HEADER TRANSFERASE 06-SEP-07 2VBA
TITLE BETA-KETOACYL-ACP SYNTHASE I (KAS) FROM E. COLI WITH BOUND AMINO-
TITLE 2 THIAZOLE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE 1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: BETA-KETOACYL-ACP SYNTHASE I, 3-OXOACYL-[ACYL-CARRIER-
COMPND 5 PROTEIN] SYNTHASE I, KAS I;
COMPND 6 EC: 2.3.1.41;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: M15;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PQE80
KEYWDS CYTOPLASM, ANTIBIOTIC, TRANSFERASE, AMINO-THIAZOLE, ACYLTRANSFERASE,
KEYWDS 2 LIPID SYNTHESIS, FATTY ACID SYNTHESIS, FATTY ACID BIOSYNTHESIS
EXPDTA X-RAY DIFFRACTION
AUTHOR G.PAPPENBERGER,T.SCHULZ-GASCH,J.BAILLY,M.HENNIG
REVDAT 4 13-DEC-23 2VBA 1 REMARK
REVDAT 3 08-MAY-19 2VBA 1 REMARK
REVDAT 2 24-FEB-09 2VBA 1 VERSN
REVDAT 1 25-DEC-07 2VBA 0
JRNL AUTH G.PAPPENBERGER,T.SCHULZ-GASCH,E.KUSZNIR,F.MUELLER,M.HENNIG
JRNL TITL STRUCTURE-ASSISTED DISCOVERY OF AN AMINOTHIAZOLE DERIVATIVE
JRNL TITL 2 AS A LEAD MOLECULE FOR INHIBITION OF BACTERIAL FATTY-ACID
JRNL TITL 3 SYNTHESIS.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 63 1208 2007
JRNL REFN ISSN 0907-4449
JRNL PMID 18084068
JRNL DOI 10.1107/S0907444907049852
REMARK 2
REMARK 2 RESOLUTION. 1.36 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.36
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.87
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.5
REMARK 3 NUMBER OF REFLECTIONS : 337314
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 + TEST SET) : 0.121
REMARK 3 R VALUE (WORKING SET) : 0.119
REMARK 3 FREE R VALUE : 0.151
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 17776
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) : 1.36
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.39
REMARK 3 REFLECTION IN BIN (WORKING SET) : 17788
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.1310
REMARK 3 BIN FREE R VALUE SET COUNT : 929
REMARK 3 BIN FREE R VALUE : 0.1870
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11768
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 16
REMARK 3 SOLVENT ATOMS : 2431
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.49
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.07000
REMARK 3 B22 (A**2) : 0.37000
REMARK 3 B33 (A**2) : -0.44000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.044
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.044
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.022
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.180
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.977
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.969
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 12150 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 16413 ; 1.581 ; 1.956
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1614 ; 5.875 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 482 ;36.461 ;24.336
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2030 ;12.162 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 66 ;19.045 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1859 ; 0.104 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9120 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 6349 ; 0.208 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 8656 ; 0.312 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 2003 ; 0.175 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 66 ; 0.211 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 93 ; 0.171 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 8111 ; 2.331 ; 0.670
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12679 ; 3.184 ; 1.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4466 ; 2.876 ; 0.670
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3734 ; 3.912 ; 1.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 2VBA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-SEP-07.
REMARK 100 THE DEPOSITION ID IS D_1290033503.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-SEP-05
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 : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97881
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 685131
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.360
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 5.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.3
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.45
REMARK 200 COMPLETENESS FOR SHELL (%) : 72.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.20000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.200
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: PDB ENTRY 1EK4
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALLIZATION CONDITIONS: HANGING
REMARK 280 DROP AGAINST 3% PEG 400, 1.9 M AMMONIUM SULPHATE, 0.1 M TRIS PH
REMARK 280 7.5 SOAK WITH 0.01M LIGAND IN 30% PEG8000, 0.1M AMMONIUM
REMARK 280 SULPHATE, 0.1M TRIS PH7.5, 0.005M TCEP, VAPOR DIFFUSION, HANGING
REMARK 280 DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 29.47500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 106.08500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 69.74000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 106.08500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.47500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 69.74000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 6810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30090 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.4 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 6970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.2 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 LYS A 405
REMARK 465 ASP A 406
REMARK 465 LYS B 405
REMARK 465 ASP B 406
REMARK 465 LYS D 405
REMARK 465 ASP D 406
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 A 62 CD NE CZ NH1 NH2
REMARK 470 LYS A 63 CD CE NZ
REMARK 470 LYS A 127 CD CE NZ
REMARK 470 LYS A 217 CE NZ
REMARK 470 LYS A 308 CE NZ
REMARK 470 GLU A 362 CD OE1 OE2
REMARK 470 GLU A 366 CD OE1 OE2
REMARK 470 GLU A 376 CD OE1 OE2
REMARK 470 GLU A 381 CD OE1 OE2
REMARK 470 LYS B 63 CG CD CE NZ
REMARK 470 LYS B 127 CE NZ
REMARK 470 LYS B 210 CE NZ
REMARK 470 LYS B 217 CE NZ
REMARK 470 LYS B 320 CD CE NZ
REMARK 470 ARG C 30 CZ NH1 NH2
REMARK 470 ARG C 62 CD NE CZ NH1 NH2
REMARK 470 LYS C 63 CD CE NZ
REMARK 470 GLU C 91 CG CD OE1 OE2
REMARK 470 LYS C 127 CE NZ
REMARK 470 LYS C 210 CE NZ
REMARK 470 LYS C 217 CE NZ
REMARK 470 LYS C 320 CG CD CE NZ
REMARK 470 GLU C 366 CD OE1 OE2
REMARK 470 ASP C 406 CB CG OD1 OD2
REMARK 470 GLU D 28 CD OE1 OE2
REMARK 470 ARG D 62 CD NE CZ NH1 NH2
REMARK 470 LYS D 63 CD CE NZ
REMARK 470 LYS D 127 CE NZ
REMARK 470 LYS D 210 CE NZ
REMARK 470 LYS D 217 CE NZ
REMARK 470 ASP D 319 CG OD1 OD2
REMARK 470 LYS D 320 CD CE NZ
REMARK 470 GLU D 366 CG CD OE1 OE2
REMARK 470 GLU D 376 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 NH1 ARG B 27 O HOH B 2095 1.38
REMARK 500 O HOH B 2299 O HOH B 2304 1.88
REMARK 500 O HOH B 2148 O HOH B 2304 1.89
REMARK 500 O HOH A 2011 O HOH A 2271 1.97
REMARK 500 O HOH C 2056 O HOH C 2057 1.98
REMARK 500 OE2 GLU C 200 O HOH C 2404 1.98
REMARK 500 O HOH D 2194 O HOH D 2200 1.99
REMARK 500 O HOH B 2376 O HOH B 2380 2.00
REMARK 500 O HOH A 2118 O HOH A 2278 2.00
REMARK 500 O HOH C 2369 O HOH C 2370 2.01
REMARK 500 OE2 GLU B 200 O HOH B 2379 2.02
REMARK 500 OE2 GLU A 200 OE1 GLN B 113 2.03
REMARK 500 O HOH C 2400 O HOH C 2404 2.04
REMARK 500 O HOH A 2077 O HOH A 2111 2.05
REMARK 500 OG1 THR A 148 O HOH A 2368 2.06
REMARK 500 O HOH A 2224 O HOH A 2353 2.07
REMARK 500 O HOH A 2297 O HOH A 2370 2.08
REMARK 500 O HOH A 2156 O HOH A 2158 2.09
REMARK 500 O HOH B 2193 O HOH B 2321 2.09
REMARK 500 NZ LYS A 151 O HOH A 2372 2.09
REMARK 500 NH1 ARG D 314 O ALA D 369 2.11
REMARK 500 O HOH D 2076 O HOH D 2550 2.12
REMARK 500 O HOH C 2327 O HOH C 2329 2.13
REMARK 500 O HOH A 2472 O HOH B 2353 2.13
REMARK 500 OE2 GLU C 200 NE2 GLN D 113 2.13
REMARK 500 O HOH A 2018 O HOH A 2088 2.14
REMARK 500 O HOH A 2041 O HOH A 2395 2.14
REMARK 500 O HOH C 2083 O HOH C 2595 2.15
REMARK 500 OD1 ASP C 319 O HOH C 2542 2.15
REMARK 500 O HOH C 2126 O HOH C 2378 2.16
REMARK 500 O HOH A 2049 O HOH A 2164 2.16
REMARK 500 O HOH C 2384 O HOH C 2467 2.17
REMARK 500 OE1 GLU A 244 O HOH A 2441 2.18
REMARK 500 O HOH C 2030 O HOH C 2123 2.19
REMARK 500 O HOH B 2058 O HOH B 2106 2.19
REMARK 500 O HOH D 2173 O HOH D 2279 2.19
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 B 2320 O HOH C 2540 4456 2.16
REMARK 500
REMARK 500 REMARK: NULL
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 B 279 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG C 98 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 LEU D 9 CB - CA - C ANGL. DEV. = 11.7 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 LYS A 53 74.68 -100.92
REMARK 500 SER A 161 43.99 -163.51
REMARK 500 ALA A 162 -129.57 53.26
REMARK 500 ARG A 220 54.20 -152.83
REMARK 500 TYR A 222 -8.40 79.23
REMARK 500 ASP A 227 32.10 -147.13
REMARK 500 ALA A 267 -118.96 -140.77
REMARK 500 SER A 301 27.31 88.00
REMARK 500 LYS A 320 52.94 -117.68
REMARK 500 LEU A 335 -115.53 57.97
REMARK 500 ASN A 372 75.69 -111.45
REMARK 500 LYS B 53 75.68 -102.61
REMARK 500 SER B 161 44.27 -165.82
REMARK 500 ALA B 162 -128.20 53.95
REMARK 500 ARG B 220 56.54 -152.48
REMARK 500 TYR B 222 -9.10 78.04
REMARK 500 ASP B 227 29.20 -146.93
REMARK 500 ALA B 267 -83.29 -139.84
REMARK 500 SER B 301 31.59 87.62
REMARK 500 LEU B 335 -114.92 59.91
REMARK 500 SER C 161 43.09 -163.02
REMARK 500 ALA C 162 -128.46 55.53
REMARK 500 ARG C 220 54.27 -156.01
REMARK 500 TYR C 222 -9.27 78.12
REMARK 500 ASP C 227 30.26 -146.91
REMARK 500 ALA C 267 -84.14 -141.83
REMARK 500 SER C 301 31.48 88.59
REMARK 500 LYS C 320 59.13 -118.09
REMARK 500 LEU C 335 -114.00 59.98
REMARK 500 LYS D 53 75.10 -105.23
REMARK 500 SER D 161 43.90 -164.97
REMARK 500 ALA D 162 -127.03 54.59
REMARK 500 ARG D 220 55.33 -155.61
REMARK 500 TYR D 222 -8.64 76.91
REMARK 500 ASP D 227 31.53 -148.14
REMARK 500 ALA D 267 -85.62 -140.59
REMARK 500 SER D 301 32.31 88.93
REMARK 500 LYS D 320 67.73 -110.67
REMARK 500 LEU D 335 -116.45 60.16
REMARK 500 ASN D 372 73.56 -109.74
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 A2030 DISTANCE = 5.92 ANGSTROMS
REMARK 525 HOH A2031 DISTANCE = 6.06 ANGSTROMS
REMARK 525 HOH A2036 DISTANCE = 6.43 ANGSTROMS
REMARK 525 HOH A2056 DISTANCE = 6.79 ANGSTROMS
REMARK 525 HOH A2057 DISTANCE = 6.31 ANGSTROMS
REMARK 525 HOH A2058 DISTANCE = 6.26 ANGSTROMS
REMARK 525 HOH A2060 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH A2062 DISTANCE = 6.04 ANGSTROMS
REMARK 525 HOH A2067 DISTANCE = 6.19 ANGSTROMS
REMARK 525 HOH A2109 DISTANCE = 6.28 ANGSTROMS
REMARK 525 HOH A2127 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH B2034 DISTANCE = 6.09 ANGSTROMS
REMARK 525 HOH B2035 DISTANCE = 6.53 ANGSTROMS
REMARK 525 HOH B2036 DISTANCE = 6.84 ANGSTROMS
REMARK 525 HOH B2056 DISTANCE = 6.42 ANGSTROMS
REMARK 525 HOH B2111 DISTANCE = 6.25 ANGSTROMS
REMARK 525 HOH B2252 DISTANCE = 6.50 ANGSTROMS
REMARK 525 HOH C2012 DISTANCE = 5.91 ANGSTROMS
REMARK 525 HOH C2013 DISTANCE = 5.93 ANGSTROMS
REMARK 525 HOH C2041 DISTANCE = 6.20 ANGSTROMS
REMARK 525 HOH C2042 DISTANCE = 6.10 ANGSTROMS
REMARK 525 HOH C2098 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH C2547 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH D2141 DISTANCE = 6.72 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P4T A1405
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1F91 RELATED DB: PDB
REMARK 900 BETA-KETOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE I IN COMPLEXWITH C10
REMARK 900 FATTY ACID SUBSTRATE
REMARK 900 RELATED ID: 1FJ8 RELATED DB: PDB
REMARK 900 THE STRUCTURE OF BETA-KETOACYL-[ACYL CARRIER PROTEIN]SYNTHASE I IN
REMARK 900 COMPLEX WITH CERULENIN, IMPLICATIONS FOR DRUGDESIGN
REMARK 900 RELATED ID: 1G5X RELATED DB: PDB
REMARK 900 THE STRUCTURE OF BETA-KETOACYL-[ACYL CARRIER PROTEIN]SYNTHASE I
REMARK 900 RELATED ID: 1H4F RELATED DB: PDB
REMARK 900 E. COLI BETA-KETOACYL [ACYL CARRIER PROTEIN ] SYNTHASE I K328R
REMARK 900 RELATED ID: 2AQ7 RELATED DB: PDB
REMARK 900 STRUCTURE-ACTIVITY RELATIONSHIPS AT THE 5- POSIITON
REMARK 900 OFTHIOLACTOMYCIN: AN INTACT 5(R)- ISOPRENE UNIT IS REQUIREDFOR
REMARK 900 ACTIVITY AGAINST THE CONDENSING ENZYMES FROMMYCOBACTERIUM
REMARK 900 TUBERCULOSIS AND ESCHERICHIA COLI
REMARK 900 RELATED ID: 2AQB RELATED DB: PDB
REMARK 900 STRUCTURE-ACTIVITY RELATIONSHIPS AT THE 5- POSITION
REMARK 900 OFTHIOLACTOMYCIN: AN INTACT 5(R)- ISOPRENE UNIT IS REQUIREDFOR
REMARK 900 ACTIVITY AGAINST THE CONDENSING ENZYMES FROMMYCOBACTERIUM
REMARK 900 TUBERCULOSIS AND ESCHERCHIA COLI
REMARK 900 RELATED ID: 2BUH RELATED DB: PDB
REMARK 900 E. COLI BETA-KETOACYL (ACYL CARRIER PROTEIN ) SYNTHASE I, 120 K
REMARK 900 RELATED ID: 2BUI RELATED DB: PDB
REMARK 900 E. COLI BETA-KETOACYL (ACYL CARRIER PROTEIN ) SYNTHASE I IN COMPLEX
REMARK 900 WITH OCTANOIC ACID , 120K
REMARK 900 RELATED ID: 2BYX RELATED DB: PDB
REMARK 900 KAS I LYS328ALA MUTANT IN COMPLEX WITH FATTY ACID
REMARK 900 RELATED ID: 2BZ3 RELATED DB: PDB
REMARK 900 STRUCTURE OF E. COLI KAS I H298E MUTANT IN COMPLEX WITH C12 FATTY
REMARK 900 ACID
REMARK 900 RELATED ID: 1DD8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BETA-KETOACYL-[ACYL CARRIER PROTEIN]SYNTHASE I
REMARK 900 FROM ESCHERICHIA COLI
REMARK 900 RELATED ID: 1EK4 RELATED DB: PDB
REMARK 900 BETA-KETOACYL [ACYL CARRIER PROTEIN] SYNTHASE I IN COMPLEXWITH
REMARK 900 DODECANOIC ACID TO 1.85 RESOLUTION
REMARK 900 RELATED ID: 1FJ4 RELATED DB: PDB
REMARK 900 THE STRUCTURE OF BETA-KETOACYL-[ACYL CARRIER PROTEIN]SYNTHASE I IN
REMARK 900 COMPLEX WITH THIOLACTOMYCIN, IMPLICATIONS FORDRUG DESIGN
REMARK 900 RELATED ID: 2BYW RELATED DB: PDB
REMARK 900 STRUCTURE OF ESCHERICHIA COLI BETA-KETOACYL ( ACYL CARRIER PROTEIN)
REMARK 900 SYNTHASE I LYS328ALA MUTANT
REMARK 900 RELATED ID: 2BYY RELATED DB: PDB
REMARK 900 E. COLI KAS I H298E MUTATION
REMARK 900 RELATED ID: 2BYZ RELATED DB: PDB
REMARK 900 STRUCTURE OF E. COLI KAS I H298Q MUTANT IN COMPLEX WITH C12 FATTY
REMARK 900 ACID
REMARK 900 RELATED ID: 2BZ4 RELATED DB: PDB
REMARK 900 STRUCTURE OF E. COLI KAS I H298Q MUTANT
REMARK 900 RELATED ID: 2VB7 RELATED DB: PDB
REMARK 900 BETA-KETOACYL-ACP SYNTHASE I (KAS) FROM E . COLI, APO STRUCTURE
REMARK 900 AFTER SOAK IN PEG SOLUTION
REMARK 900 RELATED ID: 2VB8 RELATED DB: PDB
REMARK 900 BETA-KETOACYL-ACP SYNTHASE I (KAS) FROM E . COLI WITH BOUND
REMARK 900 INHIBITOR THIOLACTOMYCIN
REMARK 900 RELATED ID: 2VB9 RELATED DB: PDB
REMARK 900 BETA-KETOACYL-ACP SYNTHASE I (KAS) FROM E . COLI, APO STRUCTURE
DBREF 2VBA A 1 406 UNP P0A953 FABB_ECOLI 1 406
DBREF 2VBA B 1 406 UNP P0A953 FABB_ECOLI 1 406
DBREF 2VBA C 1 406 UNP P0A953 FABB_ECOLI 1 406
DBREF 2VBA D 1 406 UNP P0A953 FABB_ECOLI 1 406
SEQRES 1 A 406 MET LYS ARG ALA VAL ILE THR GLY LEU GLY ILE VAL SER
SEQRES 2 A 406 SER ILE GLY ASN ASN GLN GLN GLU VAL LEU ALA SER LEU
SEQRES 3 A 406 ARG GLU GLY ARG SER GLY ILE THR PHE SER GLN GLU LEU
SEQRES 4 A 406 LYS ASP SER GLY MET ARG SER HIS VAL TRP GLY ASN VAL
SEQRES 5 A 406 LYS LEU ASP THR THR GLY LEU ILE ASP ARG LYS VAL VAL
SEQRES 6 A 406 ARG PHE MET SER ASP ALA SER ILE TYR ALA PHE LEU SER
SEQRES 7 A 406 MET GLU GLN ALA ILE ALA ASP ALA GLY LEU SER PRO GLU
SEQRES 8 A 406 ALA TYR GLN ASN ASN PRO ARG VAL GLY LEU ILE ALA GLY
SEQRES 9 A 406 SER GLY GLY GLY SER PRO ARG PHE GLN VAL PHE GLY ALA
SEQRES 10 A 406 ASP ALA MET ARG GLY PRO ARG GLY LEU LYS ALA VAL GLY
SEQRES 11 A 406 PRO TYR VAL VAL THR LYS ALA MET ALA SER GLY VAL SER
SEQRES 12 A 406 ALA CYS LEU ALA THR PRO PHE LYS ILE HIS GLY VAL ASN
SEQRES 13 A 406 TYR SER ILE SER SER ALA CYS ALA THR SER ALA HIS CYS
SEQRES 14 A 406 ILE GLY ASN ALA VAL GLU GLN ILE GLN LEU GLY LYS GLN
SEQRES 15 A 406 ASP ILE VAL PHE ALA GLY GLY GLY GLU GLU LEU CYS TRP
SEQRES 16 A 406 GLU MET ALA CYS GLU PHE ASP ALA MET GLY ALA LEU SER
SEQRES 17 A 406 THR LYS TYR ASN ASP THR PRO GLU LYS ALA SER ARG THR
SEQRES 18 A 406 TYR ASP ALA HIS ARG ASP GLY PHE VAL ILE ALA GLY GLY
SEQRES 19 A 406 GLY GLY MET VAL VAL VAL GLU GLU LEU GLU HIS ALA LEU
SEQRES 20 A 406 ALA ARG GLY ALA HIS ILE TYR ALA GLU ILE VAL GLY TYR
SEQRES 21 A 406 GLY ALA THR SER ASP GLY ALA ASP MET VAL ALA PRO SER
SEQRES 22 A 406 GLY GLU GLY ALA VAL ARG CYS MET LYS MET ALA MET HIS
SEQRES 23 A 406 GLY VAL ASP THR PRO ILE ASP TYR LEU ASN SER HIS GLY
SEQRES 24 A 406 THR SER THR PRO VAL GLY ASP VAL LYS GLU LEU ALA ALA
SEQRES 25 A 406 ILE ARG GLU VAL PHE GLY ASP LYS SER PRO ALA ILE SER
SEQRES 26 A 406 ALA THR LYS ALA MET THR GLY HIS SER LEU GLY ALA ALA
SEQRES 27 A 406 GLY VAL GLN GLU ALA ILE TYR SER LEU LEU MET LEU GLU
SEQRES 28 A 406 HIS GLY PHE ILE ALA PRO SER ILE ASN ILE GLU GLU LEU
SEQRES 29 A 406 ASP GLU GLN ALA ALA GLY LEU ASN ILE VAL THR GLU THR
SEQRES 30 A 406 THR ASP ARG GLU LEU THR THR VAL MET SER ASN SER PHE
SEQRES 31 A 406 GLY PHE GLY GLY THR ASN ALA THR LEU VAL MET ARG LYS
SEQRES 32 A 406 LEU LYS ASP
SEQRES 1 B 406 MET LYS ARG ALA VAL ILE THR GLY LEU GLY ILE VAL SER
SEQRES 2 B 406 SER ILE GLY ASN ASN GLN GLN GLU VAL LEU ALA SER LEU
SEQRES 3 B 406 ARG GLU GLY ARG SER GLY ILE THR PHE SER GLN GLU LEU
SEQRES 4 B 406 LYS ASP SER GLY MET ARG SER HIS VAL TRP GLY ASN VAL
SEQRES 5 B 406 LYS LEU ASP THR THR GLY LEU ILE ASP ARG LYS VAL VAL
SEQRES 6 B 406 ARG PHE MET SER ASP ALA SER ILE TYR ALA PHE LEU SER
SEQRES 7 B 406 MET GLU GLN ALA ILE ALA ASP ALA GLY LEU SER PRO GLU
SEQRES 8 B 406 ALA TYR GLN ASN ASN PRO ARG VAL GLY LEU ILE ALA GLY
SEQRES 9 B 406 SER GLY GLY GLY SER PRO ARG PHE GLN VAL PHE GLY ALA
SEQRES 10 B 406 ASP ALA MET ARG GLY PRO ARG GLY LEU LYS ALA VAL GLY
SEQRES 11 B 406 PRO TYR VAL VAL THR LYS ALA MET ALA SER GLY VAL SER
SEQRES 12 B 406 ALA CYS LEU ALA THR PRO PHE LYS ILE HIS GLY VAL ASN
SEQRES 13 B 406 TYR SER ILE SER SER ALA CYS ALA THR SER ALA HIS CYS
SEQRES 14 B 406 ILE GLY ASN ALA VAL GLU GLN ILE GLN LEU GLY LYS GLN
SEQRES 15 B 406 ASP ILE VAL PHE ALA GLY GLY GLY GLU GLU LEU CYS TRP
SEQRES 16 B 406 GLU MET ALA CYS GLU PHE ASP ALA MET GLY ALA LEU SER
SEQRES 17 B 406 THR LYS TYR ASN ASP THR PRO GLU LYS ALA SER ARG THR
SEQRES 18 B 406 TYR ASP ALA HIS ARG ASP GLY PHE VAL ILE ALA GLY GLY
SEQRES 19 B 406 GLY GLY MET VAL VAL VAL GLU GLU LEU GLU HIS ALA LEU
SEQRES 20 B 406 ALA ARG GLY ALA HIS ILE TYR ALA GLU ILE VAL GLY TYR
SEQRES 21 B 406 GLY ALA THR SER ASP GLY ALA ASP MET VAL ALA PRO SER
SEQRES 22 B 406 GLY GLU GLY ALA VAL ARG CYS MET LYS MET ALA MET HIS
SEQRES 23 B 406 GLY VAL ASP THR PRO ILE ASP TYR LEU ASN SER HIS GLY
SEQRES 24 B 406 THR SER THR PRO VAL GLY ASP VAL LYS GLU LEU ALA ALA
SEQRES 25 B 406 ILE ARG GLU VAL PHE GLY ASP LYS SER PRO ALA ILE SER
SEQRES 26 B 406 ALA THR LYS ALA MET THR GLY HIS SER LEU GLY ALA ALA
SEQRES 27 B 406 GLY VAL GLN GLU ALA ILE TYR SER LEU LEU MET LEU GLU
SEQRES 28 B 406 HIS GLY PHE ILE ALA PRO SER ILE ASN ILE GLU GLU LEU
SEQRES 29 B 406 ASP GLU GLN ALA ALA GLY LEU ASN ILE VAL THR GLU THR
SEQRES 30 B 406 THR ASP ARG GLU LEU THR THR VAL MET SER ASN SER PHE
SEQRES 31 B 406 GLY PHE GLY GLY THR ASN ALA THR LEU VAL MET ARG LYS
SEQRES 32 B 406 LEU LYS ASP
SEQRES 1 C 406 MET LYS ARG ALA VAL ILE THR GLY LEU GLY ILE VAL SER
SEQRES 2 C 406 SER ILE GLY ASN ASN GLN GLN GLU VAL LEU ALA SER LEU
SEQRES 3 C 406 ARG GLU GLY ARG SER GLY ILE THR PHE SER GLN GLU LEU
SEQRES 4 C 406 LYS ASP SER GLY MET ARG SER HIS VAL TRP GLY ASN VAL
SEQRES 5 C 406 LYS LEU ASP THR THR GLY LEU ILE ASP ARG LYS VAL VAL
SEQRES 6 C 406 ARG PHE MET SER ASP ALA SER ILE TYR ALA PHE LEU SER
SEQRES 7 C 406 MET GLU GLN ALA ILE ALA ASP ALA GLY LEU SER PRO GLU
SEQRES 8 C 406 ALA TYR GLN ASN ASN PRO ARG VAL GLY LEU ILE ALA GLY
SEQRES 9 C 406 SER GLY GLY GLY SER PRO ARG PHE GLN VAL PHE GLY ALA
SEQRES 10 C 406 ASP ALA MET ARG GLY PRO ARG GLY LEU LYS ALA VAL GLY
SEQRES 11 C 406 PRO TYR VAL VAL THR LYS ALA MET ALA SER GLY VAL SER
SEQRES 12 C 406 ALA CYS LEU ALA THR PRO PHE LYS ILE HIS GLY VAL ASN
SEQRES 13 C 406 TYR SER ILE SER SER ALA CYS ALA THR SER ALA HIS CYS
SEQRES 14 C 406 ILE GLY ASN ALA VAL GLU GLN ILE GLN LEU GLY LYS GLN
SEQRES 15 C 406 ASP ILE VAL PHE ALA GLY GLY GLY GLU GLU LEU CYS TRP
SEQRES 16 C 406 GLU MET ALA CYS GLU PHE ASP ALA MET GLY ALA LEU SER
SEQRES 17 C 406 THR LYS TYR ASN ASP THR PRO GLU LYS ALA SER ARG THR
SEQRES 18 C 406 TYR ASP ALA HIS ARG ASP GLY PHE VAL ILE ALA GLY GLY
SEQRES 19 C 406 GLY GLY MET VAL VAL VAL GLU GLU LEU GLU HIS ALA LEU
SEQRES 20 C 406 ALA ARG GLY ALA HIS ILE TYR ALA GLU ILE VAL GLY TYR
SEQRES 21 C 406 GLY ALA THR SER ASP GLY ALA ASP MET VAL ALA PRO SER
SEQRES 22 C 406 GLY GLU GLY ALA VAL ARG CYS MET LYS MET ALA MET HIS
SEQRES 23 C 406 GLY VAL ASP THR PRO ILE ASP TYR LEU ASN SER HIS GLY
SEQRES 24 C 406 THR SER THR PRO VAL GLY ASP VAL LYS GLU LEU ALA ALA
SEQRES 25 C 406 ILE ARG GLU VAL PHE GLY ASP LYS SER PRO ALA ILE SER
SEQRES 26 C 406 ALA THR LYS ALA MET THR GLY HIS SER LEU GLY ALA ALA
SEQRES 27 C 406 GLY VAL GLN GLU ALA ILE TYR SER LEU LEU MET LEU GLU
SEQRES 28 C 406 HIS GLY PHE ILE ALA PRO SER ILE ASN ILE GLU GLU LEU
SEQRES 29 C 406 ASP GLU GLN ALA ALA GLY LEU ASN ILE VAL THR GLU THR
SEQRES 30 C 406 THR ASP ARG GLU LEU THR THR VAL MET SER ASN SER PHE
SEQRES 31 C 406 GLY PHE GLY GLY THR ASN ALA THR LEU VAL MET ARG LYS
SEQRES 32 C 406 LEU LYS ASP
SEQRES 1 D 406 MET LYS ARG ALA VAL ILE THR GLY LEU GLY ILE VAL SER
SEQRES 2 D 406 SER ILE GLY ASN ASN GLN GLN GLU VAL LEU ALA SER LEU
SEQRES 3 D 406 ARG GLU GLY ARG SER GLY ILE THR PHE SER GLN GLU LEU
SEQRES 4 D 406 LYS ASP SER GLY MET ARG SER HIS VAL TRP GLY ASN VAL
SEQRES 5 D 406 LYS LEU ASP THR THR GLY LEU ILE ASP ARG LYS VAL VAL
SEQRES 6 D 406 ARG PHE MET SER ASP ALA SER ILE TYR ALA PHE LEU SER
SEQRES 7 D 406 MET GLU GLN ALA ILE ALA ASP ALA GLY LEU SER PRO GLU
SEQRES 8 D 406 ALA TYR GLN ASN ASN PRO ARG VAL GLY LEU ILE ALA GLY
SEQRES 9 D 406 SER GLY GLY GLY SER PRO ARG PHE GLN VAL PHE GLY ALA
SEQRES 10 D 406 ASP ALA MET ARG GLY PRO ARG GLY LEU LYS ALA VAL GLY
SEQRES 11 D 406 PRO TYR VAL VAL THR LYS ALA MET ALA SER GLY VAL SER
SEQRES 12 D 406 ALA CYS LEU ALA THR PRO PHE LYS ILE HIS GLY VAL ASN
SEQRES 13 D 406 TYR SER ILE SER SER ALA CYS ALA THR SER ALA HIS CYS
SEQRES 14 D 406 ILE GLY ASN ALA VAL GLU GLN ILE GLN LEU GLY LYS GLN
SEQRES 15 D 406 ASP ILE VAL PHE ALA GLY GLY GLY GLU GLU LEU CYS TRP
SEQRES 16 D 406 GLU MET ALA CYS GLU PHE ASP ALA MET GLY ALA LEU SER
SEQRES 17 D 406 THR LYS TYR ASN ASP THR PRO GLU LYS ALA SER ARG THR
SEQRES 18 D 406 TYR ASP ALA HIS ARG ASP GLY PHE VAL ILE ALA GLY GLY
SEQRES 19 D 406 GLY GLY MET VAL VAL VAL GLU GLU LEU GLU HIS ALA LEU
SEQRES 20 D 406 ALA ARG GLY ALA HIS ILE TYR ALA GLU ILE VAL GLY TYR
SEQRES 21 D 406 GLY ALA THR SER ASP GLY ALA ASP MET VAL ALA PRO SER
SEQRES 22 D 406 GLY GLU GLY ALA VAL ARG CYS MET LYS MET ALA MET HIS
SEQRES 23 D 406 GLY VAL ASP THR PRO ILE ASP TYR LEU ASN SER HIS GLY
SEQRES 24 D 406 THR SER THR PRO VAL GLY ASP VAL LYS GLU LEU ALA ALA
SEQRES 25 D 406 ILE ARG GLU VAL PHE GLY ASP LYS SER PRO ALA ILE SER
SEQRES 26 D 406 ALA THR LYS ALA MET THR GLY HIS SER LEU GLY ALA ALA
SEQRES 27 D 406 GLY VAL GLN GLU ALA ILE TYR SER LEU LEU MET LEU GLU
SEQRES 28 D 406 HIS GLY PHE ILE ALA PRO SER ILE ASN ILE GLU GLU LEU
SEQRES 29 D 406 ASP GLU GLN ALA ALA GLY LEU ASN ILE VAL THR GLU THR
SEQRES 30 D 406 THR ASP ARG GLU LEU THR THR VAL MET SER ASN SER PHE
SEQRES 31 D 406 GLY PHE GLY GLY THR ASN ALA THR LEU VAL MET ARG LYS
SEQRES 32 D 406 LEU LYS ASP
HET P4T A1405 16
HETNAM P4T 2-PHENYLAMINO-4-METHYL-5-ACETYL THIAZOLE
HETSYN P4T 1-[4-METHYL-2-(PHENYLAMINO)-1,3-THIAZOL-5-YL]ETHANONE
FORMUL 5 P4T C12 H12 N2 O S
FORMUL 6 HOH *2431(H2 O)
HELIX 1 1 ASN A 18 GLY A 29 1 12
HELIX 2 2 SER A 36 SER A 42 1 7
HELIX 3 3 ASP A 61 ARG A 66 1 6
HELIX 4 4 SER A 69 GLY A 87 1 19
HELIX 5 5 SER A 89 GLN A 94 1 6
HELIX 6 6 SER A 109 ARG A 121 1 13
HELIX 7 7 GLY A 125 GLY A 130 1 6
HELIX 8 8 TYR A 132 MET A 138 1 7
HELIX 9 9 SER A 140 THR A 148 1 9
HELIX 10 10 SER A 161 CYS A 163 5 3
HELIX 11 11 ALA A 164 LEU A 179 1 16
HELIX 12 12 CYS A 194 MET A 204 1 11
HELIX 13 13 THR A 214 ALA A 218 5 5
HELIX 14 14 LEU A 243 ARG A 249 1 7
HELIX 15 15 GLY A 274 HIS A 286 1 13
HELIX 16 16 THR A 302 GLY A 318 1 17
HELIX 17 17 THR A 327 GLY A 332 1 6
HELIX 18 18 SER A 334 GLY A 336 5 3
HELIX 19 19 ALA A 337 GLY A 353 1 17
HELIX 20 20 ASN B 18 GLY B 29 1 12
HELIX 21 21 SER B 36 SER B 42 1 7
HELIX 22 22 ASP B 61 ARG B 66 1 6
HELIX 23 23 SER B 69 GLY B 87 1 19
HELIX 24 24 SER B 89 GLN B 94 1 6
HELIX 25 25 SER B 109 ARG B 121 1 13
HELIX 26 26 GLY B 125 GLY B 130 1 6
HELIX 27 27 TYR B 132 MET B 138 1 7
HELIX 28 28 SER B 140 THR B 148 1 9
HELIX 29 29 SER B 161 CYS B 163 5 3
HELIX 30 30 ALA B 164 LEU B 179 1 16
HELIX 31 31 CYS B 194 MET B 204 1 11
HELIX 32 32 THR B 214 ALA B 218 5 5
HELIX 33 33 LEU B 243 ARG B 249 1 7
HELIX 34 34 GLY B 274 HIS B 286 1 13
HELIX 35 35 THR B 302 GLY B 318 1 17
HELIX 36 36 THR B 327 GLY B 332 1 6
HELIX 37 37 SER B 334 GLY B 336 5 3
HELIX 38 38 ALA B 337 GLY B 353 1 17
HELIX 39 39 ASP B 365 ALA B 369 5 5
HELIX 40 40 ASN C 18 GLY C 29 1 12
HELIX 41 41 SER C 36 SER C 42 1 7
HELIX 42 42 ASP C 61 ARG C 66 1 6
HELIX 43 43 SER C 69 GLY C 87 1 19
HELIX 44 44 SER C 89 GLN C 94 1 6
HELIX 45 45 SER C 109 ARG C 121 1 13
HELIX 46 46 GLY C 125 GLY C 130 1 6
HELIX 47 47 TYR C 132 MET C 138 1 7
HELIX 48 48 SER C 140 THR C 148 1 9
HELIX 49 49 SER C 161 CYS C 163 5 3
HELIX 50 50 ALA C 164 LEU C 179 1 16
HELIX 51 51 CYS C 194 MET C 204 1 11
HELIX 52 52 THR C 214 ALA C 218 5 5
HELIX 53 53 LEU C 243 ARG C 249 1 7
HELIX 54 54 GLY C 274 MET C 285 1 12
HELIX 55 55 THR C 302 GLY C 318 1 17
HELIX 56 56 THR C 327 GLY C 332 1 6
HELIX 57 57 SER C 334 GLY C 336 5 3
HELIX 58 58 ALA C 337 GLY C 353 1 17
HELIX 59 59 ASP C 365 ALA C 369 5 5
HELIX 60 60 ASN D 18 GLY D 29 1 12
HELIX 61 61 SER D 36 SER D 42 1 7
HELIX 62 62 ASP D 61 ARG D 66 1 6
HELIX 63 63 SER D 69 GLY D 87 1 19
HELIX 64 64 SER D 89 GLN D 94 1 6
HELIX 65 65 SER D 109 ARG D 121 1 13
HELIX 66 66 ARG D 124 GLY D 130 1 7
HELIX 67 67 TYR D 132 MET D 138 1 7
HELIX 68 68 SER D 140 THR D 148 1 9
HELIX 69 69 SER D 161 CYS D 163 5 3
HELIX 70 70 ALA D 164 LEU D 179 1 16
HELIX 71 71 CYS D 194 MET D 204 1 11
HELIX 72 72 THR D 214 ALA D 218 5 5
HELIX 73 73 LEU D 243 ARG D 249 1 7
HELIX 74 74 GLY D 274 HIS D 286 1 13
HELIX 75 75 THR D 302 GLY D 318 1 17
HELIX 76 76 THR D 327 GLY D 332 1 6
HELIX 77 77 SER D 334 GLY D 336 5 3
HELIX 78 78 ALA D 337 GLY D 353 1 17
HELIX 79 79 ASP D 365 ALA D 369 5 5
SHEET 1 AA21 ASN A 372 ILE A 373 0
SHEET 2 AA21 ALA A 323 SER A 325 1 N ILE A 324 O ASN A 372
SHEET 3 AA21 TYR A 294 ASN A 296 1 O LEU A 295 N SER A 325
SHEET 4 AA21 THR A 384 GLY A 391 1 O MET A 386 N ASN A 296
SHEET 5 AA21 THR A 395 ARG A 402 -1 O THR A 395 N GLY A 391
SHEET 6 AA21 ALA A 255 SER A 264 -1 O GLU A 256 N ARG A 402
SHEET 7 AA21 ALA A 4 VAL A 12 -1 O ALA A 4 N ILE A 257
SHEET 8 AA21 GLY A 234 GLU A 242 -1 O GLY A 235 N VAL A 12
SHEET 9 AA21 ILE A 184 GLU A 191 -1 O VAL A 185 N VAL A 240
SHEET 10 AA21 VAL A 99 GLY A 104 1 O GLY A 100 N PHE A 186
SHEET 11 AA21 ASN A 156 SER A 160 1 O TYR A 157 N ALA A 103
SHEET 12 AA21 ASN B 156 SER B 160 -1 O SER B 158 N SER A 160
SHEET 13 AA21 VAL B 99 GLY B 104 1 O LEU B 101 N TYR B 157
SHEET 14 AA21 ILE B 184 GLU B 191 1 O ILE B 184 N GLY B 100
SHEET 15 AA21 GLY B 234 GLU B 242 -1 O GLY B 234 N GLU B 191
SHEET 16 AA21 ALA B 4 VAL B 12 -1 O VAL B 5 N GLU B 241
SHEET 17 AA21 ALA B 255 SER B 264 -1 O ALA B 255 N ILE B 6
SHEET 18 AA21 THR B 395 ARG B 402 -1 O ASN B 396 N THR B 263
SHEET 19 AA21 THR B 384 GLY B 391 -1 O VAL B 385 N MET B 401
SHEET 20 AA21 TYR B 294 ASN B 296 1 O TYR B 294 N MET B 386
SHEET 21 AA21 ALA B 323 SER B 325 1 O ALA B 323 N LEU B 295
SHEET 1 AB 2 ILE A 33 PHE A 35 0
SHEET 2 AB 2 VAL A 48 GLY A 50 -1 O TRP A 49 N THR A 34
SHEET 1 AC 2 PHE A 354 ILE A 355 0
SHEET 2 AC 2 THR A 378 ASP A 379 -1 O THR A 378 N ILE A 355
SHEET 1 BA 2 ILE B 33 PHE B 35 0
SHEET 2 BA 2 VAL B 48 GLY B 50 -1 O TRP B 49 N THR B 34
SHEET 1 BB 2 PHE B 354 ILE B 355 0
SHEET 2 BB 2 THR B 378 ASP B 379 -1 O THR B 378 N ILE B 355
SHEET 1 CA21 ALA C 323 SER C 325 0
SHEET 2 CA21 TYR C 294 ASN C 296 1 O LEU C 295 N SER C 325
SHEET 3 CA21 THR C 384 GLY C 391 1 O MET C 386 N ASN C 296
SHEET 4 CA21 THR C 395 ARG C 402 -1 O THR C 395 N GLY C 391
SHEET 5 CA21 ALA C 255 SER C 264 -1 O GLU C 256 N ARG C 402
SHEET 6 CA21 ALA C 4 VAL C 12 -1 O ALA C 4 N ILE C 257
SHEET 7 CA21 GLY C 234 GLU C 242 -1 O GLY C 235 N VAL C 12
SHEET 8 CA21 ILE C 184 GLU C 191 -1 O VAL C 185 N VAL C 240
SHEET 9 CA21 VAL C 99 GLY C 104 1 O GLY C 100 N PHE C 186
SHEET 10 CA21 ASN C 156 SER C 160 1 O TYR C 157 N ALA C 103
SHEET 11 CA21 ASN D 156 SER D 160 -1 O SER D 158 N SER C 160
SHEET 12 CA21 VAL D 99 GLY D 104 1 O LEU D 101 N TYR D 157
SHEET 13 CA21 ILE D 184 GLU D 191 1 O ILE D 184 N GLY D 100
SHEET 14 CA21 GLY D 234 GLU D 242 -1 O GLY D 234 N GLU D 191
SHEET 15 CA21 ALA D 4 VAL D 12 -1 O VAL D 5 N GLU D 241
SHEET 16 CA21 ALA D 255 SER D 264 -1 O ALA D 255 N ILE D 6
SHEET 17 CA21 THR D 395 ARG D 402 -1 O ASN D 396 N THR D 263
SHEET 18 CA21 THR D 384 GLY D 391 -1 O VAL D 385 N MET D 401
SHEET 19 CA21 TYR D 294 ASN D 296 1 O TYR D 294 N MET D 386
SHEET 20 CA21 ALA D 323 SER D 325 1 O ALA D 323 N LEU D 295
SHEET 21 CA21 ASN D 372 ILE D 373 1 O ASN D 372 N ILE D 324
SHEET 1 CB 2 ILE C 33 PHE C 35 0
SHEET 2 CB 2 VAL C 48 GLY C 50 -1 O TRP C 49 N THR C 34
SHEET 1 CC 2 PHE C 354 ILE C 355 0
SHEET 2 CC 2 THR C 378 ASP C 379 -1 O THR C 378 N ILE C 355
SHEET 1 DA 2 ILE D 33 PHE D 35 0
SHEET 2 DA 2 VAL D 48 GLY D 50 -1 O TRP D 49 N THR D 34
SHEET 1 DB 2 PHE D 354 ILE D 355 0
SHEET 2 DB 2 THR D 378 ASP D 379 -1 O THR D 378 N ILE D 355
SITE 1 AC1 13 ALA A 162 CYS A 163 PHE A 201 MET A 204
SITE 2 AC1 13 PHE A 229 THR A 302 LEU A 335 PHE A 392
SITE 3 AC1 13 HOH A2248 HOH A2316 HOH A2513 HOH A2623
SITE 4 AC1 13 MET B 138
CRYST1 58.950 139.480 212.170 90.00 90.00 90.00 P 21 21 21 16
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 0.016964 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007169 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004713 0.00000
(ATOM LINES ARE NOT SHOWN.)
END