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HEADER TRANSFERASE/TRANSFERASE INHIBITOR 08-MAR-17 5V40
TITLE CRYSTAL STRUCTURE OF MTB PKS13 THIOESTERASE DOMAIN IN COMPLEX WITH
TITLE 2 INHIBITOR TAM6
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, TAM6 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 5V40 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. 1.99 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.2_1309
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.99
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.45
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 38081
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1909
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 46.4606 - 4.7968 0.98 2741 137 0.1763 0.1602
REMARK 3 2 4.7968 - 3.8079 0.99 2662 126 0.1392 0.1622
REMARK 3 3 3.8079 - 3.3267 0.99 2625 137 0.1540 0.1899
REMARK 3 4 3.3267 - 3.0226 1.00 2596 155 0.1777 0.1770
REMARK 3 5 3.0226 - 2.8060 1.00 2616 129 0.1941 0.2814
REMARK 3 6 2.8060 - 2.6406 1.00 2598 148 0.2064 0.2536
REMARK 3 7 2.6406 - 2.5084 1.00 2568 137 0.1990 0.2589
REMARK 3 8 2.5084 - 2.3992 1.00 2610 132 0.1963 0.2628
REMARK 3 9 2.3992 - 2.3068 1.00 2588 132 0.2004 0.2655
REMARK 3 10 2.3068 - 2.2272 1.00 2552 142 0.2092 0.2508
REMARK 3 11 2.2272 - 2.1576 1.00 2584 137 0.2253 0.3033
REMARK 3 12 2.1576 - 2.0959 0.99 2535 123 0.2416 0.2666
REMARK 3 13 2.0959 - 2.0407 0.98 2527 147 0.2590 0.3255
REMARK 3 14 2.0407 - 1.9909 0.93 2370 127 0.2883 0.3043
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.590
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.51
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.75
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 : 0.006 4335
REMARK 3 ANGLE : 0.863 5898
REMARK 3 CHIRALITY : 0.053 632
REMARK 3 PLANARITY : 0.007 784
REMARK 3 DIHEDRAL : 11.886 2554
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1452 THROUGH 1548 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.0602 28.8118 24.3889
REMARK 3 T TENSOR
REMARK 3 T11: 0.1998 T22: 0.1430
REMARK 3 T33: 0.1049 T12: -0.0169
REMARK 3 T13: -0.0295 T23: 0.0159
REMARK 3 L TENSOR
REMARK 3 L11: 1.3995 L22: 1.3761
REMARK 3 L33: 2.1432 L12: -0.0233
REMARK 3 L13: 0.1881 L23: 0.0750
REMARK 3 S TENSOR
REMARK 3 S11: 0.0995 S12: -0.1382 S13: -0.1329
REMARK 3 S21: 0.2995 S22: -0.0172 S23: 0.0049
REMARK 3 S31: 0.2067 S32: -0.0427 S33: -0.0696
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1549 THROUGH 1689 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.9538 30.0309 11.4210
REMARK 3 T TENSOR
REMARK 3 T11: 0.1370 T22: 0.1515
REMARK 3 T33: 0.1649 T12: 0.0148
REMARK 3 T13: 0.0209 T23: -0.0115
REMARK 3 L TENSOR
REMARK 3 L11: 2.4008 L22: 0.6923
REMARK 3 L33: 0.9063 L12: 0.2188
REMARK 3 L13: 0.7174 L23: 0.0600
REMARK 3 S TENSOR
REMARK 3 S11: 0.0390 S12: 0.0398 S13: -0.1176
REMARK 3 S21: 0.0254 S22: -0.0296 S23: 0.1840
REMARK 3 S31: 0.0499 S32: -0.0963 S33: -0.0018
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1690 THROUGH 1727 )
REMARK 3 ORIGIN FOR THE GROUP (A): 25.4518 38.4352 13.7747
REMARK 3 T TENSOR
REMARK 3 T11: 0.1893 T22: 0.2027
REMARK 3 T33: 0.2015 T12: -0.0053
REMARK 3 T13: -0.0038 T23: 0.0123
REMARK 3 L TENSOR
REMARK 3 L11: 2.1760 L22: 1.4741
REMARK 3 L33: 0.5440 L12: -0.2540
REMARK 3 L13: 0.0964 L23: -0.8819
REMARK 3 S TENSOR
REMARK 3 S11: -0.0001 S12: 0.1311 S13: 0.1595
REMARK 3 S21: 0.0835 S22: -0.0159 S23: -0.2849
REMARK 3 S31: -0.1259 S32: 0.1760 S33: 0.0594
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1451 THROUGH 1571 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.0896 66.9803 5.3223
REMARK 3 T TENSOR
REMARK 3 T11: 0.1378 T22: 0.1441
REMARK 3 T33: 0.2031 T12: 0.0172
REMARK 3 T13: -0.0288 T23: -0.0019
REMARK 3 L TENSOR
REMARK 3 L11: 1.8256 L22: 2.5249
REMARK 3 L33: 1.9927 L12: -0.2298
REMARK 3 L13: -0.8205 L23: -0.1683
REMARK 3 S TENSOR
REMARK 3 S11: -0.0437 S12: -0.0301 S13: 0.1569
REMARK 3 S21: 0.0115 S22: 0.1282 S23: -0.3139
REMARK 3 S31: 0.0405 S32: 0.1425 S33: -0.0623
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1572 THROUGH 1588 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.0365 63.1396 -14.5764
REMARK 3 T TENSOR
REMARK 3 T11: 0.5231 T22: 0.5016
REMARK 3 T33: 0.4082 T12: -0.1087
REMARK 3 T13: -0.1147 T23: 0.0955
REMARK 3 L TENSOR
REMARK 3 L11: 1.0996 L22: 1.4280
REMARK 3 L33: 1.5514 L12: 0.9771
REMARK 3 L13: 0.4281 L23: -0.5627
REMARK 3 S TENSOR
REMARK 3 S11: 0.0587 S12: -0.1083 S13: -0.1465
REMARK 3 S21: 0.2589 S22: 0.4475 S23: 0.2191
REMARK 3 S31: -0.0630 S32: -0.5000 S33: -0.1582
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1589 THROUGH 1644 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.0618 72.4283 -14.2321
REMARK 3 T TENSOR
REMARK 3 T11: 0.2643 T22: 0.2815
REMARK 3 T33: 0.2939 T12: -0.0971
REMARK 3 T13: -0.0941 T23: 0.0500
REMARK 3 L TENSOR
REMARK 3 L11: 1.0666 L22: 1.4574
REMARK 3 L33: 1.5011 L12: 0.0517
REMARK 3 L13: 0.2468 L23: 0.1112
REMARK 3 S TENSOR
REMARK 3 S11: -0.0155 S12: 0.1533 S13: -0.0105
REMARK 3 S21: -0.3478 S22: 0.1768 S23: 0.3813
REMARK 3 S31: 0.1986 S32: -0.3301 S33: -0.1343
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1645 THROUGH 1726 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.9693 56.3268 7.1900
REMARK 3 T TENSOR
REMARK 3 T11: 0.2341 T22: 0.1628
REMARK 3 T33: 0.1880 T12: 0.0158
REMARK 3 T13: 0.0009 T23: 0.0126
REMARK 3 L TENSOR
REMARK 3 L11: 1.1018 L22: 2.3613
REMARK 3 L33: 1.9296 L12: 0.0088
REMARK 3 L13: -0.2326 L23: -0.3523
REMARK 3 S TENSOR
REMARK 3 S11: -0.0485 S12: 0.0398 S13: -0.1114
REMARK 3 S21: 0.0576 S22: 0.0981 S23: 0.0882
REMARK 3 S31: 0.3797 S32: 0.0096 S33: -0.0285
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 : 2504
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5V40 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_1000226799.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JUN-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 : 23-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0332
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL CRYO-COOLED
REMARK 200 SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38140
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.990
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 (%) : 99.0
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 5.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.99
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.7
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.89500
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 (%): 43.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
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 44.00850
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.68200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 44.00850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.68200
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 ASN A 1591
REMARK 465 SER A 1621
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 PHE B 1590
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 ILE A1452 CG1 CG2 CD1
REMARK 470 GLU A1464 CG CD OE1 OE2
REMARK 470 LYS A1588 CG CD CE NZ
REMARK 470 THR A1589 OG1 CG2
REMARK 470 GLU A1600 CG CD OE1 OE2
REMARK 470 GLN A1620 CG CD OE1 NE2
REMARK 470 VAL A1623 CG1 CG2
REMARK 470 GLN A1624 CG CD OE1 NE2
REMARK 470 MET A1669 CG SD CE
REMARK 470 THR A1727 OG1 CG2
REMARK 470 GLU B1464 CG CD OE1 OE2
REMARK 470 GLU B1567 CG CD OE1 OE2
REMARK 470 GLN B1570 CG CD OE1 NE2
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 GLU B1587 CG CD OE1 OE2
REMARK 470 LYS B1588 CG CD CE NZ
REMARK 470 THR B1589 OG1 CG2
REMARK 470 ASN B1591 CG OD1 ND2
REMARK 470 VAL B1592 CG1 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 B1620 CG CD OE1 NE2
REMARK 470 GLN B1624 CG CD OE1 NE2
REMARK 470 ASP B1652 CG OD1 OD2
REMARK 470 MET B1669 CG SD CE
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 OD1 ASP A 1639 O HOH A 1901 2.16
REMARK 500 O HOH B 2048 O HOH B 2074 2.17
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 -135.76 59.11
REMARK 500 GLN A1570 71.88 -109.87
REMARK 500 PRO A1598 79.15 -68.60
REMARK 500 ALA B1465 -26.22 -140.83
REMARK 500 SER B1533 -137.54 59.12
REMARK 500 GLN B1570 72.01 -112.92
REMARK 500 PRO B1598 94.38 -69.33
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 JS1 A 1801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue JS1 B 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: 5V41 RELATED DB: PDB
REMARK 900 RELATED ID: 5V42 RELATED DB: PDB
DBREF1 5V40 A 1451 1733 UNP A0A0T9CRX1_MYCTX
DBREF2 5V40 A A0A0T9CRX1 113 395
DBREF1 5V40 B 1451 1733 UNP A0A0T9CRX1_MYCTX
DBREF2 5V40 B A0A0T9CRX1 113 395
SEQADV 5V40 SER A 1448 UNP A0A0T9CRX EXPRESSION TAG
SEQADV 5V40 ASN A 1449 UNP A0A0T9CRX EXPRESSION TAG
SEQADV 5V40 ALA A 1450 UNP A0A0T9CRX EXPRESSION TAG
SEQADV 5V40 SER B 1448 UNP A0A0T9CRX EXPRESSION TAG
SEQADV 5V40 ASN B 1449 UNP A0A0T9CRX EXPRESSION TAG
SEQADV 5V40 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 JS1 A1801 25
HET JS1 B1801 25
HETNAM JS1 ETHYL 4-[(DIMETHYLAMINO)METHYL]-5-HYDROXY-2-PHENYL-1-
HETNAM 2 JS1 BENZOFURAN-3-CARBOXYLATE
FORMUL 3 JS1 2(C20 H21 N O4)
FORMUL 5 HOH *398(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 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 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 THR B 1589 1 19
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 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 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 THR B1656 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 -0.23
CISPEP 2 GLU A 1705 PRO A 1706 0 2.94
CISPEP 3 GLY B 1525 PRO B 1526 0 1.22
CISPEP 4 GLU B 1705 PRO B 1706 0 2.04
SITE 1 AC1 11 TYR A1582 GLN A1633 SER A1636 TYR A1637
SITE 2 AC1 11 ASN A1640 ASP A1644 ASP A1666 ALA A1667
SITE 3 AC1 11 PHE A1670 GLU A1671 TYR A1674
SITE 1 AC2 10 GLN B1633 SER B1636 TYR B1637 ASN B1640
SITE 2 AC2 10 ASP B1644 ASP B1666 ALA B1667 PHE B1670
SITE 3 AC2 10 GLU B1671 TYR B1674
CRYST1 88.017 109.364 57.029 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 0.011361 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009144 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017535 0.00000
TER 2119 THR A1727
TER 4190 ARG B1726
MASTER 441 0 2 24 15 0 6 6 4636 2 50 44
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