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HEADER TRANSFERASE 08-MAR-17 5V3Z
TITLE CRYSTAL STRUCTURE OF THE D1607N MUTANT FORM OF THIOESTERASE DOMAIN OF
TITLE 2 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;
COMPND 8 MUTATION: 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, D1607N MUTANT, PKS13, MYCOBACTERIUM, POLYKETIDE
KEYWDS 2 SYNTHASE, MYCOLIC ACID CONDENSATION, TB STRUCTURAL GENOMICS
KEYWDS 3 CONSORTIUM, TBSGC, ALPHA/BETA HYDROLASE, THIOESTERASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.AGGARWAL,J.C.SACCHETTINI
REVDAT 1 05-JUL-17 5V3Z 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. 1.88 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) : 1.88
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.36
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.4
REMARK 3 NUMBER OF REFLECTIONS : 42931
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 2168
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 44.3763 - 4.6367 0.99 3157 154 0.1836 0.2038
REMARK 3 2 4.6367 - 3.6808 1.00 3000 163 0.1461 0.1855
REMARK 3 3 3.6808 - 3.2157 1.00 2955 168 0.1608 0.2051
REMARK 3 4 3.2157 - 2.9218 1.00 2962 142 0.1718 0.1943
REMARK 3 5 2.9218 - 2.7124 1.00 2941 160 0.1819 0.2530
REMARK 3 6 2.7124 - 2.5525 1.00 2960 149 0.1906 0.2509
REMARK 3 7 2.5525 - 2.4247 1.00 2898 150 0.1899 0.2693
REMARK 3 8 2.4247 - 2.3191 1.00 2943 145 0.2032 0.2784
REMARK 3 9 2.3191 - 2.2298 1.00 2899 159 0.2102 0.2610
REMARK 3 10 2.2298 - 2.1529 0.99 2849 171 0.2229 0.2575
REMARK 3 11 2.1529 - 2.0856 0.94 2742 148 0.2402 0.3180
REMARK 3 12 2.0856 - 2.0260 0.88 2561 132 0.2620 0.3037
REMARK 3 13 2.0260 - 1.9726 0.80 2293 140 0.2917 0.3058
REMARK 3 14 1.9726 - 1.9245 0.69 1985 95 0.3185 0.3634
REMARK 3 15 1.9245 - 1.8808 0.56 1618 92 0.3680 0.3715
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) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.420
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.53
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.36
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 : 0.011 4331
REMARK 3 ANGLE : 1.254 5881
REMARK 3 CHIRALITY : 0.057 636
REMARK 3 PLANARITY : 0.007 782
REMARK 3 DIHEDRAL : 12.974 1580
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1451 THROUGH 1548 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.0326 28.0270 24.9223
REMARK 3 T TENSOR
REMARK 3 T11: 0.1857 T22: 0.1545
REMARK 3 T33: 0.1441 T12: -0.0050
REMARK 3 T13: -0.0449 T23: 0.0088
REMARK 3 L TENSOR
REMARK 3 L11: 3.1142 L22: 3.0776
REMARK 3 L33: 3.2405 L12: 0.2084
REMARK 3 L13: -0.9286 L23: 0.1538
REMARK 3 S TENSOR
REMARK 3 S11: 0.1089 S12: -0.2884 S13: -0.0972
REMARK 3 S21: 0.4303 S22: -0.0253 S23: -0.0328
REMARK 3 S31: 0.1521 S32: 0.1325 S33: -0.0943
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1549 THROUGH 1626 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.4393 25.4625 10.1795
REMARK 3 T TENSOR
REMARK 3 T11: 0.2378 T22: 0.2206
REMARK 3 T33: 0.3407 T12: 0.0111
REMARK 3 T13: 0.0099 T23: -0.0215
REMARK 3 L TENSOR
REMARK 3 L11: 3.9520 L22: 1.3764
REMARK 3 L33: 1.5673 L12: -0.1194
REMARK 3 L13: 1.2542 L23: 0.1893
REMARK 3 S TENSOR
REMARK 3 S11: 0.1460 S12: 0.2193 S13: -0.3417
REMARK 3 S21: 0.0074 S22: -0.0637 S23: 0.4529
REMARK 3 S31: 0.2774 S32: -0.1711 S33: -0.0780
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1627 THROUGH 1726 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.9104 35.5892 13.1445
REMARK 3 T TENSOR
REMARK 3 T11: 0.1558 T22: 0.1588
REMARK 3 T33: 0.1469 T12: 0.0190
REMARK 3 T13: 0.0057 T23: -0.0043
REMARK 3 L TENSOR
REMARK 3 L11: 3.7877 L22: 3.5408
REMARK 3 L33: 1.6283 L12: 0.6816
REMARK 3 L13: 0.2863 L23: -0.3576
REMARK 3 S TENSOR
REMARK 3 S11: 0.0578 S12: -0.0204 S13: 0.2241
REMARK 3 S21: 0.0038 S22: -0.0297 S23: 0.0862
REMARK 3 S31: -0.0516 S32: -0.1423 S33: -0.0244
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1451 THROUGH 1606 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.6830 65.6710 0.1818
REMARK 3 T TENSOR
REMARK 3 T11: 0.1465 T22: 0.1511
REMARK 3 T33: 0.2145 T12: -0.0102
REMARK 3 T13: 0.0075 T23: -0.0057
REMARK 3 L TENSOR
REMARK 3 L11: 1.5544 L22: 2.5540
REMARK 3 L33: 2.8862 L12: -0.2599
REMARK 3 L13: -0.2223 L23: -0.7908
REMARK 3 S TENSOR
REMARK 3 S11: -0.0344 S12: 0.1218 S13: 0.0153
REMARK 3 S21: -0.1965 S22: 0.0845 S23: -0.0196
REMARK 3 S31: 0.0172 S32: 0.1954 S33: -0.0703
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1607 THROUGH 1726 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.8770 61.0178 1.2859
REMARK 3 T TENSOR
REMARK 3 T11: 0.1358 T22: 0.1835
REMARK 3 T33: 0.2869 T12: -0.0202
REMARK 3 T13: 0.0104 T23: -0.0220
REMARK 3 L TENSOR
REMARK 3 L11: 0.6609 L22: 2.7509
REMARK 3 L33: 3.1937 L12: -0.2453
REMARK 3 L13: 0.4633 L23: -1.5023
REMARK 3 S TENSOR
REMARK 3 S11: -0.0208 S12: 0.0772 S13: -0.0397
REMARK 3 S21: -0.0679 S22: 0.1107 S23: 0.2607
REMARK 3 S31: 0.2147 S32: -0.0527 S33: -0.0849
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 : 2246
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5V3Z 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_1000226798.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-MAR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
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 : 43322
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.880
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 (%) : 93.2
REMARK 200 DATA REDUNDANCY : 4.900
REMARK 200 R MERGE (I) : 0.12600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 4.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.88
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.91
REMARK 200 COMPLETENESS FOR SHELL (%) : 59.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.60
REMARK 200 R MERGE FOR SHELL (I) : 0.96100
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 (%): 44.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, 2%-4% V/V PEG400, 1.8-2 M
REMARK 280 AMMONIUM SULFATE, PH 7.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 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 44.35200
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.45200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 44.35200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.45200
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 THR A 1727
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 ASN B 1591
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 LYS A1588 CG CD CE NZ
REMARK 470 GLU A1600 CG CD OE1 OE2
REMARK 470 GLU A1608 CG CD OE1 OE2
REMARK 470 ARG A1612 CG CD NE CZ NH1 NH2
REMARK 470 SER A1621 OG
REMARK 470 GLU A1631 CG CD OE1 OE2
REMARK 470 GLN A1647 CG CD OE1 NE2
REMARK 470 GLU A1685 CG CD OE1 OE2
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 LYS B1577 CG CD CE NZ
REMARK 470 ARG B1581 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 THR B1593 OG1 CG2
REMARK 470 ILE B1594 CG1 CG2 CD1
REMARK 470 ILE B1597 CG1 CG2 CD1
REMARK 470 TYR B1599 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU B1600 CG CD OE1 OE2
REMARK 470 GLN B1620 CG CD OE1 NE2
REMARK 470 GLN B1624 CG CD OE1 NE2
REMARK 470 MET B1669 CG SD CE
REMARK 470 GLU B1713 CG CD OE1 OE2
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 1639 O HOH B 1901 2.14
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 -130.92 58.90
REMARK 500 ASP A1689 70.64 -101.62
REMARK 500 SER B1533 -130.40 57.30
REMARK 500 ASP B1689 72.89 -103.47
REMARK 500 ASP B1725 1.24 -67.48
REMARK 500
REMARK 500 REMARK: NULL
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 1PE A 1801
REMARK 610 1PE B 1802
REMARK 610 1PE B 1803
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 1801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 1801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE B 1802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE B 1803
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: 5V40 RELATED DB: PDB
REMARK 900 RELATED ID: 5V41 RELATED DB: PDB
REMARK 900 RELATED ID: 5V42 RELATED DB: PDB
DBREF1 5V3Z A 1451 1733 UNP A0A0T9CRX1_MYCTX
DBREF2 5V3Z A A0A0T9CRX1 113 395
DBREF1 5V3Z B 1451 1733 UNP A0A0T9CRX1_MYCTX
DBREF2 5V3Z B A0A0T9CRX1 113 395
SEQADV 5V3Z SER A 1448 UNP A0A0T9CRX EXPRESSION TAG
SEQADV 5V3Z ASN A 1449 UNP A0A0T9CRX EXPRESSION TAG
SEQADV 5V3Z ALA A 1450 UNP A0A0T9CRX EXPRESSION TAG
SEQADV 5V3Z ASN A 1607 UNP A0A0T9CRX ASP 269 ENGINEERED MUTATION
SEQADV 5V3Z SER B 1448 UNP A0A0T9CRX EXPRESSION TAG
SEQADV 5V3Z ASN B 1449 UNP A0A0T9CRX EXPRESSION TAG
SEQADV 5V3Z ALA B 1450 UNP A0A0T9CRX EXPRESSION TAG
SEQADV 5V3Z ASN B 1607 UNP A0A0T9CRX ASP 269 ENGINEERED MUTATION
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 ASN 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 ASN 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 1PE A1801 8
HET SO4 B1801 5
HET 1PE B1802 13
HET 1PE B1803 10
HETNAM 1PE PENTAETHYLENE GLYCOL
HETNAM SO4 SULFATE ION
HETSYN 1PE PEG400
FORMUL 3 1PE 3(C10 H22 O6)
FORMUL 4 SO4 O4 S 2-
FORMUL 7 HOH *335(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 1603 1 6
HELIX 7 AA7 ASP A 1606 SER A 1621 1 16
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 PRO A 1706 ARG A 1726 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 THR B 1589 1 19
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 THR B 1645 1 20
HELIX 22 AC4 HIS B 1664 GLU B 1671 1 8
HELIX 23 AC5 PRO B 1672 VAL B 1676 5 5
HELIX 24 AC6 GLU B 1698 ALA B 1702 5 5
HELIX 25 AC7 PRO B 1706 ASP B 1725 1 20
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 TYR A1651 MET A1659 1 O THR A1656 N VAL A1556
SHEET 8 AA1 8 VAL A1687 PRO A1694 1 O VAL A1693 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 TYR B1651 MET B1659 1 O TYR B1658 N LEU B1558
SHEET 8 AA2 8 VAL B1687 PRO B1694 1 O GLU B1691 N LEU B1657
CISPEP 1 GLY A 1525 PRO A 1526 0 1.07
CISPEP 2 GLU A 1705 PRO A 1706 0 2.23
CISPEP 3 GLY B 1525 PRO B 1526 0 -1.49
CISPEP 4 GLU B 1705 PRO B 1706 0 0.63
SITE 1 AC1 9 SER A1533 ALA A1561 ASN A1640 TYR A1663
SITE 2 AC1 9 ALA A1667 PHE A1670 TYR A1674 HIS A1699
SITE 3 AC1 9 HOH A2001
SITE 1 AC2 8 ASP B1606 ASN B1607 GLU B1608 HOH B1911
SITE 2 AC2 8 HOH B1914 HOH B1972 HOH B1977 HOH B1992
SITE 1 AC3 9 ARG B1563 ALA B1564 GLU B1566 GLU B1567
SITE 2 AC3 9 ILE B1643 ALA B1646 ILE B1648 TRP B1683
SITE 3 AC3 9 HOH B1902
SITE 1 AC4 9 SER B1533 ASP B1560 ALA B1561 ASN B1640
SITE 2 AC4 9 ILE B1643 TYR B1663 PHE B1670 HIS B1699
SITE 3 AC4 9 HOH B1909
CRYST1 88.704 108.904 58.057 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 0.011273 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009182 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017224 0.00000
TER 2132 ARG A1726
TER 4214 ARG B1726
MASTER 418 0 4 25 16 0 11 6 4583 2 36 44
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