HEADER OXIDOREDUCTASE 29-APR-13 4BKU
TITLE ENOYL-ACP REDUCTASE FABI FROM BURKHOLDERIA PSEUDOMALLEI WITH COFACTOR
TITLE 2 NADH AND INHIBITOR PT155
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE [NADH];
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ENOYL-ACP REDUCTASE FABI;
COMPND 5 EC: 1.3.1.9;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BURKHOLDERIA PSEUDOMALLEI;
SOURCE 3 ORGANISM_TAXID: 884204;
SOURCE 4 STRAIN: BP82;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET23B
KEYWDS OXIDOREDUCTASE, FATTY ACID BIOSYNTHESIS, ENOYL- ACP REDUCTASE,
KEYWDS 2 PYRIDONE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.W.HIRSCHBECK,N.LIU,C.NECKLES,P.J.TONGE,C.KISKER
REVDAT 6 20-DEC-23 4BKU 1 REMARK
REVDAT 5 28-JUN-17 4BKU 1 REMARK
REVDAT 4 10-DEC-14 4BKU 1 REMARK
REVDAT 3 13-AUG-14 4BKU 1 JRNL HETATM
REVDAT 2 30-APR-14 4BKU 1 JRNL
REVDAT 1 09-APR-14 4BKU 0
JRNL AUTH J.SCHIEBEL,A.CHANG,S.SHAH,Y.LU,L.LIU,P.PAN,M.W.HIRSCHBECK,
JRNL AUTH 2 M.TAREILUS,S.ELTSCHKNER,W.YU,J.E.CUMMINGS,S.E.KNUDSON,
JRNL AUTH 3 G.R.BOMMINENI,S.G.WALKER,R.A.SLAYDEN,C.A.SOTRIFFER,
JRNL AUTH 4 P.J.TONGE,C.KISKER
JRNL TITL RATIONAL DESIGN OF BROAD SPECTRUM ANTIBACTERIAL ACTIVITY
JRNL TITL 2 BASED ON A CLINICALLY RELEVANT ENOYL-ACYL CARRIER PROTEIN
JRNL TITL 3 (ACP) REDUCTASE INHIBITOR.
JRNL REF J.BIOL.CHEM. V. 289 15987 2014
JRNL REFN ISSN 0021-9258
JRNL PMID 24739388
JRNL DOI 10.1074/JBC.M113.532804
REMARK 2
REMARK 2 RESOLUTION. 1.84 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.84
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.58
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 22268
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.138
REMARK 3 R VALUE (WORKING SET) : 0.137
REMARK 3 FREE R VALUE : 0.162
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1140
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 28.5814 - 3.6797 0.99 2764 129 0.1404 0.1417
REMARK 3 2 3.6797 - 2.9216 1.00 2659 159 0.1321 0.1515
REMARK 3 3 2.9216 - 2.5526 1.00 2636 139 0.1357 0.1628
REMARK 3 4 2.5526 - 2.3193 1.00 2633 136 0.1300 0.1681
REMARK 3 5 2.3193 - 2.1531 1.00 2629 135 0.1223 0.1479
REMARK 3 6 2.1531 - 2.0262 1.00 2623 142 0.1303 0.1610
REMARK 3 7 2.0262 - 1.9248 1.00 2585 153 0.1385 0.2031
REMARK 3 8 1.9248 - 1.8410 1.00 2599 147 0.1913 0.2243
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.86
REMARK 3 K_SOL : 0.44
REMARK 3 B_SOL : 45.83
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 13.510
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.33230
REMARK 3 B22 (A**2) : 0.16150
REMARK 3 B33 (A**2) : 2.17080
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 2073
REMARK 3 ANGLE : 1.137 2828
REMARK 3 CHIRALITY : 0.077 325
REMARK 3 PLANARITY : 0.005 359
REMARK 3 DIHEDRAL : 14.386 762
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 2:41)
REMARK 3 ORIGIN FOR THE GROUP (A): -10.1995 -3.8069 15.0096
REMARK 3 T TENSOR
REMARK 3 T11: 0.0632 T22: 0.1190
REMARK 3 T33: 0.0759 T12: 0.0394
REMARK 3 T13: -0.0128 T23: -0.0209
REMARK 3 L TENSOR
REMARK 3 L11: 0.9870 L22: 1.6262
REMARK 3 L33: 1.7548 L12: 0.4241
REMARK 3 L13: -0.1884 L23: -0.6295
REMARK 3 S TENSOR
REMARK 3 S11: -0.0119 S12: 0.0394 S13: -0.0517
REMARK 3 S21: -0.0601 S22: 0.0313 S23: -0.0633
REMARK 3 S31: 0.0985 S32: 0.1490 S33: -0.0258
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 42:55)
REMARK 3 ORIGIN FOR THE GROUP (A): -9.1650 -10.8951 25.8298
REMARK 3 T TENSOR
REMARK 3 T11: 0.1284 T22: 0.1131
REMARK 3 T33: 0.1395 T12: 0.0242
REMARK 3 T13: -0.0648 T23: 0.0357
REMARK 3 L TENSOR
REMARK 3 L11: 5.7840 L22: 4.6189
REMARK 3 L33: 7.8508 L12: 2.7933
REMARK 3 L13: -4.2478 L23: -3.5671
REMARK 3 S TENSOR
REMARK 3 S11: 0.1110 S12: -0.3317 S13: -0.1989
REMARK 3 S21: 0.2602 S22: 0.1276 S23: 0.0295
REMARK 3 S31: 0.3212 S32: -0.0175 S33: -0.2118
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 56:178)
REMARK 3 ORIGIN FOR THE GROUP (A): -25.5830 -0.3679 19.7677
REMARK 3 T TENSOR
REMARK 3 T11: 0.0660 T22: 0.0604
REMARK 3 T33: 0.0664 T12: 0.0148
REMARK 3 T13: -0.0004 T23: -0.0073
REMARK 3 L TENSOR
REMARK 3 L11: 0.8983 L22: 0.3103
REMARK 3 L33: 0.4459 L12: 0.2128
REMARK 3 L13: 0.1368 L23: -0.0100
REMARK 3 S TENSOR
REMARK 3 S11: -0.0062 S12: -0.0350 S13: -0.0382
REMARK 3 S21: 0.0325 S22: 0.0031 S23: -0.0242
REMARK 3 S31: -0.0007 S32: 0.0270 S33: 0.0018
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 179:203)
REMARK 3 ORIGIN FOR THE GROUP (A): -23.8563 -8.3527 12.3702
REMARK 3 T TENSOR
REMARK 3 T11: 0.0652 T22: 0.0802
REMARK 3 T33: 0.0741 T12: 0.0108
REMARK 3 T13: 0.0082 T23: -0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 0.5543 L22: 3.0841
REMARK 3 L33: 1.0161 L12: 0.5481
REMARK 3 L13: -0.1640 L23: -1.0642
REMARK 3 S TENSOR
REMARK 3 S11: -0.0106 S12: -0.0432 S13: -0.0464
REMARK 3 S21: -0.0145 S22: 0.0476 S23: 0.1222
REMARK 3 S31: 0.1249 S32: 0.0329 S33: -0.0387
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 204:256)
REMARK 3 ORIGIN FOR THE GROUP (A): -22.8453 -9.2067 2.2762
REMARK 3 T TENSOR
REMARK 3 T11: 0.0609 T22: 0.0552
REMARK 3 T33: 0.0302 T12: 0.0156
REMARK 3 T13: 0.0151 T23: 0.0031
REMARK 3 L TENSOR
REMARK 3 L11: 1.1723 L22: 1.5771
REMARK 3 L33: 1.0745 L12: 0.2372
REMARK 3 L13: 0.2859 L23: 0.5121
REMARK 3 S TENSOR
REMARK 3 S11: -0.0033 S12: 0.0165 S13: -0.1321
REMARK 3 S21: 0.0254 S22: 0.0197 S23: -0.0205
REMARK 3 S31: 0.1078 S32: 0.0523 S33: -0.0131
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4BKU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-APR-13.
REMARK 100 THE DEPOSITION ID IS D_1290056686.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS HTC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22291
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.840
REMARK 200 RESOLUTION RANGE LOW (A) : 37.970
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 5.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 4.900
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.84
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.94
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.50
REMARK 200 R MERGE FOR SHELL (I) : 0.26000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3EK2
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350 200 MM (NH4)2HPO4
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
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 SMTRY1 5 1.000000 0.000000 0.000000 37.16000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 37.97500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 44.71000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 37.16000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 37.97500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 44.71000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 37.16000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 37.97500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 44.71000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 37.16000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 37.97500
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 44.71000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 18940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31400 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -119.4 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 -74.32000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 4 -1.000000 0.000000 0.000000 -74.32000
REMARK 350 BIOMT2 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A2006 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2258 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2327 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2335 LIES ON A SPECIAL POSITION.
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 MET A 1
REMARK 465 ALA A 259
REMARK 465 GLY A 260
REMARK 465 LEU A 261
REMARK 465 GLU A 262
REMARK 465 GLU A 263
REMARK 465 LYS A 264
REMARK 465 LEU A 265
REMARK 465 ALA A 266
REMARK 465 ALA A 267
REMARK 465 ALA A 268
REMARK 465 LEU A 269
REMARK 465 GLU A 270
REMARK 465 HIS A 271
REMARK 465 HIS A 272
REMARK 465 HIS A 273
REMARK 465 HIS A 274
REMARK 465 HIS A 275
REMARK 465 HIS A 276
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 O HOH A 2312 O HOH A 2313 1.91
REMARK 500 NH2 ARG A 43 O HOH A 2112 1.91
REMARK 500 O HOH A 2104 O HOH A 2164 1.94
REMARK 500 NH2 ARG A 43 O HOH A 2112 1.97
REMARK 500 O HOH A 2055 O HOH A 2056 2.09
REMARK 500 O HOH A 2057 O HOH A 2117 2.17
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 CYS A 63 106.47 -163.68
REMARK 500 ASN A 155 -22.03 76.15
REMARK 500 ASN A 157 -120.11 45.22
REMARK 500 ASP A 248 24.28 -152.77
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 A2063 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH A2197 DISTANCE = 6.02 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI A 1259
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1S5 A 1260
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4BKO RELATED DB: PDB
REMARK 900 ENOYL-ACP REDUCATASE FABV FROM BURKHOLDERIA PSEUDOMALLEI (APO)
REMARK 900 RELATED ID: 4BKQ RELATED DB: PDB
REMARK 900 ENOYL-ACP REDUCTASE FROM YERSINIA PESTIS (WILDTYPE)WITH COFACTOR
REMARK 900 NADH
REMARK 900 RELATED ID: 4BKR RELATED DB: PDB
REMARK 900 ENOYL-ACP REDUCTASE FROM YERSINIA PESTIS (WILDTYPE, REMOVED HISTAG)
REMARK 900 WITH COFACTOR NADH
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 NCBI REFERENCE SEQUENCE YP_108799.1
DBREF 4BKU A 1 263 UNP I1WHT9 I1WHT9_BURPE 1 263
SEQADV 4BKU LYS A 264 UNP I1WHT9 EXPRESSION TAG
SEQADV 4BKU LEU A 265 UNP I1WHT9 EXPRESSION TAG
SEQADV 4BKU ALA A 266 UNP I1WHT9 EXPRESSION TAG
SEQADV 4BKU ALA A 267 UNP I1WHT9 EXPRESSION TAG
SEQADV 4BKU ALA A 268 UNP I1WHT9 EXPRESSION TAG
SEQADV 4BKU LEU A 269 UNP I1WHT9 EXPRESSION TAG
SEQADV 4BKU GLU A 270 UNP I1WHT9 EXPRESSION TAG
SEQADV 4BKU HIS A 271 UNP I1WHT9 EXPRESSION TAG
SEQADV 4BKU HIS A 272 UNP I1WHT9 EXPRESSION TAG
SEQADV 4BKU HIS A 273 UNP I1WHT9 EXPRESSION TAG
SEQADV 4BKU HIS A 274 UNP I1WHT9 EXPRESSION TAG
SEQADV 4BKU HIS A 275 UNP I1WHT9 EXPRESSION TAG
SEQADV 4BKU HIS A 276 UNP I1WHT9 EXPRESSION TAG
SEQRES 1 A 276 MET GLY PHE LEU ASP GLY LYS ARG ILE LEU LEU THR GLY
SEQRES 2 A 276 LEU LEU SER ASN ARG SER ILE ALA TYR GLY ILE ALA LYS
SEQRES 3 A 276 ALA CYS LYS ARG GLU GLY ALA GLU LEU ALA PHE THR TYR
SEQRES 4 A 276 VAL GLY ASP ARG PHE LYS ASP ARG ILE THR GLU PHE ALA
SEQRES 5 A 276 ALA GLU PHE GLY SER GLU LEU VAL PHE PRO CYS ASP VAL
SEQRES 6 A 276 ALA ASP ASP ALA GLN ILE ASP ALA LEU PHE ALA SER LEU
SEQRES 7 A 276 LYS THR HIS TRP ASP SER LEU ASP GLY LEU VAL HIS SER
SEQRES 8 A 276 ILE GLY PHE ALA PRO ARG GLU ALA ILE ALA GLY ASP PHE
SEQRES 9 A 276 LEU ASP GLY LEU THR ARG GLU ASN PHE ARG ILE ALA HIS
SEQRES 10 A 276 ASP ILE SER ALA TYR SER PHE PRO ALA LEU ALA LYS ALA
SEQRES 11 A 276 ALA LEU PRO MET LEU SER ASP ASP ALA SER LEU LEU THR
SEQRES 12 A 276 LEU SER TYR LEU GLY ALA GLU ARG ALA ILE PRO ASN TYR
SEQRES 13 A 276 ASN THR MET GLY LEU ALA LYS ALA ALA LEU GLU ALA SER
SEQRES 14 A 276 VAL ARG TYR LEU ALA VAL SER LEU GLY ALA LYS GLY VAL
SEQRES 15 A 276 ARG VAL ASN ALA ILE SER ALA GLY PRO ILE LYS THR LEU
SEQRES 16 A 276 ALA ALA SER GLY ILE LYS SER PHE GLY LYS ILE LEU ASP
SEQRES 17 A 276 PHE VAL GLU SER ASN SER PRO LEU LYS ARG ASN VAL THR
SEQRES 18 A 276 ILE GLU GLN VAL GLY ASN ALA GLY ALA PHE LEU LEU SER
SEQRES 19 A 276 ASP LEU ALA SER GLY VAL THR ALA GLU VAL MET HIS VAL
SEQRES 20 A 276 ASP SER GLY PHE ASN ALA VAL VAL GLY GLY MET ALA GLY
SEQRES 21 A 276 LEU GLU GLU LYS LEU ALA ALA ALA LEU GLU HIS HIS HIS
SEQRES 22 A 276 HIS HIS HIS
HET NAI A1259 44
HET 1S5 A1260 23
HETNAM NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE
HETNAM 1S5 5-(4-AMINO-2-METHYLPHENOXY)-2-HEXYL-4-HYDROXY-1-
HETNAM 2 1S5 METHYLPYRIDINIUM
HETSYN NAI NADH
FORMUL 2 NAI C21 H29 N7 O14 P2
FORMUL 3 1S5 C19 H26 N2 O2
FORMUL 4 HOH *343(H2 O)
HELIX 1 1 SER A 19 GLU A 31 1 13
HELIX 2 2 GLY A 41 ARG A 43 5 3
HELIX 3 3 PHE A 44 PHE A 55 1 12
HELIX 4 4 ASP A 67 THR A 80 1 14
HELIX 5 5 PRO A 96 ALA A 101 5 6
HELIX 6 6 THR A 109 ALA A 121 1 13
HELIX 7 7 TYR A 122 LEU A 132 1 11
HELIX 8 8 TYR A 146 GLU A 150 5 5
HELIX 9 9 TYR A 156 ALA A 179 1 24
HELIX 10 10 PHE A 203 SER A 214 1 12
HELIX 11 11 THR A 221 SER A 234 1 14
HELIX 12 12 ASP A 235 SER A 238 5 4
HELIX 13 13 GLY A 250 VAL A 254 5 5
SHEET 1 AA 7 VAL A 60 PRO A 62 0
SHEET 2 AA 7 GLU A 34 TYR A 39 1 O PHE A 37 N PHE A 61
SHEET 3 AA 7 ARG A 8 LEU A 11 1 O ILE A 9 N ALA A 36
SHEET 4 AA 7 LEU A 85 HIS A 90 1 N ASP A 86 O ARG A 8
SHEET 5 AA 7 LEU A 135 SER A 145 1 N SER A 136 O LEU A 85
SHEET 6 AA 7 ARG A 183 ALA A 189 1 O ARG A 183 N LEU A 141
SHEET 7 AA 7 VAL A 244 VAL A 247 1 O MET A 245 N SER A 188
SITE 1 AC1 30 GLY A 13 LEU A 15 SER A 19 ILE A 20
SITE 2 AC1 30 VAL A 40 CYS A 63 ASP A 64 VAL A 65
SITE 3 AC1 30 SER A 91 ILE A 92 GLY A 93 LEU A 144
SITE 4 AC1 30 SER A 145 LYS A 163 ALA A 189 GLY A 190
SITE 5 AC1 30 PRO A 191 ILE A 192 1S5 A1260 HOH A2038
SITE 6 AC1 30 HOH A2039 HOH A2044 HOH A2053 HOH A2101
SITE 7 AC1 30 HOH A2198 HOH A2338 HOH A2339 HOH A2340
SITE 8 AC1 30 HOH A2341 HOH A2342
SITE 1 AC2 9 GLY A 93 ALA A 95 ILE A 100 PRO A 154
SITE 2 AC2 9 ASN A 155 TYR A 156 PHE A 203 ILE A 206
SITE 3 AC2 9 NAI A1259
CRYST1 74.320 75.950 89.420 90.00 90.00 90.00 I 2 2 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.013455 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013167 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011183 0.00000
(ATOM LINES ARE NOT SHOWN.)
END