HEADER OXIDOREDUCTASE 22-DEC-09 3L60
TITLE CRYSTAL STRUCTURE OF BRANCHED-CHAIN ALPHA-KETO ACID
TITLE 2 DEHYDROGENASE SUBUNIT E2 FROM MYCOBACTERIUM TUBERCULOSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL FRAGMENT, RESIDUES 155-393;
COMPND 5 SYNONYM: PROBABLE DIHYDROLIPOAMIDE S-ACETYLTRANSFERASE E2
COMPND 6 COMPONENT PDHC (LIPOATE ACETYLTRANSFERASE)
COMPND 7 (THIOLTRANSACETYLASE A);
COMPND 8 EC: 2.3.1.12;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 GENE: PDHC, RV2495C;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS STRUCTURAL GENOMICS, PSI-2, DEHYDROGENASE, PROTEIN STRUCTURE
KEYWDS 2 INITIATIVE, NEW YORK SGX RESEARCH CENTER FOR STRUCTURAL
KEYWDS 3 GENOMICS, NYSGXRC
EXPDTA X-RAY DIFFRACTION
AUTHOR W.D.ZENCHECK,J.B.BONNANO,Y.PATSKOVSKY,R.TORO,J.FREEMAN,
AUTHOR 2 J.M.SAUDER,S.K.BURLEY,S.C.ALMO,NEW YORK SGX RESEARCH CENTER
AUTHOR 3 FOR STRUCTURAL GENOMICS (NYSGXRC)
REVDAT 1 05-JAN-10 3L60 0
JRNL AUTH W.D.ZENCHECK,J.B.BONNANO,Y.PATSKOVSKY,R.TORO,
JRNL AUTH 2 J.FREEMAN,J.M.SAUDER,S.K.BURLEY,S.C.ALMO
JRNL TITL CRYSTAL STRUCTURE OF BRANCHED-CHAIN ALPHA-KETO ACID
JRNL TITL 2 DEHYDROGENASE SUBUNIT E2 FROM MYCOBACTERIUM
JRNL TITL 3 TUBERCULOSIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0089
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 17990
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 979
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1323
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.1970
REMARK 3 BIN FREE R VALUE SET COUNT : 65
REMARK 3 BIN FREE R VALUE : 0.2050
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1703
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 9
REMARK 3 SOLVENT ATOMS : 140
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.68
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.155
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.145
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.093
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.247
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.940
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1744 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1144 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2380 ; 1.448 ; 1.975
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2803 ; 0.921 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 230 ; 6.088 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 66 ;32.842 ;23.182
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 275 ;13.900 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;25.315 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 292 ; 0.077 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1950 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 334 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1143 ; 0.921 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 465 ; 0.208 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1846 ; 1.633 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 601 ; 2.142 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 533 ; 3.545 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 3L60 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-DEC-09.
REMARK 100 THE RCSB ID CODE IS RCSB056876.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-NOV-09
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18995
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -5.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 19.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 19.10
REMARK 200 R MERGE FOR SHELL (I) : 0.36000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 60% TASCIMATE, PH 7, 10% GLYCEROL,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 3
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 Z,X,Y
REMARK 290 6555 Z,-X,-Y
REMARK 290 7555 -Z,-X,Y
REMARK 290 8555 -Z,X,-Y
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z,-X
REMARK 290 11555 Y,-Z,-X
REMARK 290 12555 -Y,-Z,X
REMARK 290 13555 X+1/2,Y+1/2,Z+1/2
REMARK 290 14555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 15555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 16555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 17555 Z+1/2,X+1/2,Y+1/2
REMARK 290 18555 Z+1/2,-X+1/2,-Y+1/2
REMARK 290 19555 -Z+1/2,-X+1/2,Y+1/2
REMARK 290 20555 -Z+1/2,X+1/2,-Y+1/2
REMARK 290 21555 Y+1/2,Z+1/2,X+1/2
REMARK 290 22555 -Y+1/2,Z+1/2,-X+1/2
REMARK 290 23555 Y+1/2,-Z+1/2,-X+1/2
REMARK 290 24555 -Y+1/2,-Z+1/2,X+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 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 59.38200
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 59.38200
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 59.38200
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 59.38200
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 59.38200
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 59.38200
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 59.38200
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 59.38200
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 59.38200
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 59.38200
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 59.38200
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 59.38200
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 59.38200
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 59.38200
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 59.38200
REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 59.38200
REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 59.38200
REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 59.38200
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 59.38200
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 59.38200
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 59.38200
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 59.38200
REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 59.38200
REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 59.38200
REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 59.38200
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 59.38200
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 59.38200
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 59.38200
REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 59.38200
REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 59.38200
REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 59.38200
REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 59.38200
REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 59.38200
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 59.38200
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 59.38200
REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 59.38200
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: 9300 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -46.0 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 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT3 3 1.000000 0.000000 0.000000 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 A 8 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 51 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 152
REMARK 465 SER A 153
REMARK 465 LEU A 154
REMARK 465 ALA A 155
REMARK 465 ALA A 156
REMARK 465 ALA A 157
REMARK 465 ARG A 158
REMARK 465 GLY A 159
REMARK 465 GLY A 160
REMARK 465 VAL A 161
REMARK 465 GLY A 162
REMARK 465 ALA A 163
REMARK 465 GLY A 164
REMARK 465 GLU A 394
REMARK 465 GLY A 395
REMARK 465 HIS A 396
REMARK 465 HIS A 397
REMARK 465 HIS A 398
REMARK 465 HIS A 399
REMARK 465 HIS A 400
REMARK 465 HIS A 401
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 176 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 186 CG CD CE NZ
REMARK 470 SER A 243 OG
REMARK 470 GLU A 245 CG CD OE1 OE2
REMARK 470 ARG A 265 CG CD NE CZ NH1 NH2
REMARK 470 THR A 388 OG1 CG2
REMARK 470 LEU A 391 CG CD1 CD2
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 ASN A 237 79.53 -118.74
REMARK 500 GLU A 245 39.44 -99.91
REMARK 500 PRO A 329 30.93 -91.01
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: NYSGXRC-13665A RELATED DB: TARGETDB
DBREF 3L60 A 154 393 UNP O06159 O06159_MYCTU 154 393
SEQADV 3L60 MET A 152 UNP O06159 EXPRESSION TAG
SEQADV 3L60 SER A 153 UNP O06159 EXPRESSION TAG
SEQADV 3L60 GLU A 394 UNP O06159 EXPRESSION TAG
SEQADV 3L60 GLY A 395 UNP O06159 EXPRESSION TAG
SEQADV 3L60 HIS A 396 UNP O06159 EXPRESSION TAG
SEQADV 3L60 HIS A 397 UNP O06159 EXPRESSION TAG
SEQADV 3L60 HIS A 398 UNP O06159 EXPRESSION TAG
SEQADV 3L60 HIS A 399 UNP O06159 EXPRESSION TAG
SEQADV 3L60 HIS A 400 UNP O06159 EXPRESSION TAG
SEQADV 3L60 HIS A 401 UNP O06159 EXPRESSION TAG
SEQRES 1 A 250 MET SER LEU ALA ALA ALA ARG GLY GLY VAL GLY ALA GLY
SEQRES 2 A 250 PRO ASP VAL ARG PRO VAL HIS GLY VAL HIS ALA ARG MET
SEQRES 3 A 250 ALA GLU LYS MET THR LEU SER HIS LYS GLU ILE PRO THR
SEQRES 4 A 250 ALA LYS ALA SER VAL GLU VAL ILE CYS ALA GLU LEU LEU
SEQRES 5 A 250 ARG LEU ARG ASP ARG PHE VAL SER ALA ALA PRO GLU ILE
SEQRES 6 A 250 THR PRO PHE ALA LEU THR LEU ARG LEU LEU VAL ILE ALA
SEQRES 7 A 250 LEU LYS HIS ASN VAL ILE LEU ASN SER THR TRP VAL ASP
SEQRES 8 A 250 SER GLY GLU GLY PRO GLN VAL HIS VAL HIS ARG GLY VAL
SEQRES 9 A 250 HIS LEU GLY PHE GLY ALA ALA THR GLU ARG GLY LEU LEU
SEQRES 10 A 250 VAL PRO VAL VAL THR ASP ALA GLN ASP LYS ASN THR ARG
SEQRES 11 A 250 GLU LEU ALA SER ARG VAL ALA GLU LEU ILE THR GLY ALA
SEQRES 12 A 250 ARG GLU GLY THR LEU THR PRO ALA GLU LEU ARG GLY SER
SEQRES 13 A 250 THR PHE THR VAL SER ASN PHE GLY ALA LEU GLY VAL ASP
SEQRES 14 A 250 ASP GLY VAL PRO VAL ILE ASN HIS PRO GLU ALA ALA ILE
SEQRES 15 A 250 LEU GLY LEU GLY ALA ILE LYS PRO ARG PRO VAL VAL VAL
SEQRES 16 A 250 GLY GLY GLU VAL VAL ALA ARG PRO THR MET THR LEU THR
SEQRES 17 A 250 CYS VAL PHE ASP HIS ARG VAL VAL ASP GLY ALA GLN VAL
SEQRES 18 A 250 ALA GLN PHE MET CYS GLU LEU ARG ASP LEU ILE GLU SER
SEQRES 19 A 250 PRO GLU THR ALA LEU LEU ASP LEU GLU GLY HIS HIS HIS
SEQRES 20 A 250 HIS HIS HIS
HET UNL A 1 9
HETNAM UNL UNKNOWN LIGAND
FORMUL 3 HOH *140(H2 O)
HELIX 1 1 HIS A 171 ILE A 188 1 18
HELIX 2 2 CYS A 199 VAL A 210 1 12
HELIX 3 3 THR A 217 ASN A 233 1 17
HELIX 4 4 VAL A 234 LEU A 236 5 3
HELIX 5 5 ASP A 274 LYS A 278 5 5
HELIX 6 6 ASN A 279 GLY A 297 1 19
HELIX 7 7 THR A 300 ARG A 305 5 6
HELIX 8 8 ASN A 313 GLY A 318 5 6
HELIX 9 9 ASP A 368 SER A 385 1 18
HELIX 10 10 SER A 385 LEU A 390 1 6
SHEET 1 A 6 THR A 190 ILE A 198 0
SHEET 2 A 6 GLU A 349 ASP A 363 -1 O CYS A 360 N ALA A 193
SHEET 3 A 6 ALA A 332 LEU A 336 -1 N GLY A 335 O THR A 359
SHEET 4 A 6 PHE A 309 SER A 312 1 N SER A 312 O LEU A 334
SHEET 5 A 6 LEU A 257 PHE A 259 1 N GLY A 258 O PHE A 309
SHEET 6 A 6 VAL A 271 VAL A 272 -1 O VAL A 272 N LEU A 257
SHEET 1 B 3 THR A 190 ILE A 198 0
SHEET 2 B 3 GLU A 349 ASP A 363 -1 O CYS A 360 N ALA A 193
SHEET 3 B 3 LYS A 340 VAL A 346 -1 N VAL A 344 O VAL A 351
SHEET 1 C 2 SER A 238 VAL A 241 0
SHEET 2 C 2 GLN A 248 VAL A 251 -1 O GLN A 248 N VAL A 241
SHEET 1 D 2 ALA A 261 THR A 263 0
SHEET 2 D 2 GLY A 266 LEU A 268 -1 O LEU A 268 N ALA A 261
CISPEP 1 HIS A 328 PRO A 329 0 -1.98
CRYST1 118.764 118.764 118.764 90.00 90.00 90.00 I 2 3 24
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 0.008420 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008420 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008420 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
