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HEADER TRANSFERASE 30-OCT-18 6IOI
TITLE CRYSTAL STRUCTURE OF HOMOSERINE O-ACETYLTRANSFERASE IN COMPLEX WITH
TITLE 2 COA FROM MYCOBACTERIUM SMEGMATIS ATCC 19420
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HOMOSERINE O-ACETYLTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: HAT,HOMOSERINE TRANSACETYLASE,HTA;
COMPND 5 EC: 2.3.1.31;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM SMEGMATIS;
SOURCE 3 ORGANISM_TAXID: 1772;
SOURCE 4 GENE: METX_1, METXA, ERS451418_01697;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21_T1R(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET30A
KEYWDS TRANSFERASE, BIOSYNTHETIC PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR H.-Y.SAGONG,K.-J.KIM
REVDAT 1 04-SEP-19 6IOI 0
JRNL AUTH H.Y.SAGONG,J.HONG,K.J.KIM
JRNL TITL CRYSTAL STRUCTURE AND BIOCHEMICAL CHARACTERIZATION OF
JRNL TITL 2 O-ACETYLHOMOSERINE ACETYLTRANSFERASE FROM MYCOBACTERIUM
JRNL TITL 3 SMEGMATIS ATCC 19420.
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 517 399 2019
JRNL REFN ESSN 1090-2104
JRNL PMID 31378370
JRNL DOI 10.1016/J.BBRC.2019.07.117
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0238
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.14
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 99881
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) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5222
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7258
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.53
REMARK 3 BIN R VALUE (WORKING SET) : 0.1970
REMARK 3 BIN FREE R VALUE SET COUNT : 394
REMARK 3 BIN FREE R VALUE : 0.2490
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5482
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 96
REMARK 3 SOLVENT ATOMS : 577
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.62
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.15000
REMARK 3 B22 (A**2) : 0.68000
REMARK 3 B33 (A**2) : -0.53000
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.084
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.084
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.050
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.390
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.948
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5715 ; 0.013 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 5207 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7817 ; 1.769 ; 1.644
REMARK 3 BOND ANGLES OTHERS (DEGREES): 12019 ; 1.564 ; 1.575
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 740 ; 6.225 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 300 ;28.265 ;20.900
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 815 ;12.280 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 50 ;16.933 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 733 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6598 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1202 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 6IOI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-NOV-18.
REMARK 100 THE DEPOSITION ID IS D_1300009630.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-OCT-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 7A (6B, 6C1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97934
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 105196
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 46.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 7.10
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 9.560
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: 6IOG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 34 % (V/V) POLYETHYLENE GLYCOL (PEG)
REMARK 280 400, 0.1 M SODIUM ACETATE/ACETIC ACID PH 5.5, 0.2 M CALCIUM
REMARK 280 ACETATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 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 29.19200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 70.33500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.18300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 70.33500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.19200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 48.18300
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6080 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 ARG A 368
REMARK 465 LEU A 369
REMARK 465 GLU A 370
REMARK 465 HIS A 371
REMARK 465 HIS A 372
REMARK 465 HIS A 373
REMARK 465 HIS A 374
REMARK 465 HIS A 375
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 A 144 CD GLU A 144 OE2 0.091
REMARK 500 SER A 286 CA SER A 286 CB 0.118
REMARK 500 GLU B 216 CD GLU B 216 OE1 0.079
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 PROTEIN: 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 170 NE - CZ - NH1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG B 301 NE - CZ - NH1 ANGL. DEV. = 3.1 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 SER A 152 -133.61 64.51
REMARK 500 ASP A 206 47.97 -106.54
REMARK 500 ALA A 240 -136.33 41.36
REMARK 500 ASP A 245 -119.53 39.87
REMARK 500 ASP A 288 98.51 -170.29
REMARK 500 SER B 152 -128.90 67.94
REMARK 500 ASP B 206 47.71 -107.38
REMARK 500 ALA B 240 -135.65 40.85
REMARK 500 ASP B 245 -122.66 45.82
REMARK 500 ASP B 288 97.58 -170.46
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 COA A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue COA B 401
DBREF1 6IOI A 2 368 UNP A0A0D6HE46_MYCSM
DBREF2 6IOI A A0A0D6HE46 2 368
DBREF1 6IOI B 2 368 UNP A0A0D6HE46_MYCSM
DBREF2 6IOI B A0A0D6HE46 2 368
SEQADV 6IOI LEU A 369 UNP A0A0D6HE4 EXPRESSION TAG
SEQADV 6IOI GLU A 370 UNP A0A0D6HE4 EXPRESSION TAG
SEQADV 6IOI HIS A 371 UNP A0A0D6HE4 EXPRESSION TAG
SEQADV 6IOI HIS A 372 UNP A0A0D6HE4 EXPRESSION TAG
SEQADV 6IOI HIS A 373 UNP A0A0D6HE4 EXPRESSION TAG
SEQADV 6IOI HIS A 374 UNP A0A0D6HE4 EXPRESSION TAG
SEQADV 6IOI HIS A 375 UNP A0A0D6HE4 EXPRESSION TAG
SEQADV 6IOI LEU B 369 UNP A0A0D6HE4 EXPRESSION TAG
SEQADV 6IOI GLU B 370 UNP A0A0D6HE4 EXPRESSION TAG
SEQADV 6IOI HIS B 371 UNP A0A0D6HE4 EXPRESSION TAG
SEQADV 6IOI HIS B 372 UNP A0A0D6HE4 EXPRESSION TAG
SEQADV 6IOI HIS B 373 UNP A0A0D6HE4 EXPRESSION TAG
SEQADV 6IOI HIS B 374 UNP A0A0D6HE4 EXPRESSION TAG
SEQADV 6IOI HIS B 375 UNP A0A0D6HE4 EXPRESSION TAG
SEQRES 1 A 374 ALA THR VAL PRO LEU PRO ALA GLU GLY GLU ILE GLY LEU
SEQRES 2 A 374 VAL HIS ILE GLY ALA LEU THR LEU GLU ASN GLY THR VAL
SEQRES 3 A 374 LEU PRO ASP VAL THR ILE ALA VAL GLN ARG TRP GLY GLU
SEQRES 4 A 374 LEU ALA PRO ASP ARG GLY ASN VAL VAL MET VAL LEU HIS
SEQRES 5 A 374 ALA LEU THR GLY ASP SER HIS VAL THR GLY PRO ALA GLY
SEQRES 6 A 374 ASP GLY HIS PRO THR ALA GLY TRP TRP ASP GLY VAL ALA
SEQRES 7 A 374 GLY PRO GLY ALA PRO ILE ASP THR ASP HIS TRP CYS ALA
SEQRES 8 A 374 ILE ALA THR ASN VAL LEU GLY GLY CYS ARG GLY SER THR
SEQRES 9 A 374 GLY PRO GLY SER LEU ALA PRO ASP GLY LYS PRO TRP GLY
SEQRES 10 A 374 SER ARG PHE PRO GLN ILE THR ILE ARG ASP GLN VAL ALA
SEQRES 11 A 374 ALA ASP ARG ALA ALA LEU ALA ALA LEU GLY ILE THR GLU
SEQRES 12 A 374 VAL ALA ALA VAL VAL GLY GLY SER MET GLY GLY ALA ARG
SEQRES 13 A 374 ALA LEU GLU TRP LEU VAL THR HIS PRO ASP ASP VAL ARG
SEQRES 14 A 374 ALA GLY LEU VAL LEU ALA VAL GLY ALA ARG ALA THR ALA
SEQRES 15 A 374 ASP GLN ILE GLY THR GLN SER THR GLN VAL ALA ALA ILE
SEQRES 16 A 374 LYS ALA ASP PRO ASP TRP GLN GLY GLY ASP TYR HIS GLY
SEQRES 17 A 374 THR GLY ARG ALA PRO THR GLU GLY MET GLU ILE ALA ARG
SEQRES 18 A 374 ARG PHE ALA HIS LEU THR TYR ARG GLY GLU GLU GLU LEU
SEQRES 19 A 374 ASP ASP ARG PHE ALA ASN THR PRO GLN ASP ASP GLU ASP
SEQRES 20 A 374 PRO LEU THR GLY GLY ARG TYR ALA VAL GLN SER TYR LEU
SEQRES 21 A 374 GLU TYR GLN GLY GLY LYS LEU ALA ARG ARG PHE ASP PRO
SEQRES 22 A 374 GLY THR TYR VAL VAL LEU SER ASP ALA LEU SER SER HIS
SEQRES 23 A 374 ASP VAL GLY ARG GLY ARG GLY GLY VAL GLU ALA ALA LEU
SEQRES 24 A 374 ARG SER CYS PRO VAL PRO VAL VAL VAL GLY GLY ILE THR
SEQRES 25 A 374 SER ASP ARG LEU TYR PRO ILE ARG LEU GLN GLN GLU LEU
SEQRES 26 A 374 ALA GLU LEU LEU PRO GLY CYS GLN GLY LEU ASP VAL VAL
SEQRES 27 A 374 ASP SER ILE TYR GLY HIS ASP GLY PHE LEU VAL GLU THR
SEQRES 28 A 374 GLU LEU VAL GLY LYS LEU ILE ARG ARG THR LEU GLU LEU
SEQRES 29 A 374 ALA GLN ARG LEU GLU HIS HIS HIS HIS HIS
SEQRES 1 B 374 ALA THR VAL PRO LEU PRO ALA GLU GLY GLU ILE GLY LEU
SEQRES 2 B 374 VAL HIS ILE GLY ALA LEU THR LEU GLU ASN GLY THR VAL
SEQRES 3 B 374 LEU PRO ASP VAL THR ILE ALA VAL GLN ARG TRP GLY GLU
SEQRES 4 B 374 LEU ALA PRO ASP ARG GLY ASN VAL VAL MET VAL LEU HIS
SEQRES 5 B 374 ALA LEU THR GLY ASP SER HIS VAL THR GLY PRO ALA GLY
SEQRES 6 B 374 ASP GLY HIS PRO THR ALA GLY TRP TRP ASP GLY VAL ALA
SEQRES 7 B 374 GLY PRO GLY ALA PRO ILE ASP THR ASP HIS TRP CYS ALA
SEQRES 8 B 374 ILE ALA THR ASN VAL LEU GLY GLY CYS ARG GLY SER THR
SEQRES 9 B 374 GLY PRO GLY SER LEU ALA PRO ASP GLY LYS PRO TRP GLY
SEQRES 10 B 374 SER ARG PHE PRO GLN ILE THR ILE ARG ASP GLN VAL ALA
SEQRES 11 B 374 ALA ASP ARG ALA ALA LEU ALA ALA LEU GLY ILE THR GLU
SEQRES 12 B 374 VAL ALA ALA VAL VAL GLY GLY SER MET GLY GLY ALA ARG
SEQRES 13 B 374 ALA LEU GLU TRP LEU VAL THR HIS PRO ASP ASP VAL ARG
SEQRES 14 B 374 ALA GLY LEU VAL LEU ALA VAL GLY ALA ARG ALA THR ALA
SEQRES 15 B 374 ASP GLN ILE GLY THR GLN SER THR GLN VAL ALA ALA ILE
SEQRES 16 B 374 LYS ALA ASP PRO ASP TRP GLN GLY GLY ASP TYR HIS GLY
SEQRES 17 B 374 THR GLY ARG ALA PRO THR GLU GLY MET GLU ILE ALA ARG
SEQRES 18 B 374 ARG PHE ALA HIS LEU THR TYR ARG GLY GLU GLU GLU LEU
SEQRES 19 B 374 ASP ASP ARG PHE ALA ASN THR PRO GLN ASP ASP GLU ASP
SEQRES 20 B 374 PRO LEU THR GLY GLY ARG TYR ALA VAL GLN SER TYR LEU
SEQRES 21 B 374 GLU TYR GLN GLY GLY LYS LEU ALA ARG ARG PHE ASP PRO
SEQRES 22 B 374 GLY THR TYR VAL VAL LEU SER ASP ALA LEU SER SER HIS
SEQRES 23 B 374 ASP VAL GLY ARG GLY ARG GLY GLY VAL GLU ALA ALA LEU
SEQRES 24 B 374 ARG SER CYS PRO VAL PRO VAL VAL VAL GLY GLY ILE THR
SEQRES 25 B 374 SER ASP ARG LEU TYR PRO ILE ARG LEU GLN GLN GLU LEU
SEQRES 26 B 374 ALA GLU LEU LEU PRO GLY CYS GLN GLY LEU ASP VAL VAL
SEQRES 27 B 374 ASP SER ILE TYR GLY HIS ASP GLY PHE LEU VAL GLU THR
SEQRES 28 B 374 GLU LEU VAL GLY LYS LEU ILE ARG ARG THR LEU GLU LEU
SEQRES 29 B 374 ALA GLN ARG LEU GLU HIS HIS HIS HIS HIS
HET COA A 401 48
HET COA B 401 48
HETNAM COA COENZYME A
FORMUL 3 COA 2(C21 H36 N7 O16 P3 S)
FORMUL 5 HOH *577(H2 O)
HELIX 1 AA1 TRP A 117 PHE A 121 5 5
HELIX 2 AA2 THR A 125 LEU A 140 1 16
HELIX 3 AA3 SER A 152 HIS A 165 1 14
HELIX 4 AA4 THR A 182 ASP A 199 1 18
HELIX 5 AA5 PRO A 200 ASP A 206 5 7
HELIX 6 AA6 PRO A 214 ARG A 230 1 17
HELIX 7 AA7 GLY A 231 ALA A 240 1 10
HELIX 8 AA8 ASP A 248 GLY A 252 5 5
HELIX 9 AA9 TYR A 255 PHE A 272 1 18
HELIX 10 AB1 ASP A 273 SER A 286 1 14
HELIX 11 AB2 GLY A 295 SER A 302 1 8
HELIX 12 AB3 PRO A 319 LEU A 330 1 12
HELIX 13 AB4 TYR A 343 HIS A 345 5 3
HELIX 14 AB5 ASP A 346 GLU A 351 1 6
HELIX 15 AB6 GLU A 351 GLN A 367 1 17
HELIX 16 AB7 TRP B 117 PHE B 121 5 5
HELIX 17 AB8 THR B 125 LEU B 140 1 16
HELIX 18 AB9 SER B 152 HIS B 165 1 14
HELIX 19 AC1 THR B 182 ALA B 198 1 17
HELIX 20 AC2 ASP B 199 ASP B 206 5 8
HELIX 21 AC3 PRO B 214 ARG B 230 1 17
HELIX 22 AC4 GLY B 231 ALA B 240 1 10
HELIX 23 AC5 ASP B 248 GLY B 252 5 5
HELIX 24 AC6 TYR B 255 ARG B 270 1 16
HELIX 25 AC7 ASP B 273 SER B 286 1 14
HELIX 26 AC8 GLY B 295 SER B 302 1 8
HELIX 27 AC9 ILE B 320 LEU B 330 1 11
HELIX 28 AD1 TYR B 343 HIS B 345 5 3
HELIX 29 AD2 ASP B 346 GLU B 351 1 6
HELIX 30 AD3 GLU B 351 HIS B 372 1 22
SHEET 1 AA1 8 GLY A 13 THR A 21 0
SHEET 2 AA1 8 VAL A 27 TRP A 38 -1 O LEU A 28 N LEU A 20
SHEET 3 AA1 8 CYS A 91 THR A 95 -1 O ALA A 94 N GLN A 36
SHEET 4 AA1 8 VAL A 48 VAL A 51 1 N VAL A 51 O ILE A 93
SHEET 5 AA1 8 VAL A 145 GLY A 151 1 O ALA A 147 N MET A 50
SHEET 6 AA1 8 VAL A 169 LEU A 175 1 O LEU A 173 N VAL A 148
SHEET 7 AA1 8 VAL A 307 ILE A 312 1 O VAL A 308 N GLY A 172
SHEET 8 AA1 8 ASP A 337 VAL A 339 1 O VAL A 339 N GLY A 311
SHEET 1 AA2 2 ALA A 79 GLY A 80 0
SHEET 2 AA2 2 ILE A 85 ASP A 86 1 O ILE A 85 N GLY A 80
SHEET 1 AA3 8 GLY B 13 THR B 21 0
SHEET 2 AA3 8 VAL B 27 TRP B 38 -1 O ILE B 33 N VAL B 15
SHEET 3 AA3 8 CYS B 91 THR B 95 -1 O ALA B 92 N TRP B 38
SHEET 4 AA3 8 VAL B 48 LEU B 52 1 N VAL B 51 O ILE B 93
SHEET 5 AA3 8 VAL B 145 GLY B 151 1 O ALA B 147 N MET B 50
SHEET 6 AA3 8 VAL B 169 LEU B 175 1 O LEU B 173 N VAL B 148
SHEET 7 AA3 8 VAL B 307 ILE B 312 1 O VAL B 308 N GLY B 172
SHEET 8 AA3 8 ASP B 337 VAL B 339 1 O VAL B 339 N GLY B 311
SHEET 1 AA4 2 ALA B 79 GLY B 80 0
SHEET 2 AA4 2 ILE B 85 ASP B 86 1 O ILE B 85 N GLY B 80
SITE 1 AC1 17 LEU A 55 THR A 56 ARG A 222 ARG A 230
SITE 2 AC1 17 GLN A 244 ALA A 256 SER A 259 TYR A 260
SITE 3 AC1 17 TYR A 263 GLN A 264 LYS A 267 ASP A 346
SITE 4 AC1 17 LEU A 349 VAL A 350 HOH A 600 HOH A 663
SITE 5 AC1 17 HOH A 748
SITE 1 AC2 18 LEU B 55 THR B 56 ARG B 222 TYR B 229
SITE 2 AC2 18 ARG B 230 GLN B 244 ALA B 256 SER B 259
SITE 3 AC2 18 TYR B 260 TYR B 263 GLN B 264 LYS B 267
SITE 4 AC2 18 ASP B 346 LEU B 349 VAL B 350 HOH B 524
SITE 5 AC2 18 HOH B 525 HOH B 573
CRYST1 58.384 96.366 140.670 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.017128 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010377 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007109 0.00000
TER 2703 GLN A 367
TER 5495 HIS B 375
MASTER 332 0 2 30 20 0 10 6 6155 2 96 58
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