HEADER ISOMERASE 19-JUN-12 4FNB
TITLE CRYSTAL STRUCTURE OF THE MTB ENOYL COA ISOMERASE (RV0632C) IN COMPLEX
TITLE 2 WITH HYDROXYBUTYRL COA
CAVEAT 4FNB CHIRALITY ERROR AT C3, C3B AND C1B OF 3HC A 302
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENOYL-COA HYDRATASE/ISOMERASE FAMILY PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ENOYL-COA HYDRATASE HOMOLOG, PROBABLE ENOYL-COA HYDRATASE
COMPND 5 ECHA3 (ENOYL HYDRASE) (UNSATURATED ACYL-COA HYDRATASE) (CROTONASE);
COMPND 6 EC: 4.2.1.17;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 GENE: ECHA3, MT0660, RV0632C;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PVP16
KEYWDS STRUCTURAL GENOMICS, TB STRUCTURAL GENOMICS CONSORTIUM, TBSGC,
KEYWDS 2 CROTONASE SUPERFAMILY, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.B.BRUNING,N.GAO,E.D.HERNANDEZ,H.LI,N.DANG,L.W.HUNG,J.C.SACCHETTINI,
AUTHOR 2 TB STRUCTURAL GENOMICS CONSORTIUM (TBSGC)
REVDAT 2 13-SEP-23 4FNB 1 REMARK SEQADV
REVDAT 1 29-MAY-13 4FNB 0
JRNL AUTH J.B.BRUNING,N.GAO,E.D.HERNANDEZ,H.LI,N.DANG,L.W.HUNG,
JRNL AUTH 2 S.MORAN,J.C.SACCHETTINI
JRNL TITL CRYSTAL STRUCTURE AND MECHANISM OF THE PROKARYOTIC ENOYL COA
JRNL TITL 2 ISOMERASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.6.1_357
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 : MLHL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.07
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 20850
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.170
REMARK 3 FREE R VALUE TEST SET COUNT : 1077
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 35.0748 - 3.5989 0.99 2725 135 0.1890 0.1997
REMARK 3 2 3.5989 - 2.8570 1.00 2572 123 0.1607 0.1936
REMARK 3 3 2.8570 - 2.4959 1.00 2502 144 0.1716 0.1962
REMARK 3 4 2.4959 - 2.2678 1.00 2460 163 0.1680 0.2236
REMARK 3 5 2.2678 - 2.1053 1.00 2480 124 0.1733 0.2579
REMARK 3 6 2.1053 - 1.9811 0.99 2446 140 0.1875 0.2132
REMARK 3 7 1.9811 - 1.8819 0.98 2409 128 0.2036 0.2536
REMARK 3 8 1.8819 - 1.8000 0.90 2179 120 0.2504 0.3032
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 : 0.41
REMARK 3 B_SOL : 60.70
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.640
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.98
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.83
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.97040
REMARK 3 B22 (A**2) : -0.97040
REMARK 3 B33 (A**2) : 1.94090
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 : 0.007 1810
REMARK 3 ANGLE : 1.050 2461
REMARK 3 CHIRALITY : 0.070 281
REMARK 3 PLANARITY : 0.016 313
REMARK 3 DIHEDRAL : 16.533 685
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 0:48)
REMARK 3 ORIGIN FOR THE GROUP (A): -31.8027 2.4798 20.0045
REMARK 3 T TENSOR
REMARK 3 T11: 0.1164 T22: 0.1670
REMARK 3 T33: 0.2047 T12: 0.0008
REMARK 3 T13: -0.0000 T23: 0.0073
REMARK 3 L TENSOR
REMARK 3 L11: 0.0324 L22: 0.7800
REMARK 3 L33: 0.2465 L12: -0.1163
REMARK 3 L13: 0.0230 L23: -0.0285
REMARK 3 S TENSOR
REMARK 3 S11: 0.0098 S12: 0.0445 S13: -0.0219
REMARK 3 S21: 0.0060 S22: 0.0019 S23: 0.2846
REMARK 3 S31: -0.0248 S32: -0.1380 S33: -0.0088
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 49:81)
REMARK 3 ORIGIN FOR THE GROUP (A): -26.5318 -10.9032 16.1126
REMARK 3 T TENSOR
REMARK 3 T11: 0.1768 T22: 0.1441
REMARK 3 T33: 0.1565 T12: -0.0381
REMARK 3 T13: -0.0048 T23: -0.0049
REMARK 3 L TENSOR
REMARK 3 L11: 0.1862 L22: 0.0800
REMARK 3 L33: 0.1816 L12: -0.0466
REMARK 3 L13: 0.0672 L23: -0.0947
REMARK 3 S TENSOR
REMARK 3 S11: -0.0095 S12: 0.0272 S13: -0.0720
REMARK 3 S21: -0.0763 S22: 0.0519 S23: 0.0436
REMARK 3 S31: 0.0796 S32: -0.0194 S33: -0.0646
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 82:177)
REMARK 3 ORIGIN FOR THE GROUP (A): -13.8590 -4.7340 20.5254
REMARK 3 T TENSOR
REMARK 3 T11: 0.1165 T22: 0.1184
REMARK 3 T33: 0.1145 T12: 0.0017
REMARK 3 T13: -0.0036 T23: -0.0061
REMARK 3 L TENSOR
REMARK 3 L11: 0.0835 L22: 0.3319
REMARK 3 L33: 0.2208 L12: 0.0713
REMARK 3 L13: 0.0106 L23: -0.2342
REMARK 3 S TENSOR
REMARK 3 S11: -0.0166 S12: 0.0052 S13: -0.0153
REMARK 3 S21: 0.0439 S22: 0.0111 S23: -0.0427
REMARK 3 S31: -0.0491 S32: 0.0217 S33: 0.0033
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 178:193)
REMARK 3 ORIGIN FOR THE GROUP (A): -20.8179 6.8614 33.7254
REMARK 3 T TENSOR
REMARK 3 T11: 0.1643 T22: 0.1428
REMARK 3 T33: 0.0827 T12: -0.0050
REMARK 3 T13: 0.0104 T23: -0.0243
REMARK 3 L TENSOR
REMARK 3 L11: 0.4591 L22: 0.2496
REMARK 3 L33: 0.0224 L12: 0.0822
REMARK 3 L13: 0.0871 L23: 0.0057
REMARK 3 S TENSOR
REMARK 3 S11: 0.0811 S12: -0.1368 S13: -0.0149
REMARK 3 S21: 0.0914 S22: -0.0592 S23: 0.0549
REMARK 3 S31: -0.0155 S32: -0.0606 S33: 0.0046
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 194:211)
REMARK 3 ORIGIN FOR THE GROUP (A): -14.7233 14.9924 15.3554
REMARK 3 T TENSOR
REMARK 3 T11: 0.1537 T22: 0.1584
REMARK 3 T33: 0.1537 T12: 0.0108
REMARK 3 T13: -0.0182 T23: -0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 0.4004 L22: 0.0256
REMARK 3 L33: 0.1265 L12: -0.0028
REMARK 3 L13: 0.1618 L23: -0.0403
REMARK 3 S TENSOR
REMARK 3 S11: -0.0451 S12: 0.0182 S13: 0.1417
REMARK 3 S21: 0.0104 S22: 0.0456 S23: -0.0074
REMARK 3 S31: -0.0904 S32: -0.0022 S33: 0.0436
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN A AND RESID 212:231)
REMARK 3 ORIGIN FOR THE GROUP (A): -15.7573 -6.7782 3.6374
REMARK 3 T TENSOR
REMARK 3 T11: 0.2149 T22: 0.2173
REMARK 3 T33: 0.1089 T12: 0.0164
REMARK 3 T13: 0.0118 T23: -0.0325
REMARK 3 L TENSOR
REMARK 3 L11: 0.2720 L22: 0.8382
REMARK 3 L33: 0.0189 L12: -0.0179
REMARK 3 L13: 0.0169 L23: -0.0887
REMARK 3 S TENSOR
REMARK 3 S11: 0.0454 S12: 0.2798 S13: -0.0233
REMARK 3 S21: -0.4017 S22: -0.0371 S23: -0.1491
REMARK 3 S31: -0.0119 S32: -0.1046 S33: 0.0202
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 4FNB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUN-12.
REMARK 100 THE DEPOSITION ID IS D_1000073113.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-MAR-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL CRYO-COOLED
REMARK 200 SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK 9.9L
REMARK 200 DATA SCALING SOFTWARE : D*TREK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20872
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 35.070
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 5.960
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : 0.06200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.0000
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) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.24
REMARK 200 R MERGE FOR SHELL (I) : 0.35100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
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 4FN7 SUBUNIT A
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z
REMARK 290 10555 -Y,-X,-Z+1/2
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 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 75.77850
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 75.77850
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 75.77850
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 75.77850
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 75.77850
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 75.77850
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -106.0 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 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 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 S SO4 A 303 LIES ON A SPECIAL POSITION.
REMARK 375 O1 SO4 A 303 LIES ON A SPECIAL POSITION.
REMARK 375 S SO4 A 304 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 539 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 575 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 609 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 617 LIES ON A SPECIAL POSITION.
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 GLU A 71 CG 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 O HOH A 550 O HOH A 564 2.06
REMARK 500 O HOH A 602 O HOH A 612 2.08
REMARK 500 NH1 ARG A 193 O HOH A 631 2.17
REMARK 500 O HOH A 587 O HOH A 600 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 A 625 O HOH A 630 8555 1.82
REMARK 500 O HOH A 613 O HOH A 615 2555 2.11
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 ASP A 11 -107.39 43.65
REMARK 500 LYS A 22 -118.46 -140.97
REMARK 500 ASN A 54 -163.14 -111.45
REMARK 500 ALA A 106 -122.66 57.46
REMARK 500 THR A 158 -76.18 -91.26
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3HC A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 304
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4FN7 RELATED DB: PDB
REMARK 900 APO FORM OF ENZYME
REMARK 900 RELATED ID: 4FN8 RELATED DB: PDB
REMARK 900 ACETOACETYL BOUND FORM OF ENZYME
REMARK 900 RELATED ID: 4FND RELATED DB: PDB
REMARK 900 RELATED ID: RV0632C RELATED DB: TARGETTRACK
DBREF 4FNB A 1 231 UNP P96907 P96907_MYCTU 1 231
SEQADV 4FNB SER A 0 UNP P96907 EXPRESSION TAG
SEQRES 1 A 232 SER MET SER ASP PRO VAL SER TYR THR ARG LYS ASP SER
SEQRES 2 A 232 ILE ALA VAL ILE SER MET ASP ASP GLY LYS VAL ASN ALA
SEQRES 3 A 232 LEU GLY PRO ALA MET GLN GLN ALA LEU ASN ALA ALA ILE
SEQRES 4 A 232 ASP ASN ALA ASP ARG ASP ASP VAL GLY ALA LEU VAL ILE
SEQRES 5 A 232 THR GLY ASN GLY ARG VAL PHE SER GLY GLY PHE ASP LEU
SEQRES 6 A 232 LYS ILE LEU THR SER GLY GLU VAL GLN PRO ALA ILE ASP
SEQRES 7 A 232 MET LEU ARG GLY GLY PHE GLU LEU ALA TYR ARG LEU LEU
SEQRES 8 A 232 SER TYR PRO LYS PRO VAL VAL MET ALA CYS THR GLY HIS
SEQRES 9 A 232 ALA ILE ALA MET GLY ALA PHE LEU LEU SER CYS GLY ASP
SEQRES 10 A 232 HIS ARG VAL ALA ALA HIS ALA TYR ASN ILE GLN ALA ASN
SEQRES 11 A 232 GLU VAL ALA ILE GLY MET THR ILE PRO TYR ALA ALA LEU
SEQRES 12 A 232 GLU ILE MET LYS LEU ARG LEU THR ARG SER ALA TYR GLN
SEQRES 13 A 232 GLN ALA THR GLY LEU ALA LYS THR PHE PHE GLY GLU THR
SEQRES 14 A 232 ALA LEU ALA ALA GLY PHE ILE ASP GLU ILE ALA LEU PRO
SEQRES 15 A 232 GLU VAL VAL VAL SER ARG ALA GLU GLU ALA ALA ARG GLU
SEQRES 16 A 232 PHE ALA GLY LEU ASN GLN HIS ALA HIS ALA ALA THR LYS
SEQRES 17 A 232 LEU ARG SER ARG ALA ASP ALA LEU THR ALA ILE ARG ALA
SEQRES 18 A 232 GLY ILE ASP GLY ILE ALA ALA GLU PHE GLY LEU
HET SO4 A 301 5
HET 3HC A 302 54
HET SO4 A 303 5
HET SO4 A 304 5
HETNAM SO4 SULFATE ION
HETNAM 3HC 3-HYDROXYBUTANOYL-COENZYME A
HETSYN 3HC 3-HYDROXYBUTYRYL-COENZYME A
FORMUL 2 SO4 3(O4 S 2-)
FORMUL 3 3HC C25 H42 N7 O18 P3 S
FORMUL 6 HOH *233(H2 O)
HELIX 1 1 GLY A 27 ASP A 45 1 19
HELIX 2 2 ASP A 63 THR A 68 1 6
HELIX 3 3 GLU A 71 SER A 91 1 21
HELIX 4 4 ALA A 106 SER A 113 1 8
HELIX 5 5 ASN A 129 GLY A 134 1 6
HELIX 6 6 PRO A 138 LEU A 149 1 12
HELIX 7 7 THR A 150 LEU A 160 1 11
HELIX 8 8 PHE A 165 GLY A 173 1 9
HELIX 9 9 LEU A 180 GLU A 182 5 3
HELIX 10 10 VAL A 183 ALA A 196 1 14
HELIX 11 11 ASN A 199 SER A 210 1 12
HELIX 12 12 ARG A 211 GLY A 224 1 14
HELIX 13 13 GLY A 224 PHE A 229 1 6
SHEET 1 A 6 VAL A 5 LYS A 10 0
SHEET 2 A 6 ILE A 13 MET A 18 -1 O VAL A 15 N THR A 8
SHEET 3 A 6 ALA A 48 THR A 52 1 O VAL A 50 N ILE A 16
SHEET 4 A 6 VAL A 96 CYS A 100 1 O ALA A 99 N ILE A 51
SHEET 5 A 6 HIS A 117 ALA A 120 1 O VAL A 119 N CYS A 100
SHEET 6 A 6 GLU A 177 ILE A 178 1 O GLU A 177 N ALA A 120
SHEET 1 B 4 VAL A 57 SER A 59 0
SHEET 2 B 4 HIS A 103 ILE A 105 1 O HIS A 103 N PHE A 58
SHEET 3 B 4 ILE A 126 GLN A 127 1 O GLN A 127 N ALA A 104
SHEET 4 B 4 THR A 163 PHE A 164 -1 O PHE A 164 N ILE A 126
SITE 1 AC1 7 ASN A 40 ARG A 43 ASN A 199 GLN A 200
SITE 2 AC1 7 HIS A 201 HOH A 508 HOH A 578
SITE 1 AC2 20 SER A 2 LYS A 22 VAL A 23 ARG A 56
SITE 2 AC2 20 GLY A 60 PHE A 62 ASP A 63 LEU A 64
SITE 3 AC2 20 LEU A 67 ASN A 129 GLU A 130 ILE A 133
SITE 4 AC2 20 PRO A 138 HOH A 401 HOH A 412 HOH A 487
SITE 5 AC2 20 HOH A 562 HOH A 575 HOH A 588 HOH A 610
SITE 1 AC3 3 THR A 150 ARG A 151 HOH A 617
SITE 1 AC4 2 ARG A 9 HOH A 556
CRYST1 70.136 70.136 151.557 90.00 90.00 120.00 P 63 2 2 12
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 0.014258 0.008232 0.000000 0.00000
SCALE2 0.000000 0.016464 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006598 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
