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HEADER TRANSFERASE 28-SEP-21 7VJT
TITLE CRYSTAL STRUCTURE OF MTB PKS13-TE IN COMPLEX WITH INHIBITOR COUMESTAN
TITLE 2 DERIVATIVE 8
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYKETIDE SYNTHASE PKS13 (TERMINATION POLYKETIDE
COMPND 3 SYNTHASE);
COMPND 4 CHAIN: A, B;
COMPND 5 EC: 2.7.7.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 GENE: PKS, ERS007688_02231;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TUBERCULOSIS, MYCOBACTERIUM TUBERCULOSIS, ANTIBIOTIC, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.ZHANG,S.S.WANG,L.F.YU
REVDAT 4 29-NOV-23 7VJT 1 REMARK
REVDAT 3 26-OCT-22 7VJT 1 JRNL
REVDAT 2 19-OCT-22 7VJT 1 JRNL
REVDAT 1 28-SEP-22 7VJT 0
JRNL AUTH W.ZHANG,S.LUN,S.S.WANG,Y.P.CAI,F.YANG,J.TANG,W.R.BISHAI,
JRNL AUTH 2 L.F.YU
JRNL TITL STRUCTURE-BASED OPTIMIZATION OF COUMESTAN DERIVATIVES AS
JRNL TITL 2 POLYKETIDE SYNTHASE 13-THIOESTERASE(PKS13-TE) INHIBITORS
JRNL TITL 3 WITH IMPROVED HERG PROFILES FOR MYCOBACTERIUM TUBERCULOSIS
JRNL TITL 4 TREATMENT.
JRNL REF J.MED.CHEM. V. 65 13240 2022
JRNL REFN ISSN 0022-2623
JRNL PMID 36174223
JRNL DOI 10.1021/ACS.JMEDCHEM.2C01064
REMARK 2
REMARK 2 RESOLUTION. 1.94 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 7.1
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.94
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 81.91
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 39170
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 1974
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4264
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 54
REMARK 3 SOLVENT ATOMS : 196
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.43
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.220
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; 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 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 7VJT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-OCT-21.
REMARK 100 THE DEPOSITION ID IS D_1300024820.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-NOV-20
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : ADSC QUANTUM 315R
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39267
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.940
REMARK 200 RESOLUTION RANGE LOW (A) : 81.910
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 6.000
REMARK 200 R MERGE (I) : 0.12100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.94
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.98
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.38500
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: REFMAC
REMARK 200 STARTING MODEL: 5V3Y
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM AMMONIUM ACETATE, 100 MM SODIUM
REMARK 280 ACETATE TRIHYDRATE (PH 4.6), AND 30% (W/V) POLYETHYLENE GLYCOL
REMARK 280 4000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291.2K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 1 2 1
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+1/2
REMARK 290 4555 -X+1/2,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 27.99965
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 19.21500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 79.04314
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 27.99965
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 19.21500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 79.04314
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 1443
REMARK 465 ASN A 1444
REMARK 465 ILE A 1445
REMARK 465 GLY A 1446
REMARK 465 SER A 1447
REMARK 465 GLY A 1448
REMARK 465 GLY A 1449
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 1443
REMARK 465 ASN B 1444
REMARK 465 ILE B 1445
REMARK 465 GLY B 1446
REMARK 465 SER B 1447
REMARK 465 GLY B 1448
REMARK 465 GLY B 1449
REMARK 465 SER B 1450
REMARK 465 GLN B 1620
REMARK 465 SER B 1621
REMARK 465 GLY B 1622
REMARK 465 VAL B 1623
REMARK 465 GLN B 1624
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 SER A1450 OG
REMARK 470 GLN A1451 CG CD OE1 NE2
REMARK 470 GLU A1464 CG CD OE1 OE2
REMARK 470 GLN A1570 CG CD OE1 NE2
REMARK 470 LYS A1572 NZ
REMARK 470 LYS A1588 CD CE NZ
REMARK 470 GLU A1604 CG CD OE1 OE2
REMARK 470 ARG A1612 CG CD NE CZ NH1 NH2
REMARK 470 GLU A1685 CG CD OE1 OE2
REMARK 470 THR A1727 OG1 CG2
REMARK 470 GLU B1464 CG CD OE1 OE2
REMARK 470 GLU B1608 CG CD OE1 OE2
REMARK 470 ARG B1612 CG CD NE CZ NH1 NH2
REMARK 470 LEU B1615 CG CD1 CD2
REMARK 470 ASP B1616 CG OD1 OD2
REMARK 470 ILE B1625 CG1 CG2 CD1
REMARK 470 GLU B1713 CD OE1 OE2
REMARK 470 THR B1727 OG1 CG2
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 A1578 NE - CZ - NH1 ANGL. DEV. = 3.1 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 -130.53 57.53
REMARK 500 GLN A1570 77.38 -106.57
REMARK 500 SER B1533 -134.37 59.01
REMARK 500 GLN B1570 75.74 -106.49
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 7VJT A 1451 1733 UNP A0A654TNE3_MYCTX
DBREF2 7VJT A A0A654TNE3 335 617
DBREF1 7VJT B 1451 1733 UNP A0A654TNE3_MYCTX
DBREF2 7VJT B A0A654TNE3 335 617
SEQADV 7VJT SER A 1443 UNP A0A654TNE EXPRESSION TAG
SEQADV 7VJT ASN A 1444 UNP A0A654TNE EXPRESSION TAG
SEQADV 7VJT ILE A 1445 UNP A0A654TNE EXPRESSION TAG
SEQADV 7VJT GLY A 1446 UNP A0A654TNE EXPRESSION TAG
SEQADV 7VJT SER A 1447 UNP A0A654TNE EXPRESSION TAG
SEQADV 7VJT GLY A 1448 UNP A0A654TNE EXPRESSION TAG
SEQADV 7VJT GLY A 1449 UNP A0A654TNE EXPRESSION TAG
SEQADV 7VJT SER A 1450 UNP A0A654TNE EXPRESSION TAG
SEQADV 7VJT SER B 1443 UNP A0A654TNE EXPRESSION TAG
SEQADV 7VJT ASN B 1444 UNP A0A654TNE EXPRESSION TAG
SEQADV 7VJT ILE B 1445 UNP A0A654TNE EXPRESSION TAG
SEQADV 7VJT GLY B 1446 UNP A0A654TNE EXPRESSION TAG
SEQADV 7VJT SER B 1447 UNP A0A654TNE EXPRESSION TAG
SEQADV 7VJT GLY B 1448 UNP A0A654TNE EXPRESSION TAG
SEQADV 7VJT GLY B 1449 UNP A0A654TNE EXPRESSION TAG
SEQADV 7VJT SER B 1450 UNP A0A654TNE EXPRESSION TAG
SEQRES 1 A 291 SER ASN ILE GLY SER GLY GLY SER GLN ILE ASP GLY PHE
SEQRES 2 A 291 VAL ARG THR LEU ARG ALA ARG PRO GLU ALA GLY GLY LYS
SEQRES 3 A 291 VAL PRO VAL PHE VAL PHE HIS PRO ALA GLY GLY SER THR
SEQRES 4 A 291 VAL VAL TYR GLU PRO LEU LEU GLY ARG LEU PRO ALA ASP
SEQRES 5 A 291 THR PRO MET TYR GLY PHE GLU ARG VAL GLU GLY SER ILE
SEQRES 6 A 291 GLU GLU ARG ALA GLN GLN TYR VAL PRO LYS LEU ILE GLU
SEQRES 7 A 291 MET GLN GLY ASP GLY PRO TYR VAL LEU VAL GLY TRP SER
SEQRES 8 A 291 LEU GLY GLY VAL LEU ALA TYR ALA CYS ALA ILE GLY LEU
SEQRES 9 A 291 ARG ARG LEU GLY LYS ASP VAL ARG PHE VAL GLY LEU ILE
SEQRES 10 A 291 ASP ALA VAL ARG ALA GLY GLU GLU ILE PRO GLN THR LYS
SEQRES 11 A 291 GLU GLU ILE ARG LYS ARG TRP ASP ARG TYR ALA ALA PHE
SEQRES 12 A 291 ALA GLU LYS THR PHE ASN VAL THR ILE PRO ALA ILE PRO
SEQRES 13 A 291 TYR GLU GLN LEU GLU GLU LEU ASP ASP GLU GLY GLN VAL
SEQRES 14 A 291 ARG PHE VAL LEU ASP ALA VAL SER GLN SER GLY VAL GLN
SEQRES 15 A 291 ILE PRO ALA GLY ILE ILE GLU HIS GLN ARG THR SER TYR
SEQRES 16 A 291 LEU ASP ASN ARG ALA ILE ASP THR ALA GLN ILE GLN PRO
SEQRES 17 A 291 TYR ASP GLY HIS VAL THR LEU TYR MET ALA ASP ARG TYR
SEQRES 18 A 291 HIS ASP ASP ALA ILE MET PHE GLU PRO ARG TYR ALA VAL
SEQRES 19 A 291 ARG GLN PRO ASP GLY GLY TRP GLY GLU TYR VAL SER ASP
SEQRES 20 A 291 LEU GLU VAL VAL PRO ILE GLY GLY GLU HIS ILE GLN ALA
SEQRES 21 A 291 ILE ASP GLU PRO ILE ILE ALA LYS VAL GLY GLU HIS MET
SEQRES 22 A 291 SER ARG ALA LEU GLY GLN ILE GLU ALA ASP ARG THR SER
SEQRES 23 A 291 GLU VAL GLY LYS GLN
SEQRES 1 B 291 SER ASN ILE GLY SER GLY GLY SER GLN ILE ASP GLY PHE
SEQRES 2 B 291 VAL ARG THR LEU ARG ALA ARG PRO GLU ALA GLY GLY LYS
SEQRES 3 B 291 VAL PRO VAL PHE VAL PHE HIS PRO ALA GLY GLY SER THR
SEQRES 4 B 291 VAL VAL TYR GLU PRO LEU LEU GLY ARG LEU PRO ALA ASP
SEQRES 5 B 291 THR PRO MET TYR GLY PHE GLU ARG VAL GLU GLY SER ILE
SEQRES 6 B 291 GLU GLU ARG ALA GLN GLN TYR VAL PRO LYS LEU ILE GLU
SEQRES 7 B 291 MET GLN GLY ASP GLY PRO TYR VAL LEU VAL GLY TRP SER
SEQRES 8 B 291 LEU GLY GLY VAL LEU ALA TYR ALA CYS ALA ILE GLY LEU
SEQRES 9 B 291 ARG ARG LEU GLY LYS ASP VAL ARG PHE VAL GLY LEU ILE
SEQRES 10 B 291 ASP ALA VAL ARG ALA GLY GLU GLU ILE PRO GLN THR LYS
SEQRES 11 B 291 GLU GLU ILE ARG LYS ARG TRP ASP ARG TYR ALA ALA PHE
SEQRES 12 B 291 ALA GLU LYS THR PHE ASN VAL THR ILE PRO ALA ILE PRO
SEQRES 13 B 291 TYR GLU GLN LEU GLU GLU LEU ASP ASP GLU GLY GLN VAL
SEQRES 14 B 291 ARG PHE VAL LEU ASP ALA VAL SER GLN SER GLY VAL GLN
SEQRES 15 B 291 ILE PRO ALA GLY ILE ILE GLU HIS GLN ARG THR SER TYR
SEQRES 16 B 291 LEU ASP ASN ARG ALA ILE ASP THR ALA GLN ILE GLN PRO
SEQRES 17 B 291 TYR ASP GLY HIS VAL THR LEU TYR MET ALA ASP ARG TYR
SEQRES 18 B 291 HIS ASP ASP ALA ILE MET PHE GLU PRO ARG TYR ALA VAL
SEQRES 19 B 291 ARG GLN PRO ASP GLY GLY TRP GLY GLU TYR VAL SER ASP
SEQRES 20 B 291 LEU GLU VAL VAL PRO ILE GLY GLY GLU HIS ILE GLN ALA
SEQRES 21 B 291 ILE ASP GLU PRO ILE ILE ALA LYS VAL GLY GLU HIS MET
SEQRES 22 B 291 SER ARG ALA LEU GLY GLN ILE GLU ALA ASP ARG THR SER
SEQRES 23 B 291 GLU VAL GLY LYS GLN
HET 7IJ A1801 27
HET 7IJ B1801 27
HETNAM 7IJ 3,8-BIS(OXIDANYL)-7-(PIPERIDIN-1-YLMETHYL)-
HETNAM 2 7IJ [1]BENZOFURO[3,2-C]CHROMEN-6-ONE
FORMUL 3 7IJ 2(C21 H19 N O5)
FORMUL 5 HOH *196(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 LEU A 1605 5 8
HELIX 7 AA7 ASP A 1606 GLY A 1622 1 17
HELIX 8 AA8 PRO A 1626 ALA A 1646 1 21
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 ASN B 1591 1 21
HELIX 18 AB9 PRO B 1598 LEU B 1602 5 5
HELIX 19 AC1 ASP B 1606 SER B 1619 1 14
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 ILE B 1700 ASP B 1704 5 5
HELIX 24 AC6 PRO B 1706 THR B 1727 1 22
SHEET 1 AA1 8 GLN A1451 ASP A1453 0
SHEET 2 AA1 8 VAL A1456 ARG A1460 -1 O THR A1458 N GLN A1451
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 TYR A1651 MET A1659 1 O THR A1656 N LEU A1558
SHEET 8 AA1 8 VAL A1687 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 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 -0.90
CISPEP 2 GLU A 1705 PRO A 1706 0 0.53
CISPEP 3 GLY B 1525 PRO B 1526 0 0.36
CISPEP 4 GLU B 1705 PRO B 1706 0 -1.09
CRYST1 86.900 38.430 161.078 90.00 101.06 90.00 I 1 2 1 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 0.011508 0.000000 0.002248 0.00000
SCALE2 0.000000 0.026021 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006326 0.00000
TER 2151 THR A1727
TER 4266 THR B1727
MASTER 299 0 2 24 16 0 0 6 4514 2 54 46
END |