HEADER LYASE 21-SEP-24 9GV3 TITLE CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN NB474 MUTANT R53A,D125A AND TITLE 2 TRYPANOSOMA CONGOLENSE FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE COMPND MOL_ID: 1; COMPND 2 MOLECULE: FRUCTOSE-BISPHOSPHATE ALDOLASE; COMPND 3 CHAIN: A, B, C, D; COMPND 4 EC: 4.1.2.13; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: NB474 MUTANT R53A,D125A; COMPND 8 CHAIN: E, F, G, H; COMPND 9 ENGINEERED: YES; COMPND 10 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: TRYPANOSOMA CONGOLENSE IL3000; SOURCE 3 ORGANISM_TAXID: 1068625; SOURCE 4 GENE: TCIL3000_10_4760; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: VICUGNA PACOS; SOURCE 9 ORGANISM_TAXID: 30538; SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS COMPLEX, NANOBODY, ALDOLASE, LYASE EXPDTA X-RAY DIFFRACTION AUTHOR I.W.MCNAE,J.DORNAN,M.D.WALKINSHAW REVDAT 1 01-OCT-25 9GV3 0 JRNL AUTH A.HACISULEYMAN,J.DORNA,I.MCNAE,M.WEAR,T.BILAL,M.YUAN, JRNL AUTH 2 P.A.M.MICHELS,J.E.PINTO TORRES,S.MAGEZ,Y.G.J.STERCKX, JRNL AUTH 3 E.ERMAN,M.D.WALKINSHAW JRNL TITL THE ROLE OF WATER IN TUNING NANOBODY-ANTIGEN RECOGNITION JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.75 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 : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 97.56 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 70.5 REMARK 3 NUMBER OF REFLECTIONS : 197213 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.160 REMARK 3 FREE R VALUE : 0.188 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.979 REMARK 3 FREE R VALUE TEST SET COUNT : 9820 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) : 1.75 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.80 REMARK 3 REFLECTION IN BIN (WORKING SET) : 965 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 4.98 REMARK 3 BIN R VALUE (WORKING SET) : 0.2760 REMARK 3 BIN FREE R VALUE SET COUNT : 57 REMARK 3 BIN FREE R VALUE : 0.3240 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 15243 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 22 REMARK 3 SOLVENT ATOMS : 1343 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.24 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.24100 REMARK 3 B22 (A**2) : 0.16600 REMARK 3 B33 (A**2) : 0.07500 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.119 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.112 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.077 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.239 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.970 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.959 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 15639 ; 0.015 ; 0.012 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 21204 ; 2.224 ; 1.830 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2011 ; 6.575 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 140 ; 8.760 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2586 ;13.299 ;10.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2335 ; 0.142 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11980 ; 0.011 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 7466 ; 0.213 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 10981 ; 0.311 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1399 ; 0.159 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 7994 ; 2.635 ; 2.024 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9987 ; 3.672 ; 3.608 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 7645 ; 4.874 ; 2.364 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 11207 ; 6.628 ; 4.117 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 12 REMARK 3 REMARK 3 NCS GROUP NUMBER : 1 REMARK 3 CHAIN NAMES : A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 A 2 A 358 NULL REMARK 3 1 A 2 A 358 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 2 REMARK 3 CHAIN NAMES : A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 2 A 2 A 360 NULL REMARK 3 2 A 2 A 360 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 3 REMARK 3 CHAIN NAMES : A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 3 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 3 A 2 A 358 NULL REMARK 3 3 A 2 A 358 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 4 REMARK 3 CHAIN NAMES : A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 4 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 4 A 2 A 358 NULL REMARK 3 4 A 2 A 358 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 5 REMARK 3 CHAIN NAMES : A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 5 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 5 A 2 A 359 NULL REMARK 3 5 A 2 A 359 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 6 REMARK 3 CHAIN NAMES : A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 6 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 6 A 2 A 358 NULL REMARK 3 6 A 2 A 358 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 7 REMARK 3 CHAIN NAMES : A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 7 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 7 A 2 A 138 NULL REMARK 3 7 A 2 A 138 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 8 REMARK 3 CHAIN NAMES : A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 8 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 8 A 2 A 138 NULL REMARK 3 8 A 2 A 138 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 9 REMARK 3 CHAIN NAMES : A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 9 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 9 A 2 A 138 NULL REMARK 3 9 A 2 A 138 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 10 REMARK 3 CHAIN NAMES : A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 10 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 10 A 2 A 138 NULL REMARK 3 10 A 2 A 138 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 11 REMARK 3 CHAIN NAMES : A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 11 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 11 A 2 A 138 NULL REMARK 3 11 A 2 A 138 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 12 REMARK 3 CHAIN NAMES : A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 12 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 12 A 2 A 138 NULL REMARK 3 12 A 2 A 138 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 8 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 : Ap 2 Ap 401 REMARK 3 ORIGIN FOR THE GROUP (A): -16.2592 40.1585 -37.1531 REMARK 3 T TENSOR REMARK 3 T11: 0.0420 T22: 0.0205 REMARK 3 T33: 0.0213 T12: -0.0091 REMARK 3 T13: 0.0102 T23: 0.0023 REMARK 3 L TENSOR REMARK 3 L11: 0.6760 L22: 0.7330 REMARK 3 L33: 0.6911 L12: 0.0828 REMARK 3 L13: -0.3204 L23: 0.1594 REMARK 3 S TENSOR REMARK 3 S11: -0.0714 S12: 0.0186 S13: -0.0438 REMARK 3 S21: -0.0058 S22: 0.0291 S23: -0.1041 REMARK 3 S31: 0.0687 S32: 0.0801 S33: 0.0423 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 0 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 ORIGIN FOR THE GROUP (A): -53.3731 49.3546 -42.8198 REMARK 3 T TENSOR REMARK 3 T11: 0.0506 T22: 0.0613 REMARK 3 T33: 0.0384 T12: -0.0230 REMARK 3 T13: -0.0145 T23: 0.0085 REMARK 3 L TENSOR REMARK 3 L11: 0.6907 L22: 0.5689 REMARK 3 L33: 0.8883 L12: 0.2697 REMARK 3 L13: 0.0727 L23: 0.1126 REMARK 3 S TENSOR REMARK 3 S11: -0.0675 S12: 0.1217 S13: 0.0634 REMARK 3 S21: -0.0960 S22: 0.0421 S23: 0.1420 REMARK 3 S31: -0.0289 S32: -0.1209 S33: 0.0254 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 0 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 ORIGIN FOR THE GROUP (A): -18.7768 68.2317 -6.0391 REMARK 3 T TENSOR REMARK 3 T11: 0.0641 T22: 0.0545 REMARK 3 T33: 0.0411 T12: 0.0206 REMARK 3 T13: -0.0167 T23: -0.0255 REMARK 3 L TENSOR REMARK 3 L11: 0.7008 L22: 0.7661 REMARK 3 L33: 0.8984 L12: -0.1690 REMARK 3 L13: 0.0733 L23: 0.3002 REMARK 3 S TENSOR REMARK 3 S11: -0.0602 S12: -0.0604 S13: 0.1424 REMARK 3 S21: 0.0486 S22: 0.0969 S23: -0.1277 REMARK 3 S31: -0.0636 S32: 0.1728 S33: -0.0367 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 NUMBER OF COMPONENTS GROUP : 0 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 ORIGIN FOR THE GROUP (A): -54.5076 53.7841 -1.5620 REMARK 3 T TENSOR REMARK 3 T11: 0.0819 T22: 0.0092 REMARK 3 T33: 0.0219 T12: 0.0164 REMARK 3 T13: 0.0149 T23: 0.0120 REMARK 3 L TENSOR REMARK 3 L11: 0.8900 L22: 0.2689 REMARK 3 L33: 0.6854 L12: -0.0837 REMARK 3 L13: -0.3627 L23: 0.0930 REMARK 3 S TENSOR REMARK 3 S11: -0.0525 S12: -0.0410 S13: -0.0286 REMARK 3 S21: 0.0597 S22: 0.0401 S23: 0.0757 REMARK 3 S31: 0.0633 S32: -0.0025 S33: 0.0124 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 NUMBER OF COMPONENTS GROUP : 0 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 ORIGIN FOR THE GROUP (A): 5.1405 28.4616 -68.3730 REMARK 3 T TENSOR REMARK 3 T11: 0.0700 T22: 0.0843 REMARK 3 T33: 0.0498 T12: 0.0273 REMARK 3 T13: 0.0479 T23: 0.0458 REMARK 3 L TENSOR REMARK 3 L11: 1.5299 L22: 2.0919 REMARK 3 L33: 2.9512 L12: -0.3327 REMARK 3 L13: -0.5543 L23: 1.5819 REMARK 3 S TENSOR REMARK 3 S11: 0.0531 S12: 0.0660 S13: 0.0176 REMARK 3 S21: 0.0112 S22: -0.0244 S23: -0.0923 REMARK 3 S31: 0.1397 S32: -0.0180 S33: -0.0287 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 NUMBER OF COMPONENTS GROUP : 0 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 ORIGIN FOR THE GROUP (A): -74.3218 35.8108 -74.2965 REMARK 3 T TENSOR REMARK 3 T11: 0.1047 T22: 0.1047 REMARK 3 T33: 0.1548 T12: -0.0324 REMARK 3 T13: -0.0119 T23: -0.0011 REMARK 3 L TENSOR REMARK 3 L11: 1.2289 L22: 1.7283 REMARK 3 L33: 3.7354 L12: 0.3457 REMARK 3 L13: 0.2488 L23: -0.6576 REMARK 3 S TENSOR REMARK 3 S11: -0.0026 S12: 0.1721 S13: -0.1475 REMARK 3 S21: -0.2376 S22: 0.0141 S23: -0.1932 REMARK 3 S31: 0.1718 S32: 0.1463 S33: -0.0115 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 NUMBER OF COMPONENTS GROUP : 0 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 ORIGIN FOR THE GROUP (A): 0.6254 83.3310 25.3131 REMARK 3 T TENSOR REMARK 3 T11: 0.1286 T22: 0.2337 REMARK 3 T33: 0.0923 T12: -0.0084 REMARK 3 T13: -0.0551 T23: -0.0422 REMARK 3 L TENSOR REMARK 3 L11: 1.4493 L22: 1.6359 REMARK 3 L33: 2.9684 L12: -0.1252 REMARK 3 L13: 0.1609 L23: 1.4572 REMARK 3 S TENSOR REMARK 3 S11: 0.0390 S12: 0.0937 S13: -0.0325 REMARK 3 S21: -0.0368 S22: 0.0474 S23: -0.1293 REMARK 3 S31: -0.1203 S32: 0.2489 S33: -0.0864 REMARK 3 REMARK 3 TLS GROUP : 8 REMARK 3 NUMBER OF COMPONENTS GROUP : 0 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 ORIGIN FOR THE GROUP (A): -79.9130 61.5020 29.0965 REMARK 3 T TENSOR REMARK 3 T11: 0.0627 T22: 0.0079 REMARK 3 T33: 0.0828 T12: 0.0011 REMARK 3 T13: 0.0335 T23: 0.0079 REMARK 3 L TENSOR REMARK 3 L11: 1.3806 L22: 1.2987 REMARK 3 L33: 3.2754 L12: -0.0991 REMARK 3 L13: -0.5076 L23: 0.0184 REMARK 3 S TENSOR REMARK 3 S11: 0.0322 S12: -0.0482 S13: -0.0102 REMARK 3 S21: 0.0581 S22: 0.0123 S23: 0.0265 REMARK 3 S31: 0.0675 S32: -0.1090 S33: -0.0445 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK BULK SOLVENT REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN REMARK 3 THE INPUT FILE REMARK 4 REMARK 4 9GV3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-SEP-24. REMARK 100 THE DEPOSITION ID IS D_1292141916. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 16-JUL-22 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I24 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.6702 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2 REMARK 200 DATA SCALING SOFTWARE : STARANISO REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 999301 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750 REMARK 200 RESOLUTION RANGE LOW (A) : 97.558 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 87.6 REMARK 200 DATA REDUNDANCY : 5.100 REMARK 200 R MERGE (I) : 0.11700 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.92 REMARK 200 COMPLETENESS FOR SHELL (%) : 64.8 REMARK 200 DATA REDUNDANCY IN SHELL : 4.40 REMARK 200 R MERGE FOR SHELL (I) : 1.05800 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 (%): 58.79 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CACODYLATE PH 6.5, 100MM, PEG REMARK 280 8K 10-15%, 200MM MAGNESIUM ACETATE., VAPOR DIFFUSION, HANGING REMARK 280 DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2 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 -X+1/2,Y+1/2,-Z REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 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 -1.000000 0.000000 0.000000 101.74750 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.58300 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 101.74750 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.58300 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 20200 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 70410 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H 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 MET A 1 REMARK 465 LEU A 365 REMARK 465 TYR A 366 REMARK 465 VAL A 367 REMARK 465 ALA A 368 REMARK 465 GLY A 369 REMARK 465 ASN A 370 REMARK 465 THR A 371 REMARK 465 TYR A 372 REMARK 465 GLU A 373 REMARK 465 ASN A 374 REMARK 465 LEU A 375 REMARK 465 TYR A 376 REMARK 465 PHE A 377 REMARK 465 GLN A 378 REMARK 465 SER A 379 REMARK 465 GLY A 380 REMARK 465 GLY A 381 REMARK 465 HIS A 382 REMARK 465 HIS A 383 REMARK 465 HIS A 384 REMARK 465 HIS A 385 REMARK 465 HIS A 386 REMARK 465 HIS A 387 REMARK 465 MET B 1 REMARK 465 LYS B 360 REMARK 465 ASP B 361 REMARK 465 SER B 362 REMARK 465 GLN B 363 REMARK 465 SER B 364 REMARK 465 LEU B 365 REMARK 465 TYR B 366 REMARK 465 VAL B 367 REMARK 465 ALA B 368 REMARK 465 GLY B 369 REMARK 465 ASN B 370 REMARK 465 THR B 371 REMARK 465 TYR B 372 REMARK 465 GLU B 373 REMARK 465 ASN B 374 REMARK 465 LEU B 375 REMARK 465 TYR B 376 REMARK 465 PHE B 377 REMARK 465 GLN B 378 REMARK 465 SER B 379 REMARK 465 GLY B 380 REMARK 465 GLY B 381 REMARK 465 HIS B 382 REMARK 465 HIS B 383 REMARK 465 HIS B 384 REMARK 465 HIS B 385 REMARK 465 HIS B 386 REMARK 465 HIS B 387 REMARK 465 MET C 1 REMARK 465 SER C 362 REMARK 465 GLN C 363 REMARK 465 SER C 364 REMARK 465 LEU C 365 REMARK 465 TYR C 366 REMARK 465 VAL C 367 REMARK 465 ALA C 368 REMARK 465 GLY C 369 REMARK 465 ASN C 370 REMARK 465 THR C 371 REMARK 465 TYR C 372 REMARK 465 GLU C 373 REMARK 465 ASN C 374 REMARK 465 LEU C 375 REMARK 465 TYR C 376 REMARK 465 PHE C 377 REMARK 465 GLN C 378 REMARK 465 SER C 379 REMARK 465 GLY C 380 REMARK 465 GLY C 381 REMARK 465 HIS C 382 REMARK 465 HIS C 383 REMARK 465 HIS C 384 REMARK 465 HIS C 385 REMARK 465 HIS C 386 REMARK 465 HIS C 387 REMARK 465 MET D 1 REMARK 465 LYS D 360 REMARK 465 ASP D 361 REMARK 465 SER D 362 REMARK 465 GLN D 363 REMARK 465 SER D 364 REMARK 465 LEU D 365 REMARK 465 TYR D 366 REMARK 465 VAL D 367 REMARK 465 ALA D 368 REMARK 465 GLY D 369 REMARK 465 ASN D 370 REMARK 465 THR D 371 REMARK 465 TYR D 372 REMARK 465 GLU D 373 REMARK 465 ASN D 374 REMARK 465 LEU D 375 REMARK 465 TYR D 376 REMARK 465 PHE D 377 REMARK 465 GLN D 378 REMARK 465 SER D 379 REMARK 465 GLY D 380 REMARK 465 GLY D 381 REMARK 465 HIS D 382 REMARK 465 HIS D 383 REMARK 465 HIS D 384 REMARK 465 HIS D 385 REMARK 465 HIS D 386 REMARK 465 HIS D 387 REMARK 465 GLN E 1 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 GLN F 1 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 465 GLN G 1 REMARK 465 HIS G 139 REMARK 465 HIS G 140 REMARK 465 HIS G 141 REMARK 465 HIS G 142 REMARK 465 HIS G 143 REMARK 465 GLN H 1 REMARK 465 HIS H 139 REMARK 465 HIS H 140 REMARK 465 HIS H 141 REMARK 465 HIS H 142 REMARK 465 HIS H 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 N VAL G 2 O HOH G 201 1.86 REMARK 500 O HOH A 433 O HOH A 680 2.04 REMARK 500 O HOH A 413 O HOH A 612 2.05 REMARK 500 O HOH B 508 O HOH B 717 2.08 REMARK 500 NH2 ARG D 4 O HOH D 501 2.10 REMARK 500 O HOH E 234 O HOH E 285 2.11 REMARK 500 OE1 GLU D 210 O HOH D 502 2.11 REMARK 500 OH TYR C 15 O HOH C 501 2.12 REMARK 500 N VAL E 2 O HOH E 201 2.12 REMARK 500 CH3 ACT B 402 O HOH B 591 2.13 REMARK 500 OH TYR B 15 O HOH B 501 2.13 REMARK 500 O HOH A 609 O HOH A 657 2.15 REMARK 500 O HOH B 721 O HOH F 237 2.16 REMARK 500 O HOH C 698 O HOH C 726 2.16 REMARK 500 O HOH A 582 O HOH A 659 2.19 REMARK 500 O HOH F 227 O HOH F 232 2.19 REMARK 500 O HOH A 555 O HOH A 665 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) 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 RES CSSEQI ATM2 DEVIATION REMARK 500 GLU C 257 CD GLU C 257 OE1 0.077 REMARK 500 REMARK 500 REMARK: NULL 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 ARG A 3 CB - CA - C ANGL. DEV. = 17.3 DEGREES REMARK 500 ARG A 3 CA - CB - CG ANGL. DEV. = 20.8 DEGREES REMARK 500 MET A 73 CG - SD - CE ANGL. DEV. = 13.5 DEGREES REMARK 500 ARG A 96 CG - CD - NE ANGL. DEV. = -16.9 DEGREES REMARK 500 ARG A 108 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES REMARK 500 LYS A 163 CD - CE - NZ ANGL. DEV. = -15.8 DEGREES REMARK 500 ARG A 214 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES REMARK 500 ARG A 214 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES REMARK 500 GLU A 249 OE1 - CD - OE2 ANGL. DEV. = -8.8 DEGREES REMARK 500 LYS A 327 CB - CG - CD ANGL. DEV. = 18.1 DEGREES REMARK 500 ARG B 3 CB - CA - C ANGL. DEV. = 17.5 DEGREES REMARK 500 ARG B 3 N - CA - CB ANGL. DEV. = -11.1 DEGREES REMARK 500 ARG B 3 CA - CB - CG ANGL. DEV. = 20.5 DEGREES REMARK 500 MET B 73 CG - SD - CE ANGL. DEV. = 15.0 DEGREES REMARK 500 ARG B 108 NE - CZ - NH2 ANGL. DEV. = -4.4 DEGREES REMARK 500 MET B 134 CG - SD - CE ANGL. DEV. = 12.9 DEGREES REMARK 500 ARG B 175 NE - CZ - NH2 ANGL. DEV. = 3.0 DEGREES REMARK 500 ARG B 214 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 ARG B 214 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES REMARK 500 MET B 297 CA - CB - CG ANGL. DEV. = -13.9 DEGREES REMARK 500 ARG B 335 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES REMARK 500 ARG C 3 CB - CA - C ANGL. DEV. = 16.4 DEGREES REMARK 500 ARG C 3 CA - CB - CG ANGL. DEV. = 21.9 DEGREES REMARK 500 MET C 73 CG - SD - CE ANGL. DEV. = 10.6 DEGREES REMARK 500 GLU C 101 CG - CD - OE2 ANGL. DEV. = -14.5 DEGREES REMARK 500 LYS C 117 CD - CE - NZ ANGL. DEV. = -20.2 DEGREES REMARK 500 ARG C 214 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES REMARK 500 ARG C 214 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES REMARK 500 ARG C 229 NE - CZ - NH2 ANGL. DEV. = 4.7 DEGREES REMARK 500 MET C 289 CG - SD - CE ANGL. DEV. = 10.1 DEGREES REMARK 500 MET C 297 CA - CB - CG ANGL. DEV. = -16.3 DEGREES REMARK 500 ARG D 3 CB - CA - C ANGL. DEV. = 16.6 DEGREES REMARK 500 MET D 73 CG - SD - CE ANGL. DEV. = 11.6 DEGREES REMARK 500 LYS D 117 CD - CE - NZ ANGL. DEV. = -20.3 DEGREES REMARK 500 ARG D 214 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES REMARK 500 ARG D 214 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES REMARK 500 MET D 297 CA - CB - CG ANGL. DEV. = -15.1 DEGREES REMARK 500 LYS D 322 CB - CG - CD ANGL. DEV. = 24.2 DEGREES REMARK 500 ARG D 352 CD - NE - CZ ANGL. DEV. = 9.3 DEGREES REMARK 500 ARG F 97 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES REMARK 500 THR G 82 CA - CB - OG1 ANGL. DEV. = -17.1 DEGREES REMARK 500 ARG H 38 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 ARG H 38 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES REMARK 500 ARG H 76 NE - CZ - NH2 ANGL. DEV. = -3.5 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 VAL A 126 -54.78 73.40 REMARK 500 ALA A 313 -89.97 -104.68 REMARK 500 VAL B 126 -60.29 75.06 REMARK 500 ARG B 304 73.90 -150.27 REMARK 500 ALA B 313 -87.90 -105.76 REMARK 500 VAL C 126 -59.55 74.37 REMARK 500 ALA C 313 -87.14 -104.61 REMARK 500 VAL D 126 -56.09 74.10 REMARK 500 ALA D 313 -87.37 -107.67 REMARK 500 ASP F 106 99.50 -66.28 REMARK 500 ALA G 96 166.96 179.11 REMARK 500 TRP G 127 129.45 -39.66 REMARK 500 SER H 56 123.04 -34.93 REMARK 500 ASP H 106 96.43 -59.75 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 3 0.08 SIDE CHAIN REMARK 500 ARG B 314 0.09 SIDE CHAIN REMARK 500 ARG C 67 0.08 SIDE CHAIN REMARK 500 ARG C 314 0.12 SIDE CHAIN REMARK 500 ARG D 53 0.09 SIDE CHAIN REMARK 500 ARG E 19 0.10 SIDE CHAIN REMARK 500 ARG E 97 0.09 SIDE CHAIN REMARK 500 ARG F 97 0.11 SIDE CHAIN REMARK 500 ARG G 97 0.11 SIDE CHAIN REMARK 500 ARG H 97 0.13 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 B 761 DISTANCE = 6.11 ANGSTROMS DBREF 9GV3 A 1 372 UNP G0UWE7 G0UWE7_TRYCI 1 372 DBREF 9GV3 B 1 372 UNP G0UWE7 G0UWE7_TRYCI 1 372 DBREF 9GV3 C 1 372 UNP G0UWE7 G0UWE7_TRYCI 1 372 DBREF 9GV3 D 1 372 UNP G0UWE7 G0UWE7_TRYCI 1 372 DBREF 9GV3 E 1 143 PDB 9GV3 9GV3 1 143 DBREF 9GV3 F 1 143 PDB 9GV3 9GV3 1 143 DBREF 9GV3 G 1 143 PDB 9GV3 9GV3 1 143 DBREF 9GV3 H 1 143 PDB 9GV3 9GV3 1 143 SEQADV 9GV3 GLU A 373 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 ASN A 374 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 LEU A 375 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 TYR A 376 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 PHE A 377 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 GLN A 378 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 SER A 379 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 GLY A 380 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 GLY A 381 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 HIS A 382 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 HIS A 383 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 HIS A 384 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 HIS A 385 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 HIS A 386 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 HIS A 387 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 GLU B 373 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 ASN B 374 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 LEU B 375 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 TYR B 376 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 PHE B 377 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 GLN B 378 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 SER B 379 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 GLY B 380 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 GLY B 381 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 HIS B 382 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 HIS B 383 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 HIS B 384 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 HIS B 385 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 HIS B 386 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 HIS B 387 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 GLU C 373 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 ASN C 374 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 LEU C 375 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 TYR C 376 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 PHE C 377 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 GLN C 378 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 SER C 379 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 GLY C 380 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 GLY C 381 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 HIS C 382 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 HIS C 383 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 HIS C 384 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 HIS C 385 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 HIS C 386 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 HIS C 387 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 GLU D 373 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 ASN D 374 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 LEU D 375 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 TYR D 376 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 PHE D 377 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 GLN D 378 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 SER D 379 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 GLY D 380 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 GLY D 381 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 HIS D 382 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 HIS D 383 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 HIS D 384 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 HIS D 385 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 HIS D 386 UNP G0UWE7 EXPRESSION TAG SEQADV 9GV3 HIS D 387 UNP G0UWE7 EXPRESSION TAG SEQRES 1 A 387 MET SER ARG ARG VAL GLU VAL LEU LEU THR GLN LEU PRO SEQRES 2 A 387 ALA TYR ASN ARG LEU LYS THR PRO TYR GLU GLU GLU LEU SEQRES 3 A 387 ILE GLU THR ALA LYS LYS MET THR ALA PRO GLY LYS GLY SEQRES 4 A 387 LEU LEU ALA ALA ASP GLU SER THR GLY SER CYS SER LYS SEQRES 5 A 387 ARG PHE ALA GLY ILE GLY LEU SER ASN THR ALA GLU HIS SEQRES 6 A 387 ARG ARG GLN TYR ARG ALA LEU MET LEU GLU CYS ALA GLY SEQRES 7 A 387 PHE GLU GLN TYR ILE SER GLY VAL ILE LEU HIS ASP GLU SEQRES 8 A 387 THR VAL TYR GLN ARG ALA SER THR GLY GLU THR PHE PRO SEQRES 9 A 387 GLN LEU LEU ARG ARG ARG GLY VAL VAL PRO GLY ILE LYS SEQRES 10 A 387 THR ASP CYS GLY LEU GLU PRO LEU VAL GLU GLY ALA ASP SEQRES 11 A 387 GLY GLU GLN MET THR ALA GLY LEU ASP GLY TYR VAL LYS SEQRES 12 A 387 ARG ALA LYS LYS TYR TYR ALA VAL GLY CYS ARG PHE CYS SEQRES 13 A 387 LYS TRP ARG ASN VAL TYR LYS ILE GLN ASN GLY THR VAL SEQRES 14 A 387 SER GLU ALA VAL VAL ARG PHE ASN ALA GLU THR LEU ALA SEQRES 15 A 387 ARG TYR ALA VAL LEU SER GLN LEU CYS GLY LEU VAL PRO SEQRES 16 A 387 ILE VAL GLU PRO GLU VAL MET ILE ASP GLY THR HIS ASP SEQRES 17 A 387 ILE GLU THR CYS GLN ARG VAL SER GLN HIS VAL TRP ALA SEQRES 18 A 387 GLU VAL VAL SER ALA LEU HIS ARG HIS GLY VAL VAL TRP SEQRES 19 A 387 GLU GLY CYS LEU LEU LYS PRO ASN MET VAL VAL PRO GLY SEQRES 20 A 387 ALA GLU SER GLY GLN THR ALA THR ALA GLU GLN VAL ALA SEQRES 21 A 387 GLU TYR THR VAL LYS THR LEU ALA ARG VAL LEU PRO PRO SEQRES 22 A 387 ALA LEU PRO GLY VAL THR PHE LEU SER GLY GLY LEU SER SEQRES 23 A 387 GLU VAL MET ALA SER GLU TYR LEU ASN ALA MET ASN ASN SEQRES 24 A 387 SER PRO LEU PRO ARG PRO TRP LYS LEU THR PHE SER TYR SEQRES 25 A 387 ALA ARG ALA LEU GLN SER SER ALA ILE LYS ALA TRP GLY SEQRES 26 A 387 GLY LYS SER SER GLY VAL ALA ALA GLY ARG ARG ALA PHE SEQRES 27 A 387 MET HIS ARG ALA LYS MET ASN SER LEU ALA GLN LEU GLY SEQRES 28 A 387 ARG TYR ASN ARG GLY ASP ASP ASP LYS ASP SER GLN SER SEQRES 29 A 387 LEU TYR VAL ALA GLY ASN THR TYR GLU ASN LEU TYR PHE SEQRES 30 A 387 GLN SER GLY GLY HIS HIS HIS HIS HIS HIS SEQRES 1 B 387 MET SER ARG ARG VAL GLU VAL LEU LEU THR GLN LEU PRO SEQRES 2 B 387 ALA TYR ASN ARG LEU LYS THR PRO TYR GLU GLU GLU LEU SEQRES 3 B 387 ILE GLU THR ALA LYS LYS MET THR ALA PRO GLY LYS GLY SEQRES 4 B 387 LEU LEU ALA ALA ASP GLU SER THR GLY SER CYS SER LYS SEQRES 5 B 387 ARG PHE ALA GLY ILE GLY LEU SER ASN THR ALA GLU HIS SEQRES 6 B 387 ARG ARG GLN TYR ARG ALA LEU MET LEU GLU CYS ALA GLY SEQRES 7 B 387 PHE GLU GLN TYR ILE SER GLY VAL ILE LEU HIS ASP GLU SEQRES 8 B 387 THR VAL TYR GLN ARG ALA SER THR GLY GLU THR PHE PRO SEQRES 9 B 387 GLN LEU LEU ARG ARG ARG GLY VAL VAL PRO GLY ILE LYS SEQRES 10 B 387 THR ASP CYS GLY LEU GLU PRO LEU VAL GLU GLY ALA ASP SEQRES 11 B 387 GLY GLU GLN MET THR ALA GLY LEU ASP GLY TYR VAL LYS SEQRES 12 B 387 ARG ALA LYS LYS TYR TYR ALA VAL GLY CYS ARG PHE CYS SEQRES 13 B 387 LYS TRP ARG ASN VAL TYR LYS ILE GLN ASN GLY THR VAL SEQRES 14 B 387 SER GLU ALA VAL VAL ARG PHE ASN ALA GLU THR LEU ALA SEQRES 15 B 387 ARG TYR ALA VAL LEU SER GLN LEU CYS GLY LEU VAL PRO SEQRES 16 B 387 ILE VAL GLU PRO GLU VAL MET ILE ASP GLY THR HIS ASP SEQRES 17 B 387 ILE GLU THR CYS GLN ARG VAL SER GLN HIS VAL TRP ALA SEQRES 18 B 387 GLU VAL VAL SER ALA LEU HIS ARG HIS GLY VAL VAL TRP SEQRES 19 B 387 GLU GLY CYS LEU LEU LYS PRO ASN MET VAL VAL PRO GLY SEQRES 20 B 387 ALA GLU SER GLY GLN THR ALA THR ALA GLU GLN VAL ALA SEQRES 21 B 387 GLU TYR THR VAL LYS THR LEU ALA ARG VAL LEU PRO PRO SEQRES 22 B 387 ALA LEU PRO GLY VAL THR PHE LEU SER GLY GLY LEU SER SEQRES 23 B 387 GLU VAL MET ALA SER GLU TYR LEU ASN ALA MET ASN ASN SEQRES 24 B 387 SER PRO LEU PRO ARG PRO TRP LYS LEU THR PHE SER TYR SEQRES 25 B 387 ALA ARG ALA LEU GLN SER SER ALA ILE LYS ALA TRP GLY SEQRES 26 B 387 GLY LYS SER SER GLY VAL ALA ALA GLY ARG ARG ALA PHE SEQRES 27 B 387 MET HIS ARG ALA LYS MET ASN SER LEU ALA GLN LEU GLY SEQRES 28 B 387 ARG TYR ASN ARG GLY ASP ASP ASP LYS ASP SER GLN SER SEQRES 29 B 387 LEU TYR VAL ALA GLY ASN THR TYR GLU ASN LEU TYR PHE SEQRES 30 B 387 GLN SER GLY GLY HIS HIS HIS HIS HIS HIS SEQRES 1 C 387 MET SER ARG ARG VAL GLU VAL LEU LEU THR GLN LEU PRO SEQRES 2 C 387 ALA TYR ASN ARG LEU LYS THR PRO TYR GLU GLU GLU LEU SEQRES 3 C 387 ILE GLU THR ALA LYS LYS MET THR ALA PRO GLY LYS GLY SEQRES 4 C 387 LEU LEU ALA ALA ASP GLU SER THR GLY SER CYS SER LYS SEQRES 5 C 387 ARG PHE ALA GLY ILE GLY LEU SER ASN THR ALA GLU HIS SEQRES 6 C 387 ARG ARG GLN TYR ARG ALA LEU MET LEU GLU CYS ALA GLY SEQRES 7 C 387 PHE GLU GLN TYR ILE SER GLY VAL ILE LEU HIS ASP GLU SEQRES 8 C 387 THR VAL TYR GLN ARG ALA SER THR GLY GLU THR PHE PRO SEQRES 9 C 387 GLN LEU LEU ARG ARG ARG GLY VAL VAL PRO GLY ILE LYS SEQRES 10 C 387 THR ASP CYS GLY LEU GLU PRO LEU VAL GLU GLY ALA ASP SEQRES 11 C 387 GLY GLU GLN MET THR ALA GLY LEU ASP GLY TYR VAL LYS SEQRES 12 C 387 ARG ALA LYS LYS TYR TYR ALA VAL GLY CYS ARG PHE CYS SEQRES 13 C 387 LYS TRP ARG ASN VAL TYR LYS ILE GLN ASN GLY THR VAL SEQRES 14 C 387 SER GLU ALA VAL VAL ARG PHE ASN ALA GLU THR LEU ALA SEQRES 15 C 387 ARG TYR ALA VAL LEU SER GLN LEU CYS GLY LEU VAL PRO SEQRES 16 C 387 ILE VAL GLU PRO GLU VAL MET ILE ASP GLY THR HIS ASP SEQRES 17 C 387 ILE GLU THR CYS GLN ARG VAL SER GLN HIS VAL TRP ALA SEQRES 18 C 387 GLU VAL VAL SER ALA LEU HIS ARG HIS GLY VAL VAL TRP SEQRES 19 C 387 GLU GLY CYS LEU LEU LYS PRO ASN MET VAL VAL PRO GLY SEQRES 20 C 387 ALA GLU SER GLY GLN THR ALA THR ALA GLU GLN VAL ALA SEQRES 21 C 387 GLU TYR THR VAL LYS THR LEU ALA ARG VAL LEU PRO PRO SEQRES 22 C 387 ALA LEU PRO GLY VAL THR PHE LEU SER GLY GLY LEU SER SEQRES 23 C 387 GLU VAL MET ALA SER GLU TYR LEU ASN ALA MET ASN ASN SEQRES 24 C 387 SER PRO LEU PRO ARG PRO TRP LYS LEU THR PHE SER TYR SEQRES 25 C 387 ALA ARG ALA LEU GLN SER SER ALA ILE LYS ALA TRP GLY SEQRES 26 C 387 GLY LYS SER SER GLY VAL ALA ALA GLY ARG ARG ALA PHE SEQRES 27 C 387 MET HIS ARG ALA LYS MET ASN SER LEU ALA GLN LEU GLY SEQRES 28 C 387 ARG TYR ASN ARG GLY ASP ASP ASP LYS ASP SER GLN SER SEQRES 29 C 387 LEU TYR VAL ALA GLY ASN THR TYR GLU ASN LEU TYR PHE SEQRES 30 C 387 GLN SER GLY GLY HIS HIS HIS HIS HIS HIS SEQRES 1 D 387 MET SER ARG ARG VAL GLU VAL LEU LEU THR GLN LEU PRO SEQRES 2 D 387 ALA TYR ASN ARG LEU LYS THR PRO TYR GLU GLU GLU LEU SEQRES 3 D 387 ILE GLU THR ALA LYS LYS MET THR ALA PRO GLY LYS GLY SEQRES 4 D 387 LEU LEU ALA ALA ASP GLU SER THR GLY SER CYS SER LYS SEQRES 5 D 387 ARG PHE ALA GLY ILE GLY LEU SER ASN THR ALA GLU HIS SEQRES 6 D 387 ARG ARG GLN TYR ARG ALA LEU MET LEU GLU CYS ALA GLY SEQRES 7 D 387 PHE GLU GLN TYR ILE SER GLY VAL ILE LEU HIS ASP GLU SEQRES 8 D 387 THR VAL TYR GLN ARG ALA SER THR GLY GLU THR PHE PRO SEQRES 9 D 387 GLN LEU LEU ARG ARG ARG GLY VAL VAL PRO GLY ILE LYS SEQRES 10 D 387 THR ASP CYS GLY LEU GLU PRO LEU VAL GLU GLY ALA ASP SEQRES 11 D 387 GLY GLU GLN MET THR ALA GLY LEU ASP GLY TYR VAL LYS SEQRES 12 D 387 ARG ALA LYS LYS TYR TYR ALA VAL GLY CYS ARG PHE CYS SEQRES 13 D 387 LYS TRP ARG ASN VAL TYR LYS ILE GLN ASN GLY THR VAL SEQRES 14 D 387 SER GLU ALA VAL VAL ARG PHE ASN ALA GLU THR LEU ALA SEQRES 15 D 387 ARG TYR ALA VAL LEU SER GLN LEU CYS GLY LEU VAL PRO SEQRES 16 D 387 ILE VAL GLU PRO GLU VAL MET ILE ASP GLY THR HIS ASP SEQRES 17 D 387 ILE GLU THR CYS GLN ARG VAL SER GLN HIS VAL TRP ALA SEQRES 18 D 387 GLU VAL VAL SER ALA LEU HIS ARG HIS GLY VAL VAL TRP SEQRES 19 D 387 GLU GLY CYS LEU LEU LYS PRO ASN MET VAL VAL PRO GLY SEQRES 20 D 387 ALA GLU SER GLY GLN THR ALA THR ALA GLU GLN VAL ALA SEQRES 21 D 387 GLU TYR THR VAL LYS THR LEU ALA ARG VAL LEU PRO PRO SEQRES 22 D 387 ALA LEU PRO GLY VAL THR PHE LEU SER GLY GLY LEU SER SEQRES 23 D 387 GLU VAL MET ALA SER GLU TYR LEU ASN ALA MET ASN ASN SEQRES 24 D 387 SER PRO LEU PRO ARG PRO TRP LYS LEU THR PHE SER TYR SEQRES 25 D 387 ALA ARG ALA LEU GLN SER SER ALA ILE LYS ALA TRP GLY SEQRES 26 D 387 GLY LYS SER SER GLY VAL ALA ALA GLY ARG ARG ALA PHE SEQRES 27 D 387 MET HIS ARG ALA LYS MET ASN SER LEU ALA GLN LEU GLY SEQRES 28 D 387 ARG TYR ASN ARG GLY ASP ASP ASP LYS ASP SER GLN SER SEQRES 29 D 387 LEU TYR VAL ALA GLY ASN THR TYR GLU ASN LEU TYR PHE SEQRES 30 D 387 GLN SER GLY GLY HIS HIS HIS HIS HIS HIS SEQRES 1 E 143 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 E 143 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLU SEQRES 3 E 143 THR ALA LEU THR TYR TYR ALA ILE GLY TRP PHE ARG GLN SEQRES 4 E 143 ALA PRO GLY LYS GLU ARG GLU GLY VAL SER CYS ILE SER SEQRES 5 E 143 ALA ILE ASN SER GLY SER GLY ALA ARG THR ASP TYR ALA SEQRES 6 E 143 ASP SER VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASP SEQRES 7 E 143 ALA LYS ASN THR VAL THR LEU GLN MET ASN SER LEU GLU SEQRES 8 E 143 PRO GLU ASP THR ALA ARG TYR TYR CYS ALA LEU ASP THR SEQRES 9 E 143 THR ASP ARG TYR ASP SER ALA ASN GLY ARG TYR TYR CYS SEQRES 10 E 143 THR ILE SER SER ASP THR TYR ALA TYR TRP GLY GLN GLY SEQRES 11 E 143 THR GLN VAL THR VAL SER SER HIS HIS HIS HIS HIS HIS SEQRES 1 F 143 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 F 143 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLU SEQRES 3 F 143 THR ALA LEU THR TYR TYR ALA ILE GLY TRP PHE ARG GLN SEQRES 4 F 143 ALA PRO GLY LYS GLU ARG GLU GLY VAL SER CYS ILE SER SEQRES 5 F 143 ALA ILE ASN SER GLY SER GLY ALA ARG THR ASP TYR ALA SEQRES 6 F 143 ASP SER VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASP SEQRES 7 F 143 ALA LYS ASN THR VAL THR LEU GLN MET ASN SER LEU GLU SEQRES 8 F 143 PRO GLU ASP THR ALA ARG TYR TYR CYS ALA LEU ASP THR SEQRES 9 F 143 THR ASP ARG TYR ASP SER ALA ASN GLY ARG TYR TYR CYS SEQRES 10 F 143 THR ILE SER SER ASP THR TYR ALA TYR TRP GLY GLN GLY SEQRES 11 F 143 THR GLN VAL THR VAL SER SER HIS HIS HIS HIS HIS HIS SEQRES 1 G 143 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 G 143 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLU SEQRES 3 G 143 THR ALA LEU THR TYR TYR ALA ILE GLY TRP PHE ARG GLN SEQRES 4 G 143 ALA PRO GLY LYS GLU ARG GLU GLY VAL SER CYS ILE SER SEQRES 5 G 143 ALA ILE ASN SER GLY SER GLY ALA ARG THR ASP TYR ALA SEQRES 6 G 143 ASP SER VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASP SEQRES 7 G 143 ALA LYS ASN THR VAL THR LEU GLN MET ASN SER LEU GLU SEQRES 8 G 143 PRO GLU ASP THR ALA ARG TYR TYR CYS ALA LEU ASP THR SEQRES 9 G 143 THR ASP ARG TYR ASP SER ALA ASN GLY ARG TYR TYR CYS SEQRES 10 G 143 THR ILE SER SER ASP THR TYR ALA TYR TRP GLY GLN GLY SEQRES 11 G 143 THR GLN VAL THR VAL SER SER HIS HIS HIS HIS HIS HIS SEQRES 1 H 143 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 143 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLU SEQRES 3 H 143 THR ALA LEU THR TYR TYR ALA ILE GLY TRP PHE ARG GLN SEQRES 4 H 143 ALA PRO GLY LYS GLU ARG GLU GLY VAL SER CYS ILE SER SEQRES 5 H 143 ALA ILE ASN SER GLY SER GLY ALA ARG THR ASP TYR ALA SEQRES 6 H 143 ASP SER VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASP SEQRES 7 H 143 ALA LYS ASN THR VAL THR LEU GLN MET ASN SER LEU GLU SEQRES 8 H 143 PRO GLU ASP THR ALA ARG TYR TYR CYS ALA LEU ASP THR SEQRES 9 H 143 THR ASP ARG TYR ASP SER ALA ASN GLY ARG TYR TYR CYS SEQRES 10 H 143 THR ILE SER SER ASP THR TYR ALA TYR TRP GLY GLN GLY SEQRES 11 H 143 THR GLN VAL THR VAL SER SER HIS HIS HIS HIS HIS HIS HET ACT B 401 4 HET ACT B 402 4 HET ACT C 401 4 HET ACT C 402 4 HET GOL D 401 6 HETNAM ACT ACETATE ION HETNAM GOL GLYCEROL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 9 ACT 4(C2 H3 O2 1-) FORMUL 13 GOL C3 H8 O3 FORMUL 14 HOH *1343(H2 O) HELIX 1 AA1 THR A 10 ASN A 16 5 7 HELIX 2 AA2 TYR A 22 THR A 34 1 13 HELIX 3 AA3 SER A 46 GLY A 56 1 11 HELIX 4 AA4 THR A 62 GLU A 75 1 14 HELIX 5 AA5 GLY A 78 GLN A 81 5 4 HELIX 6 AA6 HIS A 89 TYR A 94 1 6 HELIX 7 AA7 THR A 102 ARG A 110 1 9 HELIX 8 AA8 GLY A 140 VAL A 151 1 12 HELIX 9 AA9 SER A 170 CYS A 191 1 22 HELIX 10 AB1 ASP A 208 GLY A 231 1 24 HELIX 11 AB2 VAL A 233 CYS A 237 5 5 HELIX 12 AB3 THR A 255 LEU A 271 1 17 HELIX 13 AB4 SER A 286 ASN A 298 1 13 HELIX 14 AB5 ALA A 313 GLY A 325 1 13 HELIX 15 AB6 LYS A 327 SER A 329 5 3 HELIX 16 AB7 GLY A 330 LEU A 350 1 21 HELIX 17 AB8 ASN A 354 SER A 364 1 11 HELIX 18 AB9 THR B 10 ASN B 16 5 7 HELIX 19 AC1 TYR B 22 THR B 34 1 13 HELIX 20 AC2 SER B 46 GLY B 56 1 11 HELIX 21 AC3 THR B 62 GLU B 75 1 14 HELIX 22 AC4 GLY B 78 GLN B 81 5 4 HELIX 23 AC5 HIS B 89 TYR B 94 1 6 HELIX 24 AC6 THR B 102 ARG B 110 1 9 HELIX 25 AC7 GLY B 140 VAL B 151 1 12 HELIX 26 AC8 SER B 170 CYS B 191 1 22 HELIX 27 AC9 ASP B 208 GLY B 231 1 24 HELIX 28 AD1 VAL B 233 CYS B 237 5 5 HELIX 29 AD2 THR B 255 LEU B 271 1 17 HELIX 30 AD3 SER B 286 ASN B 298 1 13 HELIX 31 AD4 ALA B 313 GLY B 325 1 13 HELIX 32 AD5 LYS B 327 SER B 329 5 3 HELIX 33 AD6 GLY B 330 LEU B 350 1 21 HELIX 34 AD7 ASN B 354 ASP B 359 1 6 HELIX 35 AD8 THR C 10 ASN C 16 5 7 HELIX 36 AD9 TYR C 22 THR C 34 1 13 HELIX 37 AE1 SER C 46 GLY C 56 1 11 HELIX 38 AE2 THR C 62 GLU C 75 1 14 HELIX 39 AE3 GLY C 78 GLN C 81 5 4 HELIX 40 AE4 HIS C 89 TYR C 94 1 6 HELIX 41 AE5 THR C 102 ARG C 110 1 9 HELIX 42 AE6 GLY C 140 VAL C 151 1 12 HELIX 43 AE7 SER C 170 CYS C 191 1 22 HELIX 44 AE8 ASP C 208 GLY C 231 1 24 HELIX 45 AE9 VAL C 233 CYS C 237 5 5 HELIX 46 AF1 THR C 255 LEU C 271 1 17 HELIX 47 AF2 SER C 286 ASN C 298 1 13 HELIX 48 AF3 ALA C 313 GLY C 325 1 13 HELIX 49 AF4 LYS C 327 SER C 329 5 3 HELIX 50 AF5 GLY C 330 LEU C 350 1 21 HELIX 51 AF6 ASN C 354 ASP C 359 1 6 HELIX 52 AF7 THR D 10 ASN D 16 5 7 HELIX 53 AF8 TYR D 22 THR D 34 1 13 HELIX 54 AF9 SER D 46 PHE D 54 1 9 HELIX 55 AG1 THR D 62 GLU D 75 1 14 HELIX 56 AG2 GLY D 78 GLN D 81 5 4 HELIX 57 AG3 HIS D 89 TYR D 94 1 6 HELIX 58 AG4 THR D 102 ARG D 110 1 9 HELIX 59 AG5 GLY D 140 VAL D 151 1 12 HELIX 60 AG6 SER D 170 CYS D 191 1 22 HELIX 61 AG7 ASP D 208 GLY D 231 1 24 HELIX 62 AG8 VAL D 233 CYS D 237 5 5 HELIX 63 AG9 THR D 255 LEU D 271 1 17 HELIX 64 AH1 SER D 286 ASN D 298 1 13 HELIX 65 AH2 ALA D 313 GLY D 325 1 13 HELIX 66 AH3 LYS D 327 SER D 329 5 3 HELIX 67 AH4 GLY D 330 LEU D 350 1 21 HELIX 68 AH5 ASN D 354 ASP D 359 1 6 HELIX 69 AH6 ALA E 28 TYR E 32 5 5 HELIX 70 AH7 ASP E 66 LYS E 69 5 4 HELIX 71 AH8 GLU E 91 THR E 95 5 5 HELIX 72 AH9 ALA F 28 TYR F 32 5 5 HELIX 73 AI1 ASP F 66 LYS F 69 5 4 HELIX 74 AI2 GLU F 91 THR F 95 5 5 HELIX 75 AI3 ALA G 28 TYR G 32 5 5 HELIX 76 AI4 ASP G 66 LYS G 69 5 4 HELIX 77 AI5 GLU G 91 THR G 95 5 5 HELIX 78 AI6 ALA H 28 TYR H 32 5 5 HELIX 79 AI7 ASP H 66 LYS H 69 5 4 HELIX 80 AI8 GLU H 91 THR H 95 5 5 SHEET 1 AA1 2 ARG A 4 LEU A 8 0 SHEET 2 AA1 2 ARG D 4 LEU D 8 -1 O VAL D 7 N VAL A 5 SHEET 1 AA2 9 GLY A 39 ALA A 43 0 SHEET 2 AA2 9 ILE A 83 LEU A 88 1 O ILE A 87 N LEU A 41 SHEET 3 AA2 9 VAL A 113 LYS A 117 1 O VAL A 113 N SER A 84 SHEET 4 AA2 9 PHE A 155 TYR A 162 1 O LYS A 157 N ILE A 116 SHEET 5 AA2 9 VAL A 194 VAL A 201 1 O GLU A 198 N ASN A 160 SHEET 6 AA2 9 LEU A 238 LEU A 239 1 O LEU A 238 N VAL A 197 SHEET 7 AA2 9 GLY A 277 PHE A 280 1 O THR A 279 N LEU A 239 SHEET 8 AA2 9 LYS A 307 TYR A 312 1 O THR A 309 N VAL A 278 SHEET 9 AA2 9 GLY A 39 ALA A 43 1 N LEU A 40 O PHE A 310 SHEET 1 AA3 2 LEU A 122 PRO A 124 0 SHEET 2 AA3 2 GLN A 133 THR A 135 -1 O MET A 134 N GLU A 123 SHEET 1 AA4 2 ARG B 4 LEU B 8 0 SHEET 2 AA4 2 ARG C 4 LEU C 8 -1 O VAL C 5 N VAL B 7 SHEET 1 AA5 9 GLY B 39 ALA B 43 0 SHEET 2 AA5 9 ILE B 83 LEU B 88 1 O ILE B 87 N LEU B 41 SHEET 3 AA5 9 VAL B 113 LYS B 117 1 O VAL B 113 N SER B 84 SHEET 4 AA5 9 PHE B 155 TYR B 162 1 O LYS B 157 N ILE B 116 SHEET 5 AA5 9 VAL B 194 VAL B 201 1 O GLU B 198 N ASN B 160 SHEET 6 AA5 9 LEU B 238 LEU B 239 1 O LEU B 238 N VAL B 197 SHEET 7 AA5 9 GLY B 277 PHE B 280 1 O THR B 279 N LEU B 239 SHEET 8 AA5 9 LYS B 307 TYR B 312 1 O LYS B 307 N VAL B 278 SHEET 9 AA5 9 GLY B 39 ALA B 43 1 N LEU B 40 O PHE B 310 SHEET 1 AA6 2 LEU B 122 PRO B 124 0 SHEET 2 AA6 2 GLN B 133 THR B 135 -1 O MET B 134 N GLU B 123 SHEET 1 AA7 9 GLY C 39 ALA C 43 0 SHEET 2 AA7 9 ILE C 83 LEU C 88 1 O ILE C 87 N LEU C 41 SHEET 3 AA7 9 VAL C 113 LYS C 117 1 O GLY C 115 N VAL C 86 SHEET 4 AA7 9 PHE C 155 TYR C 162 1 O LYS C 157 N ILE C 116 SHEET 5 AA7 9 VAL C 194 VAL C 201 1 O GLU C 198 N ASN C 160 SHEET 6 AA7 9 LEU C 238 LEU C 239 1 O LEU C 238 N VAL C 197 SHEET 7 AA7 9 GLY C 277 PHE C 280 1 O THR C 279 N LEU C 239 SHEET 8 AA7 9 LYS C 307 TYR C 312 1 O THR C 309 N VAL C 278 SHEET 9 AA7 9 GLY C 39 ALA C 43 1 N ALA C 42 O TYR C 312 SHEET 1 AA8 2 LEU C 122 PRO C 124 0 SHEET 2 AA8 2 GLN C 133 THR C 135 -1 O MET C 134 N GLU C 123 SHEET 1 AA9 9 GLY D 39 ALA D 43 0 SHEET 2 AA9 9 ILE D 83 LEU D 88 1 O ILE D 87 N LEU D 41 SHEET 3 AA9 9 VAL D 113 LYS D 117 1 O VAL D 113 N SER D 84 SHEET 4 AA9 9 PHE D 155 TYR D 162 1 O LYS D 157 N ILE D 116 SHEET 5 AA9 9 VAL D 194 VAL D 201 1 O GLU D 200 N ASN D 160 SHEET 6 AA9 9 LEU D 238 LEU D 239 1 O LEU D 238 N VAL D 197 SHEET 7 AA9 9 GLY D 277 PHE D 280 1 O THR D 279 N LEU D 239 SHEET 8 AA9 9 LYS D 307 TYR D 312 1 O LYS D 307 N VAL D 278 SHEET 9 AA9 9 GLY D 39 ALA D 43 1 N LEU D 40 O PHE D 310 SHEET 1 AB1 2 LEU D 122 PRO D 124 0 SHEET 2 AB1 2 GLN D 133 THR D 135 -1 O MET D 134 N GLU D 123 SHEET 1 AB2 4 GLN E 5 SER E 7 0 SHEET 2 AB2 4 LEU E 18 ALA E 23 -1 O SER E 21 N SER E 7 SHEET 3 AB2 4 THR E 82 MET E 87 -1 O MET E 87 N LEU E 18 SHEET 4 AB2 4 PHE E 72 ASP E 77 -1 N THR E 73 O GLN E 86 SHEET 1 AB3 6 GLY E 10 VAL E 12 0 SHEET 2 AB3 6 THR E 131 VAL E 135 1 O THR E 134 N GLY E 10 SHEET 3 AB3 6 ALA E 96 ASP E 103 -1 N TYR E 98 O THR E 131 SHEET 4 AB3 6 ILE E 34 GLN E 39 -1 N PHE E 37 O TYR E 99 SHEET 5 AB3 6 GLU E 46 ILE E 51 -1 O SER E 49 N TRP E 36 SHEET 6 AB3 6 THR E 62 TYR E 64 -1 O ASP E 63 N CYS E 50 SHEET 1 AB4 4 GLY E 10 VAL E 12 0 SHEET 2 AB4 4 THR E 131 VAL E 135 1 O THR E 134 N GLY E 10 SHEET 3 AB4 4 ALA E 96 ASP E 103 -1 N TYR E 98 O THR E 131 SHEET 4 AB4 4 TYR E 124 ALA E 125 -1 O ALA E 125 N LEU E 102 SHEET 1 AB5 2 TYR E 108 ASP E 109 0 SHEET 2 AB5 2 ARG E 114 TYR E 115 -1 O ARG E 114 N ASP E 109 SHEET 1 AB6 4 GLN F 5 SER F 7 0 SHEET 2 AB6 4 LEU F 18 ALA F 23 -1 O SER F 21 N SER F 7 SHEET 3 AB6 4 THR F 82 MET F 87 -1 O MET F 87 N LEU F 18 SHEET 4 AB6 4 PHE F 72 ASP F 77 -1 N ASP F 77 O THR F 82 SHEET 1 AB7 6 GLY F 10 VAL F 12 0 SHEET 2 AB7 6 THR F 131 VAL F 135 1 O THR F 134 N GLY F 10 SHEET 3 AB7 6 ALA F 96 ASP F 103 -1 N TYR F 98 O THR F 131 SHEET 4 AB7 6 ILE F 34 GLN F 39 -1 N PHE F 37 O TYR F 99 SHEET 5 AB7 6 GLU F 46 ILE F 51 -1 O SER F 49 N TRP F 36 SHEET 6 AB7 6 THR F 62 TYR F 64 -1 O ASP F 63 N CYS F 50 SHEET 1 AB8 4 GLY F 10 VAL F 12 0 SHEET 2 AB8 4 THR F 131 VAL F 135 1 O THR F 134 N GLY F 10 SHEET 3 AB8 4 ALA F 96 ASP F 103 -1 N TYR F 98 O THR F 131 SHEET 4 AB8 4 TYR F 124 ALA F 125 -1 O ALA F 125 N LEU F 102 SHEET 1 AB9 2 TYR F 108 ASP F 109 0 SHEET 2 AB9 2 ARG F 114 TYR F 115 -1 O ARG F 114 N ASP F 109 SHEET 1 AC1 4 GLN G 5 SER G 7 0 SHEET 2 AC1 4 LEU G 18 ALA G 23 -1 O SER G 21 N SER G 7 SHEET 3 AC1 4 THR G 82 MET G 87 -1 O MET G 87 N LEU G 18 SHEET 4 AC1 4 PHE G 72 ASP G 77 -1 N ASP G 77 O THR G 82 SHEET 1 AC2 6 GLY G 10 VAL G 12 0 SHEET 2 AC2 6 THR G 131 VAL G 135 1 O THR G 134 N GLY G 10 SHEET 3 AC2 6 ALA G 96 ASP G 103 -1 N TYR G 98 O THR G 131 SHEET 4 AC2 6 ILE G 34 GLN G 39 -1 N PHE G 37 O TYR G 99 SHEET 5 AC2 6 GLU G 46 ILE G 51 -1 O SER G 49 N TRP G 36 SHEET 6 AC2 6 THR G 62 TYR G 64 -1 O ASP G 63 N CYS G 50 SHEET 1 AC3 4 GLY G 10 VAL G 12 0 SHEET 2 AC3 4 THR G 131 VAL G 135 1 O THR G 134 N GLY G 10 SHEET 3 AC3 4 ALA G 96 ASP G 103 -1 N TYR G 98 O THR G 131 SHEET 4 AC3 4 TYR G 124 ALA G 125 -1 O ALA G 125 N LEU G 102 SHEET 1 AC4 2 TYR G 108 ASP G 109 0 SHEET 2 AC4 2 ARG G 114 TYR G 115 -1 O ARG G 114 N ASP G 109 SHEET 1 AC5 4 GLN H 5 SER H 7 0 SHEET 2 AC5 4 LEU H 18 ALA H 23 -1 O SER H 21 N SER H 7 SHEET 3 AC5 4 THR H 82 MET H 87 -1 O MET H 87 N LEU H 18 SHEET 4 AC5 4 PHE H 72 ASP H 77 -1 N ASP H 77 O THR H 82 SHEET 1 AC6 6 GLY H 10 VAL H 12 0 SHEET 2 AC6 6 THR H 131 VAL H 135 1 O THR H 134 N VAL H 12 SHEET 3 AC6 6 ALA H 96 ASP H 103 -1 N TYR H 98 O THR H 131 SHEET 4 AC6 6 ILE H 34 GLN H 39 -1 N PHE H 37 O TYR H 99 SHEET 5 AC6 6 GLU H 46 ILE H 51 -1 O SER H 49 N TRP H 36 SHEET 6 AC6 6 THR H 62 TYR H 64 -1 O ASP H 63 N CYS H 50 SHEET 1 AC7 4 GLY H 10 VAL H 12 0 SHEET 2 AC7 4 THR H 131 VAL H 135 1 O THR H 134 N VAL H 12 SHEET 3 AC7 4 ALA H 96 ASP H 103 -1 N TYR H 98 O THR H 131 SHEET 4 AC7 4 TYR H 124 ALA H 125 -1 O ALA H 125 N LEU H 102 SHEET 1 AC8 2 TYR H 108 ASP H 109 0 SHEET 2 AC8 2 ARG H 114 TYR H 115 -1 O ARG H 114 N ASP H 109 SSBOND 1 CYS E 22 CYS E 100 1555 1555 2.13 SSBOND 2 CYS E 50 CYS E 117 1555 1555 2.31 SSBOND 3 CYS F 22 CYS F 100 1555 1555 2.07 SSBOND 4 CYS F 50 CYS F 117 1555 1555 2.33 SSBOND 5 CYS G 22 CYS G 100 1555 1555 2.14 SSBOND 6 CYS G 50 CYS G 117 1555 1555 2.29 SSBOND 7 CYS H 22 CYS H 100 1555 1555 2.06 SSBOND 8 CYS H 50 CYS H 117 1555 1555 2.34 CRYST1 203.495 111.166 123.244 90.00 90.00 90.00 P 21 21 2 16 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.004914 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008996 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008114 0.00000