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HEADER BIOSYNTHETIC PROTEIN 08-AUG-23 8TQV
TITLE CRYSTAL STRUCTURE OF MTB PKS13 THIOESTERASE DOMAIN IN COMPLEX WITH
TITLE 2 INHIBITOR X20403
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYKETIDE SYNTHASE PKS13;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.3.1.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS H37RV;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: ATCC 25618 / H37RV;
SOURCE 5 GENE: PKS13;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 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 8TQV 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. 2.00 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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.49
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) (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 43951
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) : 0.224
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2277
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.91
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3227
REMARK 3 BIN R VALUE (WORKING SET) : 0.3750
REMARK 3 BIN FREE R VALUE : 0.4020
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 180
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 : 4218
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 100
REMARK 3 SOLVENT ATOMS : 91
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 65.19
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.31000
REMARK 3 B22 (A**2) : 0.05000
REMARK 3 B33 (A**2) : 0.25000
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 8TQV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-AUG-23.
REMARK 100 THE DEPOSITION ID IS D_1000276470.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-SEP-21
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) : 1.03317
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46267
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 47.490
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.20
REMARK 200 R MERGE FOR SHELL (I) : 1.12800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.300
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 (%): 56.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84
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 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-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 62.35150
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 62.35150
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
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 ILE A 1452
REMARK 465 ASP A 1453
REMARK 465 PRO A 1598
REMARK 465 TYR A 1599
REMARK 465 GLU A 1600
REMARK 465 GLN A 1601
REMARK 465 TYR B 1599
REMARK 465 GLU B 1600
REMARK 465 GLN B 1601
REMARK 465 LEU B 1602
REMARK 465 GLU B 1603
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 ARG A1612 CG CD NE CZ NH1 NH2
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 -129.44 63.41
REMARK 500 GLN A1570 60.80 -112.40
REMARK 500 SER B1533 -129.45 62.88
REMARK 500 GLN B1570 59.72 -112.37
REMARK 500 ASP B1689 79.90 -110.08
REMARK 500 ASP B1725 54.85 -111.99
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 A1554 0.08 SIDE CHAIN
REMARK 500 ARG A1641 0.07 SIDE CHAIN
REMARK 500 ARG B1581 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 8TQV A 1452 1726 UNP I6X8D2 PKS13_MYCTU 1452 1726
DBREF 8TQV B 1452 1726 UNP I6X8D2 PKS13_MYCTU 1452 1726
SEQRES 1 A 275 ILE ASP GLY PHE VAL ARG THR LEU ARG ALA ARG PRO GLU
SEQRES 2 A 275 ALA GLY GLY LYS VAL PRO VAL PHE VAL PHE HIS PRO ALA
SEQRES 3 A 275 GLY GLY SER THR VAL VAL TYR GLU PRO LEU LEU GLY ARG
SEQRES 4 A 275 LEU PRO ALA ASP THR PRO MET TYR GLY PHE GLU ARG VAL
SEQRES 5 A 275 GLU GLY SER ILE GLU GLU ARG ALA GLN GLN TYR VAL PRO
SEQRES 6 A 275 LYS LEU ILE GLU MET GLN GLY ASP GLY PRO TYR VAL LEU
SEQRES 7 A 275 VAL GLY TRP SER LEU GLY GLY VAL LEU ALA TYR ALA CYS
SEQRES 8 A 275 ALA ILE GLY LEU ARG ARG LEU GLY LYS ASP VAL ARG PHE
SEQRES 9 A 275 VAL GLY LEU ILE ASP ALA VAL ARG ALA GLY GLU GLU ILE
SEQRES 10 A 275 PRO GLN THR LYS GLU GLU ILE ARG LYS ARG TRP ASP ARG
SEQRES 11 A 275 TYR ALA ALA PHE ALA GLU LYS THR PHE ASN VAL THR ILE
SEQRES 12 A 275 PRO ALA ILE PRO TYR GLU GLN LEU GLU GLU LEU ASP ASP
SEQRES 13 A 275 GLU GLY GLN VAL ARG PHE VAL LEU ASP ALA VAL SER GLN
SEQRES 14 A 275 SER GLY VAL GLN ILE PRO ALA GLY ILE ILE GLU HIS GLN
SEQRES 15 A 275 ARG THR SER TYR LEU ASP ASN ARG ALA ILE ASP THR ALA
SEQRES 16 A 275 GLN ILE GLN PRO TYR ASP GLY HIS VAL THR LEU TYR MET
SEQRES 17 A 275 ALA ASP ARG TYR HIS ASP ASP ALA ILE MET PHE GLU PRO
SEQRES 18 A 275 ARG TYR ALA VAL ARG GLN PRO ASP GLY GLY TRP GLY GLU
SEQRES 19 A 275 TYR VAL SER ASP LEU GLU VAL VAL PRO ILE GLY GLY GLU
SEQRES 20 A 275 HIS ILE GLN ALA ILE ASP GLU PRO ILE ILE ALA LYS VAL
SEQRES 21 A 275 GLY GLU HIS MET SER ARG ALA LEU GLY GLN ILE GLU ALA
SEQRES 22 A 275 ASP ARG
SEQRES 1 B 275 ILE ASP GLY PHE VAL ARG THR LEU ARG ALA ARG PRO GLU
SEQRES 2 B 275 ALA GLY GLY LYS VAL PRO VAL PHE VAL PHE HIS PRO ALA
SEQRES 3 B 275 GLY GLY SER THR VAL VAL TYR GLU PRO LEU LEU GLY ARG
SEQRES 4 B 275 LEU PRO ALA ASP THR PRO MET TYR GLY PHE GLU ARG VAL
SEQRES 5 B 275 GLU GLY SER ILE GLU GLU ARG ALA GLN GLN TYR VAL PRO
SEQRES 6 B 275 LYS LEU ILE GLU MET GLN GLY ASP GLY PRO TYR VAL LEU
SEQRES 7 B 275 VAL GLY TRP SER LEU GLY GLY VAL LEU ALA TYR ALA CYS
SEQRES 8 B 275 ALA ILE GLY LEU ARG ARG LEU GLY LYS ASP VAL ARG PHE
SEQRES 9 B 275 VAL GLY LEU ILE ASP ALA VAL ARG ALA GLY GLU GLU ILE
SEQRES 10 B 275 PRO GLN THR LYS GLU GLU ILE ARG LYS ARG TRP ASP ARG
SEQRES 11 B 275 TYR ALA ALA PHE ALA GLU LYS THR PHE ASN VAL THR ILE
SEQRES 12 B 275 PRO ALA ILE PRO TYR GLU GLN LEU GLU GLU LEU ASP ASP
SEQRES 13 B 275 GLU GLY GLN VAL ARG PHE VAL LEU ASP ALA VAL SER GLN
SEQRES 14 B 275 SER GLY VAL GLN ILE PRO ALA GLY ILE ILE GLU HIS GLN
SEQRES 15 B 275 ARG THR SER TYR LEU ASP ASN ARG ALA ILE ASP THR ALA
SEQRES 16 B 275 GLN ILE GLN PRO TYR ASP GLY HIS VAL THR LEU TYR MET
SEQRES 17 B 275 ALA ASP ARG TYR HIS ASP ASP ALA ILE MET PHE GLU PRO
SEQRES 18 B 275 ARG TYR ALA VAL ARG GLN PRO ASP GLY GLY TRP GLY GLU
SEQRES 19 B 275 TYR VAL SER ASP LEU GLU VAL VAL PRO ILE GLY GLY GLU
SEQRES 20 B 275 HIS ILE GLN ALA ILE ASP GLU PRO ILE ILE ALA LYS VAL
SEQRES 21 B 275 GLY GLU HIS MET SER ARG ALA LEU GLY GLN ILE GLU ALA
SEQRES 22 B 275 ASP ARG
HET JS9 A1801 40
HET SO4 A1802 5
HET SO4 A1803 5
HET JS9 B1801 40
HET SO4 B1802 5
HET SO4 B1803 5
HETNAM JS9 4-(2-{(4M)-4-[(6M)-6-(2,5-DIMETHOXYPHENYL)PYRIDIN-3-
HETNAM 2 JS9 YL]-1H-1,2,3-TRIAZOL-1-YL}ETHYL)-N-{[1-
HETNAM 3 JS9 (METHOXYMETHYL)CYCLOPROPYL]METHYL}-N-METHYLBENZAMIDE
HETNAM SO4 SULFATE ION
FORMUL 3 JS9 2(C31 H35 N5 O4)
FORMUL 4 SO4 4(O4 S 2-)
FORMUL 9 HOH *91(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 ASP A 1606 SER A 1621 1 16
HELIX 7 AA7 PRO A 1626 THR A 1645 1 20
HELIX 8 AA8 HIS A 1664 GLU A 1671 1 8
HELIX 9 AA9 PRO A 1672 VAL A 1676 5 5
HELIX 10 AB1 GLU A 1698 ALA A 1702 5 5
HELIX 11 AB2 ILE A 1707 ALA A 1724 1 18
HELIX 12 AB3 SER B 1480 VAL B 1483 5 4
HELIX 13 AB4 TYR B 1484 ARG B 1490 1 7
HELIX 14 AB5 SER B 1506 GLY B 1523 1 18
HELIX 15 AB6 SER B 1533 LEU B 1549 1 17
HELIX 16 AB7 THR B 1571 ASN B 1591 1 21
HELIX 17 AB8 ASP B 1606 SER B 1621 1 16
HELIX 18 AB9 PRO B 1626 THR B 1645 1 20
HELIX 19 AC1 HIS B 1664 GLU B 1671 1 8
HELIX 20 AC2 PRO B 1672 VAL B 1676 5 5
HELIX 21 AC3 GLU B 1698 ALA B 1702 5 5
HELIX 22 AC4 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 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 GLY A1557 N LEU A1529
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 7 VAL B1456 ARG B1460 0
SHEET 2 AA2 7 MET B1497 PHE B1500 -1 O GLY B1499 N ARG B1457
SHEET 3 AA2 7 VAL B1471 PHE B1474 1 N VAL B1473 O PHE B1500
SHEET 4 AA2 7 TYR B1527 TRP B1532 1 O VAL B1530 N PHE B1472
SHEET 5 AA2 7 VAL B1553 ILE B1559 1 O GLY B1557 N LEU B1529
SHEET 6 AA2 7 VAL B1655 MET B1659 1 O THR B1656 N VAL B1556
SHEET 7 AA2 7 LEU B1690 PRO B1694 1 O GLU B1691 N LEU B1657
CISPEP 1 GLY A 1525 PRO A 1526 0 0.49
CISPEP 2 GLU A 1705 PRO A 1706 0 0.52
CISPEP 3 GLY B 1525 PRO B 1526 0 0.39
CISPEP 4 GLU B 1705 PRO B 1706 0 1.13
CRYST1 64.564 84.505 124.703 90.00 90.00 90.00 P 2 2 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 0.015489 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011834 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008019 0.00000
TER 2104 ARG A1726
TER 4220 ARG B1726
MASTER 275 0 6 22 14 0 0 6 4409 2 100 44
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