}q(X moviescenesq]q(]q]qeXversionqJ-Xnamesq]q(N]q(Xlig24q KKNK]q (]q (KXlig24q KJo]q (GGGe]q(GGGeKKNKK]q(GGGGGGGGGGGGGGGGeKNeKKK]q]q(KK]q(GxG@G#G2-G@"0G ĠGMG@G GG@"lG"EG )G@&׍@G/GG@jGV G 7@G@$qG$`G^5@G@%%`GMGG@#+G#C`GCG@#t9`G `GĠG@#5@G GG@"$GQGG@!`GKƠG;d`G@ ~GGEG@EGOG G@GVGFG@ bG G G@!u€G GG@$TGG.G@&GG!VG@(wGO@G$G@(ƧG\)G G@)tGnG{`G@)G 5?G G@'ۥGe]q(KKKKKKKKKK K K K K KKKKKKKKKKKe]q(KKKKKKKKKK K K K K KKKKKKKKKKKeXq]qNaNNNNNNeaN]q(]q(KKKJKMKe]q(KK KJKMKe]q(KKKJKMKe]q(KKKJKMKe]q(KKKJKMKe]q(KK KJKMKe]q(KKKJKMKe]q(KKKJKMKe]q (K KKJKMKe]q!(K KKJKMKe]q"(K K KJKMKe]q#(K KKJKMKe]q$(K K KJKMKe]q%(K KKJKMKe]q&(K K KJKMKe]q'(K KKJKMKe]q((K KKJKMKe]q)(KKKJKMKe]q*(KKKJKMKe]q+(KKKJKMKe]q,(KKKJKMKe]q-(KKKJKMKe]q.(KKKJKMKe]q/(KKKJKMKe]q0(KKKJKMKe]q1(KKKJKMKe]q2(KKKJKMKe]q3(KKKJKMKee]q4(]q5(MXAq6hX401q7hX00Zq8XC1q9XCq:hhhKKM-G@(33@G?G?33@GKKKKM{ KJ"KKKKKKKKKKGMy KKKKG? G?#G?¬G ĠG?=GfhNe]q;(Mh6hX401qXNq?hhhKKM-G@%QG?G?GKKKKM KJ"KKKKKKKKKKGM~ KKKKG?-G?ćG?o`GW>G?nG҈hNe]q@(Mh6hX401qAhX00ZqBXO1qCXOqDhhhKKM-G@+pG?G?QGKKKKM KJ"KKKKKKKKKKGM KKKKG?`G?ơaG?+`G?VG:)GdZ hNe]qE(Mh6hX401qFhX00ZqGXC2qHh:hhhKKM.G@'G?G?33@GKKKKM| KJ"KKKKKKKKKKGMz KKKKG?_`G?l"`G? GA `G?"GG hNe]qI(Mh6hX401qJhX00ZqKXN2qLh?hhhKKM.G@"G?G?GKKKKM KJ"KKKKKKKKKKGM KKKKG?G?^@G?GG?GhNe]qM(Mh6hX401qNhX00ZqOXO2qPhDhhhKKM.G@+QG?G?QGKKKKM KJ"KKKKKKKKKKGM KKKKG?ƀ@G?_ؠG?ƃ G?s G~Ov`G{hNe]qQ(Mh6hX401qRhX00ZqSXC3qTh:hhhKKM/G@'pG?G?33@GKKKKM} KJ"KKKKKKKKKKGM{ KKKKG?G?xl G?m`GG?@G˒@hNe]qU(Mh6hX401qVhX00ZqWXN3qXh?hhhKKM/G@$G?G?GKKKKM KJ"KKKKKKKKKKGM KKKKG?G?Ĩ`G?(GG?*@G"hNe]qY(Mh6hX401qZhX00Zq[XC4q\h:hhhKKM0G@'€G?G?33@GKKKKM~ KJ"KKKKKKKKKKGM| KKKKG?G?o`G?G G?҈GhNe]q](Mh6hX401q^hX00Zq_XC5q`h:hhhKKM1G@%3@G?G?33@GKKKKM KJ"KKKKKKKKKKGM} KKKKG?`G?Ů@G?A@GU@G?ϪGBZhNe]qa(Mh6hX401qbhX00ZqcXC6qdh:hhhKKM2G@%G?G?33@GKKKKM KJ"KKKKKKKKKKGM KKKKG? G?=G?GD G?GhNe]qe(Mh6hX401qfhX00ZqgXC7qhh:hhhKKM3G@&u€G?G?33@GKKKKM KJ"KKKKKKKKKKGM KKKKG?p@G?~G?J GG?G khNe]qi(Mh6hX401qjhX00ZqkXC8qlh:hhhKKM4G@' @G?G?33@GKKKKM KJ"KKKKKKKKKKGM KKKKG?X`G?tSG?/GC,G?v+GquhNe]qm(Mh6hX401qnhX00ZqoXC9qph:hhhKKM5G@)B`G?G?33@GKKKKM KJ"KKKKKKKKKKGM KKKKG?G?:G?zx`GuL`GPbMG0hNe]qq(Mh6hX401qrhX00ZqsXC10qth:hhhKKM6G@,G?G?33@GKKKKM KJ"KKKKKKKKKKGM KKKKG?5?G?!-G?ȷ@G?GquG hNe]qu(Mh6hX401qvhX00ZqwXC11qxh:hhhKKM7G@)=G?G?33@GKKKKM KJ"KKKKKKKKKKGM KKKKG?SG?vG?JGPbMG*6Ga hNe]qy(Mh6hX401qzhX00Zq{XC12q|h:hhhKKM8G@(k G?G?33@GKKKKM KJ"KKKKKKKKKKGM KKKKG?Q G?G?t`GxtG?|C,G2hNe]q}(Mh6hX401q~hX00ZqXC13qh:hhhKKM9G@&`G?G?33@GKKKKM KJ"KKKKKKKKKKGM KKKKG?G?=G?-`GQ G?OGhNe]q(Mh6hX401qhX00ZqXC14qh:hhhKKM:G@$ =G?G?33@GKKKKM KJ"KKKKKKKKKKGM KKKKG?@G?c G?GG?HGD hNe]q(Mh6hX401qhX00ZqXC15qh:hhhKKM;G@"€G?G?33@GKKKKM KJ"KKKKKKKKKKGM KKKKG?hG?2G?"GD G?vG2ahNe]q(Mh6hX401qhX00ZqXC16qh:hhhKKM<G@"z@G?G?33@GKKKKM KJ"KKKKKKKKKKGM KKKKG?@G?xG? GG?}@Gs hNe]q(Mh6hX401qhX00ZqXC17qh:hhhKKM=G@"LG?G?33@GKKKKM KJ"KKKKKKKKKKGM KKKKG?G?G?G G?QG`hNe]q(Mh6hX401qhX00ZqXC18qh:hhhKKM>G@"G?G?33@GKKKKM KJ"KKKKKKKKKKGM KKKKG?!-G?4G?QGnG?OG{hNe]q(Mh6hX401qhX00ZqXC19qh:hhhKKM?G@#(G?G?33@GKKKKM KJ"KKKKKKKKKKGM KKKKG?حG?aG?GN@G?hrG@hNe]q(Mh6hX401qhX00ZqXC20qh:hhhKKM@G@#B`G?G?33@GKKKKM KJ"KKKKKKKKKKGM KKKKG?G?G?`GɆG?FsG hNeeKK]q(]q(]q(G@EG@S$G@U3@e]q(G@VG@VG@VeeX P 21 21 21qeKJM NNehe]q(X3tzmqKKNK]q(]q(KX3tzmqKJo]q(GGGe]q(GGGeKKNKK]q(GGGGGGGGGGGGGGGGeKNeKKK]q]q(KK]q]qNh]q]q(G5 GX^G?]Gֿ5ZGXҁ@G?GUeAG?kvx(G]GU`G5G?+,GGGG?eaNN]q]q(X pdb_headerqKXY|HEADER TRANSFERASE/TRANSFERASE INHIBITOR 27-SEP-11 3TZM TITLE TGF-BETA RECEPTOR TYPE 1 IN COMPLEX WITH SB431542 COMPND MOL_ID: 1; COMPND 2 MOLECULE: TGF-BETA RECEPTOR TYPE-1; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: KINASE DOMAIN, UNP RESIDUES 200-503; COMPND 5 SYNONYM: TGFR-1, ACTIVIN A RECEPTOR TYPE II-LIKE PROTEIN KINASE OF COMPND 6 53KD, ACTIVIN RECEPTOR-LIKE KINASE 5, ALK-5, ALK5, SERINE/THREONINE- COMPND 7 PROTEIN KINASE RECEPTOR R4, SKR4, TGF-BETA TYPE I RECEPTOR, COMPND 8 TRANSFORMING GROWTH FACTOR-BETA RECEPTOR TYPE I, TGF-BETA RECEPTOR COMPND 9 TYPE I, TBETAR-I; COMPND 10 EC: 2.7.11.30; COMPND 11 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: TGFBR1, ALK5, SKR4; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC KEYWDS ALK5, SB431542, KINASE DOMAIN, TRANSFERASE-TRANSFERASE INHIBITOR KEYWDS 2 COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR A.A.OGUNJIMI,E.ZEQIRAJ,D.F.CECCARELLI,F.SICHERI REVDAT 2 13-SEP-23 3TZM 1 REMARK SEQADV REVDAT 1 23-MAY-12 3TZM 0 JRNL AUTH A.A.OGUNJIMI,E.ZEQIRAJ,D.F.CECCARELLI,F.SICHERI,J.L.WRANA, JRNL AUTH 2 L.DAVID JRNL TITL STRUCTURAL BASIS FOR SPECIFICITY OF TGFBETA FAMILY RECEPTOR JRNL TITL 2 SMALL MOLECULE INHIBITORS JRNL REF CELL SIGNAL V. 24 476 2012 JRNL REFN ISSN 0898-6568 JRNL PMID 21983015 JRNL DOI 10.1016/J.CELLSIG.2011.09.027 REMARK 2 REMARK 2 RESOLUTION. 1.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.5.0109 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.45 REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 96.8 REMARK 3 NUMBER OF REFLECTIONS : 30296 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) : 0.172 REMARK 3 R VALUE (WORKING SET) : 0.170 REMARK 3 FREE R VALUE : 0.205 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 1616 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) : 1.70 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.75 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2255 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.37 REMARK 3 BIN R VALUE (WORKING SET) : 0.2170 REMARK 3 BIN FREE R VALUE SET COUNT : 129 REMARK 3 BIN FREE R VALUE : 0.2490 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2368 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 29 REMARK 3 SOLVENT ATOMS : 158 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.32 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.87000 REMARK 3 B22 (A**2) : 0.82000 REMARK 3 B33 (A**2) : 0.05000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.104 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.060 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.948 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.947 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2454 ; 0.009 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3316 ; 1.232 ; 1.957 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 295 ; 5.876 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 112 ;31.326 ;22.768 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 439 ;14.135 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 23 ;13.260 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 358 ; 0.094 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1845 ; 0.005 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1465 ; 0.955 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2359 ; 1.708 ; 2.000 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 989 ; 2.621 ; 3.000 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 956 ; 4.143 ; 4.500 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): 2454 ; 1.224 ; 3.000 REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.40 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 3TZM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-OCT-11. REMARK 100 THE DEPOSITION ID IS D_1000068119. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 29-JUN-07 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 24-ID-C REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97949 REMARK 200 MONOCHROMATOR : CRYO-SI REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31955 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.8 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8 REMARK 200 DATA REDUNDANCY IN SHELL : 5.60 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.38300 REMARK 200 FOR SHELL : 5.400 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: 1PY5 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 40.73 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM IMIDAZOLE 10% PEG 8000, PH 8.0, REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 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 20.88550 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.03500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.86300 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 45.03500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.88550 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.86300 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: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A 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 195 REMARK 465 ALA A 196 REMARK 465 MET A 197 REMARK 465 GLY A 198 REMARK 465 SER A 199 REMARK 465 ASN A 370 REMARK 465 HIS A 371 REMARK 465 GLN A 497 REMARK 465 GLN A 498 REMARK 465 GLU A 499 REMARK 465 GLY A 500 REMARK 465 ILE A 501 REMARK 465 LYS A 502 REMARK 465 MET A 503 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 ILE A 201 -84.89 -101.77 REMARK 500 GLN A 324 64.23 -106.65 REMARK 500 ARG A 332 -5.96 80.10 REMARK 500 ASP A 333 44.67 -152.68 REMARK 500 ALA A 350 -169.81 -122.58 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 085 A 1 DBREF 3TZM A 200 503 UNP P36897 TGFR1_HUMAN 200 503 SEQADV 3TZM GLY A 195 UNP P36897 EXPRESSION TAG SEQADV 3TZM ALA A 196 UNP P36897 EXPRESSION TAG SEQADV 3TZM MET A 197 UNP P36897 EXPRESSION TAG SEQADV 3TZM GLY A 198 UNP P36897 EXPRESSION TAG SEQADV 3TZM SER A 199 UNP P36897 EXPRESSION TAG SEQRES 1 A 309 GLY ALA MET GLY SER THR ILE ALA ARG THR ILE VAL LEU SEQRES 2 A 309 GLN GLU SER ILE GLY LYS GLY ARG PHE GLY GLU VAL TRP SEQRES 3 A 309 ARG GLY LYS TRP ARG GLY GLU GLU VAL ALA VAL LYS ILE SEQRES 4 A 309 PHE SER SER ARG GLU GLU ARG SER TRP PHE ARG GLU ALA SEQRES 5 A 309 GLU ILE TYR GLN THR VAL MET LEU ARG HIS GLU ASN ILE SEQRES 6 A 309 LEU GLY PHE ILE ALA ALA ASP ASN LYS ASP ASN GLY THR SEQRES 7 A 309 TRP THR GLN LEU TRP LEU VAL SER ASP TYR HIS GLU HIS SEQRES 8 A 309 GLY SER LEU PHE ASP TYR LEU ASN ARG TYR THR VAL THR SEQRES 9 A 309 VAL GLU GLY MET ILE LYS LEU ALA LEU SER THR ALA SER SEQRES 10 A 309 GLY LEU ALA HIS LEU HIS MET GLU ILE VAL GLY THR GLN SEQRES 11 A 309 GLY LYS PRO ALA ILE ALA HIS ARG ASP LEU LYS SER LYS SEQRES 12 A 309 ASN ILE LEU VAL LYS LYS ASN GLY THR CYS CYS ILE ALA SEQRES 13 A 309 ASP LEU GLY LEU ALA VAL ARG HIS ASP SER ALA THR ASP SEQRES 14 A 309 THR ILE ASP ILE ALA PRO ASN HIS ARG VAL GLY THR LYS SEQRES 15 A 309 ARG TYR MET ALA PRO GLU VAL LEU ASP ASP SER ILE ASN SEQRES 16 A 309 MET LYS HIS PHE GLU SER PHE LYS ARG ALA ASP ILE TYR SEQRES 17 A 309 ALA MET GLY LEU VAL PHE TRP GLU ILE ALA ARG ARG CYS SEQRES 18 A 309 SER ILE GLY GLY ILE HIS GLU ASP TYR GLN LEU PRO TYR SEQRES 19 A 309 TYR ASP LEU VAL PRO SER ASP PRO SER VAL GLU GLU MET SEQRES 20 A 309 ARG LYS VAL VAL CYS GLU GLN LYS LEU ARG PRO ASN ILE SEQRES 21 A 309 PRO ASN ARG TRP GLN SER CYS GLU ALA LEU ARG VAL MET SEQRES 22 A 309 ALA LYS ILE MET ARG GLU CYS TRP TYR ALA ASN GLY ALA SEQRES 23 A 309 ALA ARG LEU THR ALA LEU ARG ILE LYS LYS THR LEU SER SEQRES 24 A 309 GLN LEU SER GLN GLN GLU GLY ILE LYS MET HET 085 A 1 29 HETNAM 085 4-[5-(1,3-BENZODIOXOL-5-YL)-4-(PYRIDIN-2-YL)-1H- HETNAM 2 085 IMIDAZOL-2-YL]BENZAMIDE HETSYN 085 SB431542 FORMUL 2 085 C22 H16 N4 O3 FORMUL 3 HOH *158(H2 O) HELIX 1 1 ILE A 201 ARG A 203 5 3 HELIX 2 2 SER A 235 ARG A 237 5 3 HELIX 3 3 GLU A 238 GLN A 250 1 13 HELIX 4 4 SER A 287 TYR A 295 1 9 HELIX 5 5 THR A 298 MET A 318 1 21 HELIX 6 6 LYS A 335 LYS A 337 5 3 HELIX 7 7 THR A 375 MET A 379 5 5 HELIX 8 8 ALA A 380 ASP A 385 1 6 HELIX 9 9 HIS A 392 ARG A 414 1 23 HELIX 10 10 SER A 437 CYS A 446 1 10 HELIX 11 11 PRO A 455 SER A 460 5 6 HELIX 12 12 CYS A 461 TRP A 475 1 15 HELIX 13 13 ASN A 478 ARG A 482 5 5 HELIX 14 14 THR A 484 SER A 496 1 13 SHEET 1 A 5 ILE A 205 LYS A 213 0 SHEET 2 A 5 GLU A 218 TRP A 224 -1 O VAL A 219 N GLY A 212 SHEET 3 A 5 GLU A 227 PHE A 234 -1 O VAL A 229 N GLY A 222 SHEET 4 A 5 THR A 274 ASP A 281 -1 O LEU A 278 N LYS A 232 SHEET 5 A 5 PHE A 262 ASP A 269 -1 N LYS A 268 O GLN A 275 SHEET 1 B 3 ILE A 329 ALA A 330 0 SHEET 2 B 3 VAL A 356 ASP A 359 -1 O VAL A 356 N ALA A 330 SHEET 3 B 3 THR A 364 ILE A 365 -1 O THR A 364 N ASP A 359 SHEET 1 C 2 ILE A 339 VAL A 341 0 SHEET 2 C 2 CYS A 347 ILE A 349 -1 O CYS A 348 N LEU A 340 SITE 1 AC1 17 HOH A 2 HOH A 46 HOH A 47 HOH A 153 SITE 2 AC1 17 ILE A 211 GLY A 214 ALA A 230 LYS A 232 SITE 3 AC1 17 LEU A 278 SER A 280 ASP A 281 TYR A 282 SITE 4 AC1 17 HIS A 283 LYS A 335 LYS A 337 LEU A 340 SITE 5 AC1 17 ASP A 351 CRYST1 41.771 77.726 90.070 90.00 90.00 90.00 P 21 21 21 4 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 0.023940 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012866 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011102 0.00000 qeaNN]q(]q(]q(G@D G@SnvG@Vze]q(G@VG@VG@VeeX P 21 21 21qeeaN]q]qKK]q(]q(]q(G@D G@SnvG@Vze]q(G@VG@VG@VeeX P 21 21 21qeKJM NNehe]q(X_align1qKKNJ]qhe]q(X_align2qKKNJ]qhe]q(Xlig42qKKNK]q(]q(KXlig42qKJo]q(GGGe]q(GGGeKKNKK]q(GGGGGGGGGGGGGGGGeKNeKK!K]q]q(KK]q(G 2 G@)G@G!G@(@G`GG@G@)G KGG@&OGFG ߕG@IG%G@G@#G'f@G @G@ ^`G#G`@GG@$$BG$ϠGG@!YG nG/G@ n@GG LG@![GG%9G@ǀGRG G@ #`G* G@G@!oR@G'G(`G@"<G"G=@G@!h`G@GG@&V@GGG@HpGIG@G@ GkGG@ЍG+<G G@'w`G xGdG@!nGwG5 G@$j@G:GG@!N' G,G @G@ӀGGG@@GG@G@#qGU@G@G@"@GG?G?L`G}G?pbMhNe]q(Kh6hhhX085qXCAErh:hhhKKKG@(G?G?33@GKKKKM` KJ"KKKKKKKMKKGM^ KKKKG?aG?_G?=pGGG?dhNe]r(Kh6hhhX085rXCAFrh:hhhKKKG@&33@G?G?33@GKKKKM] KJ"KKKKKKKMKKGM[ KKKKG?G?¶G?@G?[Q GbMGVhNe]r(Kh6hhhX085rXCAGrh:hhhKKKG@2LG?G?33@GKKKKMU KJ"KKKKKKKMKKGMS KKKKG?:G?G?_G}@Ge+G?>@hNe]r(Kh6hhhX085rXCAHr h:hhhKKKG@3nG?G?33@GKKKKMS KJ"KKKKKKKMKKGMQ KKKKG?`G?ҧG?!-GkPGVG?׀hNe]r (Kh6hhhX085r XCAIr h:hhhKKKG@1EG?G?33@GKKKKMT KJ"KKKKKKKMKKGMR KKKKG?/`G?G?ϠGC,G@bMG?``hNe]r (Kh6hhhX085rXCAJrh:hhhKKKG@2G?G?33@GKKKKMR KJ"KKKKKKKMKKGMP KKKKG?A@G?ѽ G?zG`@Gv+G?hNe]r(Kh6hhhX085rXCAKrh:hhhKKKG@(f`G?G?33@GKKKKML KJ"KKKKKKKMKKGMJ KKKKG?\)G?3G?¦L G׀G{Grs hNe]r(Kh6hhhX085rXCALrh:hhhKKKG@(G?G?33@GKKKKMK KJ"KKKKKKKMKKGMI KKKKG? `G?Ǘ$G?@NG`@G:G? hNe]r(Kh6hhhX085rXCAMrh:hhhKKKG@+8QG?G?33@GKKKKME KJ"KKKKKKKMKKGMC KKKKG?G?.@G?j Ga| GG?Q hNe]r(Kh6hhhX085rXCANrh:hhhKKKG@.3@G?G?33@GKKKKMH KJ"KKKKKKKMKKGMF KKKKG?G?@G? ԠGGQGhthNe]r(Kh6hhhX085rXCATrh:hhhKKKG@6`G?G?33@GKKKKMW KJ"KKKKKKKMKKGMU KKKKG?ҸQG?4G?˶EGt`G G?kPhNe]r(Kh6hhhX085r XCAUr!h:hhhKKKG@3)G?G?33@GKKKKMV KJ"KKKKKKKMKKGMT KKKKG?ЎG?G?|G{Q GOG? hNe]r"(Kh6hhhX085r#XCAVr$h:hhhKKKG@0`G?G?33@GKKKKMQ KJ"KKKKKKKMKKGMO KKKKG?ȪdG?2`G?S& GϪGG?(hNe]r%(Kh6hhhX085r&XCAWr'h:hhhKKKG@(@G?G?33@GKKKKMM KJ"KKKKKKKMKKGMK KKKKG?$ G?TɀG?=G`G_G?s hNe]r((Kh6hhhX085r)XCAXr*h:hhhKKKG@(zG?G?33@GKKKKM\ KJ"KKKKKKKMKKGMZ KKKKG?iG?ϪG?s G?GkQ G?hNe]r+(Kh6hhhX085r,XCAYr-h:hhhKKKG@*QG?G?33@GKKKKMJ KJ"KKKKKKKMKKGMH KKKKG?nG?P@G?ńMGvG[W@G?FhNe]r.(Kh6hhhX085r/XCAZr0h:hhhKKKG@+G?G?33@GKKKKMF KJ"KKKKKKKMKKGMD KKKKG?)ǀG?c G?ċCGWG,@G? hNe]r1(Kh6hhhX085r2XNAAr3h?hhhKKKG@6:@G?G?GKKKKMY KJ"KKKKKKKMKKGMW KKKKG? G?֤G?䎀GvG,<G?ihNe]r4(Kh6hhhX085r5XNAOr6h?hhhKKKG@+\)G?G?GKKKKMa KJ"KKKKKKKMKKGM_ KKKKG?_ؠG?G?0GfG?*@G? hNe]r7(Kh6hhhX085r8XNAPr9h?hhhKKKG@)`G?G?GKKKKMO KJ"KKKKKKKMKKGMM KKKKG?¹`G? G?.HG?,@G:)G?8`hNe]r:(Kh6hhhX085r;XNAQr<h?hhhKKKG@))G?G?GKKKKMZ KJ"KKKKKKKMKKGMX KKKKG?`G?G?,@GUL`G?UL`G?Ov`hNe]r=(Kh6hhhX085r>XOABr?hDhhhKKKG@7޸`G?G?QGKKKKMX KJ"KKKKKKKMKKGMV KKKKG?yG?և+G?t`G?bs GiG?e+hNe]r@(Kh6hhhX085rAXOARrBhDhhhKKKG@,G?G?QGKKKKMI KJ"KKKKKKKMKKGMG KKKKG?~G?ᰀG?1G/GWG~Ov`hNe]rC(Kh6hhhX085rDXOASrEhDhhhKKKG@/LG?G?QGKKKKMG KJ"KKKKKKKMKKGME KKKKG?*G?8`G?ěG׀GA `Go!-hNe]rF(Kh6hhhX085rGXCBArHh:hhhKKKG@+\ G?G?33@GKKKKMP KJ"KKKKKKKMKKGMN KKKKG?Ŀ`G?G?"hG*@GvG?P@hNe]rI(Kh6hhhX085rJXCBBrKh:hhhKKKG@(\ G?G?33@GKKKKMN KJ"KKKKKKKMKKGML KKKKG? kG?ȷ@G?G-G4G?ɆhNe]rL(Kh6hhhX085rMXCBCrNh:hhhKKKG@)G?G?33@GKKKKM[ KJ"KKKKKKKMKKGMY KKKKG?³gG?NJ G?G?s@NGp)`G?hNeeKK]rO(]rP(]rQ(G@D G@SnvG@Vze]rR(G@VG@VG@VeeX P 21 21 21rSeKJMb NNehe]rT(X 3tzm_cartoonrUKKNK]rV(]rW(KX 3tzm_cartoonrXKJo]rY(GGGe]rZ(GGGeKKNKK]r[(GGGGGGGGGGGGGGGGeKNeKKM(]r\]r](M(M(]r^(G*`G@7 G@@G'G@5G@G!΁G@6) G@ 7ڀG l G@9@ G@`GJ@G@6G@!AGG@4=wG@s@GroG@4pLG@G?UG@3[G@ fG@ HG@0ɠG@ @G@@G@.րG?G@mG@.a|@GQG@ $G@'aG 3G@G@($~GqG?G@+ G$`G]G@)[G&IG@G@*z@G.% G1G@0 G+ G NG@2)@G$G͠G@1% GԖ@G3G@-eG! GG@.;@G(KG G@*@G?Gp`G@/D0G@@GcL@G@/G@(@GG@0L`G@!5GFvG@0LHG@(qG8 G@,RG@*`GG@'EHG@$ G #ʀG@%G@G@G@( pG@CGpG@(G?vDGCG@/e΀GG5`G@0OĠGc GCG@3BGGQ{@G@5G"aFG+G@98G$֣GB@@G@;f@G&GG@:``G.@G  G@7F`G,G&~`G@8G)v@G*7G@6`G.G& G@2@G,\@G& G@2>G,G'`G@3nG%xlG.x@G@4%G%G0 G@1ΠG) G,G-@G@-N@G%@G/G@0hGg G3*G@/ĸG"G2G@([A@G#lG1fG@'YG@`G4$G@*؀G+b@G6G@%ເG G9VG@#`GNG8G@,`G @G5t G@Gl@G3TG@G\{G2dG?*+@GG.G=^G?`G+ՠG蛄G tG,tG@G`G'1 G@ڀGKG*nG@)GG,G@%GBG+G@*G?G,G@0aG?ɨG+Z G@3.GVG)~G@6@G[G%G@9 G2 Gr@G@;"@GI G]z@G@>/`GG@G@? G?rlGԀG@Ap GV4GӲG@AjI`G G @G@@Gy7@G"@G@=~GV GG@:.G `G!G@7?@GYG!VG@4G IG$EG@1 G G#(G@.GpG#@G@&G0G!i`G@!G@8GgUG@GG@Q7G QG@0 G?\G0G@ @G@}G?oG?5M@GdGnG@ %GtG@UG@4G GˀGA@G G?vGMG$!}`G@ tG?7GG@ȩG@GqG@8GGc@G@G9@G!RG@G.GG@GGX`G@@G%uGG?|G(UG\@G/ G.jGGǀG1:GGG/ GG G(GG눠G(@GӀGjG*cGݠG G%XGGrG _GZo`G! G"z@G G(z`G#_G,G(C@GؠG^PG& @G`G V)@G,~zGߠG#G0GGdG/UG;GG0@0GG%SG3dGPG%7G4̠GɀG EG3@G?2G%G5k<G%`G*OG8G G&`G;|G?G'@G=V G?}G 'G@@G@,G! @GAs&`G@^GGA@G@;/G{G?G@G G>ڠG@GG;Fq G@G DG:dG@G'ҾG8-G@ G+z] G5"G@X̠G,lcG2ZG@x*G0G-G@G/jG**. 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