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HEADER HYDROLASE 02-OCT-09 2WUG
TITLE CRYSTAL STRUCTURE OF S114A MUTANT OF HSAD FROM
TITLE 2 MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH HOPDA
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.L.OWEN,E.SIM,
AUTHOR 2 L.D.ELTIS
REVDAT 2 10-NOV-09 2WUG 1 AUTHOR JRNL
REVDAT 1 20-OCT-09 2WUG 0
JRNL AUTH N.A.LACK,K.C.YAM,E.D.LOWE,G.P.HORSMAN,R.L.OWEN,
JRNL AUTH 2 E.SIM,L.D.ELTIS
JRNL TITL CHARACTERIZATION OF A C-C HYDROLASE FROM
JRNL TITL 2 MYCOBACTERIUM TUBERUCLOSIS 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. 1.80 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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.49
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 3 NUMBER OF REFLECTIONS : 54360
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.167
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 2730
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 28.0431 - 4.7485 0.99 2956 161 0.1794 0.1899
REMARK 3 2 4.7485 - 3.7719 0.99 2863 150 0.1450 0.1535
REMARK 3 3 3.7719 - 3.2960 0.99 2814 157 0.1552 0.1811
REMARK 3 4 3.2960 - 2.9950 0.99 2833 147 0.1755 0.2116
REMARK 3 5 2.9950 - 2.7805 0.99 2810 159 0.1759 0.2051
REMARK 3 6 2.7805 - 2.6167 0.98 2776 136 0.1757 0.1963
REMARK 3 7 2.6167 - 2.4857 0.98 2796 151 0.1639 0.2203
REMARK 3 8 2.4857 - 2.3776 0.98 2772 154 0.1508 0.1919
REMARK 3 9 2.3776 - 2.2861 0.97 2777 119 0.1542 0.1580
REMARK 3 10 2.2861 - 2.2073 0.97 2756 137 0.1535 0.1926
REMARK 3 11 2.2073 - 2.1383 0.97 2732 138 0.1594 0.2001
REMARK 3 12 2.1383 - 2.0772 0.97 2764 150 0.1604 0.1782
REMARK 3 13 2.0772 - 2.0225 0.97 2762 128 0.1643 0.1819
REMARK 3 14 2.0225 - 1.9732 0.97 2721 156 0.1577 0.2028
REMARK 3 15 1.9732 - 1.9283 0.95 2644 169 0.1712 0.1966
REMARK 3 16 1.9283 - 1.8873 0.95 2694 142 0.1742 0.2265
REMARK 3 17 1.8873 - 1.8496 0.95 2681 132 0.1766 0.2026
REMARK 3 18 1.8496 - 1.8147 0.94 2651 146 0.1864 0.2462
REMARK 3 19 1.8147 - 1.7823 0.65 1828 98 0.1977 0.2242
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 : 50.68
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.22
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.94
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.5
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.6
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 : 0.008 NULL
REMARK 3 ANGLE : 0.774 NULL
REMARK 3 CHIRALITY : 0.063 NULL
REMARK 3 PLANARITY : 0.005 NULL
REMARK 3 DIHEDRAL : 10.420 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): -13.7086 -16.5145 29.2109
REMARK 3 T TENSOR
REMARK 3 T11: 0.0444 T22: 0.0620
REMARK 3 T33: 0.0348 T12: -0.0356
REMARK 3 T13: 0.0003 T23: 0.0034
REMARK 3 L TENSOR
REMARK 3 L11: 0.4296 L22: 0.3160
REMARK 3 L33: 0.1928 L12: -0.0502
REMARK 3 L13: -0.0814 L23: -0.0943
REMARK 3 S TENSOR
REMARK 3 S11: -0.0450 S22: 0.0448 S33: -0.0000
REMARK 3 S12: 0.0315 S13: 0.0375 S21: -0.0196
REMARK 3 S23: -0.0581 S31: -0.0277 S32: 0.0384
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN B)
REMARK 3 ORIGIN FOR THE GROUP (A): 13.3215 -44.7371 15.9484
REMARK 3 T TENSOR
REMARK 3 T11: 0.0838 T22: 0.0581
REMARK 3 T33: 0.0907 T12: -0.0488
REMARK 3 T13: -0.0319 T23: 0.0092
REMARK 3 L TENSOR
REMARK 3 L11: 0.3093 L22: 0.3426
REMARK 3 L33: 0.4987 L12: -0.3139
REMARK 3 L13: -0.1615 L23: 0.0391
REMARK 3 S TENSOR
REMARK 3 S11: -0.0023 S22: -0.0337 S33: -0.0268
REMARK 3 S12: -0.0518 S13: 0.0920 S21: 0.0485
REMARK 3 S23: -0.0959 S31: -0.1038 S32: 0.0982
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)
REMARK 3 SELECTION : (CHAIN B)
REMARK 3 ATOM PAIRS NUMBER : 2249
REMARK 3 RMSD : 0.527
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2WUG COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-OCT-09.
REMARK 100 THE PDBE ID CODE IS EBI-41307.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-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 : 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) : 1.00010
REMARK 200 MONOCHROMATOR : FIXED-EXIT LN2 COOLED
REMARK 200 DOUBLE CRYSTAL
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : RH COATED MERIDIONALLY
REMARK 200 FOCUSSING MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55165
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.80
REMARK 200 RESOLUTION RANGE LOW (A) : 29.49
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 5.0
REMARK 200 R MERGE (I) : 0.07
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.00
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.0
REMARK 200 R MERGE FOR SHELL (I) : 0.41
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.10
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 (%): 48.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 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 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 O HOH B 2119 O HOH B 2121 0.05
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 B 133 NE - CZ - NH1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG B 133 NE - CZ - NH2 ANGL. DEV. = 5.3 DEGREES
REMARK 500 ARG B 228 NE - CZ - NH1 ANGL. DEV. = 4.5 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 -120.60 51.21
REMARK 500 ALA B 114 -118.97 50.51
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 PRO B 23 -10.22
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 HPK A1290
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN A1291
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HPK B1290
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1291
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: 2WUF RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF S114A MUTANT OF HSAD
REMARK 900 FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX
REMARK 900 WITH 4,9DSHA
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 S114A MUTANT
DBREF 2WUG A 1 291 UNP P96851 P96851_MYCTU 1 291
DBREF 2WUG B 1 291 UNP P96851 P96851_MYCTU 1 291
SEQADV 2WUG ALA A 114 UNP P96851 SER 114 ENGINEERED MUTATION
SEQADV 2WUG 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 HPK A1290 16
HET SCN A1291 3
HET HPK B1290 16
HET GOL B1291 6
HETNAM GOL GLYCEROL
HETNAM HPK (3E)-2,6-DIOXO-6-PHENYLHEX-3-ENOATE
HETNAM SCN THIOCYANATE ION
FORMUL 3 GOL C3 H8 O3
FORMUL 4 HPK 2(C12 H9 O4 1-)
FORMUL 5 SCN C N S 1-
FORMUL 6 HOH *275(H2 O)
HELIX 1 1 THR A 8 THR A 12 1 5
HELIX 2 2 ALA A 50 ALA A 63 1 14
HELIX 3 3 GLN A 87 LYS A 97 1 11
HELIX 4 4 THR A 119 TYR A 127 1 9
HELIX 5 5 PRO A 128 ALA A 131 5 4
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 ALA B 63 1 14
HELIX 18 18 GLN B 87 LYS B 97 1 11
HELIX 19 19 THR B 119 TYR B 127 1 9
HELIX 20 20 PRO B 128 ALA B 131 5 4
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
CISPEP 1 ASP A 150 PRO A 151 0 -0.69
CISPEP 2 ASP B 150 PRO B 151 0 -2.01
SITE 1 AC1 12 GLY A 44 GLY A 45 GLY A 46 ALA A 49
SITE 2 AC1 12 ASN A 54 ASN A 113 ALA A 114 LEU A 115
SITE 3 AC1 12 ARG A 192 MET A 208 HIS A 269 TRP A 270
SITE 1 AC2 6 LYS A 97 TYR A 127 ALA A 129 ARG A 130
SITE 2 AC2 6 GLY B 106 ARG B 130
SITE 1 AC3 11 GLY B 45 GLY B 46 ALA B 49 ASN B 54
SITE 2 AC3 11 ASN B 113 ALA B 114 LEU B 115 VAL B 155
SITE 3 AC3 11 ARG B 192 HIS B 269 TRP B 270
SITE 1 AC4 1 TYR B 179
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 0.025482 0.999643 -0.007984 30.86480 1
MTRIX2 1 0.999668 -0.025512 -0.003644 -30.86400 1
MTRIX3 1 -0.003847 -0.007889 -0.999961 44.83840 1
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