HEADER TRANSFERASE 30-SEP-04 1XL7
TITLE CRYSTAL STRUCTURE OF MOUSE CARNITINE OCTANOYLTRANSFERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEROXISOMAL CARNITINE O-OCTANOYLTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: COT;
COMPND 5 EC: 2.3.1.137;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: CROT, COT;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: B834 DE3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS CARNITINE, OCTANOYLTRANSFERASE, SELENOMETHIONINE, HEPES, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.JOGL,Y.S.HSIAO,L.TONG
REVDAT 4 11-OCT-17 1XL7 1 REMARK
REVDAT 3 24-FEB-09 1XL7 1 VERSN
REVDAT 2 11-JAN-05 1XL7 1 JRNL
REVDAT 1 19-OCT-04 1XL7 0
JRNL AUTH G.JOGL,Y.S.HSIAO,L.TONG
JRNL TITL CRYSTAL STRUCTURE OF MOUSE CARNITINE OCTANOYLTRANSFERASE AND
JRNL TITL 2 MOLECULAR DETERMINANTS OF SUBSTRATE SELECTIVITY.
JRNL REF J.BIOL.CHEM. V. 280 738 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 15492013
JRNL DOI 10.1074/JBC.M409894200
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.92
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 299663.430
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.6
REMARK 3 NUMBER OF REFLECTIONS : 200189
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 SET) : 0.190
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.300
REMARK 3 FREE R VALUE TEST SET COUNT : 14604
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.002
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.13
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 28402
REMARK 3 BIN R VALUE (WORKING SET) : 0.2580
REMARK 3 BIN FREE R VALUE : 0.2770
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 7.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 2237
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.006
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9619
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 102
REMARK 3 SOLVENT ATOMS : 539
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.22000
REMARK 3 B22 (A**2) : 3.22000
REMARK 3 B33 (A**2) : -6.45000
REMARK 3 B12 (A**2) : 2.62000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.21
REMARK 3 ESD FROM SIGMAA (A) : 0.22
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.25
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.23
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.750
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.270 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.950 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.340 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.420 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 47.54
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : MPD.PAR
REMARK 3 PARAMETER FILE 4 : MSE.PAR
REMARK 3 PARAMETER FILE 5 : HEP.PAR
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : MPD.TOP
REMARK 3 TOPOLOGY FILE 3 : MSE.TOP
REMARK 3 TOPOLOGY FILE 4 : HEP.TOP
REMARK 3 TOPOLOGY FILE 5 : WATER.TO
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1XL7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-OCT-04.
REMARK 100 THE DEPOSITION ID IS D_1000030482.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-FEB-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9790
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 210769
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
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) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SNB, SHELX, SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM HEPES, 62%V/V MPD, PH 7.4, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
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+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 81.31500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 46.94724
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 52.86000
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 81.31500
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 46.94724
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 52.86000
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 81.31500
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 46.94724
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 52.86000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 93.89447
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 105.72000
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 93.89447
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 105.72000
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 93.89447
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 105.72000
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 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 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 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 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 GLU A 2
REMARK 465 ASN A 3
REMARK 465 GLN A 4
REMARK 465 LEU A 5
REMARK 465 THR A 6
REMARK 465 LYS A 7
REMARK 465 SER A 8
REMARK 465 VAL A 9
REMARK 465 GLU A 10
REMARK 465 SER A 403
REMARK 465 PHE A 404
REMARK 465 GLY A 405
REMARK 465 LYS A 406
REMARK 465 LYS A 407
REMARK 465 LEU A 408
REMARK 465 THR A 409
REMARK 465 LYS A 410
REMARK 465 GLU A 411
REMARK 465 GLU A 412
REMARK 465 ALA A 413
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 465 ASN B 3
REMARK 465 GLN B 4
REMARK 465 LEU B 5
REMARK 465 THR B 6
REMARK 465 LYS B 7
REMARK 465 SER B 8
REMARK 465 VAL B 9
REMARK 465 GLU B 10
REMARK 465 HIS B 611
REMARK 465 LEU B 612
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 GLY B 564 N - CA - C ANGL. DEV. = -15.1 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 TYR A 90 -65.50 -132.25
REMARK 500 VAL A 101 -40.10 -130.33
REMARK 500 PRO A 108 25.39 -69.60
REMARK 500 HIS A 112 -107.43 -134.49
REMARK 500 TRP A 114 62.55 -115.74
REMARK 500 ASN A 230 31.41 -98.20
REMARK 500 ASP A 259 117.79 -170.56
REMARK 500 TYR A 290 20.68 -147.84
REMARK 500 ARG A 445 0.18 -69.06
REMARK 500 ARG A 451 -81.68 -116.09
REMARK 500 SER A 544 147.45 -179.57
REMARK 500 ARG A 550 6.14 59.31
REMARK 500 HIS A 611 -72.61 -51.58
REMARK 500 TYR B 90 -67.16 -133.85
REMARK 500 PRO B 108 30.46 -70.31
REMARK 500 HIS B 112 -101.74 -137.83
REMARK 500 ARG B 197 58.58 39.08
REMARK 500 ASP B 259 114.65 -170.67
REMARK 500 TYR B 290 17.07 -145.43
REMARK 500 LYS B 407 24.52 -66.82
REMARK 500 LEU B 408 -41.70 -136.05
REMARK 500 ARG B 445 2.45 -69.76
REMARK 500 ARG B 451 -83.88 -112.76
REMARK 500 SER B 544 143.24 -172.12
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 EPE A 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 707
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 708
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1NDB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CARNITINE ACETYLTRANSFERASE
REMARK 900 RELATED ID: 1NDF RELATED DB: PDB
REMARK 900 CARNITINE ACETYLTRANSFERASE IN COMPLEX WITH CARNITINE
REMARK 900 RELATED ID: 1NDI RELATED DB: PDB
REMARK 900 CARNITINE ACETYLTRANSFERASE IN COMPLEX WITH COA
REMARK 900 RELATED ID: 1NM8 RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN CARNITINE ACETYLTRANSFERASE
REMARK 900 RELATED ID: 1XL8 RELATED DB: PDB
REMARK 900 STRUCTURE OF MOUSE CARNITINE OCTANOYLTRANSFERASE IN COMPLEX WITH
REMARK 900 OCTANOYLCARNITINE
REMARK 900 RELATED ID: 1XMC RELATED DB: PDB
REMARK 900 C323M MUTANT STRUCTURE OF MOUSE CARNITINE OCTANOYLTRANSFERASE
REMARK 900 RELATED ID: 1XMD RELATED DB: PDB
REMARK 900 M335V MUTANT STRUCTURE OF MOUSE CARNITINE OCTANOYLTRANSFERASE
DBREF 1XL7 A 1 612 UNP Q9DC50 OCTC_MOUSE 1 612
DBREF 1XL7 B 1 612 UNP Q9DC50 OCTC_MOUSE 1 612
SEQADV 1XL7 MSE A 127 UNP Q9DC50 MET 127 MODIFIED RESIDUE
SEQADV 1XL7 MSE A 128 UNP Q9DC50 MET 128 MODIFIED RESIDUE
SEQADV 1XL7 MSE A 156 UNP Q9DC50 MET 156 MODIFIED RESIDUE
SEQADV 1XL7 MSE A 161 UNP Q9DC50 MET 161 MODIFIED RESIDUE
SEQADV 1XL7 MSE A 177 UNP Q9DC50 MET 177 MODIFIED RESIDUE
SEQADV 1XL7 MSE A 296 UNP Q9DC50 MET 296 MODIFIED RESIDUE
SEQADV 1XL7 MSE A 333 UNP Q9DC50 MET 333 MODIFIED RESIDUE
SEQADV 1XL7 MSE A 335 UNP Q9DC50 MET 335 MODIFIED RESIDUE
SEQADV 1XL7 MSE A 443 UNP Q9DC50 MET 443 MODIFIED RESIDUE
SEQADV 1XL7 MSE A 469 UNP Q9DC50 MET 469 MODIFIED RESIDUE
SEQADV 1XL7 MSE A 483 UNP Q9DC50 MET 483 MODIFIED RESIDUE
SEQADV 1XL7 MSE A 493 UNP Q9DC50 MET 493 MODIFIED RESIDUE
SEQADV 1XL7 MSE A 494 UNP Q9DC50 MET 494 MODIFIED RESIDUE
SEQADV 1XL7 MSE A 558 UNP Q9DC50 MET 558 MODIFIED RESIDUE
SEQADV 1XL7 MSE A 595 UNP Q9DC50 MET 595 MODIFIED RESIDUE
SEQADV 1XL7 MSE A 603 UNP Q9DC50 MET 603 MODIFIED RESIDUE
SEQADV 1XL7 MSE A 607 UNP Q9DC50 MET 607 MODIFIED RESIDUE
SEQADV 1XL7 MSE B 127 UNP Q9DC50 MET 127 MODIFIED RESIDUE
SEQADV 1XL7 MSE B 128 UNP Q9DC50 MET 128 MODIFIED RESIDUE
SEQADV 1XL7 MSE B 156 UNP Q9DC50 MET 156 MODIFIED RESIDUE
SEQADV 1XL7 MSE B 161 UNP Q9DC50 MET 161 MODIFIED RESIDUE
SEQADV 1XL7 MSE B 177 UNP Q9DC50 MET 177 MODIFIED RESIDUE
SEQADV 1XL7 MSE B 296 UNP Q9DC50 MET 296 MODIFIED RESIDUE
SEQADV 1XL7 MSE B 333 UNP Q9DC50 MET 333 MODIFIED RESIDUE
SEQADV 1XL7 MSE B 335 UNP Q9DC50 MET 335 MODIFIED RESIDUE
SEQADV 1XL7 MSE B 443 UNP Q9DC50 MET 443 MODIFIED RESIDUE
SEQADV 1XL7 MSE B 469 UNP Q9DC50 MET 469 MODIFIED RESIDUE
SEQADV 1XL7 MSE B 483 UNP Q9DC50 MET 483 MODIFIED RESIDUE
SEQADV 1XL7 MSE B 493 UNP Q9DC50 MET 493 MODIFIED RESIDUE
SEQADV 1XL7 MSE B 494 UNP Q9DC50 MET 494 MODIFIED RESIDUE
SEQADV 1XL7 MSE B 558 UNP Q9DC50 MET 558 MODIFIED RESIDUE
SEQADV 1XL7 MSE B 595 UNP Q9DC50 MET 595 MODIFIED RESIDUE
SEQADV 1XL7 MSE B 603 UNP Q9DC50 MET 603 MODIFIED RESIDUE
SEQADV 1XL7 MSE B 607 UNP Q9DC50 MET 607 MODIFIED RESIDUE
SEQRES 1 A 612 MET GLU ASN GLN LEU THR LYS SER VAL GLU GLU ARG THR
SEQRES 2 A 612 PHE GLN TYR GLN ASP SER LEU PRO SER LEU PRO VAL PRO
SEQRES 3 A 612 ALA LEU GLU GLU SER LEU LYS LYS TYR LEU GLU SER VAL
SEQRES 4 A 612 LYS PRO PHE ALA ASN GLU ASP GLU TYR LYS LYS THR GLU
SEQRES 5 A 612 GLU ILE VAL GLN LYS PHE GLN GLU GLY ALA GLY LYS ARG
SEQRES 6 A 612 LEU HIS GLN LYS LEU LEU GLU ARG ALA ARG GLY LYS ARG
SEQRES 7 A 612 ASN TRP LEU GLU GLU TRP TRP LEU ASN VAL ALA TYR LEU
SEQRES 8 A 612 ASP VAL ARG ILE PRO SER GLN LEU ASN VAL ASN PHE VAL
SEQRES 9 A 612 GLY PRO CYS PRO HIS PHE GLU HIS TYR TRP PRO ALA ARG
SEQRES 10 A 612 GLU GLY THR GLN LEU GLU ARG GLY SER MSE MSE LEU TRP
SEQRES 11 A 612 HIS ASN LEU ASN TYR TRP GLN LEU LEU ARG ARG GLU LYS
SEQRES 12 A 612 LEU PRO VAL HIS LYS SER GLY ASN THR PRO LEU ASP MSE
SEQRES 13 A 612 ASN GLN PHE ARG MSE LEU PHE SER THR CYS LYS VAL PRO
SEQRES 14 A 612 GLY ILE THR ARG ASP SER ILE MSE ASN TYR PHE LYS THR
SEQRES 15 A 612 GLU SER GLU GLY HIS CYS PRO THR HIS ILE ALA VAL LEU
SEQRES 16 A 612 CYS ARG GLY ARG ALA PHE VAL PHE ASP VAL LEU HIS GLU
SEQRES 17 A 612 GLY CYS LEU ILE THR PRO PRO GLU LEU LEU ARG GLN LEU
SEQRES 18 A 612 THR TYR ILE HIS LYS LYS CYS SER ASN GLU PRO VAL GLY
SEQRES 19 A 612 PRO SER ILE ALA ALA LEU THR SER GLU GLU ARG THR ARG
SEQRES 20 A 612 TRP ALA LYS ALA ARG GLU TYR LEU ILE SER LEU ASP PRO
SEQRES 21 A 612 GLU ASN LEU THR LEU LEU GLU LYS ILE GLN THR SER LEU
SEQRES 22 A 612 PHE VAL TYR SER ILE GLU ASP SER SER PRO HIS ALA THR
SEQRES 23 A 612 PRO GLU GLU TYR SER GLN VAL PHE GLU MSE LEU LEU GLY
SEQRES 24 A 612 GLY ASP PRO SER VAL ARG TRP GLY ASP LYS SER TYR ASN
SEQRES 25 A 612 LEU ILE SER PHE ALA ASN GLY ILE PHE GLY CYS CYS CYS
SEQRES 26 A 612 ASP HIS ALA PRO TYR ASP ALA MSE VAL MSE VAL ASN ILE
SEQRES 27 A 612 ALA HIS TYR VAL ASP GLU ARG VAL LEU GLU THR GLU GLY
SEQRES 28 A 612 ARG TRP LYS GLY SER GLU LYS VAL ARG ASP ILE PRO LEU
SEQRES 29 A 612 PRO GLU GLU LEU VAL PHE THR VAL ASP GLU LYS ILE LEU
SEQRES 30 A 612 ASN ASP VAL SER GLN ALA LYS ALA GLN HIS LEU LYS ALA
SEQRES 31 A 612 ALA SER ASP LEU GLN ILE ALA ALA SER THR PHE THR SER
SEQRES 32 A 612 PHE GLY LYS LYS LEU THR LYS GLU GLU ALA LEU HIS PRO
SEQRES 33 A 612 ASP THR PHE ILE GLN LEU ALA LEU GLN LEU ALA TYR TYR
SEQRES 34 A 612 ARG LEU HIS GLY ARG PRO GLY CYS CYS TYR GLU THR ALA
SEQRES 35 A 612 MSE THR ARG TYR PHE TYR HIS GLY ARG THR GLU THR VAL
SEQRES 36 A 612 ARG SER CYS THR VAL GLU ALA VAL ARG TRP CYS GLN SER
SEQRES 37 A 612 MSE GLN ASP PRO SER ALA SER LEU LEU GLU ARG GLN GLN
SEQRES 38 A 612 LYS MSE LEU GLU ALA PHE ALA LYS HIS ASN LYS MSE MSE
SEQRES 39 A 612 LYS ASP CYS SER HIS GLY LYS GLY PHE ASP ARG HIS LEU
SEQRES 40 A 612 LEU GLY LEU LEU LEU ILE ALA LYS GLU GLU GLY LEU PRO
SEQRES 41 A 612 VAL PRO GLU LEU PHE GLU ASP PRO LEU PHE SER ARG SER
SEQRES 42 A 612 GLY GLY GLY GLY ASN PHE VAL LEU SER THR SER LEU VAL
SEQRES 43 A 612 GLY TYR LEU ARG VAL GLN GLY VAL VAL VAL PRO MSE VAL
SEQRES 44 A 612 HIS ASN GLY TYR GLY PHE PHE TYR HIS ILE ARG ASP ASP
SEQRES 45 A 612 ARG PHE VAL VAL ALA CYS SER SER TRP ARG SER CYS PRO
SEQRES 46 A 612 GLU THR ASP ALA GLU LYS LEU VAL GLN MSE ILE PHE HIS
SEQRES 47 A 612 ALA PHE HIS ASP MSE ILE GLN LEU MSE ASN THR ALA HIS
SEQRES 48 A 612 LEU
SEQRES 1 B 612 MET GLU ASN GLN LEU THR LYS SER VAL GLU GLU ARG THR
SEQRES 2 B 612 PHE GLN TYR GLN ASP SER LEU PRO SER LEU PRO VAL PRO
SEQRES 3 B 612 ALA LEU GLU GLU SER LEU LYS LYS TYR LEU GLU SER VAL
SEQRES 4 B 612 LYS PRO PHE ALA ASN GLU ASP GLU TYR LYS LYS THR GLU
SEQRES 5 B 612 GLU ILE VAL GLN LYS PHE GLN GLU GLY ALA GLY LYS ARG
SEQRES 6 B 612 LEU HIS GLN LYS LEU LEU GLU ARG ALA ARG GLY LYS ARG
SEQRES 7 B 612 ASN TRP LEU GLU GLU TRP TRP LEU ASN VAL ALA TYR LEU
SEQRES 8 B 612 ASP VAL ARG ILE PRO SER GLN LEU ASN VAL ASN PHE VAL
SEQRES 9 B 612 GLY PRO CYS PRO HIS PHE GLU HIS TYR TRP PRO ALA ARG
SEQRES 10 B 612 GLU GLY THR GLN LEU GLU ARG GLY SER MSE MSE LEU TRP
SEQRES 11 B 612 HIS ASN LEU ASN TYR TRP GLN LEU LEU ARG ARG GLU LYS
SEQRES 12 B 612 LEU PRO VAL HIS LYS SER GLY ASN THR PRO LEU ASP MSE
SEQRES 13 B 612 ASN GLN PHE ARG MSE LEU PHE SER THR CYS LYS VAL PRO
SEQRES 14 B 612 GLY ILE THR ARG ASP SER ILE MSE ASN TYR PHE LYS THR
SEQRES 15 B 612 GLU SER GLU GLY HIS CYS PRO THR HIS ILE ALA VAL LEU
SEQRES 16 B 612 CYS ARG GLY ARG ALA PHE VAL PHE ASP VAL LEU HIS GLU
SEQRES 17 B 612 GLY CYS LEU ILE THR PRO PRO GLU LEU LEU ARG GLN LEU
SEQRES 18 B 612 THR TYR ILE HIS LYS LYS CYS SER ASN GLU PRO VAL GLY
SEQRES 19 B 612 PRO SER ILE ALA ALA LEU THR SER GLU GLU ARG THR ARG
SEQRES 20 B 612 TRP ALA LYS ALA ARG GLU TYR LEU ILE SER LEU ASP PRO
SEQRES 21 B 612 GLU ASN LEU THR LEU LEU GLU LYS ILE GLN THR SER LEU
SEQRES 22 B 612 PHE VAL TYR SER ILE GLU ASP SER SER PRO HIS ALA THR
SEQRES 23 B 612 PRO GLU GLU TYR SER GLN VAL PHE GLU MSE LEU LEU GLY
SEQRES 24 B 612 GLY ASP PRO SER VAL ARG TRP GLY ASP LYS SER TYR ASN
SEQRES 25 B 612 LEU ILE SER PHE ALA ASN GLY ILE PHE GLY CYS CYS CYS
SEQRES 26 B 612 ASP HIS ALA PRO TYR ASP ALA MSE VAL MSE VAL ASN ILE
SEQRES 27 B 612 ALA HIS TYR VAL ASP GLU ARG VAL LEU GLU THR GLU GLY
SEQRES 28 B 612 ARG TRP LYS GLY SER GLU LYS VAL ARG ASP ILE PRO LEU
SEQRES 29 B 612 PRO GLU GLU LEU VAL PHE THR VAL ASP GLU LYS ILE LEU
SEQRES 30 B 612 ASN ASP VAL SER GLN ALA LYS ALA GLN HIS LEU LYS ALA
SEQRES 31 B 612 ALA SER ASP LEU GLN ILE ALA ALA SER THR PHE THR SER
SEQRES 32 B 612 PHE GLY LYS LYS LEU THR LYS GLU GLU ALA LEU HIS PRO
SEQRES 33 B 612 ASP THR PHE ILE GLN LEU ALA LEU GLN LEU ALA TYR TYR
SEQRES 34 B 612 ARG LEU HIS GLY ARG PRO GLY CYS CYS TYR GLU THR ALA
SEQRES 35 B 612 MSE THR ARG TYR PHE TYR HIS GLY ARG THR GLU THR VAL
SEQRES 36 B 612 ARG SER CYS THR VAL GLU ALA VAL ARG TRP CYS GLN SER
SEQRES 37 B 612 MSE GLN ASP PRO SER ALA SER LEU LEU GLU ARG GLN GLN
SEQRES 38 B 612 LYS MSE LEU GLU ALA PHE ALA LYS HIS ASN LYS MSE MSE
SEQRES 39 B 612 LYS ASP CYS SER HIS GLY LYS GLY PHE ASP ARG HIS LEU
SEQRES 40 B 612 LEU GLY LEU LEU LEU ILE ALA LYS GLU GLU GLY LEU PRO
SEQRES 41 B 612 VAL PRO GLU LEU PHE GLU ASP PRO LEU PHE SER ARG SER
SEQRES 42 B 612 GLY GLY GLY GLY ASN PHE VAL LEU SER THR SER LEU VAL
SEQRES 43 B 612 GLY TYR LEU ARG VAL GLN GLY VAL VAL VAL PRO MSE VAL
SEQRES 44 B 612 HIS ASN GLY TYR GLY PHE PHE TYR HIS ILE ARG ASP ASP
SEQRES 45 B 612 ARG PHE VAL VAL ALA CYS SER SER TRP ARG SER CYS PRO
SEQRES 46 B 612 GLU THR ASP ALA GLU LYS LEU VAL GLN MSE ILE PHE HIS
SEQRES 47 B 612 ALA PHE HIS ASP MSE ILE GLN LEU MSE ASN THR ALA HIS
SEQRES 48 B 612 LEU
MODRES 1XL7 MSE A 127 MET SELENOMETHIONINE
MODRES 1XL7 MSE A 128 MET SELENOMETHIONINE
MODRES 1XL7 MSE A 156 MET SELENOMETHIONINE
MODRES 1XL7 MSE A 161 MET SELENOMETHIONINE
MODRES 1XL7 MSE A 177 MET SELENOMETHIONINE
MODRES 1XL7 MSE A 296 MET SELENOMETHIONINE
MODRES 1XL7 MSE A 333 MET SELENOMETHIONINE
MODRES 1XL7 MSE A 335 MET SELENOMETHIONINE
MODRES 1XL7 MSE A 443 MET SELENOMETHIONINE
MODRES 1XL7 MSE A 469 MET SELENOMETHIONINE
MODRES 1XL7 MSE A 483 MET SELENOMETHIONINE
MODRES 1XL7 MSE A 493 MET SELENOMETHIONINE
MODRES 1XL7 MSE A 494 MET SELENOMETHIONINE
MODRES 1XL7 MSE A 558 MET SELENOMETHIONINE
MODRES 1XL7 MSE A 595 MET SELENOMETHIONINE
MODRES 1XL7 MSE A 603 MET SELENOMETHIONINE
MODRES 1XL7 MSE A 607 MET SELENOMETHIONINE
MODRES 1XL7 MSE B 127 MET SELENOMETHIONINE
MODRES 1XL7 MSE B 128 MET SELENOMETHIONINE
MODRES 1XL7 MSE B 156 MET SELENOMETHIONINE
MODRES 1XL7 MSE B 161 MET SELENOMETHIONINE
MODRES 1XL7 MSE B 177 MET SELENOMETHIONINE
MODRES 1XL7 MSE B 296 MET SELENOMETHIONINE
MODRES 1XL7 MSE B 333 MET SELENOMETHIONINE
MODRES 1XL7 MSE B 335 MET SELENOMETHIONINE
MODRES 1XL7 MSE B 443 MET SELENOMETHIONINE
MODRES 1XL7 MSE B 469 MET SELENOMETHIONINE
MODRES 1XL7 MSE B 483 MET SELENOMETHIONINE
MODRES 1XL7 MSE B 493 MET SELENOMETHIONINE
MODRES 1XL7 MSE B 494 MET SELENOMETHIONINE
MODRES 1XL7 MSE B 558 MET SELENOMETHIONINE
MODRES 1XL7 MSE B 595 MET SELENOMETHIONINE
MODRES 1XL7 MSE B 603 MET SELENOMETHIONINE
MODRES 1XL7 MSE B 607 MET SELENOMETHIONINE
HET MSE A 127 8
HET MSE A 128 8
HET MSE A 156 8
HET MSE A 161 8
HET MSE A 177 8
HET MSE A 296 8
HET MSE A 333 8
HET MSE A 335 8
HET MSE A 443 8
HET MSE A 469 8
HET MSE A 483 8
HET MSE A 493 8
HET MSE A 494 8
HET MSE A 558 8
HET MSE A 595 8
HET MSE A 603 8
HET MSE A 607 8
HET MSE B 127 8
HET MSE B 128 8
HET MSE B 156 8
HET MSE B 161 8
HET MSE B 177 8
HET MSE B 296 8
HET MSE B 333 8
HET MSE B 335 8
HET MSE B 443 8
HET MSE B 469 8
HET MSE B 483 8
HET MSE B 493 8
HET MSE B 494 8
HET MSE B 558 8
HET MSE B 595 8
HET MSE B 603 8
HET MSE B 607 8
HET EPE A 613 15
HET MPD A 614 8
HET MPD A 615 8
HET EPE B 701 15
HET MPD B 702 8
HET MPD B 703 8
HET MPD B 704 8
HET MPD B 705 8
HET MPD B 706 8
HET MPD B 707 8
HET MPD B 708 8
HETNAM MSE SELENOMETHIONINE
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETSYN EPE HEPES
FORMUL 1 MSE 34(C5 H11 N O2 SE)
FORMUL 3 EPE 2(C8 H18 N2 O4 S)
FORMUL 4 MPD 9(C6 H14 O2)
FORMUL 14 HOH *539(H2 O)
HELIX 1 1 TYR A 16 LEU A 20 5 5
HELIX 2 2 ALA A 27 LYS A 40 1 14
HELIX 3 3 PRO A 41 ALA A 43 5 3
HELIX 4 4 ASN A 44 GLY A 61 1 18
HELIX 5 5 GLY A 61 LYS A 77 1 17
HELIX 6 6 LEU A 81 TYR A 90 1 10
HELIX 7 7 PRO A 96 VAL A 101 1 6
HELIX 8 8 PRO A 108 HIS A 112 5 5
HELIX 9 9 THR A 120 ARG A 141 1 22
HELIX 10 10 MSE A 156 LEU A 162 5 7
HELIX 11 11 THR A 213 ASN A 230 1 18
HELIX 12 12 SER A 236 GLU A 243 5 8
HELIX 13 13 GLU A 244 ASP A 259 1 16
HELIX 14 14 ASP A 259 SER A 272 1 14
HELIX 15 15 TYR A 290 GLY A 299 1 10
HELIX 16 16 ASP A 301 ARG A 305 5 5
HELIX 17 17 ALA A 332 THR A 349 1 18
HELIX 18 18 ASP A 373 ASP A 393 1 21
HELIX 19 19 HIS A 415 GLY A 433 1 19
HELIX 20 20 THR A 459 ASP A 471 1 13
HELIX 21 21 SER A 475 HIS A 499 1 25
HELIX 22 22 PHE A 503 GLU A 517 1 15
HELIX 23 23 PRO A 522 GLU A 526 5 5
HELIX 24 24 ASP A 527 SER A 533 1 7
HELIX 25 25 ASP A 588 LEU A 612 1 25
HELIX 26 26 TYR B 16 LEU B 20 5 5
HELIX 27 27 ALA B 27 LYS B 40 1 14
HELIX 28 28 PRO B 41 ALA B 43 5 3
HELIX 29 29 ASN B 44 GLY B 61 1 18
HELIX 30 30 GLY B 61 GLY B 76 1 16
HELIX 31 31 LEU B 81 TYR B 90 1 10
HELIX 32 32 PRO B 96 VAL B 101 1 6
HELIX 33 33 PRO B 108 HIS B 112 5 5
HELIX 34 34 THR B 120 ARG B 141 1 22
HELIX 35 35 MSE B 156 LEU B 162 5 7
HELIX 36 36 THR B 213 ASN B 230 1 18
HELIX 37 37 SER B 236 GLU B 243 5 8
HELIX 38 38 GLU B 244 ASP B 259 1 16
HELIX 39 39 PRO B 260 SER B 272 1 13
HELIX 40 40 TYR B 290 GLY B 299 1 10
HELIX 41 41 ASP B 301 ARG B 305 5 5
HELIX 42 42 ASP B 331 GLU B 350 1 20
HELIX 43 43 ASP B 373 ASP B 393 1 21
HELIX 44 44 GLY B 405 LYS B 410 1 6
HELIX 45 45 GLU B 411 ALA B 413 5 3
HELIX 46 46 HIS B 415 GLY B 433 1 19
HELIX 47 47 THR B 459 GLN B 470 1 12
HELIX 48 48 SER B 475 HIS B 499 1 25
HELIX 49 49 PHE B 503 GLY B 518 1 16
HELIX 50 50 PRO B 522 ASP B 527 1 6
HELIX 51 51 ASP B 527 SER B 533 1 7
HELIX 52 52 ASP B 588 ALA B 610 1 23
SHEET 1 A 7 PHE A 103 PRO A 106 0
SHEET 2 A 7 PHE A 321 CYS A 325 -1 O CYS A 325 N PHE A 103
SHEET 3 A 7 ASN A 312 SER A 315 -1 N ILE A 314 O GLY A 322
SHEET 4 A 7 VAL A 275 ILE A 278 1 N SER A 277 O LEU A 313
SHEET 5 A 7 HIS A 191 CYS A 196 1 N ALA A 193 O TYR A 276
SHEET 6 A 7 ARG A 199 ASP A 204 -1 O PHE A 201 N VAL A 194
SHEET 7 A 7 GLU A 366 GLU A 367 -1 O GLU A 366 N VAL A 202
SHEET 1 B 2 LYS A 148 SER A 149 0
SHEET 2 B 2 THR A 152 PRO A 153 -1 O THR A 152 N SER A 149
SHEET 1 C 2 THR A 165 VAL A 168 0
SHEET 2 C 2 SER A 175 ASN A 178 -1 O MSE A 177 N CYS A 166
SHEET 1 D 2 LEU A 206 HIS A 207 0
SHEET 2 D 2 CYS A 210 LEU A 211 -1 O CYS A 210 N HIS A 207
SHEET 1 E 6 LEU A 394 PHE A 401 0
SHEET 2 E 6 ARG A 573 TRP A 581 -1 O PHE A 574 N PHE A 401
SHEET 3 E 6 TYR A 563 ARG A 570 -1 N PHE A 566 O ALA A 577
SHEET 4 E 6 LEU A 541 LEU A 545 1 N SER A 542 O PHE A 565
SHEET 5 E 6 CYS A 438 MSE A 443 1 N TYR A 439 O LEU A 541
SHEET 6 E 6 THR A 452 ARG A 456 -1 O GLU A 453 N ALA A 442
SHEET 1 F 7 PHE B 103 PRO B 106 0
SHEET 2 F 7 PHE B 321 CYS B 325 -1 O CYS B 325 N PHE B 103
SHEET 3 F 7 ASN B 312 SER B 315 -1 N ILE B 314 O GLY B 322
SHEET 4 F 7 VAL B 275 ILE B 278 1 N SER B 277 O LEU B 313
SHEET 5 F 7 HIS B 191 CYS B 196 1 N ALA B 193 O TYR B 276
SHEET 6 F 7 ARG B 199 ASP B 204 -1 O PHE B 201 N VAL B 194
SHEET 7 F 7 GLU B 366 GLU B 367 -1 O GLU B 366 N VAL B 202
SHEET 1 G 2 LYS B 148 SER B 149 0
SHEET 2 G 2 THR B 152 PRO B 153 -1 O THR B 152 N SER B 149
SHEET 1 H 2 THR B 165 VAL B 168 0
SHEET 2 H 2 SER B 175 ASN B 178 -1 O MSE B 177 N CYS B 166
SHEET 1 I 2 LEU B 206 HIS B 207 0
SHEET 2 I 2 CYS B 210 LEU B 211 -1 O CYS B 210 N HIS B 207
SHEET 1 J 6 LEU B 394 PHE B 401 0
SHEET 2 J 6 ARG B 573 TRP B 581 -1 O PHE B 574 N PHE B 401
SHEET 3 J 6 TYR B 563 ARG B 570 -1 N PHE B 566 O ALA B 577
SHEET 4 J 6 LEU B 541 LEU B 545 1 N SER B 542 O PHE B 565
SHEET 5 J 6 CYS B 438 MSE B 443 1 N TYR B 439 O LEU B 541
SHEET 6 J 6 THR B 452 ARG B 456 -1 O GLU B 453 N ALA B 442
LINK C SER A 126 N MSE A 127 1555 1555 1.33
LINK C MSE A 127 N MSE A 128 1555 1555 1.33
LINK C MSE A 128 N LEU A 129 1555 1555 1.33
LINK C ASP A 155 N MSE A 156 1555 1555 1.33
LINK C MSE A 156 N ASN A 157 1555 1555 1.33
LINK C ARG A 160 N MSE A 161 1555 1555 1.33
LINK C MSE A 161 N LEU A 162 1555 1555 1.33
LINK C ILE A 176 N MSE A 177 1555 1555 1.33
LINK C MSE A 177 N ASN A 178 1555 1555 1.33
LINK C GLU A 295 N MSE A 296 1555 1555 1.33
LINK C MSE A 296 N LEU A 297 1555 1555 1.33
LINK C ALA A 332 N MSE A 333 1555 1555 1.33
LINK C MSE A 333 N VAL A 334 1555 1555 1.33
LINK C VAL A 334 N MSE A 335 1555 1555 1.33
LINK C MSE A 335 N VAL A 336 1555 1555 1.33
LINK C ALA A 442 N MSE A 443 1555 1555 1.33
LINK C MSE A 443 N THR A 444 1555 1555 1.33
LINK C SER A 468 N MSE A 469 1555 1555 1.33
LINK C MSE A 469 N GLN A 470 1555 1555 1.33
LINK C LYS A 482 N MSE A 483 1555 1555 1.33
LINK C MSE A 483 N LEU A 484 1555 1555 1.33
LINK C LYS A 492 N MSE A 493 1555 1555 1.33
LINK C MSE A 493 N MSE A 494 1555 1555 1.33
LINK C MSE A 494 N LYS A 495 1555 1555 1.33
LINK C PRO A 557 N MSE A 558 1555 1555 1.33
LINK C MSE A 558 N VAL A 559 1555 1555 1.33
LINK C GLN A 594 N MSE A 595 1555 1555 1.33
LINK C MSE A 595 N ILE A 596 1555 1555 1.33
LINK C ASP A 602 N MSE A 603 1555 1555 1.33
LINK C MSE A 603 N ILE A 604 1555 1555 1.33
LINK C LEU A 606 N MSE A 607 1555 1555 1.33
LINK C MSE A 607 N ASN A 608 1555 1555 1.33
LINK C SER B 126 N MSE B 127 1555 1555 1.33
LINK C MSE B 127 N MSE B 128 1555 1555 1.33
LINK C MSE B 128 N LEU B 129 1555 1555 1.33
LINK C ASP B 155 N MSE B 156 1555 1555 1.33
LINK C MSE B 156 N ASN B 157 1555 1555 1.33
LINK C ARG B 160 N MSE B 161 1555 1555 1.33
LINK C MSE B 161 N LEU B 162 1555 1555 1.33
LINK C ILE B 176 N MSE B 177 1555 1555 1.33
LINK C MSE B 177 N ASN B 178 1555 1555 1.33
LINK C GLU B 295 N MSE B 296 1555 1555 1.33
LINK C MSE B 296 N LEU B 297 1555 1555 1.33
LINK C ALA B 332 N MSE B 333 1555 1555 1.33
LINK C MSE B 333 N VAL B 334 1555 1555 1.33
LINK C VAL B 334 N MSE B 335 1555 1555 1.33
LINK C MSE B 335 N VAL B 336 1555 1555 1.33
LINK C ALA B 442 N MSE B 443 1555 1555 1.33
LINK C MSE B 443 N THR B 444 1555 1555 1.33
LINK C SER B 468 N MSE B 469 1555 1555 1.33
LINK C MSE B 469 N GLN B 470 1555 1555 1.33
LINK C LYS B 482 N MSE B 483 1555 1555 1.33
LINK C MSE B 483 N LEU B 484 1555 1555 1.33
LINK C LYS B 492 N MSE B 493 1555 1555 1.33
LINK C MSE B 493 N MSE B 494 1555 1555 1.33
LINK C MSE B 494 N LYS B 495 1555 1555 1.33
LINK C PRO B 557 N MSE B 558 1555 1555 1.33
LINK C MSE B 558 N VAL B 559 1555 1555 1.33
LINK C GLN B 594 N MSE B 595 1555 1555 1.33
LINK C MSE B 595 N ILE B 596 1555 1555 1.33
LINK C ASP B 602 N MSE B 603 1555 1555 1.33
LINK C MSE B 603 N ILE B 604 1555 1555 1.33
LINK C LEU B 606 N MSE B 607 1555 1555 1.33
LINK C MSE B 607 N ASN B 608 1555 1555 1.33
SITE 1 AC1 11 TRP A 85 TYR A 90 HIS A 327 ASP A 331
SITE 2 AC1 11 TYR A 439 THR A 441 THR A 452 HOH A 621
SITE 3 AC1 11 HOH A 654 HOH A 668 HOH A 683
SITE 1 AC2 14 TRP B 85 TYR B 90 HIS B 327 ASP B 331
SITE 2 AC2 14 TYR B 439 THR B 441 THR B 452 MSE B 558
SITE 3 AC2 14 MPD B 702 MPD B 707 HOH B 711 HOH B 865
SITE 4 AC2 14 HOH B 924 HOH B1018
SITE 1 AC3 5 HIS A 327 ASP A 331 ALA A 332 SER A 544
SITE 2 AC3 5 PHE A 566
SITE 1 AC4 4 GLN B 68 GLU B 72 ARG B 75 LEU B 258
SITE 1 AC5 8 PHE B 103 HIS B 327 ALA B 332 THR B 441
SITE 2 AC5 8 PHE B 566 EPE B 701 HOH B 865 HOH B1018
SITE 1 AC6 5 HIS B 191 PHE B 203 ASP B 204 LYS B 268
SITE 2 AC6 5 GLU B 366
SITE 1 AC7 1 PRO B 153
SITE 1 AC8 6 LYS B 33 GLU B 52 GLN B 56 GLN B 59
SITE 2 AC8 6 GLU B 366 HOH B 836
SITE 1 AC9 5 LEU B 71 ARG B 75 SER B 257 LEU B 258
SITE 2 AC9 5 PRO B 260
SITE 1 BC1 4 TYR B 439 GLY B 537 EPE B 701 HOH B 924
SITE 1 BC2 3 SER B 126 TRP B 353 HOH B 861
CRYST1 162.630 162.630 158.580 90.00 90.00 120.00 H 3 18
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 0.006149 0.003550 0.000000 0.00000
SCALE2 0.000000 0.007100 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006306 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
