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HEADER TRANSFERASE/TRANSFERASE INHIBITOR 08-MAR-17 5V3Y
TITLE CRYSTAL STRUCTURE OF MTB PKS13 THIOESTERASE DOMAIN IN COMPLEX WITH
TITLE 2 INHIBITOR TAM16
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, TAM16 COMPLEX, PKS13, MYCOBACTERIUM, POLYKETIDE
KEYWDS 2 SYNTHASE, MYCOLIC ACID CONDENSATION, TB STRUCTURAL GENOMICS
KEYWDS 3 CONSORTIUM, TBSGC, ALPHA/BETA HYDROLASE, THIOESTERASE-TRANSFERASE
KEYWDS 4 INHIBITOR COMPLEX, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.AGGARWAL,J.C.SACCHETTINI
REVDAT 1 05-JUL-17 5V3Y 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. 1.98 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) : 1.98
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.58
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.3
REMARK 3 NUMBER OF REFLECTIONS : 36725
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 : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 1861
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 34.5891 - 4.6522 1.00 3078 149 0.1879 0.2381
REMARK 3 2 4.6522 - 3.6939 0.93 2622 146 0.1626 0.1805
REMARK 3 3 3.6939 - 3.2274 0.87 2486 126 0.1783 0.2321
REMARK 3 4 3.2274 - 2.9325 1.00 2872 171 0.1872 0.2496
REMARK 3 5 2.9325 - 2.7224 1.00 2859 138 0.1967 0.2586
REMARK 3 6 2.7224 - 2.5619 1.00 2862 164 0.1874 0.2195
REMARK 3 7 2.5619 - 2.4336 1.00 2863 144 0.1892 0.2164
REMARK 3 8 2.4336 - 2.3277 1.00 2851 152 0.2008 0.2294
REMARK 3 9 2.3277 - 2.2381 0.68 1917 97 0.2713 0.2790
REMARK 3 10 2.2381 - 2.1609 0.72 2015 114 0.2377 0.3238
REMARK 3 11 2.1609 - 2.0934 1.00 2819 163 0.2397 0.3041
REMARK 3 12 2.0934 - 2.0335 0.99 2783 151 0.3185 0.3985
REMARK 3 13 2.0335 - 1.9800 1.00 2837 146 0.2502 0.3181
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) : 25.360
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.53
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 : 0.007 4306
REMARK 3 ANGLE : 1.085 5863
REMARK 3 CHIRALITY : 0.071 626
REMARK 3 PLANARITY : 0.006 776
REMARK 3 DIHEDRAL : 12.499 1556
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 1453 THROUGH 1571 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.3241 30.6406 23.4371
REMARK 3 T TENSOR
REMARK 3 T11: 0.1581 T22: 0.1574
REMARK 3 T33: 0.1249 T12: 0.0090
REMARK 3 T13: 0.0013 T23: 0.0053
REMARK 3 L TENSOR
REMARK 3 L11: 3.0638 L22: 2.4809
REMARK 3 L33: 3.3248 L12: 0.1187
REMARK 3 L13: 0.3172 L23: -0.3812
REMARK 3 S TENSOR
REMARK 3 S11: 0.0215 S12: -0.3347 S13: -0.0851
REMARK 3 S21: 0.2461 S22: 0.0467 S23: 0.1146
REMARK 3 S31: 0.1597 S32: -0.1092 S33: -0.0407
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1572 THROUGH 1590 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.1132 25.2331 2.5811
REMARK 3 T TENSOR
REMARK 3 T11: 0.2632 T22: 0.2861
REMARK 3 T33: 0.4426 T12: -0.0064
REMARK 3 T13: -0.0587 T23: -0.0201
REMARK 3 L TENSOR
REMARK 3 L11: 7.9088 L22: 4.4446
REMARK 3 L33: 8.9586 L12: -1.7812
REMARK 3 L13: -3.6882 L23: 3.4159
REMARK 3 S TENSOR
REMARK 3 S11: 0.0356 S12: 0.1557 S13: -0.0344
REMARK 3 S21: 0.1689 S22: 0.3613 S23: -0.6438
REMARK 3 S31: 0.0297 S32: 0.5438 S33: -0.3417
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1591 THROUGH 1626 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.0399 18.0357 9.0886
REMARK 3 T TENSOR
REMARK 3 T11: 0.5649 T22: 0.4370
REMARK 3 T33: 0.4084 T12: -0.1773
REMARK 3 T13: 0.0098 T23: -0.0097
REMARK 3 L TENSOR
REMARK 3 L11: 7.4690 L22: 2.7249
REMARK 3 L33: 4.0243 L12: -1.9900
REMARK 3 L13: 1.2045 L23: 0.3704
REMARK 3 S TENSOR
REMARK 3 S11: 0.2174 S12: -0.9148 S13: -0.4495
REMARK 3 S21: -0.8070 S22: -0.0851 S23: 0.2594
REMARK 3 S31: 0.2584 S32: -0.3868 S33: -0.0595
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1627 THROUGH 1689 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.7490 34.2323 11.9028
REMARK 3 T TENSOR
REMARK 3 T11: 0.1292 T22: 0.2067
REMARK 3 T33: 0.1509 T12: 0.0334
REMARK 3 T13: 0.0071 T23: 0.0178
REMARK 3 L TENSOR
REMARK 3 L11: 4.0182 L22: 4.6204
REMARK 3 L33: 3.6206 L12: 1.2681
REMARK 3 L13: 0.9281 L23: 0.2571
REMARK 3 S TENSOR
REMARK 3 S11: -0.0273 S12: 0.1379 S13: 0.0439
REMARK 3 S21: -0.1694 S22: -0.0343 S23: 0.2452
REMARK 3 S31: -0.0081 S32: -0.3341 S33: 0.0536
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1690 THROUGH 1727 )
REMARK 3 ORIGIN FOR THE GROUP (A): 25.4792 38.2788 13.9092
REMARK 3 T TENSOR
REMARK 3 T11: 0.1311 T22: 0.1488
REMARK 3 T33: 0.2195 T12: -0.0123
REMARK 3 T13: 0.0437 T23: 0.0334
REMARK 3 L TENSOR
REMARK 3 L11: 5.5903 L22: 3.9288
REMARK 3 L33: 5.1521 L12: 0.3408
REMARK 3 L13: 1.5722 L23: -0.4573
REMARK 3 S TENSOR
REMARK 3 S11: -0.0177 S12: 0.1122 S13: 0.3396
REMARK 3 S21: 0.1406 S22: -0.0464 S23: -0.2325
REMARK 3 S31: -0.1058 S32: 0.4390 S33: -0.0705
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1451 THROUGH 1571 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.1152 66.3877 4.6800
REMARK 3 T TENSOR
REMARK 3 T11: 0.1853 T22: 0.1771
REMARK 3 T33: 0.4070 T12: -0.0090
REMARK 3 T13: -0.0101 T23: -0.0262
REMARK 3 L TENSOR
REMARK 3 L11: 2.5288 L22: 3.8461
REMARK 3 L33: 3.1953 L12: -0.3662
REMARK 3 L13: -0.1518 L23: 0.0341
REMARK 3 S TENSOR
REMARK 3 S11: -0.0929 S12: 0.0336 S13: 0.3573
REMARK 3 S21: 0.0101 S22: 0.1508 S23: -0.8044
REMARK 3 S31: -0.1593 S32: 0.4182 S33: -0.0225
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1572 THROUGH 1726 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.9388 62.3659 -2.9454
REMARK 3 T TENSOR
REMARK 3 T11: 0.2056 T22: 0.2219
REMARK 3 T33: 0.2478 T12: -0.0640
REMARK 3 T13: 0.0239 T23: -0.0135
REMARK 3 L TENSOR
REMARK 3 L11: 1.0628 L22: 3.2925
REMARK 3 L33: 3.3086 L12: -0.6929
REMARK 3 L13: 0.5413 L23: -2.0048
REMARK 3 S TENSOR
REMARK 3 S11: -0.0739 S12: 0.0717 S13: -0.0462
REMARK 3 S21: -0.1655 S22: 0.2233 S23: 0.1625
REMARK 3 S31: 0.2979 S32: -0.2304 S33: -0.1635
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 : 2128
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5V3Y 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_1000226797.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-FEB-15
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 : 41704
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
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 (%) : 94.1
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.14700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 5.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.5
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.90700
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 (%): 43.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
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 44.81350
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.38100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 44.81350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.38100
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 SER A 1619
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 GLU B 1464
REMARK 465 ALA B 1465
REMARK 465 GLY B 1466
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 ASN A1591 CG OD1 ND2
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 VAL A1614 CG1 CG2
REMARK 470 LEU A1615 CG CD1 CD2
REMARK 470 ASP A1616 CG OD1 OD2
REMARK 470 VAL A1618 CG1 CG2
REMARK 470 MET A1669 CG SD CE
REMARK 470 THR A1727 OG1 CG2
REMARK 470 GLN B1451 CG CD OE1 NE2
REMARK 470 GLU B1508 CG CD OE1 OE2
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 LYS B1577 CG CD CE NZ
REMARK 470 GLU B1587 CG CD OE1 OE2
REMARK 470 LYS B1588 CG CD CE NZ
REMARK 470 THR B1589 OG1 CG2
REMARK 470 PHE B1590 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN B1591 CG OD1 ND2
REMARK 470 VAL B1592 CG1 CG2
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 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 OD1 ASP B 1453 O HOH B 1901 1.75
REMARK 500 OE1 GLU B 1713 O HOH B 1902 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A1717 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
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 -135.17 61.52
REMARK 500 GLN A1570 71.61 -102.74
REMARK 500 SER B1533 -136.61 61.55
REMARK 500 GLN B1570 77.74 -117.01
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 5V8 A 1801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5V8 B 1801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 1802
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: 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 5V3Y A 1451 1733 UNP A0A0T9CRX1_MYCTX
DBREF2 5V3Y A A0A0T9CRX1 113 395
DBREF1 5V3Y B 1451 1733 UNP A0A0T9CRX1_MYCTX
DBREF2 5V3Y B A0A0T9CRX1 113 395
SEQADV 5V3Y SER A 1448 UNP A0A0T9CRX EXPRESSION TAG
SEQADV 5V3Y ASN A 1449 UNP A0A0T9CRX EXPRESSION TAG
SEQADV 5V3Y ALA A 1450 UNP A0A0T9CRX EXPRESSION TAG
SEQADV 5V3Y SER B 1448 UNP A0A0T9CRX EXPRESSION TAG
SEQADV 5V3Y ASN B 1449 UNP A0A0T9CRX EXPRESSION TAG
SEQADV 5V3Y 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 5V8 A1801 28
HET 5V8 B1801 28
HET SO4 B1802 5
HETNAM 5V8 2-(4-HYDROXYPHENYL)-~{N}-METHYL-5-OXIDANYL-4-
HETNAM 2 5V8 (PIPERIDIN-1-YLMETHYL)-1-BENZOFURAN-3-CARBOXAMIDE
HETNAM SO4 SULFATE ION
FORMUL 3 5V8 2(C22 H24 N2 O4)
FORMUL 5 SO4 O4 S 2-
FORMUL 6 HOH *309(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 VAL A 1618 1 13
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 PHE B 1590 1 20
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 ASP B 1725 1 20
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 TYR A1498
SHEET 4 AA1 7 TYR A1527 TRP A1532 1 O VAL A1528 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 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 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 -0.78
CISPEP 2 GLU A 1705 PRO A 1706 0 1.55
CISPEP 3 GLY B 1525 PRO B 1526 0 -0.07
CISPEP 4 GLU B 1705 PRO B 1706 0 1.90
SITE 1 AC1 11 GLN A1633 SER A1636 TYR A1637 ASN A1640
SITE 2 AC1 11 ASP A1644 ASP A1666 ALA A1667 PHE A1670
SITE 3 AC1 11 GLU A1671 TYR A1674 HOH A1988
SITE 1 AC2 13 TYR B1582 GLN B1633 SER B1636 TYR B1637
SITE 2 AC2 13 ASN B1640 ILE B1643 ASP B1644 ASP B1666
SITE 3 AC2 13 ALA B1667 PHE B1670 GLU B1671 TYR B1674
SITE 4 AC2 13 HOH B1922
SITE 1 AC3 5 SER B1506 ILE B1507 GLU B1508 GLN B1647
SITE 2 AC3 5 HOH B1942
CRYST1 89.627 108.762 56.735 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 0.011157 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009194 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017626 0.00000
TER 2081 THR A1727
TER 4157 ARG B1726
MASTER 465 0 3 24 15 0 9 6 4525 2 61 44
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