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HEADER BIOSYNTHETIC PROTEIN 09-AUG-23 8TR4
TITLE CRYSTAL STRUCTURE OF MTB PKS13 THIOESTERASE DOMAIN IN COMPLEX WITH
TITLE 2 INHIBITOR X20404
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYKETIDE SYNTHASE PKS13;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: TERMINATION POLYKETIDE SYNTHASE;
COMPND 5 EC: 2.3.1.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 GENE: PKS13, RV3800C;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS POLYKETIDE SYNTHASE, THIOESTERASE, BIOSYNTHETIC PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR I.V.KRIEGER,J.C.SACCHETTINI
REVDAT 1 24-APR-24 8TR4 0
JRNL AUTH I.V.KRIEGER,S.YALAMANCHILI,P.DICKSON,C.A.ENGELHART,
JRNL AUTH 2 M.D.ZIMMERMAN,J.WOOD,E.CLARY,J.NGUYEN,N.THORNTON,
JRNL AUTH 3 P.A.CENTRELLA,B.CHAN,J.W.CUOZZO,M.GENGENBACHER,M.A.GUIE,
JRNL AUTH 4 J.P.GUILINGER,C.BIENSTOCK,H.HARTL,C.D.HUPP,R.JETSON,T.SATOH,
JRNL AUTH 5 J.T.S.YEOMAN,Y.ZHANG,V.DARTOIS,D.SCHNAPPINGER,A.D.KEEFE,
JRNL AUTH 6 J.C.SACCHETTINI
JRNL TITL INHIBITORS OF THE THIOESTERASE ACTIVITY OF MYCOBACTERIUM
JRNL TITL 2 TUBERCULOSIS PKS13 DISCOVERED USING DNA-ENCODED CHEMICAL
JRNL TITL 3 LIBRARY SCREENING.
JRNL REF ACS INFECT DIS. 2024
JRNL REFN ESSN 2373-8227
JRNL PMID 38577994
JRNL DOI 10.1021/ACSINFECDIS.3C00592
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PDB-REDO
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.37
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 91.4
REMARK 3 NUMBER OF REFLECTIONS : 28866
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1511
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 67.36
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1544
REMARK 3 BIN R VALUE (WORKING SET) : 0.2760
REMARK 3 BIN FREE R VALUE : 0.3340
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 76
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4292
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 98
REMARK 3 SOLVENT ATOMS : 272
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.25000
REMARK 3 B22 (A**2) : -0.39000
REMARK 3 B33 (A**2) : 0.14000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: U VALUES : WITH TLS ADDED
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 3 U VALUES : RESIDUAL ONLY
REMARK 4
REMARK 4 8TR4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-AUG-23.
REMARK 100 THE DEPOSITION ID IS D_1000276489.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-DEC-20
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 : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00003
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30403
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 48.370
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.1
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.08800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.16
REMARK 200 COMPLETENESS FOR SHELL (%) : 68.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.60
REMARK 200 R MERGE FOR SHELL (I) : 0.64800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.67
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, HANGING
REMARK 280 DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21
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,Y+1/2,-Z+1/2
REMARK 290 4555 -X,-Y+1/2,Z+1/2
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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.79600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 54.69100
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.79600
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 54.69100
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 VAL A 1592
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 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 -136.53 66.38
REMARK 500 GLN A1570 63.62 -105.44
REMARK 500 THR A1589 -128.57 -73.98
REMARK 500 ALA A1596 96.16 -42.55
REMARK 500 ILE A1597 119.67 -17.10
REMARK 500 SER B1533 -137.25 67.19
REMARK 500 GLN B1570 64.14 -106.82
REMARK 500 ALA B1596 95.27 167.53
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A1460 0.09 SIDE CHAIN
REMARK 500 ARG A1502 0.10 SIDE CHAIN
REMARK 500 ARG A1548 0.09 SIDE CHAIN
REMARK 500 ARG A1554 0.09 SIDE CHAIN
REMARK 500 ARG A1576 0.08 SIDE CHAIN
REMARK 500 ARG A1612 0.11 SIDE CHAIN
REMARK 500 ARG B1460 0.08 SIDE CHAIN
REMARK 500 ARG B1502 0.10 SIDE CHAIN
REMARK 500 ARG B1548 0.20 SIDE CHAIN
REMARK 500 ARG B1554 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 8TQG RELATED DB: PDB
REMARK 900 RELATED ID: 8TQV RELATED DB: PDB
DBREF 8TR4 A 1451 1733 UNP I6X8D2 PKS13_MYCTU 1451 1733
DBREF 8TR4 B 1451 1733 UNP I6X8D2 PKS13_MYCTU 1451 1733
SEQADV 8TR4 SER A 1448 UNP I6X8D2 EXPRESSION TAG
SEQADV 8TR4 ASN A 1449 UNP I6X8D2 EXPRESSION TAG
SEQADV 8TR4 ALA A 1450 UNP I6X8D2 EXPRESSION TAG
SEQADV 8TR4 SER B 1448 UNP I6X8D2 EXPRESSION TAG
SEQADV 8TR4 ASN B 1449 UNP I6X8D2 EXPRESSION TAG
SEQADV 8TR4 ALA B 1450 UNP I6X8D2 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 K6C A1801 34
HET SO4 A1802 5
HET SO4 A1803 5
HET SO4 A1804 5
HET SO4 A1805 5
HET K6C B1801 34
HET SO4 B1802 5
HET SO4 B1803 5
HETNAM K6C 4-(2-{(4M)-4-[(6M)-6-(2,5-DIMETHOXYPHENYL)PYRIDIN-3-
HETNAM 2 K6C YL]-1H-1,2,3-TRIAZOL-1-YL}ETHYL)-N,N-DIMETHYLBENZAMIDE
HETNAM SO4 SULFATE ION
FORMUL 3 K6C 2(C26 H27 N5 O3)
FORMUL 4 SO4 6(O4 S 2-)
FORMUL 11 HOH *272(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 THR A 1589 1 19
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 ALA A 1642 1 17
HELIX 9 AA9 ILE A 1643 ALA A 1646 5 4
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 ARG A 1726 1 20
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 ALA B 1642 1 17
HELIX 22 AC4 ILE B 1643 ALA B 1646 5 4
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 ILE B 1707 ARG B 1726 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 GLY A1557 N LEU A1529
SHEET 7 AA1 8 VAL A1655 MET A1659 1 O TYR A1658 N LEU A1558
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 GLY B1557 N LEU B1529
SHEET 7 AA2 8 VAL B1655 MET B1659 1 O TYR B1658 N LEU B1558
SHEET 8 AA2 8 LEU B1690 PRO B1694 1 O GLU B1691 N VAL B1655
CISPEP 1 GLY A 1525 PRO A 1526 0 0.24
CISPEP 2 GLU A 1705 PRO A 1706 0 -0.99
CISPEP 3 GLU B 1705 PRO B 1706 0 -2.05
CRYST1 57.942 87.592 109.382 90.00 90.00 90.00 P 2 21 21 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 0.017259 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011417 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009142 0.00000
TER 2179 THR A1727
TER 4315 ARG B1726
MASTER 296 0 8 26 16 0 0 6 4662 2 98 44
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