753 REMARK 3 L33: 7.6927 L12: -1.4657 REMARK 3 L13: -2.0529 L23: -1.1898 REMARK 3 S TENSOR REMARK 3 S11: -0.1479 S12: 0.046 S13: 0.5427 REMARK 3 S21: 0.046 S22: -0.0699 S23: -1.196 REMARK 3 S31: 0.5427 S32: -1.196 S33: 0.2179 REMARK 3 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: { F|* } REMARK 3 ORIGIN FOR THE GROUP (A): 90.0858 -38.9803 4.7815 REMARK 3 T TENSOR REMARK 3 T11: 0.1204 T22: -0.0442 REMARK 3 T33: 0.0506 T12: -0.0035 REMARK 3 T13: 0.1253 T23: 0.0328 REMARK 3 L TENSOR REMARK 3 L11: 10.2354 L22: 4.9218 REMARK 3 L33: 3.0215 L12: 1.8172 REMARK 3 L13: 0.0061 L23: 1.1906 REMARK 3 S TENSOR REMARK 3 S11: -0.3434 S12: -0.1884 S13: 0.6287 REMARK 3 S21: -0.1884 S22: 0.288 S23: 0.1997 REMARK 3 S31: 0.6287 S32: 0.1997 S33: 0.0554 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 8VTE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JAN-24. REMARK 100 THE DEPOSITION ID IS D_1000281104. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 19-SEP-20 REMARK 200 TEMPERATURE (KELVIN) : 300 REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 17-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 S 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOPROC REMARK 200 DATA SCALING SOFTWARE : STARANISO REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49814 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.290 REMARK 200 RESOLUTION RANGE LOW (A) : 33.210 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 93.7 REMARK 200 DATA REDUNDANCY : 6.700 REMARK 200 R MERGE (I) : 0.09100 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 14.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.29 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.50 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 : 1.600 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 59.54 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.04 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.02M D-GLUCOSE; 0.02M D-MANNOSE; REMARK 280 0.02M D-GALACTOSE; 0.02M L-FUCOSE; 0.02M D-XYLOSE; 0.02M N- REMARK 280 ACETYL-D-GLUCOSAMINE; 0.1M IMIDAZOLE, 0.1M MES; 20%V/V GLYCEROL; REMARK 280 10% PEG4K, PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE REMARK 280 300K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -Y,X,Z REMARK 290 4555 Y,-X,Z REMARK 290 5555 X+1/2,Y+1/2,Z+1/2 REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -Y+1/2,X+1/2,Z+1/2 REMARK 290 8555 Y+1/2,-X+1/2,Z+1/2 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 0.00000 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 0.00000 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 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 106.84450 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 106.84450 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 33.21400 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 106.84450 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 106.84450 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 33.21400 REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 106.84450 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 106.84450 REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 33.21400 REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 106.84450 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 106.84450 REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 33.21400 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E 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 APPLY THE FOLLOWING TO CHAINS: C, D, 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 SER B 229 REMARK 465 CYS B 230 REMARK 465 ASP B 231 REMARK 465 GLU C 219 REMARK 465 CYS C 220 REMARK 465 SER D 229 REMARK 465 CYS D 230 REMARK 465 ASP D 231 REMARK 465 MET E 22 REMARK 465 MET E 23 REMARK 465 THR E 24 REMARK 465 SER E 48 REMARK 465 SER E 49 REMARK 465 THR E 50 REMARK 465 LEU E 127 REMARK 465 GLU E 128 REMARK 465 SER E 129 REMARK 465 SER E 130 REMARK 465 VAL E 131 REMARK 465 ALA E 132 REMARK 465 GLU E 133 REMARK 465 HIS E 134 REMARK 465 GLY E 135 REMARK 465 ALA E 136 REMARK 465 ARG E 137 REMARK 465 HIS E 138 REMARK 465 HIS E 139 REMARK 465 HIS E 140 REMARK 465 HIS E 141 REMARK 465 HIS E 142 REMARK 465 HIS E 143 REMARK 465 SER F 129 REMARK 465 SER F 130 REMARK 465 VAL F 131 REMARK 465 ALA F 132 REMARK 465 GLU F 133 REMARK 465 HIS F 134 REMARK 465 GLY F 135 REMARK 465 ALA F 136 REMARK 465 ARG F 137 REMARK 465 HIS F 138 REMARK 465 HIS F 139 REMARK 465 HIS F 140 REMARK 465 HIS F 141 REMARK 465 HIS F 142 REMARK 465 HIS F 143 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 O ASP A 88 HH TYR A 92 1.53 REMARK 500 O ILE A 2 HG1 THR A 103 1.55 REMARK 500 HG1 THR E 55 O HIS E 111 1.56 REMARK 500 HD22 ASN B 211 OD1 ASP B 222 1.56 REMARK 500 O ASP C 88 HH TYR C 92 1.57 REMARK 500 H GLY B 69 O HOH B 307 1.57 REMARK 500 O GLN C 130 HG SER C 133 1.60 REMARK 500 HZ3 LYS F 82 O HOH C 302 1.60 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 ALA A 57 -35.75 66.59 REMARK 500 ASN A 144 76.68 43.20 REMARK 500 GLU A 219 3.75 58.82 REMARK 500 SER B 15 -21.55 77.99 REMARK 500 SER B 30 21.75 -79.16 REMARK 500 ARG B 56 -72.56 -104.84 REMARK 500 THR B 104 56.93 -104.32 REMARK 500 ALA C 57 -39.11 63.92 REMARK 500 ASN C 144 102.66 43.59 REMARK 500 SER D 15 -6.08 78.94 REMARK 500 SER D 30 31.00 -87.89 REMARK 500 LYS D 58 149.28 -170.20 REMARK 500 THR D 104 70.12 -106.03 REMARK 500 LEU D 138 74.23 -110.90 REMARK 500 ASP D 158 71.39 55.03 REMARK 500 THR D 205 -41.40 -153.21 REMARK 500 GLN E 62 -93.65 60.79 REMARK 500 ARG E 84 27.73 -143.49 REMARK 500 GLN F 62 -116.53 61.88 REMARK 500 LEU F 91 39.57 -93.55 REMARK 500 REMARK 500 REMARK: NULL DBREF 8VTE A 1 220 PDB 8VTE 8VTE 1 220 DBREF 8VTE B 1 231 PDB 8VTE 8VTE 1 231 DBREF 8VTE C 1 220 PDB 8VTE 8VTE 1 220 DBREF 8VTE D 1 231 PDB 8VTE 8VTE 1 231 DBREF 8VTE E 22 137 UNP Q495A1 TIGIT_HUMAN 22 137 DBREF 8VTE F 22 137 UNP Q495A1 TIGIT_HUMAN 22 137 SEQADV 8VTE HIS E 138 UNP Q495A1 EXPRESSION TAG SEQADV 8VTE HIS E 139 UNP Q495A1 EXPRESSION TAG SEQADV 8VTE HIS E 140 UNP Q495A1 EXPRESSION TAG SEQADV 8VTE HIS E 141 UNP Q495A1 EXPRESSION TAG SEQADV 8VTE HIS E 142 UNP Q495A1 EXPRESSION TAG SEQADV 8VTE HIS E 143 UNP Q495A1 EXPRESSION TAG SEQADV 8VTE HIS F 138 UNP Q495A1 EXPRESSION TAG SEQADV 8VTE HIS F 139 UNP Q495A1 EXPRESSION TAG SEQADV 8VTE HIS F 140 UNP Q495A1 EXPRESSION TAG SEQADV 8VTE HIS F 141 UNP Q495A1 EXPRESSION TAG SEQADV 8VTE HIS F 142 UNP Q495A1 EXPRESSION TAG SEQADV 8VTE HIS F 143 UNP Q495A1 EXPRESSION TAG SEQRES 1 A 220 ASP ILE VAL MET THR GLN SER PRO ASP SER LEU ALA VAL SEQRES 2 A 220 SER LEU GLY GLU ARG ALA THR ILE ASN CYS LYS SER SER SEQRES 3 A 220 GLN THR VAL LEU TYR SER SER ASN ASN LYS LYS TYR LEU SEQRES 4 A 220 ALA TRP TYR GLN GLN LYS PRO GLY GLN PRO PRO ASN LEU SEQRES 5 A 220 LEU ILE TYR TRP ALA SER THR ARG GLU SER GLY VAL PRO SEQRES 6 A 220 ASP ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR SEQRES 7 A 220 LEU THR ILE SER SER LEU GLN ALA GLU ASP VAL ALA VAL SEQRES 8 A 220 TYR TYR CYS GLN GLN TYR TYR SER THR PRO PHE THR PHE SEQRES 9 A 220 GLY PRO GLY THR LYS VAL GLU ILE LYS ARG THR VAL ALA SEQRES 10 A 220 ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN SEQRES 11 A 220 LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN SEQRES 12 A 220 ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL SEQRES 13 A 220 ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL SEQRES 14 A 220 THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SEQRES 15 A 220 SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS SEQRES 16 A 220 LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SEQRES 17 A 220 SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 B 230 GLU VAL GLN LEU GLN GLN SER GLY PRO GLY LEU VAL LYS SEQRES 2 B 230 PRO SER GLN THR LEU SER LEU THR CYS ALA ILE SER GLY SEQRES 3 B 230 ASP SER VAL SER SER ASN SER ALA ALA TRP ASN TRP ILE SEQRES 4 B 230 ARG GLN SER PRO SER ARG GLY LEU GLU TRP LEU GLY LYS SEQRES 5 B 230 THR TYR TYR ARG PHE LYS TRP TYR SER ASP TYR ALA VAL SEQRES 6 B 230 SER VAL LYS GLY ARG ILE THR ILE ASN PRO ASP THR SER SEQRES 7 B 230 LYS ASN GLN PHE SER LEU GLN LEU ASN SER VAL THR PRO SEQRES 8 B 230 GLU ASP THR ALA VAL PHE TYR CYS THR ARG GLU SER THR SEQRES 9 B 230 THR TYR ASP LEU LEU ALA GLY PRO PHE ASP TYR TRP GLY SEQRES 10 B 230 GLN GLY THR LEU VAL THR VAL SER SER ALA SER THR LYS SEQRES 11 B 230 GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER SEQRES 12 B 230 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS SEQRES 13 B 230 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 14 B 230 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 15 B 230 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL SEQRES 16 B 230 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE SEQRES 17 B 230 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP SEQRES 18 B 230 LYS LYS VAL GLU PRO LYS SER CYS ASP SEQRES 1 C 220 ASP ILE VAL MET 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 THR VAL LEU TYR SER SER ASN ASN LYS LYS TYR LEU SEQRES 4 C 220 ALA TRP TYR GLN GLN LYS PRO GLY GLN PRO PRO ASN 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 PHE THR PHE SEQRES 9 C 220 GLY PRO 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 230 GLU VAL GLN LEU GLN GLN SER GLY PRO GLY LEU VAL LYS SEQRES 2 D 230 PRO SER GLN THR LEU SER LEU THR CYS ALA ILE SER GLY SEQRES 3 D 230 ASP SER VAL SER SER ASN SER ALA ALA TRP ASN TRP ILE SEQRES 4 D 230 ARG GLN SER PRO SER ARG GLY LEU GLU TRP LEU GLY LYS SEQRES 5 D 230 THR TYR TYR ARG PHE LYS TRP TYR SER ASP TYR ALA VAL SEQRES 6 D 230 SER VAL LYS GLY ARG ILE THR ILE ASN PRO ASP THR SER SEQRES 7 D 230 LYS ASN GLN PHE SER LEU GLN LEU ASN SER VAL THR PRO SEQRES 8 D 230 GLU ASP THR ALA VAL PHE TYR CYS THR ARG GLU SER THR SEQRES 9 D 230 THR TYR ASP LEU LEU ALA GLY PRO PHE ASP TYR TRP GLY SEQRES 10 D 230 GLN GLY THR LEU VAL THR VAL SER SER ALA SER THR LYS SEQRES 11 D 230 GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER SEQRES 12 D 230 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS SEQRES 13 D 230 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 14 D 230 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 15 D 230 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL SEQRES 16 D 230 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE SEQRES 17 D 230 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP SEQRES 18 D 230 LYS LYS VAL GLU PRO LYS SER CYS ASP SEQRES 1 E 122 MET MET THR GLY THR ILE GLU THR THR GLY ASN ILE SER SEQRES 2 E 122 ALA GLU LYS GLY GLY SER ILE ILE LEU GLN CYS HIS LEU SEQRES 3 E 122 SER SER THR THR ALA GLN VAL THR GLN VAL ASN TRP GLU SEQRES 4 E 122 GLN GLN ASP GLN LEU LEU ALA ILE CYS ASN ALA ASP LEU SEQRES 5 E 122 GLY TRP HIS ILE SER PRO SER PHE LYS ASP ARG VAL ALA SEQRES 6 E 122 PRO GLY PRO GLY LEU GLY LEU THR LEU GLN SER LEU THR SEQRES 7 E 122 VAL ASN ASP THR GLY GLU TYR PHE CYS ILE TYR HIS THR SEQRES 8 E 122 TYR PRO ASP GLY THR TYR THR GLY ARG ILE PHE LEU GLU SEQRES 9 E 122 VAL LEU GLU SER SER VAL ALA GLU HIS GLY ALA ARG HIS SEQRES 10 E 122 HIS HIS HIS HIS HIS SEQRES 1 F 122 MET MET THR GLY THR ILE GLU THR THR GLY ASN ILE SER SEQRES 2 F 122 ALA GLU LYS GLY GLY SER ILE ILE LEU GLN CYS HIS LEU SEQRES 3 F 122 SER SER THR THR ALA GLN VAL THR GLN VAL ASN TRP GLU SEQRES 4 F 122 GLN GLN ASP GLN LEU LEU ALA ILE CYS ASN ALA ASP LEU SEQRES 5 F 122 GLY TRP HIS ILE SER PRO SER PHE LYS ASP ARG VAL ALA SEQRES 6 F 122 PRO GLY PRO GLY LEU GLY LEU THR LEU GLN SER LEU THR SEQRES 7 F 122 VAL ASN ASP THR GLY GLU TYR PHE CYS ILE TYR HIS THR SEQRES 8 F 122 TYR PRO ASP GLY THR TYR THR GLY ARG ILE PHE LEU GLU SEQRES 9 F 122 VAL LEU GLU SER SER VAL ALA GLU HIS GLY ALA ARG HIS SEQRES 10 F 122 HIS HIS HIS HIS HIS FORMUL 7 HOH *425(H2 O) HELIX 1 AA1 GLN A 85 VAL A 89 5 5 HELIX 2 AA2 SER A 127 GLY A 134 1 8 HELIX 3 AA3 LYS A 189 GLU A 193 1 5 HELIX 4 AA4 THR B 90 THR B 94 5 5 HELIX 5 AA5 SER B 170 ALA B 172 5 3 HELIX 6 AA6 SER B 201 GLY B 204 5 4 HELIX 7 AA7 LYS B 215 ASN B 218 5 4 HELIX 8 AA8 GLN C 85 VAL C 89 5 5 HELIX 9 AA9 SER C 127 SER C 133 1 7 HELIX 10 AB1 LYS C 189 GLU C 193 1 5 HELIX 11 AB2 THR D 90 THR D 94 5 5 HELIX 12 AB3 LYS D 215 ASN D 218 5 4 HELIX 13 AB4 THR E 99 THR E 103 5 5 HELIX 14 AB5 THR F 99 THR F 103 5 5 SHEET 1 AA1 4 MET A 4 THR A 5 0 SHEET 2 AA1 4 ALA A 19 SER A 25 -1 O LYS A 24 N THR A 5 SHEET 3 AA1 4 ASP A 76 ILE A 81 -1 O PHE A 77 N CYS A 23 SHEET 4 AA1 4 PHE A 68 SER A 73 -1 N SER A 69 O THR A 80 SHEET 1 AA2 6 SER A 10 SER A 14 0 SHEET 2 AA2 6 THR A 108 LYS A 113 1 O GLU A 111 N LEU A 11 SHEET 3 AA2 6 ALA A 90 GLN A 96 -1 N ALA A 90 O VAL A 110 SHEET 4 AA2 6 LEU A 39 GLN A 44 -1 N TYR A 42 O TYR A 93 SHEET 5 AA2 6 ASN A 51 TYR A 55 -1 O LEU A 53 N TRP A 41 SHEET 6 AA2 6 THR A 59 ARG A 60 -1 O THR A 59 N TYR A 55 SHEET 1 AA3 4 SER A 10 SER A 14 0 SHEET 2 AA3 4 THR A 108 LYS A 113 1 O GLU A 111 N LEU A 11 SHEET 3 AA3 4 ALA A 90 GLN A 96 -1 N ALA A 90 O VAL A 110 SHEET 4 AA3 4 THR A 103 PHE A 104 -1 O THR A 103 N GLN A 96 SHEET 1 AA4 2 LEU A 30 TYR A 31 0 SHEET 2 AA4 2 LYS A 36 LYS A 37 -1 O LYS A 36 N TYR A 31 SHEET 1 AA5 4 SER A 120 PHE A 124 0 SHEET 2 AA5 4 THR A 135 PHE A 145 -1 O LEU A 141 N PHE A 122 SHEET 3 AA5 4 TYR A 179 SER A 188 -1 O LEU A 181 N LEU A 142 SHEET 4 AA5 4 SER A 165 VAL A 169 -1 N GLN A 166 O THR A 184 SHEET 1 AA6 4 ALA A 159 LEU A 160 0 SHEET 2 AA6 4 LYS A 151 VAL A 156 -1 N VAL A 156 O ALA A 159 SHEET 3 AA6 4 VAL A 197 THR A 203 -1 O ALA A 199 N LYS A 155 SHEET 4 AA6 4 VAL A 211 ASN A 216 -1 O VAL A 211 N VAL A 202 SHEET 1 AA7 4 GLN B 3 SER B 7 0 SHEET 2 AA7 4 LEU B 18 SER B 25 -1 O SER B 25 N GLN B 3 SHEET 3 AA7 4 GLN B 81 LEU B 86 -1 O LEU B 86 N LEU B 18 SHEET 4 AA7 4 ILE B 71 THR B 72 -1 N THR B 72 O GLN B 85 SHEET 1 AA8 4 GLN B 3 SER B 7 0 SHEET 2 AA8 4 LEU B 18 SER B 25 -1 O SER B 25 N GLN B 3 SHEET 3 AA8 4 GLN B 81 LEU B 86 -1 O LEU B 86 N LEU B 18 SHEET 4 AA8 4 PRO B 75 ASP B 76 -1 N ASP B 76 O GLN B 81 SHEET 1 AA9 6 LEU B 11 VAL B 12 0 SHEET 2 AA9 6 THR B 121 VAL B 125 1 O THR B 124 N VAL B 12 SHEET 3 AA9 6 ALA B 95 SER B 103 -1 N PHE B 97 O THR B 121 SHEET 4 AA9 6 ALA B 34 SER B 42 -1 N ILE B 39 O TYR B 98 SHEET 5 AA9 6 GLY B 46 TYR B 55 -1 O LEU B 50 N TRP B 38 SHEET 6 AA9 6 TRP B 59 TYR B 63 -1 O TYR B 60 N TYR B 54 SHEET 1 AB1 4 LEU B 11 VAL B 12 0 SHEET 2 AB1 4 THR B 121 VAL B 125 1 O THR B 124 N VAL B 12 SHEET 3 AB1 4 ALA B 95 SER B 103 -1 N PHE B 97 O THR B 121 SHEET 4 AB1 4 PHE B 114 TRP B 117 -1 O TYR B 116 N ARG B 101 SHEET 1 AB2 4 SER B 134 LEU B 138 0 SHEET 2 AB2 4 THR B 149 TYR B 159 -1 O LYS B 157 N SER B 134 SHEET 3 AB2 4 TYR B 190 PRO B 199 -1 O TYR B 190 N TYR B 159 SHEET 4 AB2 4 VAL B 177 THR B 179 -1 N HIS B 178 O VAL B 195 SHEET 1 AB3 4 SER B 134 LEU B 138 0 SHEET 2 AB3 4 THR B 149 TYR B 159 -1 O LYS B 157 N SER B 134 SHEET 3 AB3 4 TYR B 190 PRO B 199 -1 O TYR B 190 N TYR B 159 SHEET 4 AB3 4 VAL B 183 LEU B 184 -1 N VAL B 183 O SER B 191 SHEET 1 AB4 3 THR B 165 TRP B 168 0 SHEET 2 AB4 3 TYR B 208 HIS B 214 -1 O ASN B 211 N SER B 167 SHEET 3 AB4 3 THR B 219 VAL B 225 -1 O VAL B 221 N VAL B 212 SHEET 1 AB5 4 MET C 4 THR C 5 0 SHEET 2 AB5 4 ALA C 19 SER C 25 -1 O LYS C 24 N THR C 5 SHEET 3 AB5 4 ASP C 76 ILE C 81 -1 O PHE C 77 N CYS C 23 SHEET 4 AB5 4 PHE C 68 SER C 73 -1 N SER C 69 O THR C 80 SHEET 1 AB6 6 SER C 10 SER C 14 0 SHEET 2 AB6 6 THR C 108 LYS C 113 1 O GLU C 111 N LEU C 11 SHEET 3 AB6 6 ALA C 90 GLN C 96 -1 N ALA C 90 O VAL C 110 SHEET 4 AB6 6 LEU C 39 GLN C 44 -1 N ALA C 40 O GLN C 95 SHEET 5 AB6 6 ASN C 51 TYR C 55 -1 O ASN C 51 N GLN C 43 SHEET 6 AB6 6 THR C 59 ARG C 60 -1 O THR C 59 N TYR C 55 SHEET 1 AB7 4 SER C 10 SER C 14 0 SHEET 2 AB7 4 THR C 108 LYS C 113 1 O GLU C 111 N LEU C 11 SHEET 3 AB7 4 ALA C 90 GLN C 96 -1 N ALA C 90 O VAL C 110 SHEET 4 AB7 4 THR C 103 PHE C 104 -1 O THR C 103 N GLN C 96 SHEET 1 AB8 4 SER C 120 PHE C 124 0 SHEET 2 AB8 4 THR C 135 PHE C 145 -1 O LEU C 141 N PHE C 122 SHEET 3 AB8 4 TYR C 179 SER C 188 -1 O LEU C 187 N ALA C 136 SHEET 4 AB8 4 SER C 165 VAL C 169 -1 N SER C 168 O SER C 182 SHEET 1 AB9 3 ALA C 150 VAL C 156 0 SHEET 2 AB9 3 TYR C 198 HIS C 204 -1 O ALA C 199 N LYS C 155 SHEET 3 AB9 3 VAL C 211 PHE C 215 -1 O VAL C 211 N VAL C 202 SHEET 1 AC1 4 GLN D 3 SER D 7 0 SHEET 2 AC1 4 LEU D 18 SER D 25 -1 O ALA D 23 N GLN D 5 SHEET 3 AC1 4 GLN D 81 LEU D 86 -1 O LEU D 86 N LEU D 18 SHEET 4 AC1 4 ILE D 71 THR D 72 -1 N THR D 72 O GLN D 85 SHEET 1 AC2 4 GLN D 3 SER D 7 0 SHEET 2 AC2 4 LEU D 18 SER D 25 -1 O ALA D 23 N GLN D 5 SHEET 3 AC2 4 GLN D 81 LEU D 86 -1 O LEU D 86 N LEU D 18 SHEET 4 AC2 4 PRO D 75 ASP D 76 -1 N ASP D 76 O GLN D 81 SHEET 1 AC3 6 LEU D 11 VAL D 12 0 SHEET 2 AC3 6 THR D 121 VAL D 125 1 O THR D 124 N VAL D 12 SHEET 3 AC3 6 ALA D 95 SER D 103 -1 N ALA D 95 O VAL D 123 SHEET 4 AC3 6 ALA D 34 SER D 42 -1 N ILE D 39 O TYR D 98 SHEET 5 AC3 6 GLY D 46 TYR D 55 -1 O THR D 53 N TRP D 36 SHEET 6 AC3 6 TRP D 59 TYR D 63 -1 O TYR D 60 N TYR D 54 SHEET 1 AC4 4 LEU D 11 VAL D 12 0 SHEET 2 AC4 4 THR D 121 VAL D 125 1 O THR D 124 N VAL D 12 SHEET 3 AC4 4 ALA D 95 SER D 103 -1 N ALA D 95 O VAL D 123 SHEET 4 AC4 4 PHE D 114 TRP D 117 -1 O TYR D 116 N ARG D 101 SHEET 1 AC5 4 SER D 134 LEU D 138 0 SHEET 2 AC5 4 THR D 149 TYR D 159 -1 O LEU D 155 N PHE D 136 SHEET 3 AC5 4 TYR D 190 PRO D 199 -1 O TYR D 190 N TYR D 159 SHEET 4 AC5 4 VAL D 177 THR D 179 -1 N HIS D 178 O VAL D 195 SHEET 1 AC6 4 SER D 134 LEU D 138 0 SHEET 2 AC6 4 THR D 149 TYR D 159 -1 O LEU D 155 N PHE D 136 SHEET 3 AC6 4 TYR D 190 PRO D 199 -1 O TYR D 190 N TYR D 159 SHEET 4 AC6 4 VAL D 183 LEU D 184 -1 N VAL D 183 O SER D 191 SHEET 1 AC7 3 THR D 165 TRP D 168 0 SHEET 2 AC7 3 ILE D 209 HIS D 214 -1 O ASN D 211 N SER D 167 SHEET 3 AC7 3 THR D 219 LYS D 224 -1 O THR D 219 N HIS D 214 SHEET 1 AC8 2 GLU E 28 THR E 29 0 SHEET 2 AC8 2 CYS E 45 HIS E 46 -1 O HIS E 46 N GLU E 28 SHEET 1 AC9 6 ILE E 33 SER E 34 0 SHEET 2 AC9 6 ARG E 121 GLU E 125 1 O GLU E 125 N ILE E 33 SHEET 3 AC9 6 GLY E 104 TYR E 113 -1 N GLY E 104 O LEU E 124 SHEET 4 AC9 6 GLN E 53 GLN E 61 -1 N ASN E 58 O ILE E 109 SHEET 5 AC9 6 GLN E 64 ASN E 70 -1 O ALA E 67 N TRP E 59 SHEET 6 AC9 6 GLY E 74 ILE E 77 -1 O HIS E 76 N ILE E 68 SHEET 1 AD1 4 ILE E 33 SER E 34 0 SHEET 2 AD1 4 ARG E 121 GLU E 125 1 O GLU E 125 N ILE E 33 SHEET 3 AD1 4 GLY E 104 TYR E 113 -1 N GLY E 104 O LEU E 124 SHEET 4 AD1 4 GLY E 116 TYR E 118 -1 O TYR E 118 N TYR E 110 SHEET 1 AD2 3 ILE E 41 LEU E 43 0 SHEET 2 AD2 3 LEU E 93 LEU E 95 -1 O LEU E 93 N LEU E 43 SHEET 3 AD2 3 VAL E 85 PRO E 87 -1 N ALA E 86 O THR E 94 SHEET 1 AD3 2 THR F 26 THR F 29 0 SHEET 2 AD3 2 CYS F 45 SER F 48 -1 O SER F 48 N THR F 26 SHEET 1 AD4 6 ASN F 32 GLU F 36 0 SHEET 2 AD4 6 GLY F 116 LEU F 127 1 O PHE F 123 N ILE F 33 SHEET 3 AD4 6 GLY F 104 TYR F 113 -1 N THR F 112 O GLY F 116 SHEET 4 AD4 6 GLN F 53 GLN F 61 -1 N GLN F 56 O HIS F 111 SHEET 5 AD4 6 GLN F 64 ASN F 70 -1 O LEU F 66 N TRP F 59 SHEET 6 AD4 6 GLY F 74 ILE F 77 -1 O GLY F 74 N ASN F 70 SHEET 1 AD5 3 ILE F 41 LEU F 43 0 SHEET 2 AD5 3 LEU F 93 LEU F 95 -1 O LEU F 93 N LEU F 43 SHEET 3 AD5 3 VAL F 85 PRO F 87 -1 N ALA F 86 O THR F 94 SSBOND 1 CYS A 23 CYS A 94 1555 1555 2.05 SSBOND 2 CYS A 140 CYS A 200 1555 1555 2.02 SSBOND 3 CYS B 22 CYS B 99 1555 1555 2.05 SSBOND 4 CYS B 154 CYS B 210 1555 1555 2.03 SSBOND 5 CYS C 23 CYS C 94 1555 1555 2.05 SSBOND 6 CYS C 140 CYS C 200 1555 1555 2.03 SSBOND 7 CYS D 22 CYS D 99 1555 1555 2.05 SSBOND 8 CYS D 154 CYS D 210 1555 1555 2.03 SSBOND 9 CYS E 45 CYS E 108 1555 1555 2.04 SSBOND 10 CYS F 45 CYS F 108 1555 1555 2.03 CISPEP 1 THR A 100 PRO A 101 0 -1.46 CISPEP 2 TYR A 146 PRO A 147 0 1.68 CISPEP 3 PHE B 160 PRO B 161 0 -6.87 CISPEP 4 GLU B 162 PRO B 163 0 0.98 CISPEP 5 THR C 100 PRO C 101 0 0.71 CISPEP 6 TYR C 146 PRO C 147 0 0.17 CISPEP 7 PHE D 160 PRO D 161 0 -6.78 CISPEP 8 GLU D 162 PRO D 163 0 4.72 CISPEP 9 TYR E 113 PRO E 114 0 -1.06 CISPEP 10 TYR F 113 PRO F 114 0 -0.97 CRYST1 213.689 213.689 66.428 90.00 90.00 90.00 I 4 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 0.004680 0.000000 0.000000 0.00000 SCALE2 0.000000 0.004680 0.000000 0.00000 SCALE3 0.000000 0.000000 0.015054 0.00000