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HEADER HYDROLASE 02-OCT-09 2WUF
TITLE CRYSTAL STRUCTURE OF S114A MUTANT OF HSAD FROM
TITLE 2 MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH 4,9DSHA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 2-HYDROXY-6-OXO-6-PHENYLHEXA-2,4-DIENOATE
COMPND 3 HYDROLASE BPHD;
COMPND 4 CHAIN: A, B;
COMPND 5 SYNONYM: HSAD, 2-HYDROXY-6-PHENYLHEXA-2\,4-DIENOIC ACID
COMPND 6 HYDROLASE;
COMPND 7 EC: 3.7.1.8;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 668369;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: DH5[ALPHA];
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PT7-7
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.A.LACK,K.C.YAM,E.D.LOWE,G.P.HORSMAN,R.OWEN,E.SIM,
AUTHOR 2 L.D.ELTIS
REVDAT 2 10-NOV-09 2WUF 1 JRNL
REVDAT 1 20-OCT-09 2WUF 0
JRNL AUTH N.A.LACK,K.C.YAM,E.D.LOWE,G.P.HORSMAN,R.OWEN,E.SIM,
JRNL AUTH 2 L.D.ELTIS
JRNL TITL CHARACTERIZATION OF A C-C HYDROLASE FROM
JRNL TITL 2 MYCOBACTERIUM TUBERCULOSIS INVOLVED IN CHOLESTEROL
JRNL TITL 3 METABOLISM
JRNL REF J.BIOL.CHEM. 2009
JRNL REFN ESSN 1083-351X
JRNL PMID 19875455
JRNL DOI 10.1074/JBC.M109.058081
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.59
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.0
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 42140
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.1
REMARK 3 FREE R VALUE TEST SET COUNT : 2252
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 40.5992 - 4.7853 0.93 2692 168 0.2192 0.2184
REMARK 3 2 4.7853 - 3.7992 0.94 2660 146 0.1575 0.1712
REMARK 3 3 3.7992 - 3.3192 0.97 2737 147 0.1749 0.1931
REMARK 3 4 3.3192 - 3.0158 0.97 2699 149 0.2120 0.2285
REMARK 3 5 3.0158 - 2.7997 0.97 2702 158 0.2154 0.2273
REMARK 3 6 2.7997 - 2.6347 0.97 2723 133 0.2192 0.2544
REMARK 3 7 2.6347 - 2.5027 0.97 2716 134 0.2156 0.3049
REMARK 3 8 2.5027 - 2.3938 0.97 2672 143 0.1967 0.2388
REMARK 3 9 2.3938 - 2.3017 0.96 2651 160 0.1967 0.2554
REMARK 3 10 2.3017 - 2.2223 0.96 2676 128 0.1989 0.2410
REMARK 3 11 2.2223 - 2.1528 0.95 2614 129 0.2132 0.2788
REMARK 3 12 2.1528 - 2.0912 0.95 2618 152 0.2103 0.2453
REMARK 3 13 2.0912 - 2.0362 0.92 2523 140 0.2189 0.2566
REMARK 3 14 2.0362 - 1.9865 0.91 2561 137 0.2244 0.2646
REMARK 3 15 1.9865 - 1.9414 0.89 2482 110 0.2445 0.3156
REMARK 3 16 1.9414 - 1.9000 0.88 2414 118 0.2530 0.3337
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.39
REMARK 3 B_SOL : 75.10
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.31
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.99
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.5
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.4
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 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 : 0.010 NULL
REMARK 3 ANGLE : 0.820 NULL
REMARK 3 CHIRALITY : 0.071 NULL
REMARK 3 PLANARITY : 0.004 NULL
REMARK 3 DIHEDRAL : 11.16 NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A)
REMARK 3 ORIGIN FOR THE GROUP (A): -13.6530 -16.5513 29.0404
REMARK 3 T TENSOR
REMARK 3 T11: 0.1679 T22: 0.1907
REMARK 3 T33: 0.1281 T12: 0.0084
REMARK 3 T13: 0.0290 T23: 0.0223
REMARK 3 L TENSOR
REMARK 3 L11: 0.7863 L22: 0.2269
REMARK 3 L33: 0.1460 L12: 0.2254
REMARK 3 L13: -0.1083 L23: -0.2139
REMARK 3 S TENSOR
REMARK 3 S11: 0.0463 S22: 0.0748 S33: 0.0076
REMARK 3 S12: 0.1816 S13: 0.2029 S21: 0.0975
REMARK 3 S23: 0.0069 S31: -0.0343 S32: -0.0002
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN B)
REMARK 3 ORIGIN FOR THE GROUP (A): 13.1530 -44.7212 16.1311
REMARK 3 T TENSOR
REMARK 3 T11: 0.1300 T22: 0.1011
REMARK 3 T33: 0.1811 T12: -0.0602
REMARK 3 T13: -0.0615 T23: 0.0393
REMARK 3 L TENSOR
REMARK 3 L11: 0.1360 L22: 0.4706
REMARK 3 L33: 0.4976 L12: -0.1208
REMARK 3 L13: -0.1860 L23: -0.0560
REMARK 3 S TENSOR
REMARK 3 S11: 0.0373 S22: -0.1139 S33: -0.0263
REMARK 3 S12: -0.0012 S13: -0.0080 S21: 0.1580
REMARK 3 S23: -0.2318 S31: -0.1145 S32: 0.0964
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: (CHAIN A AND (RESSEQ 7:209 OR
REMARK 3 RESSEQ 213:288 ))
REMARK 3 SELECTION : (CHAIN B AND (RESSEQ 7:209 OR
REMARK 3 RESSEQ 213:288 ))
REMARK 3 ATOM PAIRS NUMBER : 2257
REMARK 3 RMSD : 0.618
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2WUF COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-OCT-09.
REMARK 100 THE PDBE ID CODE IS EBI-41309.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-SEP-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97570
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : KIRKPATRICK BAEZ BIMORPH
REMARK 200 MIRROR PAIR FOR HORIZONTAL
REMARK 200 AND VERTICAL FOCUSSING
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46107
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.90
REMARK 200 RESOLUTION RANGE LOW (A) : 40.59
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 3.5
REMARK 200 R MERGE (I) : 0.10
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.90
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.5
REMARK 200 R MERGE FOR SHELL (I) : 0.42
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.00
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: PDB ENTRY 2WUD
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 200MM KSCN, 24% PEG 3350, 100MM
REMARK 280 BIS-TRIS PROPANE PH 7.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: F 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,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y+1/2,Z+1/2
REMARK 290 7555 -X,Y+1/2,-Z+1/2
REMARK 290 8555 X,-Y+1/2,-Z+1/2
REMARK 290 9555 X+1/2,Y,Z+1/2
REMARK 290 10555 -X+1/2,-Y,Z+1/2
REMARK 290 11555 -X+1/2,Y,-Z+1/2
REMARK 290 12555 X+1/2,-Y,-Z+1/2
REMARK 290 13555 X+1/2,Y+1/2,Z
REMARK 290 14555 -X+1/2,-Y+1/2,Z
REMARK 290 15555 -X+1/2,Y+1/2,-Z
REMARK 290 16555 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 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 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 58.98550
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 90.44650
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 58.98550
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 90.44650
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 58.98550
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 90.44650
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 58.98550
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 90.44650
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 55.94150
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 90.44650
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 55.94150
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 90.44650
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 55.94150
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 90.44650
REMARK 290 SMTRY1 12 1.000000 0.000000 0.000000 55.94150
REMARK 290 SMTRY2 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 90.44650
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 55.94150
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 58.98550
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 55.94150
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 58.98550
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 55.94150
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 58.98550
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 55.94150
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 58.98550
REMARK 290 SMTRY3 16 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 GENERATING THE BIOMOLECULE
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: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1720 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.12 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 -55.94150
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 90.44650
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.7 KCAL/MOL
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 350 BIOMT1 2 1.000000 0.000000 0.000000 -0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 -117.97100
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, SER 114 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, SER 114 TO ALA
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 THR A 2
REMARK 465 ALA A 3
REMARK 465 THR A 4
REMARK 465 GLU A 5
REMARK 465 GLU A 6
REMARK 465 GLY A 289
REMARK 465 GLY A 290
REMARK 465 ARG A 291
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 ALA B 3
REMARK 465 THR B 4
REMARK 465 GLU B 5
REMARK 465 GLU B 6
REMARK 465 GLY B 289
REMARK 465 GLY B 290
REMARK 465 ARG B 291
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 O1 GOL A 1289 O HOH A 2089 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU B 153 CD GLU B 153 OE2 -0.086
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: 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 A 133 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG B 133 NE - CZ - NH1 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ARG B 133 NE - CZ - NH2 ANGL. DEV. = 6.1 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 ALA A 114 -125.47 52.38
REMARK 500 VAL A 243 -60.25 -100.72
REMARK 500 ASN B 58 -43.88 -130.93
REMARK 500 ALA B 114 -126.05 60.77
REMARK 500 ASP B 216 40.64 -97.32
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 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KEM B1289
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1289
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1290
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN A1290
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2WUD RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF S114A MUTANT OF HSAD
REMARK 900 FROM MYCOBACTERIUM TUBERCULOSIS
REMARK 900 RELATED ID: 2VF2 RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF HSAD FROM
REMARK 900 MYCOBACTERIUM TUBERCULOSIS
REMARK 900 RELATED ID: 2WUE RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF S114A MUTANT OF HSAD
REMARK 900 FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX
REMARK 900 WITH HOPODA
REMARK 900 RELATED ID: 2WUG RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF S114A MUTANT OF HSAD
REMARK 900 FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX
REMARK 900 WITH HOPDA
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 S114A MUTANT
DBREF 2WUF A 1 291 UNP P96851 P96851_MYCTU 1 291
DBREF 2WUF B 1 291 UNP P96851 P96851_MYCTU 1 291
SEQADV 2WUF ALA A 114 UNP P96851 SER 114 ENGINEERED MUTATION
SEQADV 2WUF ALA B 114 UNP P96851 SER 114 ENGINEERED MUTATION
SEQRES 1 A 291 MET THR ALA THR GLU GLU LEU THR PHE GLU SER THR SER
SEQRES 2 A 291 ARG PHE ALA GLU VAL ASP VAL ASP GLY PRO LEU LYS LEU
SEQRES 3 A 291 HIS TYR HIS GLU ALA GLY VAL GLY ASN ASP GLN THR VAL
SEQRES 4 A 291 VAL LEU LEU HIS GLY GLY GLY PRO GLY ALA ALA SER TRP
SEQRES 5 A 291 THR ASN PHE SER ARG ASN ILE ALA VAL LEU ALA ARG HIS
SEQRES 6 A 291 PHE HIS VAL LEU ALA VAL ASP GLN PRO GLY TYR GLY HIS
SEQRES 7 A 291 SER ASP LYS ARG ALA GLU HIS GLY GLN PHE ASN ARG TYR
SEQRES 8 A 291 ALA ALA MET ALA LEU LYS GLY LEU PHE ASP GLN LEU GLY
SEQRES 9 A 291 LEU GLY ARG VAL PRO LEU VAL GLY ASN ALA LEU GLY GLY
SEQRES 10 A 291 GLY THR ALA VAL ARG PHE ALA LEU ASP TYR PRO ALA ARG
SEQRES 11 A 291 ALA GLY ARG LEU VAL LEU MET GLY PRO GLY GLY LEU SER
SEQRES 12 A 291 ILE ASN LEU PHE ALA PRO ASP PRO THR GLU GLY VAL LYS
SEQRES 13 A 291 ARG LEU SER LYS PHE SER VAL ALA PRO THR ARG GLU ASN
SEQRES 14 A 291 LEU GLU ALA PHE LEU ARG VAL MET VAL TYR ASP LYS ASN
SEQRES 15 A 291 LEU ILE THR PRO GLU LEU VAL ASP GLN ARG PHE ALA LEU
SEQRES 16 A 291 ALA SER THR PRO GLU SER LEU THR ALA THR ARG ALA MET
SEQRES 17 A 291 GLY LYS SER PHE ALA GLY ALA ASP PHE GLU ALA GLY MET
SEQRES 18 A 291 MET TRP ARG GLU VAL TYR ARG LEU ARG GLN PRO VAL LEU
SEQRES 19 A 291 LEU ILE TRP GLY ARG GLU ASP ARG VAL ASN PRO LEU ASP
SEQRES 20 A 291 GLY ALA LEU VAL ALA LEU LYS THR ILE PRO ARG ALA GLN
SEQRES 21 A 291 LEU HIS VAL PHE GLY GLN CYS GLY HIS TRP VAL GLN VAL
SEQRES 22 A 291 GLU LYS PHE ASP GLU PHE ASN LYS LEU THR ILE GLU PHE
SEQRES 23 A 291 LEU GLY GLY GLY ARG
SEQRES 1 B 291 MET THR ALA THR GLU GLU LEU THR PHE GLU SER THR SER
SEQRES 2 B 291 ARG PHE ALA GLU VAL ASP VAL ASP GLY PRO LEU LYS LEU
SEQRES 3 B 291 HIS TYR HIS GLU ALA GLY VAL GLY ASN ASP GLN THR VAL
SEQRES 4 B 291 VAL LEU LEU HIS GLY GLY GLY PRO GLY ALA ALA SER TRP
SEQRES 5 B 291 THR ASN PHE SER ARG ASN ILE ALA VAL LEU ALA ARG HIS
SEQRES 6 B 291 PHE HIS VAL LEU ALA VAL ASP GLN PRO GLY TYR GLY HIS
SEQRES 7 B 291 SER ASP LYS ARG ALA GLU HIS GLY GLN PHE ASN ARG TYR
SEQRES 8 B 291 ALA ALA MET ALA LEU LYS GLY LEU PHE ASP GLN LEU GLY
SEQRES 9 B 291 LEU GLY ARG VAL PRO LEU VAL GLY ASN ALA LEU GLY GLY
SEQRES 10 B 291 GLY THR ALA VAL ARG PHE ALA LEU ASP TYR PRO ALA ARG
SEQRES 11 B 291 ALA GLY ARG LEU VAL LEU MET GLY PRO GLY GLY LEU SER
SEQRES 12 B 291 ILE ASN LEU PHE ALA PRO ASP PRO THR GLU GLY VAL LYS
SEQRES 13 B 291 ARG LEU SER LYS PHE SER VAL ALA PRO THR ARG GLU ASN
SEQRES 14 B 291 LEU GLU ALA PHE LEU ARG VAL MET VAL TYR ASP LYS ASN
SEQRES 15 B 291 LEU ILE THR PRO GLU LEU VAL ASP GLN ARG PHE ALA LEU
SEQRES 16 B 291 ALA SER THR PRO GLU SER LEU THR ALA THR ARG ALA MET
SEQRES 17 B 291 GLY LYS SER PHE ALA GLY ALA ASP PHE GLU ALA GLY MET
SEQRES 18 B 291 MET TRP ARG GLU VAL TYR ARG LEU ARG GLN PRO VAL LEU
SEQRES 19 B 291 LEU ILE TRP GLY ARG GLU ASP ARG VAL ASN PRO LEU ASP
SEQRES 20 B 291 GLY ALA LEU VAL ALA LEU LYS THR ILE PRO ARG ALA GLN
SEQRES 21 B 291 LEU HIS VAL PHE GLY GLN CYS GLY HIS TRP VAL GLN VAL
SEQRES 22 B 291 GLU LYS PHE ASP GLU PHE ASN LYS LEU THR ILE GLU PHE
SEQRES 23 B 291 LEU GLY GLY GLY ARG
HET KEM B1289 25
HET GOL A1289 6
HET GOL B1290 6
HET SCN A1290 3
HETNAM KEM (3E,5R)-8-[(1S,3AR,4R,7AS)-1-HYDROXY-7A-
HETNAM 2 KEM METHYL-5-OXOOCTAHYDRO-1H-INDEN-4-YL]-5-METHYL-2,6-
HETNAM 3 KEM DIOXOOCT-3-ENOATE
HETNAM GOL GLYCEROL
HETNAM SCN THIOCYANATE ION
FORMUL 3 KEM C19 H25 O6 1-
FORMUL 4 GOL 2(C3 H8 O3)
FORMUL 5 SCN C N S 1-
FORMUL 6 HOH *183(H2 O)
HELIX 1 1 THR A 8 THR A 12 1 5
HELIX 2 2 ALA A 50 PHE A 55 1 6
HELIX 3 3 ASN A 58 ALA A 63 1 6
HELIX 4 4 GLN A 87 LYS A 97 1 11
HELIX 5 5 THR A 119 TYR A 127 1 9
HELIX 6 6 VAL A 155 ALA A 164 1 10
HELIX 7 7 THR A 166 VAL A 176 1 11
HELIX 8 8 ASP A 180 ILE A 184 5 5
HELIX 9 9 THR A 185 SER A 197 1 13
HELIX 10 10 THR A 198 MET A 208 1 11
HELIX 11 11 MET A 221 GLU A 225 5 5
HELIX 12 12 GLU A 225 LEU A 229 5 5
HELIX 13 13 ALA A 249 ILE A 256 1 8
HELIX 14 14 TRP A 270 LYS A 275 1 6
HELIX 15 15 LYS A 275 LEU A 287 1 13
HELIX 16 16 THR B 8 THR B 12 1 5
HELIX 17 17 ALA B 50 PHE B 55 1 6
HELIX 18 18 PHE B 55 ALA B 63 1 9
HELIX 19 19 GLN B 87 LYS B 97 1 11
HELIX 20 20 THR B 119 TYR B 127 1 9
HELIX 21 21 VAL B 155 ALA B 164 1 10
HELIX 22 22 THR B 166 VAL B 176 1 11
HELIX 23 23 ASP B 180 ILE B 184 5 5
HELIX 24 24 THR B 185 SER B 197 1 13
HELIX 25 25 THR B 198 MET B 208 1 11
HELIX 26 26 MET B 221 GLU B 225 5 5
HELIX 27 27 GLU B 225 LEU B 229 5 5
HELIX 28 28 ALA B 249 ILE B 256 1 8
HELIX 29 29 TRP B 270 LYS B 275 1 6
HELIX 30 30 LYS B 275 LEU B 287 1 13
SHEET 1 AA 5 SER A 13 VAL A 18 0
SHEET 2 AA 5 LEU A 24 ALA A 31 -1 O LEU A 24 N VAL A 18
SHEET 3 AA 5 HIS A 67 VAL A 71 -1 O VAL A 68 N ALA A 31
SHEET 4 AA 5 THR A 38 LEU A 42 1 O VAL A 39 N LEU A 69
SHEET 5 AA 5 LEU A 110 VAL A 111 1 O VAL A 111 N LEU A 42
SHEET 1 AB 3 LEU A 134 LEU A 136 0
SHEET 2 AB 3 VAL A 233 TRP A 237 1 O LEU A 234 N LEU A 136
SHEET 3 AB 3 ALA A 259 VAL A 263 1 O GLN A 260 N LEU A 235
SHEET 1 BA 5 SER B 13 VAL B 18 0
SHEET 2 BA 5 LEU B 24 ALA B 31 -1 O LEU B 24 N VAL B 18
SHEET 3 BA 5 HIS B 67 VAL B 71 -1 O VAL B 68 N ALA B 31
SHEET 4 BA 5 THR B 38 LEU B 42 1 O VAL B 39 N LEU B 69
SHEET 5 BA 5 LEU B 110 VAL B 111 1 O VAL B 111 N LEU B 42
SHEET 1 BB 3 LEU B 134 LEU B 136 0
SHEET 2 BB 3 VAL B 233 TRP B 237 1 O LEU B 234 N LEU B 136
SHEET 3 BB 3 ALA B 259 VAL B 263 1 O GLN B 260 N LEU B 235
LINK CZ BARG B 130 S SCN A1290 13455 1555 1.99
LINK NH1BARG B 130 C SCN A1290 13455 1555 1.08
LINK NH2BARG B 130 C SCN A1290 13455 1555 1.27
LINK CZ BARG B 130 N SCN A1290 13455 1555 1.16
LINK NH1BARG B 130 N SCN A1290 13455 1555 0.93
LINK NE BARG B 130 N SCN A1290 13455 1555 1.56
CISPEP 1 ASP A 150 PRO A 151 0 -0.04
CISPEP 2 ASP B 150 PRO B 151 0 -3.21
SITE 1 AC1 13 GLY B 44 GLY B 45 GLY B 46 ALA B 49
SITE 2 AC1 13 ASN B 54 ALA B 114 LEU B 115 LEU B 158
SITE 3 AC1 13 ARG B 192 PHE B 212 HIS B 269 TRP B 270
SITE 4 AC1 13 HOH B2093
SITE 1 AC2 5 PHE A 9 TRP A 52 HOH A2089 HOH A2090
SITE 2 AC2 5 ARG B 167
SITE 1 AC3 1 PHE B 15
SITE 1 AC4 5 ARG A 130 TYR B 127 PRO B 128 ALA B 129
SITE 2 AC4 5 ARG B 130
CRYST1 111.883 117.971 180.893 90.00 90.00 90.00 F 2 2 2 32
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 0.008938 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008477 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005528 0.00000
MTRIX1 1 0.025519 0.999653 -0.006465 30.92380 1
MTRIX2 1 0.999663 -0.025549 -0.004620 -30.90240 1
MTRIX3 1 -0.004783 -0.006345 -0.999968 44.96370 1
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