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HEADER TRANSFERASE/TRANSFERASE INHIBITOR 08-MAR-17 5V42
TITLE CRYSTAL STRUCTURE OF MTB PKS13 THIOESTERASE DOMAIN IN COMPLEX WITH
TITLE 2 INHIBITOR TAM3
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, TAM3 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 5V42 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
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) : 1.99
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.76
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 87.9
REMARK 3 NUMBER OF REFLECTIONS : 34440
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 1718
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 33.7682 - 4.5454 0.87 2890 142 0.1687 0.1820
REMARK 3 2 4.5454 - 3.6091 0.84 2459 137 0.1548 0.1663
REMARK 3 3 3.6091 - 3.1533 0.88 2687 144 0.1732 0.2396
REMARK 3 4 3.1533 - 2.8652 0.92 2853 166 0.2003 0.2462
REMARK 3 5 2.8652 - 2.6599 0.93 2917 131 0.2037 0.2787
REMARK 3 6 2.6599 - 2.5031 0.94 2887 143 0.2027 0.2269
REMARK 3 7 2.5031 - 2.3778 0.94 2881 150 0.2034 0.2961
REMARK 3 8 2.3778 - 2.2743 0.94 2892 160 0.2246 0.2946
REMARK 3 9 2.2743 - 2.1868 0.68 2081 109 0.3422 0.3844
REMARK 3 10 2.1868 - 2.1113 0.93 2822 153 0.2557 0.2831
REMARK 3 11 2.1113 - 2.0453 0.92 2842 136 0.2744 0.3320
REMARK 3 12 2.0453 - 1.9869 0.83 2511 147 0.2973 0.3339
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) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.880
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 34.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.27
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 4267
REMARK 3 ANGLE : 1.119 5802
REMARK 3 CHIRALITY : 0.048 618
REMARK 3 PLANARITY : 0.006 769
REMARK 3 DIHEDRAL : 13.455 1551
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 1454 THROUGH 1549 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.7879 29.1981 24.5643
REMARK 3 T TENSOR
REMARK 3 T11: 0.3074 T22: 0.2667
REMARK 3 T33: 0.2651 T12: 0.0115
REMARK 3 T13: -0.0103 T23: 0.0083
REMARK 3 L TENSOR
REMARK 3 L11: 1.3205 L22: 1.3161
REMARK 3 L33: 2.6122 L12: 0.1854
REMARK 3 L13: -0.3673 L23: -0.3315
REMARK 3 S TENSOR
REMARK 3 S11: 0.0178 S12: -0.1065 S13: -0.0714
REMARK 3 S21: 0.0977 S22: 0.0595 S23: 0.0586
REMARK 3 S31: 0.1430 S32: -0.0625 S33: -0.0605
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1550 THROUGH 1571 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.9812 38.5251 17.9480
REMARK 3 T TENSOR
REMARK 3 T11: 0.2918 T22: 0.2804
REMARK 3 T33: 0.3519 T12: 0.0203
REMARK 3 T13: 0.0268 T23: 0.0013
REMARK 3 L TENSOR
REMARK 3 L11: 0.8503 L22: 1.1371
REMARK 3 L33: 1.3736 L12: 0.3993
REMARK 3 L13: -0.9173 L23: -0.4940
REMARK 3 S TENSOR
REMARK 3 S11: 0.0952 S12: 0.0948 S13: 0.1581
REMARK 3 S21: -0.0160 S22: 0.1833 S23: 0.2200
REMARK 3 S31: -0.0674 S32: 0.0030 S33: -0.1326
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1572 THROUGH 1590 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.3393 25.5927 3.4288
REMARK 3 T TENSOR
REMARK 3 T11: 0.3791 T22: 0.4202
REMARK 3 T33: 0.4838 T12: -0.0103
REMARK 3 T13: -0.0483 T23: -0.0027
REMARK 3 L TENSOR
REMARK 3 L11: 1.9064 L22: 2.9633
REMARK 3 L33: 3.7034 L12: -0.1279
REMARK 3 L13: -0.2714 L23: 1.5903
REMARK 3 S TENSOR
REMARK 3 S11: -0.1662 S12: 0.3619 S13: -0.0629
REMARK 3 S21: -0.2780 S22: -0.1372 S23: 0.2901
REMARK 3 S31: -0.3155 S32: 0.3070 S33: 0.0807
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1591 THROUGH 1664 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.2309 26.1435 12.3750
REMARK 3 T TENSOR
REMARK 3 T11: 0.3479 T22: 0.3592
REMARK 3 T33: 0.3100 T12: -0.0149
REMARK 3 T13: 0.0151 T23: -0.0184
REMARK 3 L TENSOR
REMARK 3 L11: 2.3827 L22: 1.6606
REMARK 3 L33: 0.8988 L12: 0.3007
REMARK 3 L13: 0.5522 L23: 0.1243
REMARK 3 S TENSOR
REMARK 3 S11: 0.0785 S12: 0.0856 S13: -0.2372
REMARK 3 S21: 0.0373 S22: -0.0767 S23: 0.1248
REMARK 3 S31: 0.1592 S32: -0.1515 S33: 0.0014
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1665 THROUGH 1689 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.5893 39.6734 8.8943
REMARK 3 T TENSOR
REMARK 3 T11: 0.2225 T22: 0.3240
REMARK 3 T33: 0.2971 T12: 0.0294
REMARK 3 T13: 0.0256 T23: 0.0400
REMARK 3 L TENSOR
REMARK 3 L11: 2.3660 L22: 2.0818
REMARK 3 L33: 2.4325 L12: 0.9004
REMARK 3 L13: 1.4779 L23: -0.6751
REMARK 3 S TENSOR
REMARK 3 S11: 0.0664 S12: 0.2024 S13: 0.1429
REMARK 3 S21: -0.0848 S22: -0.0413 S23: 0.1504
REMARK 3 S31: -0.0958 S32: -0.3549 S33: -0.0449
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1690 THROUGH 1727 )
REMARK 3 ORIGIN FOR THE GROUP (A): 25.4652 38.5006 14.0591
REMARK 3 T TENSOR
REMARK 3 T11: 0.2908 T22: 0.2891
REMARK 3 T33: 0.3126 T12: -0.0098
REMARK 3 T13: 0.0125 T23: 0.0229
REMARK 3 L TENSOR
REMARK 3 L11: 1.9980 L22: 1.4765
REMARK 3 L33: 0.8093 L12: -0.3630
REMARK 3 L13: -0.1929 L23: -1.0031
REMARK 3 S TENSOR
REMARK 3 S11: -0.0319 S12: 0.1748 S13: 0.3419
REMARK 3 S21: -0.0019 S22: -0.1033 S23: -0.2326
REMARK 3 S31: -0.0632 S32: 0.2716 S33: 0.0979
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1451 THROUGH 1571 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.9579 66.6177 4.8092
REMARK 3 T TENSOR
REMARK 3 T11: 0.2792 T22: 0.2647
REMARK 3 T33: 0.3455 T12: 0.0000
REMARK 3 T13: 0.0222 T23: 0.0129
REMARK 3 L TENSOR
REMARK 3 L11: 1.8791 L22: 2.5814
REMARK 3 L33: 2.1516 L12: -0.0156
REMARK 3 L13: 0.0399 L23: 0.5044
REMARK 3 S TENSOR
REMARK 3 S11: 0.0252 S12: 0.0846 S13: 0.1852
REMARK 3 S21: -0.0961 S22: 0.0399 S23: -0.4367
REMARK 3 S31: -0.0407 S32: 0.1191 S33: -0.0371
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1572 THROUGH 1626 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.2473 70.0025 -17.2452
REMARK 3 T TENSOR
REMARK 3 T11: 0.4180 T22: 0.4748
REMARK 3 T33: 0.4014 T12: -0.0965
REMARK 3 T13: -0.0308 T23: 0.1046
REMARK 3 L TENSOR
REMARK 3 L11: 1.4112 L22: 2.6758
REMARK 3 L33: 1.3211 L12: 0.1272
REMARK 3 L13: 1.3772 L23: 0.2779
REMARK 3 S TENSOR
REMARK 3 S11: -0.1923 S12: -0.1133 S13: -0.0257
REMARK 3 S21: -0.3825 S22: 0.4317 S23: 0.3276
REMARK 3 S31: -0.0373 S32: -0.2530 S33: -0.1125
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1627 THROUGH 1689 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.4817 59.0789 -1.8592
REMARK 3 T TENSOR
REMARK 3 T11: 0.3317 T22: 0.3056
REMARK 3 T33: 0.3761 T12: -0.0293
REMARK 3 T13: 0.0141 T23: -0.0143
REMARK 3 L TENSOR
REMARK 3 L11: 0.8428 L22: 1.7559
REMARK 3 L33: 1.9430 L12: 0.0624
REMARK 3 L13: 0.6091 L23: -1.2042
REMARK 3 S TENSOR
REMARK 3 S11: -0.0440 S12: 0.1609 S13: -0.0869
REMARK 3 S21: -0.1417 S22: 0.1405 S23: 0.0374
REMARK 3 S31: 0.2273 S32: 0.0376 S33: -0.0782
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1690 THROUGH 1726 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.7730 59.2145 15.5796
REMARK 3 T TENSOR
REMARK 3 T11: 0.3771 T22: 0.3031
REMARK 3 T33: 0.3231 T12: 0.0237
REMARK 3 T13: -0.0192 T23: 0.0263
REMARK 3 L TENSOR
REMARK 3 L11: 0.9628 L22: 2.1027
REMARK 3 L33: 1.4278 L12: 0.2357
REMARK 3 L13: -0.4718 L23: 0.4297
REMARK 3 S TENSOR
REMARK 3 S11: -0.1004 S12: -0.2300 S13: 0.1326
REMARK 3 S21: 0.5218 S22: 0.0790 S23: -0.0709
REMARK 3 S31: 0.1240 S32: -0.0347 S33: 0.0014
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 : 2331
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5V42 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_1000226801.
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) : 1.0032
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 : 34501
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.987
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 (%) : 88.0
REMARK 200 DATA REDUNDANCY : 5.200
REMARK 200 R MERGE (I) : 0.10600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.1000
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 (%) : 83.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.40
REMARK 200 R MERGE FOR SHELL (I) : 0.94000
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 (%): 43.78
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 44.68100
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.69950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 44.68100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.69950
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 ASP A 1453
REMARK 465 THR A 1593
REMARK 465 ILE A 1594
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 GLU B 1464
REMARK 465 ALA B 1465
REMARK 465 GLY B 1466
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 GLU A1464 CG CD OE1 OE2
REMARK 470 GLU A1567 CG CD OE1 OE2
REMARK 470 GLU A1587 CG CD OE1 OE2
REMARK 470 LYS A1588 CG CD CE NZ
REMARK 470 GLU A1600 CG CD OE1 OE2
REMARK 470 GLU A1608 CG CD OE1 OE2
REMARK 470 PHE A1613 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU A1615 CG CD1 CD2
REMARK 470 ASP A1616 CG OD1 OD2
REMARK 470 VAL A1618 CG1 CG2
REMARK 470 SER A1619 OG
REMARK 470 GLN A1620 CG CD OE1 NE2
REMARK 470 ILE A1625 CG1 CG2 CD1
REMARK 470 ILE A1630 CG1 CG2 CD1
REMARK 470 MET A1669 CG SD CE
REMARK 470 GLN B1451 CG CD OE1 NE2
REMARK 470 GLU B1508 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 ILE B1575 CG1 CG2 CD1
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 GLU B1587 CG CD OE1 OE2
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 ILE B1625 CG1 CG2 CD1
REMARK 470 MET B1669 CG SD CE
REMARK 470 ASP B1725 CG OD1 OD2
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 1987 O HOH B 1997 2.01
REMARK 500 O HOH A 2007 O HOH A 2031 2.14
REMARK 500 OD1 ASP B 1453 O HOH B 1901 2.15
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 -134.47 59.54
REMARK 500 GLN A1570 69.84 -105.65
REMARK 500 SER B1533 -134.97 59.15
REMARK 500 GLN B1570 72.12 -110.90
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 I66 A 1801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue I66 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: 5V40 RELATED DB: PDB
REMARK 900 RELATED ID: 5V41 RELATED DB: PDB
DBREF1 5V42 A 1451 1733 UNP A0A0T9CRX1_MYCTX
DBREF2 5V42 A A0A0T9CRX1 113 395
DBREF1 5V42 B 1451 1733 UNP A0A0T9CRX1_MYCTX
DBREF2 5V42 B A0A0T9CRX1 113 395
SEQADV 5V42 SER A 1448 UNP A0A0T9CRX EXPRESSION TAG
SEQADV 5V42 ASN A 1449 UNP A0A0T9CRX EXPRESSION TAG
SEQADV 5V42 ALA A 1450 UNP A0A0T9CRX EXPRESSION TAG
SEQADV 5V42 SER B 1448 UNP A0A0T9CRX EXPRESSION TAG
SEQADV 5V42 ASN B 1449 UNP A0A0T9CRX EXPRESSION TAG
SEQADV 5V42 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 I66 A1801 27
HET I66 B1801 27
HETNAM I66 ETHYL 5-HYDROXY-2-PHENYL-4-(PYRROLIDIN-1-YLMETHYL)-1-
HETNAM 2 I66 BENZOFURAN-3-CARBOXYLATE
FORMUL 3 I66 2(C22 H23 N O4)
FORMUL 5 HOH *247(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 GLU A 1604 1 7
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 GLN B 1620 1 15
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 ILE A1559 N GLY A1531
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 ILE B1559 N GLY B1531
SHEET 7 AA2 8 VAL B1655 MET B1659 1 O THR B1656 N VAL B1556
SHEET 8 AA2 8 LEU B1690 PRO B1694 1 O GLU B1691 N LEU B1657
CISPEP 1 GLY A 1525 PRO A 1526 0 2.57
CISPEP 2 GLU A 1705 PRO A 1706 0 3.52
CISPEP 3 GLY B 1525 PRO B 1526 0 2.89
CISPEP 4 GLU B 1705 PRO B 1706 0 2.51
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 TYR B1637 ASN B1640 ARG B1641
SITE 2 AC2 10 ASP B1644 ASP B1666 ALA B1667 PHE B1670
SITE 3 AC2 10 GLU B1671 TYR B1674
CRYST1 89.362 109.399 56.895 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 0.011190 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009141 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017576 0.00000
TER 2060 THR A1727
TER 4117 ARG B1726
MASTER 492 0 2 24 15 0 6 6 4416 2 54 44
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