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HEADER TRANSFERASE/TRANSFERASE INHIBITOR 08-MAR-17 5V3X
TITLE CRYSTAL STRUCTURE OF MTB PKS13 THIOESTERASE DOMAIN IN COMPLEX WITH
TITLE 2 INHIBITOR TAM1
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, TAM1 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 5V3X 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. 1.94 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) : 1.94
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.59
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.7
REMARK 3 NUMBER OF REFLECTIONS : 39731
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1992
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 34.5918 - 4.6623 0.97 2975 180 0.1884 0.2322
REMARK 3 2 4.6623 - 3.7020 0.97 2822 164 0.1619 0.1950
REMARK 3 3 3.7020 - 3.2344 0.86 2487 136 0.1811 0.2356
REMARK 3 4 3.2344 - 2.9389 1.00 2890 146 0.2003 0.2724
REMARK 3 5 2.9389 - 2.7283 1.00 2873 156 0.2088 0.2725
REMARK 3 6 2.7283 - 2.5675 1.00 2886 133 0.2042 0.2574
REMARK 3 7 2.5675 - 2.4390 1.00 2860 147 0.1919 0.2435
REMARK 3 8 2.4390 - 2.3328 1.00 2829 155 0.1967 0.2564
REMARK 3 9 2.3328 - 2.2430 0.67 1892 88 0.2495 0.2896
REMARK 3 10 2.2430 - 2.1657 0.76 2139 120 0.2681 0.3621
REMARK 3 11 2.1657 - 2.0979 1.00 2855 146 0.2245 0.2607
REMARK 3 12 2.0979 - 2.0380 1.00 2808 148 0.2510 0.3000
REMARK 3 13 2.0380 - 1.9843 1.00 2848 150 0.2465 0.2925
REMARK 3 14 1.9843 - 1.9359 0.91 2575 123 0.3088 0.3247
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) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.050
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.93
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.95
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 : 0.008 4262
REMARK 3 ANGLE : 1.130 5801
REMARK 3 CHIRALITY : 0.048 618
REMARK 3 PLANARITY : 0.006 771
REMARK 3 DIHEDRAL : 15.252 1534
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 10
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1453 THROUGH 1571 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.4591 30.8861 23.5227
REMARK 3 T TENSOR
REMARK 3 T11: 0.1757 T22: 0.1700
REMARK 3 T33: 0.1609 T12: -0.0041
REMARK 3 T13: -0.0030 T23: -0.0009
REMARK 3 L TENSOR
REMARK 3 L11: 3.1876 L22: 2.3459
REMARK 3 L33: 4.1002 L12: -0.0504
REMARK 3 L13: 0.6091 L23: -0.3209
REMARK 3 S TENSOR
REMARK 3 S11: 0.1103 S12: -0.3295 S13: -0.0787
REMARK 3 S21: 0.2155 S22: 0.0013 S23: 0.0671
REMARK 3 S31: 0.2637 S32: -0.0772 S33: -0.0624
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1572 THROUGH 1626 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.1090 21.3668 7.0261
REMARK 3 T TENSOR
REMARK 3 T11: 0.4436 T22: 0.3662
REMARK 3 T33: 0.4162 T12: -0.0339
REMARK 3 T13: 0.0309 T23: -0.1154
REMARK 3 L TENSOR
REMARK 3 L11: 7.5426 L22: 1.9760
REMARK 3 L33: 3.1869 L12: -1.3108
REMARK 3 L13: -0.3853 L23: -1.4432
REMARK 3 S TENSOR
REMARK 3 S11: -0.1359 S12: -0.0020 S13: -0.5583
REMARK 3 S21: 0.3053 S22: -0.1895 S23: 0.5583
REMARK 3 S31: 0.4626 S32: -0.1599 S33: 0.1936
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1627 THROUGH 1644 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.5348 21.2503 12.6912
REMARK 3 T TENSOR
REMARK 3 T11: 0.3279 T22: 0.2665
REMARK 3 T33: 0.4154 T12: 0.0045
REMARK 3 T13: -0.0122 T23: -0.0324
REMARK 3 L TENSOR
REMARK 3 L11: 3.7647 L22: 9.1725
REMARK 3 L33: 3.1381 L12: 0.6986
REMARK 3 L13: 0.0800 L23: 1.4928
REMARK 3 S TENSOR
REMARK 3 S11: -0.0484 S12: 0.3900 S13: -0.7442
REMARK 3 S21: -0.1418 S22: -0.0722 S23: 0.2220
REMARK 3 S31: 0.8588 S32: 0.1383 S33: -0.1287
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1645 THROUGH 1727 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.2518 39.3381 12.7713
REMARK 3 T TENSOR
REMARK 3 T11: 0.1757 T22: 0.1471
REMARK 3 T33: 0.1635 T12: 0.0264
REMARK 3 T13: 0.0044 T23: 0.0386
REMARK 3 L TENSOR
REMARK 3 L11: 5.0623 L22: 3.0064
REMARK 3 L33: 2.7546 L12: 0.3290
REMARK 3 L13: 0.3155 L23: -0.5602
REMARK 3 S TENSOR
REMARK 3 S11: 0.0192 S12: 0.2556 S13: 0.3197
REMARK 3 S21: -0.0425 S22: -0.0077 S23: -0.0213
REMARK 3 S31: -0.1630 S32: 0.0621 S33: 0.0690
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1451 THROUGH 1526 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.8570 71.0306 6.9901
REMARK 3 T TENSOR
REMARK 3 T11: 0.2045 T22: 0.1889
REMARK 3 T33: 0.4163 T12: -0.0036
REMARK 3 T13: -0.0397 T23: -0.0248
REMARK 3 L TENSOR
REMARK 3 L11: 3.7422 L22: 4.2796
REMARK 3 L33: 5.9599 L12: -0.1058
REMARK 3 L13: -1.8416 L23: -0.7952
REMARK 3 S TENSOR
REMARK 3 S11: -0.0193 S12: 0.0442 S13: 0.6430
REMARK 3 S21: 0.0460 S22: 0.1645 S23: -0.5810
REMARK 3 S31: -0.1641 S32: 0.4102 S33: -0.0429
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1527 THROUGH 1571 )
REMARK 3 ORIGIN FOR THE GROUP (A): 25.4575 59.1635 1.1605
REMARK 3 T TENSOR
REMARK 3 T11: 0.2781 T22: 0.1426
REMARK 3 T33: 0.3092 T12: 0.0167
REMARK 3 T13: 0.0320 T23: 0.0213
REMARK 3 L TENSOR
REMARK 3 L11: 3.4305 L22: 3.6428
REMARK 3 L33: 4.0137 L12: -0.0234
REMARK 3 L13: -1.3004 L23: 0.3987
REMARK 3 S TENSOR
REMARK 3 S11: -0.2520 S12: 0.0665 S13: 0.0116
REMARK 3 S21: -0.3551 S22: 0.1507 S23: -0.4957
REMARK 3 S31: 0.2718 S32: 0.0711 S33: 0.0210
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1572 THROUGH 1626 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.4442 69.8183 -17.7649
REMARK 3 T TENSOR
REMARK 3 T11: 0.3655 T22: 0.5107
REMARK 3 T33: 0.3442 T12: -0.1668
REMARK 3 T13: -0.0884 T23: 0.1125
REMARK 3 L TENSOR
REMARK 3 L11: 4.6505 L22: 9.3240
REMARK 3 L33: 3.6442 L12: 0.3635
REMARK 3 L13: 0.1238 L23: 2.2456
REMARK 3 S TENSOR
REMARK 3 S11: -0.2021 S12: 0.2226 S13: 0.0269
REMARK 3 S21: -0.5969 S22: 0.3641 S23: 0.7618
REMARK 3 S31: 0.2556 S32: -0.3731 S33: -0.1598
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1627 THROUGH 1644 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.6757 71.6706 -7.7101
REMARK 3 T TENSOR
REMARK 3 T11: 0.2764 T22: 0.2616
REMARK 3 T33: 0.3293 T12: -0.0631
REMARK 3 T13: -0.0435 T23: 0.0742
REMARK 3 L TENSOR
REMARK 3 L11: 7.6555 L22: 5.3234
REMARK 3 L33: 5.1390 L12: -6.3809
REMARK 3 L13: -1.2296 L23: 1.3209
REMARK 3 S TENSOR
REMARK 3 S11: -0.0906 S12: -0.2623 S13: 0.0300
REMARK 3 S21: 0.3989 S22: 0.3430 S23: 0.3087
REMARK 3 S31: 0.1341 S32: 0.1353 S33: -0.0647
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1645 THROUGH 1689 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.2161 54.0972 0.3888
REMARK 3 T TENSOR
REMARK 3 T11: 0.3852 T22: 0.1468
REMARK 3 T33: 0.2245 T12: -0.0481
REMARK 3 T13: 0.0156 T23: -0.0251
REMARK 3 L TENSOR
REMARK 3 L11: 7.7050 L22: 4.1442
REMARK 3 L33: 3.8640 L12: -1.4786
REMARK 3 L13: 1.5839 L23: -1.1658
REMARK 3 S TENSOR
REMARK 3 S11: 0.0090 S12: 0.4441 S13: -0.3810
REMARK 3 S21: -0.4724 S22: 0.0505 S23: 0.0392
REMARK 3 S31: 0.4272 S32: -0.1508 S33: -0.0376
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1690 THROUGH 1726 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.6160 58.9707 15.4019
REMARK 3 T TENSOR
REMARK 3 T11: 0.3363 T22: 0.1919
REMARK 3 T33: 0.1869 T12: 0.0422
REMARK 3 T13: 0.0033 T23: 0.0138
REMARK 3 L TENSOR
REMARK 3 L11: 4.4104 L22: 5.2093
REMARK 3 L33: 6.4219 L12: 1.2733
REMARK 3 L13: 1.0029 L23: 1.1716
REMARK 3 S TENSOR
REMARK 3 S11: -0.1258 S12: -0.4652 S13: 0.1542
REMARK 3 S21: 0.5351 S22: 0.1730 S23: -0.2523
REMARK 3 S31: 0.2664 S32: 0.0487 S33: -0.0533
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 : 2347
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5V3X 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_1000226796.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-MAR-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) : 0.979
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 : 40346
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.936
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 (%) : 95.4
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.11800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.94
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.10
REMARK 200 R MERGE FOR SHELL (I) : 0.98000
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 (%): 43.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
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 44.60350
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.77300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 44.60350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.77300
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 GLN A 1620
REMARK 465 SER A 1621
REMARK 465 GLY A 1622
REMARK 465 VAL A 1623
REMARK 465 GLN A 1624
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 GLY B 1466
REMARK 465 THR B 1589
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 ARG A1547 CG CD NE CZ NH1 NH2
REMARK 470 GLU A1587 CG CD OE1 OE2
REMARK 470 LYS A1588 CG CD CE NZ
REMARK 470 VAL A1592 CG1 CG2
REMARK 470 THR A1593 OG1 CG2
REMARK 470 ILE A1594 CG1 CG2 CD1
REMARK 470 ILE A1597 CG1 CG2 CD1
REMARK 470 GLU A1600 CG CD OE1 OE2
REMARK 470 GLU A1604 CG CD OE1 OE2
REMARK 470 ARG A1612 CG CD NE CZ NH1 NH2
REMARK 470 PHE A1613 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL A1614 CG1 CG2
REMARK 470 LEU A1615 CG CD1 CD2
REMARK 470 VAL A1618 CG1 CG2
REMARK 470 SER A1619 OG
REMARK 470 ILE A1625 CG1 CG2 CD1
REMARK 470 ILE A1630 CG1 CG2 CD1
REMARK 470 GLU A1631 CG CD OE1 OE2
REMARK 470 MET A1669 CG SD CE
REMARK 470 THR A1727 OG1 CG2
REMARK 470 GLN B1451 CG CD OE1 NE2
REMARK 470 ILE B1452 CG1 CG2 CD1
REMARK 470 ASP B1453 CG OD1 OD2
REMARK 470 GLU B1464 CG CD OE1 OE2
REMARK 470 GLU B1567 CG CD OE1 OE2
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 PHE B1585 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU B1587 CG CD OE1 OE2
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 ASP B1652 CG OD1 OD2
REMARK 470 MET B1669 CG SD CE
REMARK 470 GLU B1713 CG CD OE1 OE2
REMARK 470 ARG B1726 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH B 1901 O HOH B 2000 2.10
REMARK 500 NH1 ARG B 1563 O HOH B 1901 2.11
REMARK 500 O THR A 1589 O HOH A 1901 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE2 GLU A 1485 OE2 GLU B 1608 3545 1.71
REMARK 500 OE1 GLU A 1485 NH1 ARG B 1634 3545 1.71
REMARK 500 OE2 GLU A 1485 CG GLU B 1608 3545 2.01
REMARK 500 OE2 GLU A 1485 CD GLU B 1608 3545 2.04
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 SER A1533 -132.85 61.61
REMARK 500 GLN A1570 76.65 -109.06
REMARK 500 PRO A1595 -168.73 -72.77
REMARK 500 SER B1533 -131.74 59.69
REMARK 500 GLN B1570 78.07 -108.59
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 A2050 DISTANCE = 6.43 ANGSTROMS
REMARK 525 HOH B2009 DISTANCE = 6.09 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue I28 A 1801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue I28 B 1801
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5V3W 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: 5V41 RELATED DB: PDB
REMARK 900 RELATED ID: 5V42 RELATED DB: PDB
DBREF1 5V3X A 1451 1733 UNP A0A0T9CRX1_MYCTX
DBREF2 5V3X A A0A0T9CRX1 113 395
DBREF1 5V3X B 1451 1733 UNP A0A0T9CRX1_MYCTX
DBREF2 5V3X B A0A0T9CRX1 113 395
SEQADV 5V3X SER A 1448 UNP A0A0T9CRX EXPRESSION TAG
SEQADV 5V3X ASN A 1449 UNP A0A0T9CRX EXPRESSION TAG
SEQADV 5V3X ALA A 1450 UNP A0A0T9CRX EXPRESSION TAG
SEQADV 5V3X SER B 1448 UNP A0A0T9CRX EXPRESSION TAG
SEQADV 5V3X ASN B 1449 UNP A0A0T9CRX EXPRESSION TAG
SEQADV 5V3X 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 I28 A1801 29
HET I28 B1801 29
HETNAM I28 ETHYL 5-HYDROXY-4-[(4-METHYLPIPERIDIN-1-YL)METHYL]-2-
HETNAM 2 I28 PHENYL-1-BENZOFURAN-3-CARBOXYLATE
FORMUL 3 I28 2(C24 H27 N O4)
FORMUL 5 HOH *259(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 PHE A 1590 1 20
HELIX 6 AA6 PRO A 1598 GLU A 1603 1 6
HELIX 7 AA7 ASP A 1606 SER A 1619 1 14
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 ARG B 1490 1 7
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 LYS B 1588 1 18
HELIX 18 AB9 PRO B 1598 GLU B 1603 1 6
HELIX 19 AC1 ASP B 1606 SER B 1621 1 16
HELIX 20 AC2 PRO B 1626 ALA B 1646 1 21
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 TYR A1658 N LEU A1558
SHEET 7 AA1 7 LEU A1690 PRO A1694 1 O GLU A1691 N LEU A1657
SHEET 1 AA2 8 ILE B1452 ASP B1453 0
SHEET 2 AA2 8 VAL B1456 ARG B1460 -1 O VAL B1456 N ASP B1453
SHEET 3 AA2 8 MET B1497 PHE B1500 -1 O GLY B1499 N ARG B1457
SHEET 4 AA2 8 VAL B1471 PHE B1474 1 N VAL B1473 O PHE B1500
SHEET 5 AA2 8 TYR B1527 TRP B1532 1 O VAL B1530 N PHE B1472
SHEET 6 AA2 8 VAL B1553 ILE B1559 1 O GLY B1557 N LEU B1529
SHEET 7 AA2 8 VAL B1655 MET B1659 1 O TYR B1658 N LEU B1558
SHEET 8 AA2 8 LEU B1690 PRO B1694 1 O GLU B1691 N LEU B1657
CISPEP 1 GLY A 1525 PRO A 1526 0 -1.22
CISPEP 2 GLU A 1705 PRO A 1706 0 1.42
CISPEP 3 GLY B 1525 PRO B 1526 0 -0.73
CISPEP 4 GLU B 1705 PRO B 1706 0 0.79
SITE 1 AC1 11 GLN A1633 SER A1636 TYR A1637 ASN A1640
SITE 2 AC1 11 ASP A1644 TYR A1663 ASP A1666 ALA A1667
SITE 3 AC1 11 PHE A1670 GLU A1671 TYR A1674
SITE 1 AC2 11 TYR B1582 GLN B1633 TYR B1637 ASN B1640
SITE 2 AC2 11 ASP B1644 TYR B1663 ALA B1667 PHE B1670
SITE 3 AC2 11 GLU B1671 TYR B1674 HOH B1937
CRYST1 89.207 109.546 57.019 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 0.011210 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009129 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017538 0.00000
TER 2052 THR A1727
TER 4101 ARG B1726
MASTER 538 0 2 24 15 0 6 6 4416 2 58 44
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