HEADER TRANSFERASE 13-JAN-15 4XL4
TITLE CRYSTAL STRUCTURE OF THIOLASE FROM CLOSTRIDIUM ACETOBUTYLICUM IN
TITLE 2 COMPLEX WITH COA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYL-COA ACETYLTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.3.1.9;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM ACETOBUTYLICUM (STRAIN EA 2018);
SOURCE 3 ORGANISM_TAXID: 863638;
SOURCE 4 STRAIN: EA 2018;
SOURCE 5 GENE: CEA_G2880;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: B834;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET30A
KEYWDS TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.KIM,S.C.HA,J.W.AHN,E.J.KIM,J.H.LIM,K.J.KIM
REVDAT 3 08-NOV-23 4XL4 1 REMARK
REVDAT 2 14-OCT-15 4XL4 1 SHEET
REVDAT 1 07-OCT-15 4XL4 0
SPRSDE 07-OCT-15 4XL4 4N46
JRNL AUTH S.KIM,Y.S.JANG,S.C.HA,J.W.AHN,E.J.KIM,J.HONG LIM,C.CHO,
JRNL AUTH 2 Y.SHIN RYU,S.KUK LEE,S.Y.LEE,K.J.KIM
JRNL TITL REDOX-SWITCH REGULATORY MECHANISM OF THIOLASE FROM
JRNL TITL 2 CLOSTRIDIUM ACETOBUTYLICUM
JRNL REF NAT COMMUN V. 6 8410 2015
JRNL REFN ESSN 2041-1723
JRNL PMID 26391388
JRNL DOI 10.1038/NCOMMS9410
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 61614
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) : 0.144
REMARK 3 R VALUE (WORKING SET) : 0.142
REMARK 3 FREE R VALUE : 0.183
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3291
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4384
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.47
REMARK 3 BIN R VALUE (WORKING SET) : 0.1720
REMARK 3 BIN FREE R VALUE SET COUNT : 230
REMARK 3 BIN FREE R VALUE : 0.2300
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5784
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 138
REMARK 3 SOLVENT ATOMS : 636
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.17
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.73000
REMARK 3 B22 (A**2) : 0.50000
REMARK 3 B33 (A**2) : 0.23000
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): 0.119
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.115
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.075
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.525
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.952
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6040 ; 0.018 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5970 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8160 ; 1.886 ; 1.992
REMARK 3 BOND ANGLES OTHERS (DEGREES): 13767 ; 0.899 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 790 ; 6.303 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 224 ;37.482 ;25.625
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1049 ;15.872 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ; 9.332 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 933 ; 0.121 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6822 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1228 ; 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): 3154 ; 1.940 ; 2.043
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3153 ; 1.940 ; 2.042
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3946 ; 2.697 ; 3.053
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 4XL4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-JAN-15.
REMARK 100 THE DEPOSITION ID IS D_1000205878.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-DEC-14
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 4.2
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
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 : 65291
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
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 : 7.000
REMARK 200 R MERGE (I) : 0.09100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 33.1000
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) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.00
REMARK 200 R MERGE FOR SHELL (I) : 0.28200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.600
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: 4N45
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, K-CITRATE, NACL, PH 4.2,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 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+1/2,Y+1/2,-Z
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 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 102.15350
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.08550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 102.15350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 27.08550
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 300 REMARK: BIOLOGICAL UNIT IS THE SAME AS ASYM.
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: 7230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 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 LEU A 393
REMARK 465 GLU A 394
REMARK 465 HIS 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 LEU B 393
REMARK 465 GLU B 394
REMARK 465 HIS B 395
REMARK 465 HIS B 396
REMARK 465 HIS B 397
REMARK 465 HIS B 398
REMARK 465 HIS B 399
REMARK 465 HIS B 400
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 LYS A 19 -116.16 -116.26
REMARK 500 ASN A 64 74.86 51.09
REMARK 500 VAL A 87 -131.84 51.85
REMARK 500 ARG A 133 -61.80 70.73
REMARK 500 ASP A 214 16.56 -144.58
REMARK 500 LYS B 19 -116.90 -116.58
REMARK 500 ASN B 64 75.93 49.64
REMARK 500 VAL B 87 -128.84 51.33
REMARK 500 ARG B 133 -60.76 70.53
REMARK 500 ASP B 214 11.67 -141.42
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PRO A 349 ILE A 350 -145.06
REMARK 500 PRO B 349 ILE B 350 -148.55
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 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 950 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH A 951 DISTANCE = 5.92 ANGSTROMS
REMARK 525 HOH B 884 DISTANCE = 6.05 ANGSTROMS
REMARK 525 HOH B 885 DISTANCE = 7.19 ANGSTROMS
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 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue COA B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 503
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4XL2 RELATED DB: PDB
REMARK 900 RELATED ID: 4XL3 RELATED DB: PDB
DBREF 4XL4 A 1 392 UNP F0K5D8 F0K5D8_CLOAE 1 392
DBREF 4XL4 B 1 392 UNP F0K5D8 F0K5D8_CLOAE 1 392
SEQADV 4XL4 SER A 378 UNP F0K5D8 CYS 378 ENGINEERED MUTATION
SEQADV 4XL4 LEU A 393 UNP F0K5D8 EXPRESSION TAG
SEQADV 4XL4 GLU A 394 UNP F0K5D8 EXPRESSION TAG
SEQADV 4XL4 HIS A 395 UNP F0K5D8 EXPRESSION TAG
SEQADV 4XL4 HIS A 396 UNP F0K5D8 EXPRESSION TAG
SEQADV 4XL4 HIS A 397 UNP F0K5D8 EXPRESSION TAG
SEQADV 4XL4 HIS A 398 UNP F0K5D8 EXPRESSION TAG
SEQADV 4XL4 HIS A 399 UNP F0K5D8 EXPRESSION TAG
SEQADV 4XL4 HIS A 400 UNP F0K5D8 EXPRESSION TAG
SEQADV 4XL4 SER B 378 UNP F0K5D8 CYS 378 ENGINEERED MUTATION
SEQADV 4XL4 LEU B 393 UNP F0K5D8 EXPRESSION TAG
SEQADV 4XL4 GLU B 394 UNP F0K5D8 EXPRESSION TAG
SEQADV 4XL4 HIS B 395 UNP F0K5D8 EXPRESSION TAG
SEQADV 4XL4 HIS B 396 UNP F0K5D8 EXPRESSION TAG
SEQADV 4XL4 HIS B 397 UNP F0K5D8 EXPRESSION TAG
SEQADV 4XL4 HIS B 398 UNP F0K5D8 EXPRESSION TAG
SEQADV 4XL4 HIS B 399 UNP F0K5D8 EXPRESSION TAG
SEQADV 4XL4 HIS B 400 UNP F0K5D8 EXPRESSION TAG
SEQRES 1 A 400 MET LYS GLU VAL VAL ILE ALA SER ALA VAL ARG THR ALA
SEQRES 2 A 400 ILE GLY SER TYR GLY LYS SER LEU LYS ASP VAL PRO ALA
SEQRES 3 A 400 VAL ASP LEU GLY ALA THR ALA ILE LYS GLU ALA VAL LYS
SEQRES 4 A 400 LYS ALA GLY ILE LYS PRO GLU ASP VAL ASN GLU VAL ILE
SEQRES 5 A 400 LEU GLY ASN VAL LEU GLN ALA GLY LEU GLY GLN ASN PRO
SEQRES 6 A 400 ALA ARG GLN ALA SER PHE LYS ALA GLY LEU PRO VAL GLU
SEQRES 7 A 400 ILE PRO ALA MET THR ILE ASN LYS VAL CYS GLY SER GLY
SEQRES 8 A 400 LEU ARG THR VAL SER LEU ALA ALA GLN ILE ILE LYS ALA
SEQRES 9 A 400 GLY ASP ALA ASP VAL ILE ILE ALA GLY GLY MET GLU ASN
SEQRES 10 A 400 MET SER ARG ALA PRO TYR LEU ALA ASN ASN ALA ARG TRP
SEQRES 11 A 400 GLY TYR ARG MET GLY ASN ALA LYS PHE VAL ASP GLU MET
SEQRES 12 A 400 ILE THR ASP GLY LEU TRP ASP ALA PHE ASN ASP TYR HIS
SEQRES 13 A 400 MET GLY ILE THR ALA GLU ASN ILE ALA GLU ARG TRP ASN
SEQRES 14 A 400 ILE SER ARG GLU GLU GLN ASP GLU PHE ALA LEU ALA SER
SEQRES 15 A 400 GLN LYS LYS ALA GLU GLU ALA ILE LYS SER GLY GLN PHE
SEQRES 16 A 400 LYS ASP GLU ILE VAL PRO VAL VAL ILE LYS GLY ARG LYS
SEQRES 17 A 400 GLY GLU THR VAL VAL ASP THR ASP GLU HIS PRO ARG PHE
SEQRES 18 A 400 GLY SER THR ILE GLU GLY LEU ALA LYS LEU LYS PRO ALA
SEQRES 19 A 400 PHE LYS LYS ASP GLY THR VAL THR ALA GLY ASN ALA SER
SEQRES 20 A 400 GLY LEU ASN ASP CYS ALA ALA VAL LEU VAL ILE MET SER
SEQRES 21 A 400 ALA GLU LYS ALA LYS GLU LEU GLY VAL LYS PRO LEU ALA
SEQRES 22 A 400 LYS ILE VAL SER TYR GLY SER ALA GLY VAL ASP PRO ALA
SEQRES 23 A 400 ILE MET GLY TYR GLY PRO PHE TYR ALA THR LYS ALA ALA
SEQRES 24 A 400 ILE GLU LYS ALA GLY TRP THR VAL ASP GLU LEU ASP LEU
SEQRES 25 A 400 ILE GLU SER ASN GLU ALA PHE ALA ALA GLN SER LEU ALA
SEQRES 26 A 400 VAL ALA LYS ASP LEU LYS PHE ASP MET ASN LYS VAL ASN
SEQRES 27 A 400 VAL ASN GLY GLY ALA ILE ALA LEU GLY HIS PRO ILE GLY
SEQRES 28 A 400 ALA SER GLY ALA ARG ILE LEU VAL THR LEU VAL HIS ALA
SEQRES 29 A 400 MET GLN LYS ARG ASP ALA LYS LYS GLY LEU ALA THR LEU
SEQRES 30 A 400 SER ILE GLY GLY GLY GLN GLY THR ALA ILE LEU LEU GLU
SEQRES 31 A 400 LYS CYS LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 400 MET LYS GLU VAL VAL ILE ALA SER ALA VAL ARG THR ALA
SEQRES 2 B 400 ILE GLY SER TYR GLY LYS SER LEU LYS ASP VAL PRO ALA
SEQRES 3 B 400 VAL ASP LEU GLY ALA THR ALA ILE LYS GLU ALA VAL LYS
SEQRES 4 B 400 LYS ALA GLY ILE LYS PRO GLU ASP VAL ASN GLU VAL ILE
SEQRES 5 B 400 LEU GLY ASN VAL LEU GLN ALA GLY LEU GLY GLN ASN PRO
SEQRES 6 B 400 ALA ARG GLN ALA SER PHE LYS ALA GLY LEU PRO VAL GLU
SEQRES 7 B 400 ILE PRO ALA MET THR ILE ASN LYS VAL CYS GLY SER GLY
SEQRES 8 B 400 LEU ARG THR VAL SER LEU ALA ALA GLN ILE ILE LYS ALA
SEQRES 9 B 400 GLY ASP ALA ASP VAL ILE ILE ALA GLY GLY MET GLU ASN
SEQRES 10 B 400 MET SER ARG ALA PRO TYR LEU ALA ASN ASN ALA ARG TRP
SEQRES 11 B 400 GLY TYR ARG MET GLY ASN ALA LYS PHE VAL ASP GLU MET
SEQRES 12 B 400 ILE THR ASP GLY LEU TRP ASP ALA PHE ASN ASP TYR HIS
SEQRES 13 B 400 MET GLY ILE THR ALA GLU ASN ILE ALA GLU ARG TRP ASN
SEQRES 14 B 400 ILE SER ARG GLU GLU GLN ASP GLU PHE ALA LEU ALA SER
SEQRES 15 B 400 GLN LYS LYS ALA GLU GLU ALA ILE LYS SER GLY GLN PHE
SEQRES 16 B 400 LYS ASP GLU ILE VAL PRO VAL VAL ILE LYS GLY ARG LYS
SEQRES 17 B 400 GLY GLU THR VAL VAL ASP THR ASP GLU HIS PRO ARG PHE
SEQRES 18 B 400 GLY SER THR ILE GLU GLY LEU ALA LYS LEU LYS PRO ALA
SEQRES 19 B 400 PHE LYS LYS ASP GLY THR VAL THR ALA GLY ASN ALA SER
SEQRES 20 B 400 GLY LEU ASN ASP CYS ALA ALA VAL LEU VAL ILE MET SER
SEQRES 21 B 400 ALA GLU LYS ALA LYS GLU LEU GLY VAL LYS PRO LEU ALA
SEQRES 22 B 400 LYS ILE VAL SER TYR GLY SER ALA GLY VAL ASP PRO ALA
SEQRES 23 B 400 ILE MET GLY TYR GLY PRO PHE TYR ALA THR LYS ALA ALA
SEQRES 24 B 400 ILE GLU LYS ALA GLY TRP THR VAL ASP GLU LEU ASP LEU
SEQRES 25 B 400 ILE GLU SER ASN GLU ALA PHE ALA ALA GLN SER LEU ALA
SEQRES 26 B 400 VAL ALA LYS ASP LEU LYS PHE ASP MET ASN LYS VAL ASN
SEQRES 27 B 400 VAL ASN GLY GLY ALA ILE ALA LEU GLY HIS PRO ILE GLY
SEQRES 28 B 400 ALA SER GLY ALA ARG ILE LEU VAL THR LEU VAL HIS ALA
SEQRES 29 B 400 MET GLN LYS ARG ASP ALA LYS LYS GLY LEU ALA THR LEU
SEQRES 30 B 400 SER ILE GLY GLY GLY GLN GLY THR ALA ILE LEU LEU GLU
SEQRES 31 B 400 LYS CYS LEU GLU HIS HIS HIS HIS HIS HIS
HET COA A 501 48
HET GOL A 502 6
HET GOL A 503 6
HET GOL A 504 6
HET GOL A 505 6
HET GOL A 506 6
HET COA B 501 48
HET GOL B 502 6
HET GOL B 503 6
HETNAM COA COENZYME A
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 COA 2(C21 H36 N7 O16 P3 S)
FORMUL 4 GOL 7(C3 H8 O3)
FORMUL 12 HOH *636(H2 O)
HELIX 1 AA1 PRO A 25 GLY A 42 1 18
HELIX 2 AA2 LYS A 44 VAL A 48 5 5
HELIX 3 AA3 ASN A 64 ALA A 73 1 10
HELIX 4 AA4 LYS A 86 CYS A 88 5 3
HELIX 5 AA5 GLY A 89 ALA A 104 1 16
HELIX 6 AA6 GLU A 142 LEU A 148 1 7
HELIX 7 AA7 HIS A 156 TRP A 168 1 13
HELIX 8 AA8 SER A 171 SER A 192 1 22
HELIX 9 AA9 THR A 224 LYS A 230 1 7
HELIX 10 AB1 ALA A 261 LEU A 267 1 7
HELIX 11 AB2 ASP A 284 GLY A 289 5 6
HELIX 12 AB3 TYR A 290 GLY A 304 1 15
HELIX 13 AB4 THR A 306 LEU A 310 5 5
HELIX 14 AB5 PHE A 319 LYS A 331 1 13
HELIX 15 AB6 ASP A 333 VAL A 337 5 5
HELIX 16 AB7 GLY A 342 GLY A 347 1 6
HELIX 17 AB8 PRO A 349 ASP A 369 1 21
HELIX 18 AB9 PRO B 25 GLY B 42 1 18
HELIX 19 AC1 LYS B 44 VAL B 48 5 5
HELIX 20 AC2 ASN B 64 ALA B 73 1 10
HELIX 21 AC3 LYS B 86 CYS B 88 5 3
HELIX 22 AC4 GLY B 89 ALA B 104 1 16
HELIX 23 AC5 GLU B 142 LEU B 148 1 7
HELIX 24 AC6 HIS B 156 ASN B 169 1 14
HELIX 25 AC7 SER B 171 SER B 192 1 22
HELIX 26 AC8 THR B 224 LEU B 231 1 8
HELIX 27 AC9 ALA B 261 LEU B 267 1 7
HELIX 28 AD1 ASP B 284 GLY B 289 5 6
HELIX 29 AD2 TYR B 290 GLY B 304 1 15
HELIX 30 AD3 THR B 306 LEU B 310 5 5
HELIX 31 AD4 PHE B 319 LYS B 331 1 13
HELIX 32 AD5 ASP B 333 VAL B 337 5 5
HELIX 33 AD6 GLY B 342 GLY B 347 1 6
HELIX 34 AD7 PRO B 349 ASP B 369 1 21
SHEET 1 AA1 7 LEU A 312 SER A 315 0
SHEET 2 AA1 7 LYS A 372 ILE A 379 1 O LEU A 374 N GLU A 314
SHEET 3 AA1 7 GLN A 383 LYS A 391 -1 O ILE A 387 N ALA A 375
SHEET 4 AA1 7 ALA A 273 GLY A 282 -1 N SER A 277 O LEU A 388
SHEET 5 AA1 7 VAL A 4 ARG A 11 -1 N ILE A 6 O ALA A 273
SHEET 6 AA1 7 ASN A 250 SER A 260 -1 O MET A 259 N VAL A 5
SHEET 7 AA1 7 GLY A 15 SER A 16 -1 N GLY A 15 O ASP A 251
SHEET 1 AA210 GLY A 15 SER A 16 0
SHEET 2 AA210 ASN A 250 SER A 260 -1 O ASP A 251 N GLY A 15
SHEET 3 AA210 VAL A 109 ASN A 117 -1 N ILE A 110 O ILE A 258
SHEET 4 AA210 GLU A 50 GLY A 54 1 N ILE A 52 O ILE A 111
SHEET 5 AA210 ALA A 81 ASN A 85 1 O MET A 82 N VAL A 51
SHEET 6 AA210 ALA B 81 ASN B 85 -1 O ASN B 85 N THR A 83
SHEET 7 AA210 GLU B 50 GLY B 54 1 N LEU B 53 O ILE B 84
SHEET 8 AA210 VAL B 109 ASN B 117 1 O GLY B 113 N GLY B 54
SHEET 9 AA210 ASN B 250 SER B 260 -1 O ILE B 258 N ILE B 110
SHEET 10 AA210 GLY B 15 SER B 16 -1 N GLY B 15 O ASP B 251
SHEET 1 AA315 LEU A 312 SER A 315 0
SHEET 2 AA315 LYS A 372 ILE A 379 1 O LEU A 374 N GLU A 314
SHEET 3 AA315 GLN A 383 LYS A 391 -1 O ILE A 387 N ALA A 375
SHEET 4 AA315 ALA A 273 GLY A 282 -1 N SER A 277 O LEU A 388
SHEET 5 AA315 VAL A 4 ARG A 11 -1 N ILE A 6 O ALA A 273
SHEET 6 AA315 ASN A 250 SER A 260 -1 O MET A 259 N VAL A 5
SHEET 7 AA315 VAL A 109 ASN A 117 -1 N ILE A 110 O ILE A 258
SHEET 8 AA315 GLU A 50 GLY A 54 1 N ILE A 52 O ILE A 111
SHEET 9 AA315 ALA A 81 ASN A 85 1 O MET A 82 N VAL A 51
SHEET 10 AA315 ALA B 81 ASN B 85 -1 O ASN B 85 N THR A 83
SHEET 11 AA315 GLU B 50 GLY B 54 1 N LEU B 53 O ILE B 84
SHEET 12 AA315 VAL B 109 ASN B 117 1 O GLY B 113 N GLY B 54
SHEET 13 AA315 ASN B 250 SER B 260 -1 O ILE B 258 N ILE B 110
SHEET 14 AA315 VAL B 4 THR B 12 -1 N VAL B 10 O VAL B 255
SHEET 15 AA315 ILE B 199 VAL B 200 1 O VAL B 200 N ARG B 11
SHEET 1 AA4 5 VAL B 4 THR B 12 0
SHEET 2 AA4 5 ALA B 273 GLY B 282 -1 O ILE B 275 N VAL B 4
SHEET 3 AA4 5 GLN B 383 GLU B 390 -1 O GLU B 390 N LYS B 274
SHEET 4 AA4 5 LYS B 372 ILE B 379 -1 N GLY B 373 O LEU B 389
SHEET 5 AA4 5 LEU B 312 SER B 315 1 N GLU B 314 O LEU B 374
SHEET 1 AA5 4 VAL A 140 ASP A 141 0
SHEET 2 AA5 4 TYR A 123 ALA A 125 -1 N LEU A 124 O VAL A 140
SHEET 3 AA5 4 TYR B 123 ALA B 125 -1 O ALA B 125 N TYR A 123
SHEET 4 AA5 4 VAL B 140 ASP B 141 -1 O VAL B 140 N LEU B 124
SHEET 1 AA6 2 VAL A 202 LYS A 205 0
SHEET 2 AA6 2 GLU A 210 VAL A 213 -1 O VAL A 213 N VAL A 202
SHEET 1 AA7 2 VAL B 202 LYS B 205 0
SHEET 2 AA7 2 GLU B 210 VAL B 213 -1 O THR B 211 N ILE B 204
SITE 1 AC1 21 CYS A 88 LEU A 148 HIS A 156 ARG A 220
SITE 2 AC1 21 LEU A 231 SER A 247 PHE A 319 HIS A 348
SITE 3 AC1 21 HOH A 658 HOH A 663 HOH A 676 HOH A 697
SITE 4 AC1 21 HOH A 747 HOH A 753 HOH A 758 HOH A 763
SITE 5 AC1 21 HOH A 770 HOH A 797 HOH A 830 HOH A 844
SITE 6 AC1 21 ARG B 133
SITE 1 AC2 9 ARG A 93 SER A 96 GLN A 100 TYR A 278
SITE 2 AC2 9 GLY A 279 SER A 280 GLU B 50 ILE B 101
SITE 3 AC2 9 HOH B 839
SITE 1 AC3 9 VAL A 10 GLU A 36 LYS A 40 ASP A 197
SITE 2 AC3 9 GLU A 198 ILE A 199 VAL A 200 HOH A 614
SITE 3 AC3 9 HOH A 694
SITE 1 AC4 7 LYS A 35 VAL A 38 LYS A 39 PRO A 45
SITE 2 AC4 7 ALA A 73 LEU A 75 HOH A 776
SITE 1 AC5 4 ASN A 136 ALA A 137 LYS A 138 LYS B 138
SITE 1 AC6 4 LYS A 297 ASP A 329 HOH A 604 HOH A 843
SITE 1 AC7 23 ARG A 133 CYS B 88 LEU B 148 HIS B 156
SITE 2 AC7 23 ARG B 220 SER B 223 LEU B 231 SER B 247
SITE 3 AC7 23 MET B 288 PHE B 319 HIS B 348 HOH B 630
SITE 4 AC7 23 HOH B 650 HOH B 663 HOH B 684 HOH B 695
SITE 5 AC7 23 HOH B 702 HOH B 718 HOH B 756 HOH B 760
SITE 6 AC7 23 HOH B 761 HOH B 793 HOH B 797
SITE 1 AC8 7 VAL B 10 LYS B 40 LYS B 196 ASP B 197
SITE 2 AC8 7 GLU B 198 ILE B 199 VAL B 200
SITE 1 AC9 5 GLU A 78 GLY B 282 TYR B 294 HOH B 607
SITE 2 AC9 5 HOH B 639
CRYST1 204.307 54.171 73.112 90.00 90.00 90.00 P 21 21 2 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 0.004895 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018460 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013678 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
