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HEADER TRANSFERASE/TRANSFERASE INHIBITOR 08-MAR-17 5V41
TITLE CRYSTAL STRUCTURE OF MTB PKS13 THIOESTERASE DOMAIN IN COMPLEX WITH
TITLE 2 INHIBITOR TAM5
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYKETIDE SYNTHASE PKS13 (TERMINATION POLYKETIDE
COMPND 3 SYNTHASE);
COMPND 4 CHAIN: A, B;
COMPND 5 FRAGMENT: THIOESTERASE DOMAIN (UNP RESIDUES 113-395);
COMPND 6 EC: 2.7.7.-;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 GENE: PKS, ERS027654_02263;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS THIOESTERASE DOMAIN, TAM5 COMPLEX, PKS13, MYCOBACTERIUM, POLYKETIDE
KEYWDS 2 SYNTHASE, MYCOLIC ACID CONDENSATION, TB STRUCTURAL GENOMICS
KEYWDS 3 CONSORTIUM, TBSGC, ALPHA/BETA HYDROLASE, THIOESTERASE, TRANSFERASE-
KEYWDS 4 TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.AGGARWAL,J.C.SACCHETTINI
REVDAT 1 05-JUL-17 5V41 0
JRNL AUTH A.AGGARWAL,M.K.PARAI,N.SHETTY,D.WALLIS,L.WOOLHISER,
JRNL AUTH 2 C.HASTINGS,N.K.DUTTA,S.GALAVIZ,R.C.DHAKAL,R.SHRESTHA,
JRNL AUTH 3 S.WAKABAYASHI,C.WALPOLE,D.MATTHEWS,D.FLOYD,P.SCULLION,
JRNL AUTH 4 J.RILEY,O.EPEMOLU,S.NORVAL,T.SNAVELY,G.T.ROBERTSON,
JRNL AUTH 5 E.J.RUBIN,T.R.IOERGER,F.A.SIRGEL,R.MERWE,P.HELDEN,P.KELLER,
JRNL AUTH 6 E.C.BOTTGER,P.C.KARAKOUSIS,A.J.LENAERTS,J.C.SACCHETTINI
JRNL TITL DEVELOPMENT OF A NOVEL LEAD THAT TARGETS M. TUBERCULOSIS
JRNL TITL 2 POLYKETIDE SYNTHASE 13.
JRNL REF CELL(CAMBRIDGE,MASS.) 2017
JRNL REFN ISSN 0092-8674
JRNL DOI 10.1016/J.CELL.2017.06.025
REMARK 2
REMARK 2 RESOLUTION. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.20
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.7
REMARK 3 NUMBER OF REFLECTIONS : 33653
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 1702
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 48.2118 - 4.6943 0.98 2957 169 0.1753 0.1878
REMARK 3 2 4.6943 - 3.7264 0.98 2815 176 0.1607 0.1924
REMARK 3 3 3.7264 - 3.2555 0.86 2486 124 0.1825 0.2499
REMARK 3 4 3.2555 - 2.9579 1.00 2819 165 0.2059 0.2550
REMARK 3 5 2.9579 - 2.7459 1.00 2833 143 0.2187 0.2754
REMARK 3 6 2.7459 - 2.5840 1.00 2829 142 0.2226 0.2777
REMARK 3 7 2.5840 - 2.4546 1.00 2845 130 0.2120 0.2754
REMARK 3 8 2.4546 - 2.3478 1.00 2797 139 0.2201 0.2501
REMARK 3 9 2.3478 - 2.2574 0.82 2314 132 0.2457 0.3323
REMARK 3 10 2.2574 - 2.1795 0.70 1964 98 0.3547 0.3828
REMARK 3 11 2.1795 - 2.1113 0.99 2744 152 0.2412 0.2846
REMARK 3 12 2.1113 - 2.0510 0.91 2548 132 0.2787 0.3483
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.110
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.18
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.005 4259
REMARK 3 ANGLE : 0.882 5791
REMARK 3 CHIRALITY : 0.034 626
REMARK 3 PLANARITY : 0.004 768
REMARK 3 DIHEDRAL : 13.764 1546
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 11
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1453 THROUGH 1548 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.8589 28.9284 24.5159
REMARK 3 T TENSOR
REMARK 3 T11: 0.1701 T22: 0.1582
REMARK 3 T33: 0.1181 T12: -0.0043
REMARK 3 T13: -0.0214 T23: -0.0138
REMARK 3 L TENSOR
REMARK 3 L11: 1.4305 L22: 1.4546
REMARK 3 L33: 3.0511 L12: -0.1286
REMARK 3 L13: -0.5719 L23: -0.3445
REMARK 3 S TENSOR
REMARK 3 S11: 0.0273 S12: -0.0635 S13: -0.0274
REMARK 3 S21: 0.1939 S22: 0.0197 S23: -0.0051
REMARK 3 S31: 0.2480 S32: -0.0455 S33: -0.0228
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1549 THROUGH 1571 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.1298 38.5573 19.0168
REMARK 3 T TENSOR
REMARK 3 T11: 0.2431 T22: 0.1811
REMARK 3 T33: 0.2494 T12: 0.0079
REMARK 3 T13: -0.0019 T23: 0.0051
REMARK 3 L TENSOR
REMARK 3 L11: 1.6652 L22: 1.2547
REMARK 3 L33: 0.7813 L12: 0.2318
REMARK 3 L13: -0.6626 L23: 0.1648
REMARK 3 S TENSOR
REMARK 3 S11: 0.0705 S12: 0.0102 S13: 0.3128
REMARK 3 S21: 0.0459 S22: 0.0846 S23: 0.1421
REMARK 3 S31: -0.0038 S32: -0.0139 S33: -0.0756
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1572 THROUGH 1590 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.3137 25.7036 3.1395
REMARK 3 T TENSOR
REMARK 3 T11: 0.2351 T22: 0.2773
REMARK 3 T33: 0.3334 T12: 0.0151
REMARK 3 T13: -0.0394 T23: -0.0508
REMARK 3 L TENSOR
REMARK 3 L11: 3.5650 L22: 4.1169
REMARK 3 L33: 4.9399 L12: -0.4591
REMARK 3 L13: -0.6507 L23: 1.3844
REMARK 3 S TENSOR
REMARK 3 S11: -0.0584 S12: 0.1596 S13: 0.2072
REMARK 3 S21: -0.2525 S22: 0.1008 S23: 0.1519
REMARK 3 S31: 0.0372 S32: 0.2147 S33: 0.0079
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1591 THROUGH 1626 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.8744 17.3619 10.3710
REMARK 3 T TENSOR
REMARK 3 T11: 0.3667 T22: 0.3736
REMARK 3 T33: 0.5167 T12: -0.0631
REMARK 3 T13: 0.0069 T23: -0.0684
REMARK 3 L TENSOR
REMARK 3 L11: 0.9740 L22: 1.2671
REMARK 3 L33: 0.6663 L12: -0.4791
REMARK 3 L13: -0.7287 L23: 0.3349
REMARK 3 S TENSOR
REMARK 3 S11: -0.0748 S12: 0.0509 S13: -0.4162
REMARK 3 S21: -0.2675 S22: -0.0102 S23: 0.2891
REMARK 3 S31: 0.0286 S32: -0.0226 S33: 0.1128
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1627 THROUGH 1644 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.9784 21.1090 12.3710
REMARK 3 T TENSOR
REMARK 3 T11: 0.2034 T22: 0.2334
REMARK 3 T33: 0.2729 T12: -0.0278
REMARK 3 T13: -0.0344 T23: -0.0342
REMARK 3 L TENSOR
REMARK 3 L11: 1.5011 L22: 5.9180
REMARK 3 L33: 1.4019 L12: -0.5289
REMARK 3 L13: -0.2336 L23: 0.8935
REMARK 3 S TENSOR
REMARK 3 S11: 0.0261 S12: 0.1172 S13: -0.3090
REMARK 3 S21: 0.2266 S22: -0.1837 S23: 0.0964
REMARK 3 S31: 0.1565 S32: -0.0066 S33: 0.1400
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1645 THROUGH 1689 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.8690 39.8856 11.6979
REMARK 3 T TENSOR
REMARK 3 T11: 0.1512 T22: 0.2037
REMARK 3 T33: 0.2187 T12: 0.0313
REMARK 3 T13: 0.0064 T23: 0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 2.5089 L22: 1.9638
REMARK 3 L33: 1.9868 L12: 0.5666
REMARK 3 L13: 1.5066 L23: -1.0671
REMARK 3 S TENSOR
REMARK 3 S11: -0.0934 S12: 0.1384 S13: 0.3249
REMARK 3 S21: -0.0881 S22: 0.0014 S23: 0.1675
REMARK 3 S31: -0.1305 S32: -0.0832 S33: 0.0680
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1690 THROUGH 1706 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.0656 36.4559 7.2401
REMARK 3 T TENSOR
REMARK 3 T11: 0.2525 T22: 0.2418
REMARK 3 T33: 0.1946 T12: 0.0124
REMARK 3 T13: 0.0030 T23: 0.0363
REMARK 3 L TENSOR
REMARK 3 L11: 2.4792 L22: 2.0188
REMARK 3 L33: 1.0451 L12: -1.0736
REMARK 3 L13: -0.8488 L23: -0.4264
REMARK 3 S TENSOR
REMARK 3 S11: -0.0233 S12: 0.2930 S13: 0.0329
REMARK 3 S21: -0.2258 S22: -0.0159 S23: -0.1679
REMARK 3 S31: 0.2546 S32: 0.0868 S33: 0.0503
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1707 THROUGH 1727 )
REMARK 3 ORIGIN FOR THE GROUP (A): 29.7770 39.9980 19.4557
REMARK 3 T TENSOR
REMARK 3 T11: 0.2025 T22: 0.1968
REMARK 3 T33: 0.2681 T12: -0.0322
REMARK 3 T13: -0.0367 T23: 0.0332
REMARK 3 L TENSOR
REMARK 3 L11: 2.8372 L22: 2.5439
REMARK 3 L33: 3.7964 L12: 0.6944
REMARK 3 L13: 1.5035 L23: 0.8755
REMARK 3 S TENSOR
REMARK 3 S11: -0.1527 S12: 0.0357 S13: 0.3848
REMARK 3 S21: 0.0449 S22: -0.0617 S23: 0.0107
REMARK 3 S31: -0.5234 S32: 0.4768 S33: 0.2304
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1452 THROUGH 1571 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.2584 66.8620 5.3890
REMARK 3 T TENSOR
REMARK 3 T11: 0.1578 T22: 0.1651
REMARK 3 T33: 0.2209 T12: 0.0030
REMARK 3 T13: 0.0089 T23: -0.0024
REMARK 3 L TENSOR
REMARK 3 L11: 1.5569 L22: 2.4156
REMARK 3 L33: 2.3199 L12: -0.2585
REMARK 3 L13: -0.5055 L23: -0.0991
REMARK 3 S TENSOR
REMARK 3 S11: 0.0002 S12: 0.0338 S13: 0.1967
REMARK 3 S21: -0.0839 S22: 0.0426 S23: -0.3202
REMARK 3 S31: -0.0636 S32: 0.2169 S33: -0.0376
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1572 THROUGH 1644 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.4802 70.4401 -14.7547
REMARK 3 T TENSOR
REMARK 3 T11: 0.3287 T22: 0.3449
REMARK 3 T33: 0.3484 T12: -0.1205
REMARK 3 T13: -0.0569 T23: 0.0899
REMARK 3 L TENSOR
REMARK 3 L11: 1.6307 L22: 2.1577
REMARK 3 L33: 2.4519 L12: -0.2074
REMARK 3 L13: 0.9132 L23: 0.6730
REMARK 3 S TENSOR
REMARK 3 S11: 0.0844 S12: 0.1152 S13: -0.1374
REMARK 3 S21: -0.2388 S22: 0.2413 S23: 0.4415
REMARK 3 S31: 0.4887 S32: -0.5217 S33: -0.2284
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1645 THROUGH 1726 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.9754 56.4346 7.5987
REMARK 3 T TENSOR
REMARK 3 T11: 0.2604 T22: 0.1776
REMARK 3 T33: 0.2185 T12: 0.0360
REMARK 3 T13: 0.0183 T23: 0.0154
REMARK 3 L TENSOR
REMARK 3 L11: 1.5566 L22: 2.9180
REMARK 3 L33: 2.1718 L12: 0.7269
REMARK 3 L13: 0.3994 L23: -0.0503
REMARK 3 S TENSOR
REMARK 3 S11: 0.0815 S12: 0.0598 S13: -0.1189
REMARK 3 S21: -0.1600 S22: 0.0821 S23: 0.0715
REMARK 3 S31: 0.2595 S32: 0.0019 S33: -0.1254
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN B
REMARK 3 ATOM PAIRS NUMBER : 2366
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5V41 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-MAR-17.
REMARK 100 THE DEPOSITION ID IS D_1000226800.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-APR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0075
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33859
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.7
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : 0.15000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 5.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.09
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.30
REMARK 200 R MERGE FOR SHELL (I) : 0.98100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: PDB ENTRY 5V3W
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS-HCL, 2.0-1.8 M AMMONIUM
REMARK 280 SULFATE, 2%-5% V/V PPG P400, PH 8.5, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 290K
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 44.45300
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.86250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 44.45300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.86250
REMARK 290 SMTRY3 4 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: MONOMERIC
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER A 1448
REMARK 465 ASN A 1449
REMARK 465 ALA A 1450
REMARK 465 GLN A 1451
REMARK 465 ILE A 1452
REMARK 465 THR A 1593
REMARK 465 ILE A 1594
REMARK 465 GLY A 1622
REMARK 465 SER A 1728
REMARK 465 GLU A 1729
REMARK 465 VAL A 1730
REMARK 465 GLY A 1731
REMARK 465 LYS A 1732
REMARK 465 GLN A 1733
REMARK 465 SER B 1448
REMARK 465 ASN B 1449
REMARK 465 ALA B 1450
REMARK 465 GLN B 1451
REMARK 465 PHE B 1590
REMARK 465 ASN B 1591
REMARK 465 VAL B 1592
REMARK 465 THR B 1727
REMARK 465 SER B 1728
REMARK 465 GLU B 1729
REMARK 465 VAL B 1730
REMARK 465 GLY B 1731
REMARK 465 LYS B 1732
REMARK 465 GLN B 1733
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 ASP A1453 CG OD1 OD2
REMARK 470 GLU A1464 CG CD OE1 OE2
REMARK 470 GLU A1567 CG CD OE1 OE2
REMARK 470 ASN A1591 CG OD1 ND2
REMARK 470 VAL A1592 CG1 CG2
REMARK 470 GLU A1600 CG CD OE1 OE2
REMARK 470 GLU A1604 CG CD OE1 OE2
REMARK 470 GLN A1620 CG CD OE1 NE2
REMARK 470 SER A1621 OG
REMARK 470 VAL A1623 CG1 CG2
REMARK 470 GLN A1624 CG CD OE1 NE2
REMARK 470 THR A1727 OG1 CG2
REMARK 470 ASP B1453 CG OD1 OD2
REMARK 470 GLU B1464 CG CD OE1 OE2
REMARK 470 ASP B1524 CG OD1 OD2
REMARK 470 GLU B1566 CG CD OE1 OE2
REMARK 470 GLU B1567 CG CD OE1 OE2
REMARK 470 LYS B1572 CG CD CE NZ
REMARK 470 GLU B1573 CG CD OE1 OE2
REMARK 470 ARG B1576 CG CD NE CZ NH1 NH2
REMARK 470 LYS B1577 CG CD CE NZ
REMARK 470 TYR B1582 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 PHE B1585 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS B1588 CG CD CE NZ
REMARK 470 THR B1593 OG1 CG2
REMARK 470 ILE B1594 CG1 CG2 CD1
REMARK 470 ILE B1597 CG1 CG2 CD1
REMARK 470 TYR B1599 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU B1600 CG CD OE1 OE2
REMARK 470 GLN B1624 CG CD OE1 NE2
REMARK 470 GLN B1647 CG CD OE1 NE2
REMARK 470 GLN B1649 CG CD OE1 NE2
REMARK 470 ASP B1652 CG OD1 OD2
REMARK 470 MET B1669 CG SD CE
REMARK 470 PHE B1670 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU B1685 CG CD OE1 OE2
REMARK 470 ASP B1725 CG OD1 OD2
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 SER A1533 -131.67 60.44
REMARK 500 GLN A1570 66.67 -101.81
REMARK 500 GLN A1620 97.44 -65.04
REMARK 500 SER B1533 -126.40 57.50
REMARK 500 GLN B1570 67.48 -100.33
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 B1924 DISTANCE = 6.69 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue J24 A 1801
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5V3W RELATED DB: PDB
REMARK 900 RELATED ID: 5V3X RELATED DB: PDB
REMARK 900 RELATED ID: 5V3Y RELATED DB: PDB
REMARK 900 RELATED ID: 5V3Z RELATED DB: PDB
REMARK 900 RELATED ID: 5V40 RELATED DB: PDB
REMARK 900 RELATED ID: 5V42 RELATED DB: PDB
DBREF1 5V41 A 1451 1733 UNP A0A0T9CRX1_MYCTX
DBREF2 5V41 A A0A0T9CRX1 113 395
DBREF1 5V41 B 1451 1733 UNP A0A0T9CRX1_MYCTX
DBREF2 5V41 B A0A0T9CRX1 113 395
SEQADV 5V41 SER A 1448 UNP A0A0T9CRX EXPRESSION TAG
SEQADV 5V41 ASN A 1449 UNP A0A0T9CRX EXPRESSION TAG
SEQADV 5V41 ALA A 1450 UNP A0A0T9CRX EXPRESSION TAG
SEQADV 5V41 SER B 1448 UNP A0A0T9CRX EXPRESSION TAG
SEQADV 5V41 ASN B 1449 UNP A0A0T9CRX EXPRESSION TAG
SEQADV 5V41 ALA B 1450 UNP A0A0T9CRX EXPRESSION TAG
SEQRES 1 A 286 SER ASN ALA GLN ILE ASP GLY PHE VAL ARG THR LEU ARG
SEQRES 2 A 286 ALA ARG PRO GLU ALA GLY GLY LYS VAL PRO VAL PHE VAL
SEQRES 3 A 286 PHE HIS PRO ALA GLY GLY SER THR VAL VAL TYR GLU PRO
SEQRES 4 A 286 LEU LEU GLY ARG LEU PRO ALA ASP THR PRO MET TYR GLY
SEQRES 5 A 286 PHE GLU ARG VAL GLU GLY SER ILE GLU GLU ARG ALA GLN
SEQRES 6 A 286 GLN TYR VAL PRO LYS LEU ILE GLU MET GLN GLY ASP GLY
SEQRES 7 A 286 PRO TYR VAL LEU VAL GLY TRP SER LEU GLY GLY VAL LEU
SEQRES 8 A 286 ALA TYR ALA CYS ALA ILE GLY LEU ARG ARG LEU GLY LYS
SEQRES 9 A 286 ASP VAL ARG PHE VAL GLY LEU ILE ASP ALA VAL ARG ALA
SEQRES 10 A 286 GLY GLU GLU ILE PRO GLN THR LYS GLU GLU ILE ARG LYS
SEQRES 11 A 286 ARG TRP ASP ARG TYR ALA ALA PHE ALA GLU LYS THR PHE
SEQRES 12 A 286 ASN VAL THR ILE PRO ALA ILE PRO TYR GLU GLN LEU GLU
SEQRES 13 A 286 GLU LEU ASP ASP GLU GLY GLN VAL ARG PHE VAL LEU ASP
SEQRES 14 A 286 ALA VAL SER GLN SER GLY VAL GLN ILE PRO ALA GLY ILE
SEQRES 15 A 286 ILE GLU HIS GLN ARG THR SER TYR LEU ASP ASN ARG ALA
SEQRES 16 A 286 ILE ASP THR ALA GLN ILE GLN PRO TYR ASP GLY HIS VAL
SEQRES 17 A 286 THR LEU TYR MET ALA ASP ARG TYR HIS ASP ASP ALA ILE
SEQRES 18 A 286 MET PHE GLU PRO ARG TYR ALA VAL ARG GLN PRO ASP GLY
SEQRES 19 A 286 GLY TRP GLY GLU TYR VAL SER ASP LEU GLU VAL VAL PRO
SEQRES 20 A 286 ILE GLY GLY GLU HIS ILE GLN ALA ILE ASP GLU PRO ILE
SEQRES 21 A 286 ILE ALA LYS VAL GLY GLU HIS MET SER ARG ALA LEU GLY
SEQRES 22 A 286 GLN ILE GLU ALA ASP ARG THR SER GLU VAL GLY LYS GLN
SEQRES 1 B 286 SER ASN ALA GLN ILE ASP GLY PHE VAL ARG THR LEU ARG
SEQRES 2 B 286 ALA ARG PRO GLU ALA GLY GLY LYS VAL PRO VAL PHE VAL
SEQRES 3 B 286 PHE HIS PRO ALA GLY GLY SER THR VAL VAL TYR GLU PRO
SEQRES 4 B 286 LEU LEU GLY ARG LEU PRO ALA ASP THR PRO MET TYR GLY
SEQRES 5 B 286 PHE GLU ARG VAL GLU GLY SER ILE GLU GLU ARG ALA GLN
SEQRES 6 B 286 GLN TYR VAL PRO LYS LEU ILE GLU MET GLN GLY ASP GLY
SEQRES 7 B 286 PRO TYR VAL LEU VAL GLY TRP SER LEU GLY GLY VAL LEU
SEQRES 8 B 286 ALA TYR ALA CYS ALA ILE GLY LEU ARG ARG LEU GLY LYS
SEQRES 9 B 286 ASP VAL ARG PHE VAL GLY LEU ILE ASP ALA VAL ARG ALA
SEQRES 10 B 286 GLY GLU GLU ILE PRO GLN THR LYS GLU GLU ILE ARG LYS
SEQRES 11 B 286 ARG TRP ASP ARG TYR ALA ALA PHE ALA GLU LYS THR PHE
SEQRES 12 B 286 ASN VAL THR ILE PRO ALA ILE PRO TYR GLU GLN LEU GLU
SEQRES 13 B 286 GLU LEU ASP ASP GLU GLY GLN VAL ARG PHE VAL LEU ASP
SEQRES 14 B 286 ALA VAL SER GLN SER GLY VAL GLN ILE PRO ALA GLY ILE
SEQRES 15 B 286 ILE GLU HIS GLN ARG THR SER TYR LEU ASP ASN ARG ALA
SEQRES 16 B 286 ILE ASP THR ALA GLN ILE GLN PRO TYR ASP GLY HIS VAL
SEQRES 17 B 286 THR LEU TYR MET ALA ASP ARG TYR HIS ASP ASP ALA ILE
SEQRES 18 B 286 MET PHE GLU PRO ARG TYR ALA VAL ARG GLN PRO ASP GLY
SEQRES 19 B 286 GLY TRP GLY GLU TYR VAL SER ASP LEU GLU VAL VAL PRO
SEQRES 20 B 286 ILE GLY GLY GLU HIS ILE GLN ALA ILE ASP GLU PRO ILE
SEQRES 21 B 286 ILE ALA LYS VAL GLY GLU HIS MET SER ARG ALA LEU GLY
SEQRES 22 B 286 GLN ILE GLU ALA ASP ARG THR SER GLU VAL GLY LYS GLN
HET J24 A1801 28
HETNAM J24 ETHYL 5-HYDROXY-4-(MORPHOLIN-4-YLMETHYL)-2-PHENYL-1-
HETNAM 2 J24 BENZOFURAN-3-CARBOXYLATE
FORMUL 3 J24 C22 H23 N O5
FORMUL 4 HOH *301(H2 O)
HELIX 1 AA1 SER A 1480 VAL A 1483 5 4
HELIX 2 AA2 TYR A 1484 ARG A 1490 1 7
HELIX 3 AA3 SER A 1506 GLY A 1523 1 18
HELIX 4 AA4 SER A 1533 LEU A 1549 1 17
HELIX 5 AA5 THR A 1571 ASN A 1591 1 21
HELIX 6 AA6 PRO A 1598 LEU A 1605 1 8
HELIX 7 AA7 ASP A 1606 GLN A 1620 1 15
HELIX 8 AA8 PRO A 1626 THR A 1645 1 20
HELIX 9 AA9 HIS A 1664 GLU A 1671 1 8
HELIX 10 AB1 PRO A 1672 VAL A 1676 5 5
HELIX 11 AB2 GLU A 1698 ALA A 1702 5 5
HELIX 12 AB3 PRO A 1706 THR A 1727 1 22
HELIX 13 AB4 SER B 1480 VAL B 1483 5 4
HELIX 14 AB5 TYR B 1484 GLY B 1489 1 6
HELIX 15 AB6 SER B 1506 GLY B 1523 1 18
HELIX 16 AB7 SER B 1533 LEU B 1549 1 17
HELIX 17 AB8 THR B 1571 THR B 1589 1 19
HELIX 18 AB9 PRO B 1598 GLU B 1603 1 6
HELIX 19 AC1 ASP B 1606 GLY B 1622 1 17
HELIX 20 AC2 PRO B 1626 THR B 1645 1 20
HELIX 21 AC3 HIS B 1664 GLU B 1671 1 8
HELIX 22 AC4 PRO B 1672 VAL B 1676 5 5
HELIX 23 AC5 GLU B 1698 ALA B 1702 5 5
HELIX 24 AC6 PRO B 1706 ARG B 1726 1 21
SHEET 1 AA1 7 VAL A1456 ARG A1460 0
SHEET 2 AA1 7 MET A1497 PHE A1500 -1 O GLY A1499 N ARG A1457
SHEET 3 AA1 7 VAL A1471 PHE A1474 1 N VAL A1473 O PHE A1500
SHEET 4 AA1 7 TYR A1527 TRP A1532 1 O VAL A1530 N PHE A1472
SHEET 5 AA1 7 VAL A1553 ILE A1559 1 O GLY A1557 N LEU A1529
SHEET 6 AA1 7 VAL A1655 MET A1659 1 O THR A1656 N VAL A1556
SHEET 7 AA1 7 LEU A1690 PRO A1694 1 O VAL A1693 N LEU A1657
SHEET 1 AA2 7 VAL B1456 ARG B1460 0
SHEET 2 AA2 7 MET B1497 PHE B1500 -1 O GLY B1499 N ARG B1457
SHEET 3 AA2 7 VAL B1471 PHE B1474 1 N VAL B1473 O PHE B1500
SHEET 4 AA2 7 TYR B1527 TRP B1532 1 O VAL B1528 N PHE B1472
SHEET 5 AA2 7 VAL B1553 ILE B1559 1 O GLY B1557 N LEU B1529
SHEET 6 AA2 7 VAL B1655 MET B1659 1 O THR B1656 N LEU B1558
SHEET 7 AA2 7 LEU B1690 PRO B1694 1 O GLU B1691 N LEU B1657
CISPEP 1 GLY A 1525 PRO A 1526 0 3.96
CISPEP 2 GLU A 1705 PRO A 1706 0 0.76
CISPEP 3 GLY B 1525 PRO B 1526 0 5.11
CISPEP 4 GLU B 1705 PRO B 1706 0 0.84
SITE 1 AC1 12 TYR A1582 SER A1636 TYR A1637 ASN A1640
SITE 2 AC1 12 ILE A1643 ASP A1644 TYR A1663 ASP A1666
SITE 3 AC1 12 ALA A1667 PHE A1670 GLU A1671 TYR A1674
CRYST1 88.906 109.725 57.359 90.00 90.00 90.00 P 21 21 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.011248 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009114 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017434 0.00000
TER 2105 THR A1727
TER 4138 ARG B1726
MASTER 503 0 1 24 14 0 3 6 4465 2 28 44
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