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HEADER TRANSFERASE 08-MAR-17 5V3W
TITLE CRYSTAL STRUCTURE OF THE APO FORM OF THIOESTERASE DOMAIN OF MTB PKS13
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, PKS13, MYCOBACTERIUM, POLYKETIDE SYNTHASE,
KEYWDS 2 MYCOLIC ACID CONDENSATION, TB STRUCTURAL GENOMICS CONSORTIUM, TBSGC,
KEYWDS 3 ALPHA/BETA HYDROLASE, THIOESTERASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.AGGARWAL,J.C.SACCHETTINI
REVDAT 1 05-JUL-17 5V3W 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. 1.72 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) : 1.72
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.25
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 58467
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.201
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 2959
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 39.2601 - 4.7517 0.99 2840 139 0.1787 0.1767
REMARK 3 2 4.7517 - 3.7725 1.00 2727 145 0.1420 0.1621
REMARK 3 3 3.7725 - 3.2959 0.99 2692 141 0.1601 0.1783
REMARK 3 4 3.2959 - 2.9947 1.00 2664 167 0.1773 0.2206
REMARK 3 5 2.9947 - 2.7801 1.00 2658 142 0.1793 0.2077
REMARK 3 6 2.7801 - 2.6162 1.00 2680 141 0.1766 0.2194
REMARK 3 7 2.6162 - 2.4852 1.00 2639 151 0.1709 0.2042
REMARK 3 8 2.4852 - 2.3771 1.00 2664 142 0.1645 0.2038
REMARK 3 9 2.3771 - 2.2856 1.00 2635 142 0.1588 0.2318
REMARK 3 10 2.2856 - 2.2067 0.99 2616 140 0.1924 0.2439
REMARK 3 11 2.2067 - 2.1377 1.00 2634 143 0.1589 0.1847
REMARK 3 12 2.1377 - 2.0766 1.00 2642 141 0.1655 0.1901
REMARK 3 13 2.0766 - 2.0219 1.00 2632 150 0.1575 0.2068
REMARK 3 14 2.0219 - 1.9726 1.00 2608 154 0.1587 0.2011
REMARK 3 15 1.9726 - 1.9278 1.00 2592 129 0.1819 0.2403
REMARK 3 16 1.9278 - 1.8867 0.99 2654 129 0.2214 0.2645
REMARK 3 17 1.8867 - 1.8490 1.00 2619 141 0.1708 0.2015
REMARK 3 18 1.8490 - 1.8141 1.00 2621 129 0.1661 0.2103
REMARK 3 19 1.8141 - 1.7817 1.00 2610 155 0.1720 0.2343
REMARK 3 20 1.7817 - 1.7515 1.00 2612 131 0.1876 0.2437
REMARK 3 21 1.7515 - 1.7233 0.92 2469 107 0.1970 0.2240
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) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.220
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.04
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.71
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 : 0.010 4347
REMARK 3 ANGLE : 1.249 5901
REMARK 3 CHIRALITY : 0.056 636
REMARK 3 PLANARITY : 0.007 787
REMARK 3 DIHEDRAL : 13.599 1596
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1451 THROUGH 1590 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.5967 28.4162 20.7124
REMARK 3 T TENSOR
REMARK 3 T11: 0.1140 T22: 0.1133
REMARK 3 T33: 0.0802 T12: -0.0068
REMARK 3 T13: 0.0073 T23: -0.0021
REMARK 3 L TENSOR
REMARK 3 L11: 1.5049 L22: 0.8278
REMARK 3 L33: 0.6491 L12: 0.1667
REMARK 3 L13: 0.4491 L23: -0.0034
REMARK 3 S TENSOR
REMARK 3 S11: 0.0460 S12: -0.1135 S13: -0.0144
REMARK 3 S21: 0.1185 S22: -0.0502 S23: 0.0119
REMARK 3 S31: 0.0003 S32: -0.0222 S33: 0.0005
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1591 THROUGH 1645 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.1087 17.4835 10.5855
REMARK 3 T TENSOR
REMARK 3 T11: 0.2183 T22: 0.2461
REMARK 3 T33: 0.1819 T12: -0.0324
REMARK 3 T13: -0.0005 T23: 0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 1.5023 L22: 6.4438
REMARK 3 L33: 1.4101 L12: -0.2770
REMARK 3 L13: 0.0510 L23: 3.1264
REMARK 3 S TENSOR
REMARK 3 S11: 0.1190 S12: 0.1091 S13: -0.1317
REMARK 3 S21: 0.4254 S22: -0.3110 S23: 0.2525
REMARK 3 S31: 0.1855 S32: -0.3224 S33: 0.1590
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1646 THROUGH 1727 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.7725 37.8281 13.4785
REMARK 3 T TENSOR
REMARK 3 T11: 0.1134 T22: 0.0959
REMARK 3 T33: 0.1177 T12: -0.0083
REMARK 3 T13: 0.0100 T23: 0.0098
REMARK 3 L TENSOR
REMARK 3 L11: 2.6903 L22: 2.0692
REMARK 3 L33: 1.6894 L12: 0.1902
REMARK 3 L13: 0.8152 L23: -0.3523
REMARK 3 S TENSOR
REMARK 3 S11: -0.0405 S12: -0.0114 S13: 0.1896
REMARK 3 S21: 0.0726 S22: -0.0181 S23: 0.0517
REMARK 3 S31: -0.1463 S32: -0.0484 S33: 0.0624
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1451 THROUGH 1571 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.8387 63.9590 4.7137
REMARK 3 T TENSOR
REMARK 3 T11: 0.0730 T22: 0.0974
REMARK 3 T33: 0.0942 T12: 0.0007
REMARK 3 T13: -0.0008 T23: -0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 1.1552 L22: 1.8233
REMARK 3 L33: 1.6709 L12: 0.0169
REMARK 3 L13: -0.0285 L23: 0.0266
REMARK 3 S TENSOR
REMARK 3 S11: 0.0140 S12: -0.0273 S13: 0.0041
REMARK 3 S21: -0.0577 S22: -0.0010 S23: -0.0858
REMARK 3 S31: -0.0569 S32: 0.1278 S33: -0.0225
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1572 THROUGH 1645 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.7286 67.1741 -15.4144
REMARK 3 T TENSOR
REMARK 3 T11: 0.2290 T22: 0.2264
REMARK 3 T33: 0.2594 T12: -0.0173
REMARK 3 T13: -0.0847 T23: 0.0067
REMARK 3 L TENSOR
REMARK 3 L11: 1.2552 L22: 1.3895
REMARK 3 L33: 1.9631 L12: -0.0849
REMARK 3 L13: 1.0244 L23: -1.2619
REMARK 3 S TENSOR
REMARK 3 S11: 0.1309 S12: 0.1752 S13: -0.0828
REMARK 3 S21: -0.4680 S22: 0.0685 S23: 0.3940
REMARK 3 S31: 0.2689 S32: -0.1693 S33: -0.0807
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1646 THROUGH 1726 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.1846 54.3374 7.4179
REMARK 3 T TENSOR
REMARK 3 T11: 0.0963 T22: 0.0971
REMARK 3 T33: 0.1405 T12: -0.0137
REMARK 3 T13: 0.0152 T23: 0.0082
REMARK 3 L TENSOR
REMARK 3 L11: 1.1891 L22: 1.9301
REMARK 3 L33: 2.1630 L12: 0.0114
REMARK 3 L13: 0.5832 L23: -0.0802
REMARK 3 S TENSOR
REMARK 3 S11: -0.0041 S12: 0.0413 S13: -0.0843
REMARK 3 S21: 0.0969 S22: 0.0092 S23: 0.1289
REMARK 3 S31: 0.1020 S32: 0.0041 S33: -0.0531
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 : 2479
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5V3W 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_1000226793.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-DEC-12
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 : 58556
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.720
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 (%) : 99.8
REMARK 200 DATA REDUNDANCY : 7.700
REMARK 200 R MERGE (I) : 0.08900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.72
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.75
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 6.40
REMARK 200 R MERGE FOR SHELL (I) : 0.54800
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: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3TEJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.95
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 44.33300
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 53.45650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 44.33300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 53.45650
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 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 THR B 1589
REMARK 465 PHE B 1590
REMARK 465 ASN B 1591
REMARK 465 VAL B 1592
REMARK 465 THR B 1593
REMARK 465 ILE B 1594
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 A1600 CG CD OE1 OE2
REMARK 470 GLN A1647 CG CD OE1 NE2
REMARK 470 MET A1669 CG SD CE
REMARK 470 THR A1727 OG1 CG2
REMARK 470 GLN B1451 CG CD OE1 NE2
REMARK 470 GLU B1464 CG CD OE1 OE2
REMARK 470 GLU B1573 CG CD OE1 OE2
REMARK 470 ARG B1576 CG CD NE CZ NH1 NH2
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 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 VAL B1623 CG1 CG2
REMARK 470 GLN B1624 CG CD OE1 NE2
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 1661 O HOH A 1901 1.89
REMARK 500 O HOH A 1985 O HOH A 2143 2.08
REMARK 500 O HOH B 1940 O HOH B 2091 2.12
REMARK 500 O HOH B 1903 O HOH B 1940 2.18
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 O HOH A 2000 O HOH B 2084 2565 2.03
REMARK 500 O HOH B 1948 O HOH B 2085 2665 2.18
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 -132.30 60.98
REMARK 500 GLN A1570 71.87 -103.10
REMARK 500 ALA A1596 128.05 -38.92
REMARK 500 SER B1533 -132.76 62.20
REMARK 500 GLN B1570 68.95 -102.57
REMARK 500 GLN B1624 70.57 -113.61
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 A2154 DISTANCE = 6.47 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 2Q5 A 1801
REMARK 610 2Q5 B 1801
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 2Q5 A 1801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 2Q5 B 1801
REMARK 900
REMARK 900 RELATED ENTRIES
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
REMARK 900 RELATED ID: 5V42 RELATED DB: PDB
DBREF1 5V3W A 1451 1733 UNP A0A0T9CRX1_MYCTX
DBREF2 5V3W A A0A0T9CRX1 113 395
DBREF1 5V3W B 1451 1733 UNP A0A0T9CRX1_MYCTX
DBREF2 5V3W B A0A0T9CRX1 113 395
SEQADV 5V3W SER A 1448 UNP A0A0T9CRX EXPRESSION TAG
SEQADV 5V3W ASN A 1449 UNP A0A0T9CRX EXPRESSION TAG
SEQADV 5V3W ALA A 1450 UNP A0A0T9CRX EXPRESSION TAG
SEQADV 5V3W SER B 1448 UNP A0A0T9CRX EXPRESSION TAG
SEQADV 5V3W ASN B 1449 UNP A0A0T9CRX EXPRESSION TAG
SEQADV 5V3W 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 2Q5 A1801 10
HET 2Q5 B1801 13
HETNAM 2Q5 (2R)-2-{[(2R)-2-{[(2S)-2-{[(2R)-2-
HETNAM 2 2Q5 HYDROXYPROPYL]OXY}PROPYL]OXY}PROPYL]OXY}PROPAN-1-OL
FORMUL 3 2Q5 2(C12 H26 O5)
FORMUL 5 HOH *471(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 ILE A 1643 1 18
HELIX 9 AA9 ASP A 1644 ALA A 1646 5 3
HELIX 10 AB1 HIS A 1664 GLU A 1671 1 8
HELIX 11 AB2 PRO A 1672 VAL A 1676 5 5
HELIX 12 AB3 GLU A 1698 ALA A 1702 5 5
HELIX 13 AB4 ILE A 1707 THR A 1727 1 21
HELIX 14 AB5 SER B 1480 VAL B 1483 5 4
HELIX 15 AB6 TYR B 1484 ARG B 1490 1 7
HELIX 16 AB7 SER B 1506 GLY B 1523 1 18
HELIX 17 AB8 SER B 1533 LEU B 1549 1 17
HELIX 18 AB9 THR B 1571 LYS B 1588 1 18
HELIX 19 AC1 PRO B 1598 GLU B 1603 1 6
HELIX 20 AC2 ASP B 1606 SER B 1621 1 16
HELIX 21 AC3 PRO B 1626 ILE B 1643 1 18
HELIX 22 AC4 ASP B 1644 ALA B 1646 5 3
HELIX 23 AC5 HIS B 1664 GLU B 1671 1 8
HELIX 24 AC6 PRO B 1672 VAL B 1676 5 5
HELIX 25 AC7 GLU B 1698 ALA B 1702 5 5
HELIX 26 AC8 PRO B 1706 ARG B 1726 1 21
SHEET 1 AA1 8 ILE A1452 ASP A1453 0
SHEET 2 AA1 8 VAL A1456 ARG A1460 -1 O VAL A1456 N ASP A1453
SHEET 3 AA1 8 MET A1497 PHE A1500 -1 O GLY A1499 N ARG A1457
SHEET 4 AA1 8 VAL A1471 PHE A1474 1 N VAL A1473 O PHE A1500
SHEET 5 AA1 8 TYR A1527 TRP A1532 1 O VAL A1530 N PHE A1472
SHEET 6 AA1 8 VAL A1553 ILE A1559 1 O ILE A1559 N GLY A1531
SHEET 7 AA1 8 VAL A1655 MET A1659 1 O THR A1656 N VAL A1556
SHEET 8 AA1 8 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 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 2.07
CISPEP 2 GLU A 1705 PRO A 1706 0 3.39
CISPEP 3 GLY B 1525 PRO B 1526 0 2.13
CISPEP 4 GLU B 1705 PRO B 1706 0 3.94
SITE 1 AC1 10 SER A1533 ASP A1560 ALA A1561 VAL A1562
SITE 2 AC1 10 ASN A1640 ILE A1643 TYR A1663 TYR A1674
SITE 3 AC1 10 HIS A1699 HOH A1985
SITE 1 AC2 11 SER B1533 VAL B1537 ASP B1560 ALA B1561
SITE 2 AC2 11 ASN B1640 TYR B1663 HIS B1664 ALA B1667
SITE 3 AC2 11 TYR B1674 HIS B1699 HOH B1902
CRYST1 88.666 106.913 57.815 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 0.011278 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009353 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017297 0.00000
TER 2161 THR A1727
TER 4229 ARG B1726
MASTER 461 0 2 26 16 0 6 6 4721 2 23 44
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