HEADER HYDROLASE 28-AUG-24 9GLZ TITLE KRAS-G12D-GMPPNP IN COMPLEX WITH THE NANOBODY KM12-AM COMPND MOL_ID: 1; COMPND 2 MOLECULE: GTPASE KRAS; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: KI-RAS; COMPND 5 EC: 3.6.5.2; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: NANOBODY KM12-AM; COMPND 9 CHAIN: C, D; COMPND 10 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: KRAS, DROARD_R09727; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_TAXID: 9606; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS GTPASE, SIGNALING PROTEIN, SMALL G-PROTEIN, HYDROLASE EXPDTA X-RAY DIFFRACTION AUTHOR N.OSTERMANN,F.ZINK REVDAT 1 10-DEC-25 9GLZ 0 JRNL AUTH K.S.BEYER,J.KLEIN,S.KATZ,P.WELKER,M.LANTER,D.GUTHY, JRNL AUTH 2 K.POLLEHN,A.GLUCK-GADE,M.BLEU,J.DESOGUS,M.HATTENBERGER, JRNL AUTH 3 D.BORRELLO,W.ABDUL RAHMAN,F.ZINK,N.OSTERMANN,W.JAHNKE, JRNL AUTH 4 C.E.DUMELIN,L.LEDER,O.ESSER,L.MULLER,A.MARZINZIK,R.CEBE, JRNL AUTH 5 K.MULLER,G.G.GALLI,L.TORDELLA,S.COTESTA,S.M.BRACHMANN, JRNL AUTH 6 S.M.MAIRA JRNL TITL IDENTIFICATION AND CHARACTERIZATION OF BINDERS TO A CRYPTIC JRNL TITL 2 AND FUNCTIONAL POCKET IN KRAS. JRNL REF NAT COMMUN V. 16 10836 2025 JRNL REFN ESSN 2041-1723 JRNL PMID 41330964 JRNL DOI 10.1038/S41467-025-65844-3 REMARK 2 REMARK 2 RESOLUTION. 2.10 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) : 2.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.73 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 3 NUMBER OF REFLECTIONS : 31891 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) : 0.241 REMARK 3 R VALUE (WORKING SET) : 0.239 REMARK 3 FREE R VALUE : 0.277 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 1638 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) : 2.10 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.12 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.87 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) : 0.3058 REMARK 3 BIN FREE R VALUE : 0.3314 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : 36 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 : 4189 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 66 REMARK 3 SOLVENT ATOMS : 176 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.15 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.87640 REMARK 3 B22 (A**2) : 2.74820 REMARK 3 B33 (A**2) : -1.87180 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) : 0.320 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.284 REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.216 REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.281 REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.217 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 : 0.931 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.911 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 4332 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 5884 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 1469 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL REMARK 3 GENERAL PLANES : 746 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 4332 ; 10.000 ; HARMONIC REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : 583 ; 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 : 3337 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.008 REMARK 3 BOND ANGLES (DEGREES) : 0.93 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.12 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.73 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 12 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: {A|*} REMARK 3 ORIGIN FOR THE GROUP (A): -14.4649 -19.6396 -14.3275 REMARK 3 T TENSOR REMARK 3 T11: -0.0488 T22: 0.052 REMARK 3 T33: -0.0598 T12: -0.0131 REMARK 3 T13: 0.0204 T23: -0.009 REMARK 3 L TENSOR REMARK 3 L11: 2.609 L22: 0.8643 REMARK 3 L33: 1.779 L12: 0.2056 REMARK 3 L13: -0.8001 L23: 0.0171 REMARK 3 S TENSOR REMARK 3 S11: 0.1913 S12: 0.0638 S13: -0.0696 REMARK 3 S21: 0.0638 S22: -0.0937 S23: 0.2688 REMARK 3 S31: -0.0696 S32: 0.2688 S33: -0.0976 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: {B|*} REMARK 3 ORIGIN FOR THE GROUP (A): -21.7368 -17.3885 15.7713 REMARK 3 T TENSOR REMARK 3 T11: -0.0144 T22: -0.0303 REMARK 3 T33: -0.0297 T12: 0.0024 REMARK 3 T13: 0.0287 T23: 0.0201 REMARK 3 L TENSOR REMARK 3 L11: 1.575 L22: 2.0519 REMARK 3 L33: 2.4911 L12: 0.397 REMARK 3 L13: -0.4269 L23: -0.5608 REMARK 3 S TENSOR REMARK 3 S11: 0.0544 S12: 0.0693 S13: -0.1969 REMARK 3 S21: 0.0693 S22: 0.0863 S23: -0.0899 REMARK 3 S31: -0.1969 S32: -0.0899 S33: -0.1407 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: {C|2 - 31} REMARK 3 ORIGIN FOR THE GROUP (A): -51.945 -11.6355 -6.3554 REMARK 3 T TENSOR REMARK 3 T11: -0.4839 T22: 0.0385 REMARK 3 T33: 0.1446 T12: 0.055 REMARK 3 T13: -0.0886 T23: -0.4236 REMARK 3 L TENSOR REMARK 3 L11: 1.8556 L22: 6.699 REMARK 3 L33: 8.9667 L12: -1.0246 REMARK 3 L13: -0.3204 L23: 5.1706 REMARK 3 S TENSOR REMARK 3 S11: 0.0112 S12: -0.5196 S13: 0.0576 REMARK 3 S21: -0.5196 S22: -1.404 S23: -1.3384 REMARK 3 S31: 0.0576 S32: -1.3384 S33: 1.3928 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: {C|32 - 61} REMARK 3 ORIGIN FOR THE GROUP (A): -41.008 -13.5216 -3.374 REMARK 3 T TENSOR REMARK 3 T11: -0.1017 T22: -0.0357 REMARK 3 T33: -0.0902 T12: -0.0853 REMARK 3 T13: 0.0333 T23: -0.0024 REMARK 3 L TENSOR REMARK 3 L11: 3.4326 L22: 11.2801 REMARK 3 L33: 9.0895 L12: -3.3064 REMARK 3 L13: -2.8233 L23: 6.694 REMARK 3 S TENSOR REMARK 3 S11: 0.144 S12: 0.6533 S13: 0.4395 REMARK 3 S21: 0.6533 S22: -0.5133 S23: -0.4713 REMARK 3 S31: 0.4395 S32: -0.4713 S33: 0.3692 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: {C|62 - 90} REMARK 3 ORIGIN FOR THE GROUP (A): -49.0149 -17.3565 0.3596 REMARK 3 T TENSOR REMARK 3 T11: -0.2825 T22: -0.1403 REMARK 3 T33: 0.0497 T12: -0.3666 REMARK 3 T13: 0.3697 T23: -0.2929 REMARK 3 L TENSOR REMARK 3 L11: 7.5383 L22: 14.773 REMARK 3 L33: 19.0024 L12: 0.0194 REMARK 3 L13: -4.0938 L23: 2.6414 REMARK 3 S TENSOR REMARK 3 S11: 0.2006 S12: 1.6327 S13: 1.2102 REMARK 3 S21: 1.6327 S22: -1.4321 S23: -1.3409 REMARK 3 S31: 1.2102 S32: -1.3409 S33: 1.2315 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: {C|91 - 113} REMARK 3 ORIGIN FOR THE GROUP (A): -37.7398 -10.997 -9.283 REMARK 3 T TENSOR REMARK 3 T11: -0.0516 T22: -0.0241 REMARK 3 T33: -0.1218 T12: 0.037 REMARK 3 T13: -0.0226 T23: -0.003 REMARK 3 L TENSOR REMARK 3 L11: 5.3915 L22: 8.4233 REMARK 3 L33: 6.6524 L12: -1.8823 REMARK 3 L13: -3.4699 L23: 7.1906 REMARK 3 S TENSOR REMARK 3 S11: 0.1729 S12: -0.6506 S13: -0.3146 REMARK 3 S21: -0.6506 S22: -0.3705 S23: -0.054 REMARK 3 S31: -0.3146 S32: -0.054 S33: 0.1975 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: {C|114 - 121} REMARK 3 ORIGIN FOR THE GROUP (A): -49.1242 -4.522 -2.2675 REMARK 3 T TENSOR REMARK 3 T11: -0.2691 T22: 0.0549 REMARK 3 T33: 0.0175 T12: 0.0691 REMARK 3 T13: -0.0448 T23: -0.4127 REMARK 3 L TENSOR REMARK 3 L11: 10.319 L22: 14.0039 REMARK 3 L33: 4.5925 L12: 0.1273 REMARK 3 L13: -2.4624 L23: 2.1333 REMARK 3 S TENSOR REMARK 3 S11: 0.264 S12: -0.2147 S13: -0.1755 REMARK 3 S21: -0.2147 S22: -1.1579 S23: -1.0757 REMARK 3 S31: -0.1755 S32: -1.0757 S33: 0.8938 REMARK 3 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: {D|3 - 24} REMARK 3 ORIGIN FOR THE GROUP (A): 18.8297 -10.2753 4.0333 REMARK 3 T TENSOR REMARK 3 T11: -0.4939 T22: -0.0651 REMARK 3 T33: -0.1256 T12: -0.0351 REMARK 3 T13: -0.0639 T23: 0.2295 REMARK 3 L TENSOR REMARK 3 L11: 9.4777 L22: 0.7017 REMARK 3 L33: 19.7959 L12: 4.0465 REMARK 3 L13: -8.4587 L23: -2.3175 REMARK 3 S TENSOR REMARK 3 S11: -0.0923 S12: 0.1788 S13: 0.7179 REMARK 3 S21: 0.1788 S22: -0.2754 S23: 0.5797 REMARK 3 S31: 0.7179 S32: 0.5797 S33: 0.3678 REMARK 3 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: {D|32 - 61} REMARK 3 ORIGIN FOR THE GROUP (A): 5.4956 -12.6687 6.0578 REMARK 3 T TENSOR REMARK 3 T11: -0.2113 T22: 0.3165 REMARK 3 T33: -0.2769 T12: 0.0019 REMARK 3 T13: -0.0135 T23: 0.1111 REMARK 3 L TENSOR REMARK 3 L11: 4.4308 L22: 16.5342 REMARK 3 L33: 8.9893 L12: 7.4068 REMARK 3 L13: -5.1815 L23: -8.7312 REMARK 3 S TENSOR REMARK 3 S11: 0.5202 S12: 0.0008 S13: -0.1099 REMARK 3 S21: 0.0008 S22: -1.1126 S23: 1.007 REMARK 3 S31: -0.1099 S32: 1.007 S33: 0.5924 REMARK 3 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: {D|65 - 90} REMARK 3 ORIGIN FOR THE GROUP (A): 14.6602 -16.1227 3.0675 REMARK 3 T TENSOR REMARK 3 T11: -0.186 T22: -0.064 REMARK 3 T33: -0.1897 T12: 0.2992 REMARK 3 T13: 0.0519 T23: 0.208 REMARK 3 L TENSOR REMARK 3 L11: 11.2286 L22: 7.6169 REMARK 3 L33: 0 L12: -0.7913 REMARK 3 L13: -5.6924 L23: 4.7462 REMARK 3 S TENSOR REMARK 3 S11: 0.7367 S12: -0.8016 S13: 0.7342 REMARK 3 S21: -0.8016 S22: -0.896 S23: -0.135 REMARK 3 S31: 0.7342 S32: -0.135 S33: 0.1592 REMARK 3 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: {D|91 - 113} REMARK 3 ORIGIN FOR THE GROUP (A): 1.8586 -9.0952 10.3206 REMARK 3 T TENSOR REMARK 3 T11: -0.0633 T22: 0.2425 REMARK 3 T33: -0.2459 T12: -0.3337 REMARK 3 T13: 0.0644 T23: -0.0643 REMARK 3 L TENSOR REMARK 3 L11: 1.9999 L22: 7.7673 REMARK 3 L33: 9.6393 L12: -1.01 REMARK 3 L13: 0.7567 L23: -8.7312 REMARK 3 S TENSOR REMARK 3 S11: 0.5469 S12: 1.0974 S13: -0.7309 REMARK 3 S21: 1.0974 S22: -1.0859 S23: 0.9027 REMARK 3 S31: -0.7309 S32: 0.9027 S33: 0.539 REMARK 3 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: {D|114 - 122} REMARK 3 ORIGIN FOR THE GROUP (A): 14.0299 -4.1391 2.5027 REMARK 3 T TENSOR REMARK 3 T11: -0.1958 T22: 0.7321 REMARK 3 T33: -0.0327 T12: -0.3462 REMARK 3 T13: 0.0609 T23: 0.4559 REMARK 3 L TENSOR REMARK 3 L11: 6.5487 L22: 7.6026 REMARK 3 L33: 0 L12: 1.6324 REMARK 3 L13: -2.89 L23: 2.2882 REMARK 3 S TENSOR REMARK 3 S11: 0.241 S12: 0.2988 S13: 0.4268 REMARK 3 S21: 0.2988 S22: -0.6474 S23: 0.6337 REMARK 3 S31: 0.4268 S32: 0.6337 S33: 0.4065 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9GLZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-AUG-24. REMARK 100 THE DEPOSITION ID IS D_1292141367. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 19-DEC-19 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SLS REMARK 200 BEAMLINE : X06SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.000043 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43995 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.760 REMARK 200 RESOLUTION RANGE LOW (A) : 61.160 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.1 REMARK 200 DATA REDUNDANCY : 10.10 REMARK 200 R MERGE (I) : 0.07800 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 14.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.76 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.88 REMARK 200 COMPLETENESS FOR SHELL (%) : 56.4 REMARK 200 DATA REDUNDANCY IN SHELL : 12.30 REMARK 200 R MERGE FOR SHELL (I) : 1.57000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.400 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: 1AKNG REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 38.14 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 1000, 0.2 M LINO3, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 295K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -X,Y,-Z+1/2 REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 52.80750 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 52.80750 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 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 42.03600 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 61.16000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 42.03600 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 61.16000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 52.80750 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 42.03600 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 61.16000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 52.80750 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 42.03600 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 61.16000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 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 GLY A 0 REMARK 465 GLN A 61 REMARK 465 GLU A 62 REMARK 465 GLU A 63 REMARK 465 TYR A 64 REMARK 465 SER A 65 REMARK 465 ALA A 66 REMARK 465 MET A 67 REMARK 465 ARG A 68 REMARK 465 LYS A 169 REMARK 465 GLY B 0 REMARK 465 GLN B 61 REMARK 465 GLU B 62 REMARK 465 GLU B 63 REMARK 465 TYR B 64 REMARK 465 SER B 65 REMARK 465 ALA B 66 REMARK 465 MET B 67 REMARK 465 LYS B 169 REMARK 465 GLN C 1 REMARK 465 VAL C 8 REMARK 465 GLY C 9 REMARK 465 ALA C 74 REMARK 465 LYS C 75 REMARK 465 VAL C 122 REMARK 465 SER C 123 REMARK 465 SER C 124 REMARK 465 GLY C 125 REMARK 465 GLY C 126 REMARK 465 GLY C 127 REMARK 465 GLY C 128 REMARK 465 SER C 129 REMARK 465 GLU C 130 REMARK 465 PHE C 131 REMARK 465 ARG C 132 REMARK 465 HIS C 133 REMARK 465 ASP C 134 REMARK 465 SER C 135 REMARK 465 GLN D 1 REMARK 465 VAL D 2 REMARK 465 VAL D 8 REMARK 465 GLY D 9 REMARK 465 GLY D 10 REMARK 465 SER D 25 REMARK 465 GLY D 26 REMARK 465 PRO D 27 REMARK 465 SER D 28 REMARK 465 LEU D 29 REMARK 465 ASP D 30 REMARK 465 LEU D 31 REMARK 465 SER D 62 REMARK 465 VAL D 63 REMARK 465 GLU D 64 REMARK 465 ALA D 74 REMARK 465 LYS D 75 REMARK 465 ARG D 76 REMARK 465 SER D 123 REMARK 465 SER D 124 REMARK 465 GLY D 125 REMARK 465 GLY D 126 REMARK 465 GLY D 127 REMARK 465 GLY D 128 REMARK 465 SER D 129 REMARK 465 GLU D 130 REMARK 465 PHE D 131 REMARK 465 ARG D 132 REMARK 465 HIS D 133 REMARK 465 ASP D 134 REMARK 465 SER D 135 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 GLU A 98 CG CD OE1 OE2 REMARK 470 ASP A 105 CG OD1 OD2 REMARK 470 LYS A 165 CG CD CE NZ REMARK 470 GLU A 168 CG CD OE1 OE2 REMARK 470 LYS B 42 CG CD CE NZ REMARK 470 LYS B 88 CG CD CE NZ REMARK 470 LEU C 11 CG CD1 CD2 REMARK 470 SER C 25 OG REMARK 470 ASP C 30 CG OD1 OD2 REMARK 470 ARG C 76 CG CD NE CZ NH1 NH2 REMARK 470 THR C 77 OG1 CG2 REMARK 470 THR C 84 OG1 CG2 REMARK 470 GLU C 88 CG CD OE1 OE2 REMARK 470 MET C 109 CG SD CE REMARK 470 ASP C 112 CG OD1 OD2 REMARK 470 GLN D 3 CG CD OE1 NE2 REMARK 470 LEU D 4 CG CD1 CD2 REMARK 470 VAL D 5 CG1 CG2 REMARK 470 LEU D 11 CG CD1 CD2 REMARK 470 VAL D 12 CG1 CG2 REMARK 470 GLN D 13 CG CD OE1 NE2 REMARK 470 SER D 17 OG REMARK 470 LEU D 20 CG CD1 CD2 REMARK 470 SER D 21 OG REMARK 470 LYS D 43 CG CD CE NZ REMARK 470 GLU D 46 CG CD OE1 OE2 REMARK 470 SER D 49 OG REMARK 470 ASP D 61 CG OD1 OD2 REMARK 470 ASP D 72 CG OD1 OD2 REMARK 470 SER D 73 OG REMARK 470 LEU D 85 CG CD1 CD2 REMARK 470 GLU D 88 CG CD OE1 OE2 REMARK 470 ARG D 99 CG CD NE CZ NH1 NH2 REMARK 470 MET D 109 CG SD CE REMARK 470 ASP D 112 CG OD1 OD2 REMARK 470 SER D 113 OG REMARK 470 LEU D 119 CG CD1 CD2 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 ASP A 33 85.01 -169.08 REMARK 500 ILE A 36 -60.91 -101.96 REMARK 500 GLU A 37 122.16 -170.72 REMARK 500 ASP A 108 52.05 -144.87 REMARK 500 LYS A 117 35.16 72.55 REMARK 500 SER A 122 54.37 -101.18 REMARK 500 ASP B 108 66.25 -110.34 REMARK 500 ARG B 149 -2.35 82.83 REMARK 500 PHE C 102 100.99 -161.28 REMARK 500 PRO D 41 109.50 -54.94 REMARK 500 PHE D 102 87.45 -167.20 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MG A1001 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 SER A 17 OG REMARK 620 2 THR A 35 OG1 82.8 REMARK 620 3 GNP A1002 O2B 92.0 166.6 REMARK 620 4 GNP A1002 O3G 170.6 88.9 95.2 REMARK 620 5 HOH A1106 O 92.2 94.9 97.7 92.9 REMARK 620 6 HOH A1123 O 84.8 82.2 85.0 89.7 176.0 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MG B1001 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GNP B1002 O3G REMARK 620 2 GNP B1002 O2B 109.2 REMARK 620 3 HOH B1103 O 80.6 101.2 REMARK 620 4 HOH B1131 O 124.9 113.6 58.6 REMARK 620 5 HOH B1135 O 101.6 76.2 177.0 120.9 REMARK 620 N 1 2 3 4 DBREF1 9GLZ A 1 169 UNP A0A7K5XXT4_9CHAR DBREF2 9GLZ A A0A7K5XXT4 1 169 DBREF1 9GLZ B 1 169 UNP A0A7K5XXT4_9CHAR DBREF2 9GLZ B A0A7K5XXT4 1 169 DBREF 9GLZ C 1 135 PDB 9GLZ 9GLZ 1 135 DBREF 9GLZ D 1 135 PDB 9GLZ 9GLZ 1 135 SEQADV 9GLZ GLY A 0 UNP A0A7K5XXT EXPRESSION TAG SEQADV 9GLZ ASP A 12 UNP A0A7K5XXT GLY 12 ENGINEERED MUTATION SEQADV 9GLZ SER A 51 UNP A0A7K5XXT CYS 51 ENGINEERED MUTATION SEQADV 9GLZ LEU A 80 UNP A0A7K5XXT CYS 80 ENGINEERED MUTATION SEQADV 9GLZ SER A 118 UNP A0A7K5XXT CYS 118 ENGINEERED MUTATION SEQADV 9GLZ GLY B 0 UNP A0A7K5XXT EXPRESSION TAG SEQADV 9GLZ ASP B 12 UNP A0A7K5XXT GLY 12 ENGINEERED MUTATION SEQADV 9GLZ SER B 51 UNP A0A7K5XXT CYS 51 ENGINEERED MUTATION SEQADV 9GLZ LEU B 80 UNP A0A7K5XXT CYS 80 ENGINEERED MUTATION SEQADV 9GLZ SER B 118 UNP A0A7K5XXT CYS 118 ENGINEERED MUTATION SEQRES 1 A 170 GLY MET THR GLU TYR LYS LEU VAL VAL VAL GLY ALA ASP SEQRES 2 A 170 GLY VAL GLY LYS SER ALA LEU THR ILE GLN LEU ILE GLN SEQRES 3 A 170 ASN HIS PHE VAL ASP GLU TYR ASP PRO THR ILE GLU ASP SEQRES 4 A 170 SER TYR ARG LYS GLN VAL VAL ILE ASP GLY GLU THR SER SEQRES 5 A 170 LEU LEU ASP ILE LEU ASP THR ALA GLY GLN GLU GLU TYR SEQRES 6 A 170 SER ALA MET ARG ASP GLN TYR MET ARG THR GLY GLU GLY SEQRES 7 A 170 PHE LEU LEU VAL PHE ALA ILE ASN ASN THR LYS SER PHE SEQRES 8 A 170 GLU ASP ILE HIS HIS TYR ARG GLU GLN ILE LYS ARG VAL SEQRES 9 A 170 LYS ASP SER GLU ASP VAL PRO MET VAL LEU VAL GLY ASN SEQRES 10 A 170 LYS SER ASP LEU PRO SER ARG THR VAL ASP THR LYS GLN SEQRES 11 A 170 ALA GLN ASP LEU ALA ARG SER TYR GLY ILE PRO PHE ILE SEQRES 12 A 170 GLU THR SER ALA LYS THR ARG GLN GLY VAL ASP ASP ALA SEQRES 13 A 170 PHE TYR THR LEU VAL ARG GLU ILE ARG LYS HIS LYS GLU SEQRES 14 A 170 LYS SEQRES 1 B 170 GLY MET THR GLU TYR LYS LEU VAL VAL VAL GLY ALA ASP SEQRES 2 B 170 GLY VAL GLY LYS SER ALA LEU THR ILE GLN LEU ILE GLN SEQRES 3 B 170 ASN HIS PHE VAL ASP GLU TYR ASP PRO THR ILE GLU ASP SEQRES 4 B 170 SER TYR ARG LYS GLN VAL VAL ILE ASP GLY GLU THR SER SEQRES 5 B 170 LEU LEU ASP ILE LEU ASP THR ALA GLY GLN GLU GLU TYR SEQRES 6 B 170 SER ALA MET ARG ASP GLN TYR MET ARG THR GLY GLU GLY SEQRES 7 B 170 PHE LEU LEU VAL PHE ALA ILE ASN ASN THR LYS SER PHE SEQRES 8 B 170 GLU ASP ILE HIS HIS TYR ARG GLU GLN ILE LYS ARG VAL SEQRES 9 B 170 LYS ASP SER GLU ASP VAL PRO MET VAL LEU VAL GLY ASN SEQRES 10 B 170 LYS SER ASP LEU PRO SER ARG THR VAL ASP THR LYS GLN SEQRES 11 B 170 ALA GLN ASP LEU ALA ARG SER TYR GLY ILE PRO PHE ILE SEQRES 12 B 170 GLU THR SER ALA LYS THR ARG GLN GLY VAL ASP ASP ALA SEQRES 13 B 170 PHE TYR THR LEU VAL ARG GLU ILE ARG LYS HIS LYS GLU SEQRES 14 B 170 LYS SEQRES 1 C 135 GLN VAL GLN LEU VAL GLU SER VAL GLY GLY LEU VAL GLN SEQRES 2 C 135 PRO GLY ASP SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 C 135 PRO SER LEU ASP LEU TYR GLY THR ALA TRP PHE ARG GLN SEQRES 4 C 135 VAL PRO GLY LYS GLU ARG GLU PHE VAL SER HIS ILE ASP SEQRES 5 C 135 ARG SER GLY ILE THR ILE TYR ALA ASP SER VAL GLU GLY SEQRES 6 C 135 ARG PHE THR ILE SER ARG ASP SER ALA LYS ARG THR VAL SEQRES 7 C 135 TYR LEU GLN MET ASN THR LEU ALA PRO GLU ASP THR ALA SEQRES 8 C 135 ALA TYR TYR CYS ALA ALA THR ARG SER ASN PHE TYR PHE SEQRES 9 C 135 PRO ARG GLU ASP MET SER TYR ASP SER TRP GLY GLN GLY SEQRES 10 C 135 THR LEU VAL THR VAL SER SER GLY GLY GLY GLY SER GLU SEQRES 11 C 135 PHE ARG HIS ASP SER SEQRES 1 D 135 GLN VAL GLN LEU VAL GLU SER VAL GLY GLY LEU VAL GLN SEQRES 2 D 135 PRO GLY ASP SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 D 135 PRO SER LEU ASP LEU TYR GLY THR ALA TRP PHE ARG GLN SEQRES 4 D 135 VAL PRO GLY LYS GLU ARG GLU PHE VAL SER HIS ILE ASP SEQRES 5 D 135 ARG SER GLY ILE THR ILE TYR ALA ASP SER VAL GLU GLY SEQRES 6 D 135 ARG PHE THR ILE SER ARG ASP SER ALA LYS ARG THR VAL SEQRES 7 D 135 TYR LEU GLN MET ASN THR LEU ALA PRO GLU ASP THR ALA SEQRES 8 D 135 ALA TYR TYR CYS ALA ALA THR ARG SER ASN PHE TYR PHE SEQRES 9 D 135 PRO ARG GLU ASP MET SER TYR ASP SER TRP GLY GLN GLY SEQRES 10 D 135 THR LEU VAL THR VAL SER SER GLY GLY GLY GLY SER GLU SEQRES 11 D 135 PHE ARG HIS ASP SER HET MG A1001 1 HET GNP A1002 32 HET MG B1001 1 HET GNP B1002 32 HETNAM MG MAGNESIUM ION HETNAM GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER FORMUL 5 MG 2(MG 2+) FORMUL 6 GNP 2(C10 H17 N6 O13 P3) FORMUL 9 HOH *176(H2 O) HELIX 1 AA1 GLY A 15 ASN A 26 1 12 HELIX 2 AA2 GLN A 70 GLY A 75 1 6 HELIX 3 AA3 ASN A 86 LYS A 104 1 19 HELIX 4 AA4 ASP A 126 TYR A 137 1 12 HELIX 5 AA5 GLY A 151 GLU A 168 1 18 HELIX 6 AA6 GLY B 15 ASN B 26 1 12 HELIX 7 AA7 ASP B 69 GLY B 75 1 7 HELIX 8 AA8 ASN B 86 ASP B 92 1 7 HELIX 9 AA9 ASP B 92 ASP B 105 1 14 HELIX 10 AB1 ASP B 126 GLY B 138 1 13 HELIX 11 AB2 GLY B 151 LYS B 167 1 17 HELIX 12 AB3 SER C 28 TYR C 32 5 5 HELIX 13 AB4 ALA C 86 THR C 90 5 5 HELIX 14 AB5 GLU C 107 TYR C 111 5 5 HELIX 15 AB6 ALA D 86 THR D 90 5 5 HELIX 16 AB7 GLU D 107 TYR D 111 5 5 SHEET 1 AA1 8 PHE A 141 GLU A 143 0 SHEET 2 AA1 8 MET A 111 ASN A 116 1 N LEU A 113 O ILE A 142 SHEET 3 AA1 8 GLY A 77 ALA A 83 1 N LEU A 80 O VAL A 114 SHEET 4 AA1 8 GLU A 3 GLY A 10 1 N VAL A 9 O VAL A 81 SHEET 5 AA1 8 GLU A 49 ASP A 57 1 O ASP A 54 N LEU A 6 SHEET 6 AA1 8 ASP A 38 ILE A 46 -1 N ASP A 38 O ASP A 57 SHEET 7 AA1 8 GLU B 37 ILE B 46 -1 O SER B 39 N SER A 39 SHEET 8 AA1 8 PHE C 102 TYR C 103 0 SHEET 1 AA2 8 PHE B 141 GLU B 143 0 SHEET 2 AA2 8 MET B 111 ASN B 116 1 N LEU B 113 O ILE B 142 SHEET 3 AA2 8 GLY B 77 ALA B 83 1 N LEU B 80 O VAL B 114 SHEET 4 AA2 8 GLU B 3 VAL B 9 1 N VAL B 9 O VAL B 81 SHEET 5 AA2 8 GLU B 49 THR B 58 1 O LEU B 56 N VAL B 8 SHEET 6 AA2 8 GLU B 37 ILE B 46 -1 N ASP B 38 O ASP B 57 SHEET 7 AA2 8 ASP A 38 ILE A 46 -1 N SER A 39 O SER B 39 SHEET 8 AA2 8 PHE D 102 TYR D 103 0 SHEET 1 AA3 4 GLN C 3 GLU C 6 0 SHEET 2 AA3 4 LEU C 18 SER C 25 -1 O ALA C 23 N VAL C 5 SHEET 3 AA3 4 THR C 77 MET C 82 -1 O MET C 82 N LEU C 18 SHEET 4 AA3 4 PHE C 67 ARG C 71 -1 N THR C 68 O GLN C 81 SHEET 1 AA4 5 THR C 57 TYR C 59 0 SHEET 2 AA4 5 ARG C 45 ILE C 51 -1 N HIS C 50 O ILE C 58 SHEET 3 AA4 5 GLY C 33 GLN C 39 -1 N ARG C 38 O GLU C 46 SHEET 4 AA4 5 ALA C 91 THR C 98 -1 O TYR C 94 N PHE C 37 SHEET 5 AA4 5 SER C 113 TRP C 114 -1 O SER C 113 N ALA C 97 SHEET 1 AA5 5 THR C 57 TYR C 59 0 SHEET 2 AA5 5 ARG C 45 ILE C 51 -1 N HIS C 50 O ILE C 58 SHEET 3 AA5 5 GLY C 33 GLN C 39 -1 N ARG C 38 O GLU C 46 SHEET 4 AA5 5 ALA C 91 THR C 98 -1 O TYR C 94 N PHE C 37 SHEET 5 AA5 5 THR C 118 VAL C 120 -1 O THR C 118 N TYR C 93 SHEET 1 AA6 4 VAL D 5 GLU D 6 0 SHEET 2 AA6 4 LEU D 18 ALA D 23 -1 O ALA D 23 N VAL D 5 SHEET 3 AA6 4 VAL D 78 MET D 82 -1 O MET D 82 N LEU D 18 SHEET 4 AA6 4 PHE D 67 ARG D 71 -1 N THR D 68 O GLN D 81 SHEET 1 AA7 5 THR D 57 TYR D 59 0 SHEET 2 AA7 5 ARG D 45 ILE D 51 -1 N HIS D 50 O ILE D 58 SHEET 3 AA7 5 GLY D 33 GLN D 39 -1 N ARG D 38 O GLU D 46 SHEET 4 AA7 5 ALA D 91 THR D 98 -1 O TYR D 94 N PHE D 37 SHEET 5 AA7 5 SER D 113 TRP D 114 -1 O SER D 113 N ALA D 97 SHEET 1 AA8 5 THR D 57 TYR D 59 0 SHEET 2 AA8 5 ARG D 45 ILE D 51 -1 N HIS D 50 O ILE D 58 SHEET 3 AA8 5 GLY D 33 GLN D 39 -1 N ARG D 38 O GLU D 46 SHEET 4 AA8 5 ALA D 91 THR D 98 -1 O TYR D 94 N PHE D 37 SHEET 5 AA8 5 THR D 118 VAL D 120 -1 O THR D 118 N TYR D 93 SSBOND 1 CYS C 22 CYS C 95 1555 1555 2.05 SSBOND 2 CYS D 22 CYS D 95 1555 1555 2.03 LINK OG SER A 17 MG MG A1001 1555 1555 2.16 LINK OG1 THR A 35 MG MG A1001 1555 1555 2.16 LINK MG MG A1001 O2B GNP A1002 1555 1555 2.15 LINK MG MG A1001 O3G GNP A1002 1555 1555 2.08 LINK MG MG A1001 O HOH A1106 1555 1555 1.95 LINK MG MG A1001 O HOH A1123 1555 1555 2.07 LINK MG MG B1001 O3G GNP B1002 1555 1555 1.92 LINK MG MG B1001 O2B GNP B1002 1555 1555 2.22 LINK MG MG B1001 O HOH B1103 1555 1555 2.74 LINK MG MG B1001 O HOH B1131 1555 1555 2.14 LINK MG MG B1001 O HOH B1135 1555 1555 2.67 CRYST1 84.072 122.320 105.615 90.00 90.00 90.00 C 2 2 21 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 0.011895 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008175 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009468 0.00000