HEADER TRANSFERASE 10-FEB-06 2DEB
TITLE CRYSTAL STRUCTURE OF RAT CARNITINE PALMITOYLTRANSFERASE 2 IN SPACE
TITLE 2 GROUP C2221
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARNITINE O-PALMITOYLTRANSFERASE II, MITOCHONDRIAL;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CPT II;
COMPND 5 EC: 2.3.1.21;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS CENTRAL SIX-STRANDED BETA-SHEET, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.C.RUFER,R.THOMA,J.BENZ,M.STIHLE,B.GSELL,E.DE ROO,D.W.BANNER,
AUTHOR 2 F.MUELLER,O.CHOMIENNE,M.HENNIG
REVDAT 4 29-JUL-20 2DEB 1 COMPND REMARK SEQADV HETNAM
REVDAT 4 2 1 LINK SITE
REVDAT 3 11-OCT-17 2DEB 1 REMARK
REVDAT 2 24-FEB-09 2DEB 1 VERSN
REVDAT 1 10-FEB-07 2DEB 0
JRNL AUTH A.C.RUFER,R.THOMA,J.BENZ,M.STIHLE,B.GSELL,E.DE ROO,
JRNL AUTH 2 D.W.BANNER,F.MUELLER,O.CHOMIENNE,M.HENNIG
JRNL TITL THE CRYSTAL STRUCTURE OF CARNITINE PALMITOYLTRANSFERASE 2
JRNL TITL 2 AND IMPLICATIONS FOR DIABETES TREATMENT
JRNL REF STRUCTURE V. 14 713 2006
JRNL REFN ISSN 0969-2126
JRNL PMID 16615901
JRNL DOI 10.1016/J.STR.2006.01.008
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 23.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 179022
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) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.194
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 9462
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) : 13116
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.70
REMARK 3 BIN R VALUE (WORKING SET) : 0.1700
REMARK 3 BIN FREE R VALUE SET COUNT : 695
REMARK 3 BIN FREE R VALUE : 0.2200
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9978
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 110
REMARK 3 SOLVENT ATOMS : 1364
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.49
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.22000
REMARK 3 B22 (A**2) : -0.29000
REMARK 3 B33 (A**2) : 0.08000
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): 0.079
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.080
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.048
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.295
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10433 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 9282 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14153 ; 1.227 ; 1.961
REMARK 3 BOND ANGLES OTHERS (DEGREES): 21662 ; 0.790 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1251 ; 5.601 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 504 ;33.660 ;23.730
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1739 ;11.533 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 69 ;14.676 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1554 ; 0.072 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11502 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2177 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2188 ; 0.216 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 9315 ; 0.181 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5123 ; 0.183 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 5578 ; 0.084 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1007 ; 0.134 ; 0.200
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): 24 ; 0.174 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 105 ; 0.246 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 67 ; 0.131 ; 0.200
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): 6408 ; 2.404 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2508 ; 0.714 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10180 ; 3.083 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4455 ; 4.767 ; 4.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3973 ; 6.808 ; 6.000
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 : BABINET MODEL WITH 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
REMARK 4
REMARK 4 2DEB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-FEB-06.
REMARK 100 THE DEPOSITION ID IS D_1000025316.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-AUG-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97899
REMARK 200 MONOCHROMATOR : LN2 COOLED FIXED-EXIT SI(111)
REMARK 200 MONOCHROMATOR (19.65M, FOCUSING
REMARK 200 SAGITTAL-HORIZONTAL) BENDABLE
REMARK 200 MIRROR (20.50 M FOCUSING
REMARK 200 MERIDIONAL-VERTICAL)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MAR
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 188487
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 23.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.0400
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) : 1.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.21200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 7.240
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.23
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.15M DL-MALIC ACID 20% (W/V) PEG 3350
REMARK 280 , PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 155.22000
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 155.22000
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 1.000000 0.000000 0.000000 47.59000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 48.64500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 47.59000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 48.64500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 155.22000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 47.59000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 48.64500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 155.22000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 47.59000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 48.64500
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
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 6
REMARK 465 GLY A 7
REMARK 465 SER A 8
REMARK 465 SER A 9
REMARK 465 HIS A 10
REMARK 465 HIS A 11
REMARK 465 HIS A 12
REMARK 465 HIS A 13
REMARK 465 HIS A 14
REMARK 465 HIS A 15
REMARK 465 SER A 16
REMARK 465 SER A 17
REMARK 465 GLY A 18
REMARK 465 LEU A 19
REMARK 465 VAL A 20
REMARK 465 PRO A 21
REMARK 465 ARG A 22
REMARK 465 GLY A 23
REMARK 465 SER A 24
REMARK 465 HIS A 25
REMARK 465 MET A 26
REMARK 465 ALA A 27
REMARK 465 VAL A 28
REMARK 465 SER A 29
REMARK 465 GLY A 30
REMARK 465 PRO A 31
REMARK 465 MET B 6
REMARK 465 GLY B 7
REMARK 465 SER B 8
REMARK 465 SER B 9
REMARK 465 HIS B 10
REMARK 465 HIS B 11
REMARK 465 HIS B 12
REMARK 465 HIS B 13
REMARK 465 HIS B 14
REMARK 465 HIS B 15
REMARK 465 SER B 16
REMARK 465 SER B 17
REMARK 465 GLY B 18
REMARK 465 LEU B 19
REMARK 465 VAL B 20
REMARK 465 PRO B 21
REMARK 465 ARG B 22
REMARK 465 GLY B 23
REMARK 465 SER B 24
REMARK 465 HIS B 25
REMARK 465 MET B 26
REMARK 465 ALA B 27
REMARK 465 VAL B 28
REMARK 465 SER B 29
REMARK 465 GLY B 30
REMARK 465 PRO B 31
REMARK 465 THR B 658
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 2384 O HOH A 2437 2.01
REMARK 500 O HOH B 2789 O HOH B 2937 2.15
REMARK 500 CZ ARG A 518 O HOH A 2544 2.16
REMARK 500 O TYR A 574 NE2 GLN A 580 2.18
REMARK 500 NE ARG A 518 O HOH A 2544 2.18
REMARK 500
REMARK 500 REMARK: NULL
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 MSE A 135 SE MSE A 135 CE -1.032
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 MSE B 61 CG - SE - CE ANGL. DEV. = -21.2 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 LEU A 129 -54.08 71.19
REMARK 500 PHE A 131 -45.33 -132.56
REMARK 500 ASN A 230 -58.09 74.98
REMARK 500 HIS A 344 -30.65 -145.49
REMARK 500 ARG A 498 -116.29 -127.54
REMARK 500 LEU B 129 -52.55 72.02
REMARK 500 PHE B 131 -49.92 -130.52
REMARK 500 ASN B 230 -53.88 74.51
REMARK 500 ASN B 265 116.90 -39.73
REMARK 500 ASP B 329 41.21 -108.52
REMARK 500 HIS B 344 -30.32 -146.51
REMARK 500 ARG B 498 -117.06 -124.70
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 COA A 2350
REMARK 610 PLM A 2351
REMARK 610 COA B 2360
REMARK 610 PLM B 1600
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2FW3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF RAT CARNITINE PALMITOYLTRANSFERASE 2 IN
REMARK 900 COMPLEX WITH ANTIDIABETIC DRUG ST1326
REMARK 900 RELATED ID: 2FYO RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF RAT CARNITINE PALMITOYLTRANSFERASE 2 IN SPACE
REMARK 900 GROUP P43212
DBREF 2DEB A 27 658 UNP P18886 CPT2_RAT 27 658
DBREF 2DEB B 27 658 UNP P18886 CPT2_RAT 27 658
SEQADV 2DEB MET A 6 UNP P18886 EXPRESSION TAG
SEQADV 2DEB GLY A 7 UNP P18886 EXPRESSION TAG
SEQADV 2DEB SER A 8 UNP P18886 EXPRESSION TAG
SEQADV 2DEB SER A 9 UNP P18886 EXPRESSION TAG
SEQADV 2DEB HIS A 10 UNP P18886 EXPRESSION TAG
SEQADV 2DEB HIS A 11 UNP P18886 EXPRESSION TAG
SEQADV 2DEB HIS A 12 UNP P18886 EXPRESSION TAG
SEQADV 2DEB HIS A 13 UNP P18886 EXPRESSION TAG
SEQADV 2DEB HIS A 14 UNP P18886 EXPRESSION TAG
SEQADV 2DEB HIS A 15 UNP P18886 EXPRESSION TAG
SEQADV 2DEB SER A 16 UNP P18886 EXPRESSION TAG
SEQADV 2DEB SER A 17 UNP P18886 EXPRESSION TAG
SEQADV 2DEB GLY A 18 UNP P18886 EXPRESSION TAG
SEQADV 2DEB LEU A 19 UNP P18886 EXPRESSION TAG
SEQADV 2DEB VAL A 20 UNP P18886 EXPRESSION TAG
SEQADV 2DEB PRO A 21 UNP P18886 EXPRESSION TAG
SEQADV 2DEB ARG A 22 UNP P18886 EXPRESSION TAG
SEQADV 2DEB GLY A 23 UNP P18886 EXPRESSION TAG
SEQADV 2DEB SER A 24 UNP P18886 EXPRESSION TAG
SEQADV 2DEB HIS A 25 UNP P18886 EXPRESSION TAG
SEQADV 2DEB MET A 26 UNP P18886 EXPRESSION TAG
SEQADV 2DEB MSE A 43 UNP P18886 MET 43 MODIFIED RESIDUE
SEQADV 2DEB MSE A 61 UNP P18886 MET 61 MODIFIED RESIDUE
SEQADV 2DEB MSE A 119 UNP P18886 MET 119 MODIFIED RESIDUE
SEQADV 2DEB MSE A 135 UNP P18886 MET 135 MODIFIED RESIDUE
SEQADV 2DEB MSE A 214 UNP P18886 MET 214 MODIFIED RESIDUE
SEQADV 2DEB MSE A 332 UNP P18886 MET 332 MODIFIED RESIDUE
SEQADV 2DEB MSE A 342 UNP P18886 MET 342 MODIFIED RESIDUE
SEQADV 2DEB MSE A 473 UNP P18886 MET 473 MODIFIED RESIDUE
SEQADV 2DEB MSE A 531 UNP P18886 MET 531 MODIFIED RESIDUE
SEQADV 2DEB MSE A 532 UNP P18886 MET 532 MODIFIED RESIDUE
SEQADV 2DEB MSE A 548 UNP P18886 MET 548 MODIFIED RESIDUE
SEQADV 2DEB MSE A 582 UNP P18886 MET 582 MODIFIED RESIDUE
SEQADV 2DEB MET B 6 UNP P18886 EXPRESSION TAG
SEQADV 2DEB GLY B 7 UNP P18886 EXPRESSION TAG
SEQADV 2DEB SER B 8 UNP P18886 EXPRESSION TAG
SEQADV 2DEB SER B 9 UNP P18886 EXPRESSION TAG
SEQADV 2DEB HIS B 10 UNP P18886 EXPRESSION TAG
SEQADV 2DEB HIS B 11 UNP P18886 EXPRESSION TAG
SEQADV 2DEB HIS B 12 UNP P18886 EXPRESSION TAG
SEQADV 2DEB HIS B 13 UNP P18886 EXPRESSION TAG
SEQADV 2DEB HIS B 14 UNP P18886 EXPRESSION TAG
SEQADV 2DEB HIS B 15 UNP P18886 EXPRESSION TAG
SEQADV 2DEB SER B 16 UNP P18886 EXPRESSION TAG
SEQADV 2DEB SER B 17 UNP P18886 EXPRESSION TAG
SEQADV 2DEB GLY B 18 UNP P18886 EXPRESSION TAG
SEQADV 2DEB LEU B 19 UNP P18886 EXPRESSION TAG
SEQADV 2DEB VAL B 20 UNP P18886 EXPRESSION TAG
SEQADV 2DEB PRO B 21 UNP P18886 EXPRESSION TAG
SEQADV 2DEB ARG B 22 UNP P18886 EXPRESSION TAG
SEQADV 2DEB GLY B 23 UNP P18886 EXPRESSION TAG
SEQADV 2DEB SER B 24 UNP P18886 EXPRESSION TAG
SEQADV 2DEB HIS B 25 UNP P18886 EXPRESSION TAG
SEQADV 2DEB MET B 26 UNP P18886 EXPRESSION TAG
SEQADV 2DEB MSE B 43 UNP P18886 MET 43 MODIFIED RESIDUE
SEQADV 2DEB MSE B 61 UNP P18886 MET 61 MODIFIED RESIDUE
SEQADV 2DEB MSE B 119 UNP P18886 MET 119 MODIFIED RESIDUE
SEQADV 2DEB MSE B 135 UNP P18886 MET 135 MODIFIED RESIDUE
SEQADV 2DEB MSE B 214 UNP P18886 MET 214 MODIFIED RESIDUE
SEQADV 2DEB MSE B 332 UNP P18886 MET 332 MODIFIED RESIDUE
SEQADV 2DEB MSE B 342 UNP P18886 MET 342 MODIFIED RESIDUE
SEQADV 2DEB MSE B 473 UNP P18886 MET 473 MODIFIED RESIDUE
SEQADV 2DEB MSE B 531 UNP P18886 MET 531 MODIFIED RESIDUE
SEQADV 2DEB MSE B 532 UNP P18886 MET 532 MODIFIED RESIDUE
SEQADV 2DEB MSE B 548 UNP P18886 MET 548 MODIFIED RESIDUE
SEQADV 2DEB MSE B 582 UNP P18886 MET 582 MODIFIED RESIDUE
SEQRES 1 A 653 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 653 LEU VAL PRO ARG GLY SER HIS MET ALA VAL SER GLY PRO
SEQRES 3 A 653 ASP ASP TYR LEU GLN HIS SER ILE VAL PRO THR MSE HIS
SEQRES 4 A 653 TYR GLN ASP SER LEU PRO ARG LEU PRO ILE PRO LYS LEU
SEQRES 5 A 653 GLU ASP THR MSE LYS ARG TYR LEU ASN ALA GLN LYS PRO
SEQRES 6 A 653 LEU LEU ASP ASP SER GLN PHE ARG ARG THR GLU ALA LEU
SEQRES 7 A 653 CYS LYS ASN PHE GLU THR GLY VAL GLY LYS GLU LEU HIS
SEQRES 8 A 653 ALA HIS LEU LEU ALA GLN ASP LYS GLN ASN LYS HIS THR
SEQRES 9 A 653 SER TYR ILE SER GLY PRO TRP PHE ASP MSE TYR LEU THR
SEQRES 10 A 653 ALA ARG ASP SER ILE VAL LEU ASN PHE ASN PRO PHE MSE
SEQRES 11 A 653 ALA PHE ASN PRO ASP PRO LYS SER GLU TYR ASN ASP GLN
SEQRES 12 A 653 LEU THR ARG ALA THR ASN LEU THR VAL SER ALA VAL ARG
SEQRES 13 A 653 PHE LEU LYS THR LEU GLN ALA GLY LEU LEU GLU PRO GLU
SEQRES 14 A 653 VAL PHE HIS LEU ASN PRO SER LYS SER ASP THR ASP ALA
SEQRES 15 A 653 PHE LYS ARG LEU ILE ARG PHE VAL PRO PRO SER LEU SER
SEQRES 16 A 653 TRP TYR GLY ALA TYR LEU VAL ASN ALA TYR PRO LEU ASP
SEQRES 17 A 653 MSE SER GLN TYR PHE ARG LEU PHE ASN SER THR ARG ILE
SEQRES 18 A 653 PRO ARG PRO ASN ARG ASP GLU LEU PHE THR ASP THR LYS
SEQRES 19 A 653 ALA ARG HIS LEU LEU VAL LEU ARG LYS GLY HIS PHE TYR
SEQRES 20 A 653 VAL PHE ASP VAL LEU ASP GLN ASP GLY ASN ILE VAL ASN
SEQRES 21 A 653 PRO LEU GLU ILE GLN ALA HIS LEU LYS TYR ILE LEU SER
SEQRES 22 A 653 ASP SER SER PRO VAL PRO GLU PHE PRO VAL ALA TYR LEU
SEQRES 23 A 653 THR SER GLU ASN ARG ASP VAL TRP ALA GLU LEU ARG GLN
SEQRES 24 A 653 LYS LEU ILE PHE ASP GLY ASN GLU GLU THR LEU LYS LYS
SEQRES 25 A 653 VAL ASP SER ALA VAL PHE CYS LEU CYS LEU ASP ASP PHE
SEQRES 26 A 653 PRO MSE LYS ASP LEU ILE HIS LEU SER HIS THR MSE LEU
SEQRES 27 A 653 HIS GLY ASP GLY THR ASN ARG TRP PHE ASP LYS SER PHE
SEQRES 28 A 653 ASN LEU ILE VAL ALA GLU ASP GLY THR ALA ALA VAL HIS
SEQRES 29 A 653 PHE GLU HIS SER TRP GLY ASP GLY VAL ALA VAL LEU ARG
SEQRES 30 A 653 PHE PHE ASN GLU VAL PHE ARG ASP SER THR GLN THR PRO
SEQRES 31 A 653 ALA ILE THR PRO GLN SER GLN PRO ALA ALA THR ASN SER
SEQRES 32 A 653 SER ALA SER VAL GLU THR LEU SER PHE ASN LEU SER GLY
SEQRES 33 A 653 ALA LEU LYS ALA GLY ILE THR ALA ALA LYS GLU LYS PHE
SEQRES 34 A 653 ASP THR THR VAL LYS THR LEU SER ILE ASP SER ILE GLN
SEQRES 35 A 653 PHE GLN ARG GLY GLY LYS GLU PHE LEU LYS LYS LYS GLN
SEQRES 36 A 653 LEU SER PRO ASP ALA VAL ALA GLN LEU ALA PHE GLN MSE
SEQRES 37 A 653 ALA PHE LEU ARG GLN TYR GLY GLN THR VAL ALA THR TYR
SEQRES 38 A 653 GLU SER CYS SER THR ALA ALA PHE LYS HIS GLY ARG THR
SEQRES 39 A 653 GLU THR ILE ARG PRO ALA SER ILE PHE THR LYS ARG CYS
SEQRES 40 A 653 SER GLU ALA PHE VAL ARG ASP PRO SER LYS HIS SER VAL
SEQRES 41 A 653 GLY GLU LEU GLN HIS MSE MSE ALA GLU CYS SER LYS TYR
SEQRES 42 A 653 HIS GLY GLN LEU THR LYS GLU ALA ALA MSE GLY GLN GLY
SEQRES 43 A 653 PHE ASP ARG HIS LEU TYR ALA LEU ARG TYR LEU ALA THR
SEQRES 44 A 653 ALA ARG GLY LEU ASN LEU PRO GLU LEU TYR LEU ASP PRO
SEQRES 45 A 653 ALA TYR GLN GLN MSE ASN HIS ASN ILE LEU SER THR SER
SEQRES 46 A 653 THR LEU ASN SER PRO ALA VAL SER LEU GLY GLY PHE ALA
SEQRES 47 A 653 PRO VAL VAL PRO ASP GLY PHE GLY ILE ALA TYR ALA VAL
SEQRES 48 A 653 HIS ASP ASP TRP ILE GLY CYS ASN VAL SER SER TYR SER
SEQRES 49 A 653 GLY ARG ASN ALA ARG GLU PHE LEU HIS CYS VAL GLN LYS
SEQRES 50 A 653 CYS LEU GLU ASP ILE PHE ASP ALA LEU GLU GLY LYS ALA
SEQRES 51 A 653 ILE LYS THR
SEQRES 1 B 653 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 653 LEU VAL PRO ARG GLY SER HIS MET ALA VAL SER GLY PRO
SEQRES 3 B 653 ASP ASP TYR LEU GLN HIS SER ILE VAL PRO THR MSE HIS
SEQRES 4 B 653 TYR GLN ASP SER LEU PRO ARG LEU PRO ILE PRO LYS LEU
SEQRES 5 B 653 GLU ASP THR MSE LYS ARG TYR LEU ASN ALA GLN LYS PRO
SEQRES 6 B 653 LEU LEU ASP ASP SER GLN PHE ARG ARG THR GLU ALA LEU
SEQRES 7 B 653 CYS LYS ASN PHE GLU THR GLY VAL GLY LYS GLU LEU HIS
SEQRES 8 B 653 ALA HIS LEU LEU ALA GLN ASP LYS GLN ASN LYS HIS THR
SEQRES 9 B 653 SER TYR ILE SER GLY PRO TRP PHE ASP MSE TYR LEU THR
SEQRES 10 B 653 ALA ARG ASP SER ILE VAL LEU ASN PHE ASN PRO PHE MSE
SEQRES 11 B 653 ALA PHE ASN PRO ASP PRO LYS SER GLU TYR ASN ASP GLN
SEQRES 12 B 653 LEU THR ARG ALA THR ASN LEU THR VAL SER ALA VAL ARG
SEQRES 13 B 653 PHE LEU LYS THR LEU GLN ALA GLY LEU LEU GLU PRO GLU
SEQRES 14 B 653 VAL PHE HIS LEU ASN PRO SER LYS SER ASP THR ASP ALA
SEQRES 15 B 653 PHE LYS ARG LEU ILE ARG PHE VAL PRO PRO SER LEU SER
SEQRES 16 B 653 TRP TYR GLY ALA TYR LEU VAL ASN ALA TYR PRO LEU ASP
SEQRES 17 B 653 MSE SER GLN TYR PHE ARG LEU PHE ASN SER THR ARG ILE
SEQRES 18 B 653 PRO ARG PRO ASN ARG ASP GLU LEU PHE THR ASP THR LYS
SEQRES 19 B 653 ALA ARG HIS LEU LEU VAL LEU ARG LYS GLY HIS PHE TYR
SEQRES 20 B 653 VAL PHE ASP VAL LEU ASP GLN ASP GLY ASN ILE VAL ASN
SEQRES 21 B 653 PRO LEU GLU ILE GLN ALA HIS LEU LYS TYR ILE LEU SER
SEQRES 22 B 653 ASP SER SER PRO VAL PRO GLU PHE PRO VAL ALA TYR LEU
SEQRES 23 B 653 THR SER GLU ASN ARG ASP VAL TRP ALA GLU LEU ARG GLN
SEQRES 24 B 653 LYS LEU ILE PHE ASP GLY ASN GLU GLU THR LEU LYS LYS
SEQRES 25 B 653 VAL ASP SER ALA VAL PHE CYS LEU CYS LEU ASP ASP PHE
SEQRES 26 B 653 PRO MSE LYS ASP LEU ILE HIS LEU SER HIS THR MSE LEU
SEQRES 27 B 653 HIS GLY ASP GLY THR ASN ARG TRP PHE ASP LYS SER PHE
SEQRES 28 B 653 ASN LEU ILE VAL ALA GLU ASP GLY THR ALA ALA VAL HIS
SEQRES 29 B 653 PHE GLU HIS SER TRP GLY ASP GLY VAL ALA VAL LEU ARG
SEQRES 30 B 653 PHE PHE ASN GLU VAL PHE ARG ASP SER THR GLN THR PRO
SEQRES 31 B 653 ALA ILE THR PRO GLN SER GLN PRO ALA ALA THR ASN SER
SEQRES 32 B 653 SER ALA SER VAL GLU THR LEU SER PHE ASN LEU SER GLY
SEQRES 33 B 653 ALA LEU LYS ALA GLY ILE THR ALA ALA LYS GLU LYS PHE
SEQRES 34 B 653 ASP THR THR VAL LYS THR LEU SER ILE ASP SER ILE GLN
SEQRES 35 B 653 PHE GLN ARG GLY GLY LYS GLU PHE LEU LYS LYS LYS GLN
SEQRES 36 B 653 LEU SER PRO ASP ALA VAL ALA GLN LEU ALA PHE GLN MSE
SEQRES 37 B 653 ALA PHE LEU ARG GLN TYR GLY GLN THR VAL ALA THR TYR
SEQRES 38 B 653 GLU SER CYS SER THR ALA ALA PHE LYS HIS GLY ARG THR
SEQRES 39 B 653 GLU THR ILE ARG PRO ALA SER ILE PHE THR LYS ARG CYS
SEQRES 40 B 653 SER GLU ALA PHE VAL ARG ASP PRO SER LYS HIS SER VAL
SEQRES 41 B 653 GLY GLU LEU GLN HIS MSE MSE ALA GLU CYS SER LYS TYR
SEQRES 42 B 653 HIS GLY GLN LEU THR LYS GLU ALA ALA MSE GLY GLN GLY
SEQRES 43 B 653 PHE ASP ARG HIS LEU TYR ALA LEU ARG TYR LEU ALA THR
SEQRES 44 B 653 ALA ARG GLY LEU ASN LEU PRO GLU LEU TYR LEU ASP PRO
SEQRES 45 B 653 ALA TYR GLN GLN MSE ASN HIS ASN ILE LEU SER THR SER
SEQRES 46 B 653 THR LEU ASN SER PRO ALA VAL SER LEU GLY GLY PHE ALA
SEQRES 47 B 653 PRO VAL VAL PRO ASP GLY PHE GLY ILE ALA TYR ALA VAL
SEQRES 48 B 653 HIS ASP ASP TRP ILE GLY CYS ASN VAL SER SER TYR SER
SEQRES 49 B 653 GLY ARG ASN ALA ARG GLU PHE LEU HIS CYS VAL GLN LYS
SEQRES 50 B 653 CYS LEU GLU ASP ILE PHE ASP ALA LEU GLU GLY LYS ALA
SEQRES 51 B 653 ILE LYS THR
MODRES 2DEB MSE A 43 MET SELENOMETHIONINE
MODRES 2DEB MSE A 61 MET SELENOMETHIONINE
MODRES 2DEB MSE A 119 MET SELENOMETHIONINE
MODRES 2DEB MSE A 135 MET SELENOMETHIONINE
MODRES 2DEB MSE A 214 MET SELENOMETHIONINE
MODRES 2DEB MSE A 332 MET SELENOMETHIONINE
MODRES 2DEB MSE A 342 MET SELENOMETHIONINE
MODRES 2DEB MSE A 473 MET SELENOMETHIONINE
MODRES 2DEB MSE A 531 MET SELENOMETHIONINE
MODRES 2DEB MSE A 532 MET SELENOMETHIONINE
MODRES 2DEB MSE A 548 MET SELENOMETHIONINE
MODRES 2DEB MSE A 582 MET SELENOMETHIONINE
MODRES 2DEB MSE B 43 MET SELENOMETHIONINE
MODRES 2DEB MSE B 61 MET SELENOMETHIONINE
MODRES 2DEB MSE B 119 MET SELENOMETHIONINE
MODRES 2DEB MSE B 135 MET SELENOMETHIONINE
MODRES 2DEB MSE B 214 MET SELENOMETHIONINE
MODRES 2DEB MSE B 332 MET SELENOMETHIONINE
MODRES 2DEB MSE B 342 MET SELENOMETHIONINE
MODRES 2DEB MSE B 473 MET SELENOMETHIONINE
MODRES 2DEB MSE B 531 MET SELENOMETHIONINE
MODRES 2DEB MSE B 532 MET SELENOMETHIONINE
MODRES 2DEB MSE B 548 MET SELENOMETHIONINE
MODRES 2DEB MSE B 582 MET SELENOMETHIONINE
HET MSE A 43 8
HET MSE A 61 8
HET MSE A 119 8
HET MSE A 135 8
HET MSE A 214 8
HET MSE A 332 8
HET MSE A 342 8
HET MSE A 473 8
HET MSE A 531 8
HET MSE A 532 8
HET MSE A 548 8
HET MSE A 582 8
HET MSE B 43 8
HET MSE B 61 8
HET MSE B 119 8
HET MSE B 135 8
HET MSE B 214 8
HET MSE B 332 8
HET MSE B 342 8
HET MSE B 473 8
HET MSE B 531 8
HET MSE B 532 8
HET MSE B 548 8
HET MSE B 582 8
HET COA A2350 31
HET PLM A2351 16
HET BOG B1736 20
HET COA B2360 27
HET PLM B1600 16
HETNAM MSE SELENOMETHIONINE
HETNAM COA COENZYME A
HETNAM PLM PALMITIC ACID
HETNAM BOG OCTYL BETA-D-GLUCOPYRANOSIDE
FORMUL 1 MSE 24(C5 H11 N O2 SE)
FORMUL 3 COA 2(C21 H36 N7 O16 P3 S)
FORMUL 4 PLM 2(C16 H32 O2)
FORMUL 5 BOG C14 H28 O6
FORMUL 8 HOH *1364(H2 O)
HELIX 1 1 TYR A 45 LEU A 49 5 5
HELIX 2 2 LYS A 56 LYS A 69 1 14
HELIX 3 3 ASP A 73 GLY A 90 1 18
HELIX 4 4 GLY A 90 ASN A 106 1 17
HELIX 5 5 ILE A 112 ALA A 123 1 12
HELIX 6 6 LYS A 142 ASN A 146 5 5
HELIX 7 7 ASP A 147 ALA A 168 1 22
HELIX 8 8 ASN A 179 ASP A 184 1 6
HELIX 9 9 THR A 185 ARG A 193 1 9
HELIX 10 10 LEU A 199 VAL A 207 1 9
HELIX 11 11 GLN A 216 PHE A 221 5 6
HELIX 12 12 ASN A 265 ASP A 279 1 15
HELIX 13 13 PRO A 287 GLU A 294 5 8
HELIX 14 14 ASN A 295 ASP A 309 1 15
HELIX 15 15 ASN A 311 ALA A 321 1 11
HELIX 16 16 ASP A 334 HIS A 344 1 11
HELIX 17 17 GLY A 377 THR A 394 1 18
HELIX 18 18 ASN A 407 VAL A 412 1 6
HELIX 19 19 SER A 420 LYS A 439 1 20
HELIX 20 20 GLY A 452 LYS A 459 1 8
HELIX 21 21 SER A 462 GLY A 480 1 19
HELIX 22 22 SER A 506 ARG A 518 1 13
HELIX 23 23 ASP A 519 HIS A 523 5 5
HELIX 24 24 SER A 524 MSE A 548 1 25
HELIX 25 25 PHE A 552 ARG A 566 1 15
HELIX 26 26 PRO A 571 LEU A 575 5 5
HELIX 27 27 ASP A 576 ASN A 583 1 8
HELIX 28 28 ASN A 632 GLU A 652 1 21
HELIX 29 29 TYR B 45 LEU B 49 5 5
HELIX 30 30 LYS B 56 LYS B 69 1 14
HELIX 31 31 ASP B 73 GLY B 90 1 18
HELIX 32 32 GLY B 90 GLN B 105 1 16
HELIX 33 33 ILE B 112 ALA B 123 1 12
HELIX 34 34 LYS B 142 ASN B 146 5 5
HELIX 35 35 ASP B 147 ALA B 168 1 22
HELIX 36 36 ASN B 179 ASP B 184 1 6
HELIX 37 37 THR B 185 ARG B 193 1 9
HELIX 38 38 LEU B 199 LEU B 206 1 8
HELIX 39 39 GLN B 216 PHE B 221 5 6
HELIX 40 40 ASN B 265 ASP B 279 1 15
HELIX 41 41 PRO B 287 GLU B 294 5 8
HELIX 42 42 ASN B 295 ASP B 309 1 15
HELIX 43 43 ASN B 311 ALA B 321 1 11
HELIX 44 44 ASP B 334 HIS B 344 1 11
HELIX 45 45 GLY B 377 THR B 394 1 18
HELIX 46 46 ASN B 407 VAL B 412 1 6
HELIX 47 47 SER B 420 THR B 440 1 21
HELIX 48 48 GLY B 452 LYS B 459 1 8
HELIX 49 49 SER B 462 GLY B 480 1 19
HELIX 50 50 SER B 506 ARG B 518 1 13
HELIX 51 51 ASP B 519 HIS B 523 5 5
HELIX 52 52 SER B 524 MSE B 548 1 25
HELIX 53 53 PHE B 552 ARG B 566 1 15
HELIX 54 54 PRO B 571 LEU B 575 5 5
HELIX 55 55 ASP B 576 ASN B 583 1 8
HELIX 56 56 ASN B 632 GLU B 652 1 21
SHEET 1 A 8 GLU A 413 THR A 414 0
SHEET 2 A 8 HIS A 250 ASP A 255 -1 N VAL A 253 O GLU A 413
SHEET 3 A 8 HIS A 242 ARG A 247 -1 N LEU A 243 O PHE A 254
SHEET 4 A 8 CYS A 324 LEU A 327 1 O LEU A 325 N LEU A 244
SHEET 5 A 8 PHE A 356 VAL A 360 1 O LEU A 358 N CYS A 326
SHEET 6 A 8 ALA A 366 PHE A 370 -1 O HIS A 369 N ASN A 357
SHEET 7 A 8 PHE A 134 PHE A 137 -1 N MSE A 135 O VAL A 368
SHEET 8 A 8 VAL A 597 GLY A 601 -1 O LEU A 599 N ALA A 136
SHEET 1 B 2 VAL A 175 HIS A 177 0
SHEET 2 B 2 ALA A 209 PRO A 211 -1 O TYR A 210 N PHE A 176
SHEET 1 C 2 SER A 223 ILE A 226 0
SHEET 2 C 2 GLU A 233 THR A 236 -1 O GLU A 233 N ILE A 226
SHEET 1 D 6 SER A 442 PHE A 448 0
SHEET 2 D 6 ILE A 621 SER A 627 -1 O ILE A 621 N PHE A 448
SHEET 3 D 6 PHE A 610 VAL A 616 -1 N ALA A 613 O ASN A 624
SHEET 4 D 6 LEU A 587 THR A 591 1 N SER A 588 O ILE A 612
SHEET 5 D 6 THR A 485 SER A 490 1 N TYR A 486 O LEU A 587
SHEET 6 D 6 THR A 499 ILE A 502 -1 O ILE A 502 N GLU A 487
SHEET 1 E 8 GLU B 413 THR B 414 0
SHEET 2 E 8 HIS B 250 ASP B 255 -1 N VAL B 253 O GLU B 413
SHEET 3 E 8 HIS B 242 ARG B 247 -1 N LEU B 243 O PHE B 254
SHEET 4 E 8 CYS B 324 LEU B 327 1 O LEU B 325 N LEU B 244
SHEET 5 E 8 PHE B 356 VAL B 360 1 O LEU B 358 N CYS B 326
SHEET 6 E 8 ALA B 366 PHE B 370 -1 O HIS B 369 N ASN B 357
SHEET 7 E 8 PHE B 134 PHE B 137 -1 N MSE B 135 O VAL B 368
SHEET 8 E 8 VAL B 597 GLY B 601 -1 O LEU B 599 N ALA B 136
SHEET 1 F 2 VAL B 175 HIS B 177 0
SHEET 2 F 2 ALA B 209 PRO B 211 -1 O TYR B 210 N PHE B 176
SHEET 1 G 2 SER B 223 ILE B 226 0
SHEET 2 G 2 GLU B 233 THR B 236 -1 O GLU B 233 N ILE B 226
SHEET 1 H 6 SER B 442 PHE B 448 0
SHEET 2 H 6 ILE B 621 SER B 627 -1 O ILE B 621 N PHE B 448
SHEET 3 H 6 PHE B 610 VAL B 616 -1 N ALA B 613 O ASN B 624
SHEET 4 H 6 LEU B 587 THR B 591 1 N SER B 588 O ILE B 612
SHEET 5 H 6 THR B 485 SER B 490 1 N TYR B 486 O LEU B 587
SHEET 6 H 6 THR B 499 ILE B 502 -1 O ILE B 502 N GLU B 487
LINK C THR A 42 N MSE A 43 1555 1555 1.34
LINK C MSE A 43 N HIS A 44 1555 1555 1.33
LINK C THR A 60 N MSE A 61 1555 1555 1.33
LINK C MSE A 61 N LYS A 62 1555 1555 1.33
LINK C ASP A 118 N MSE A 119 1555 1555 1.32
LINK C MSE A 119 N TYR A 120 1555 1555 1.33
LINK C PHE A 134 N MSE A 135 1555 1555 1.33
LINK C MSE A 135 N ALA A 136 1555 1555 1.33
LINK C ASP A 213 N MSE A 214 1555 1555 1.33
LINK C MSE A 214 N SER A 215 1555 1555 1.33
LINK C PRO A 331 N MSE A 332 1555 1555 1.33
LINK C MSE A 332 N LYS A 333 1555 1555 1.32
LINK C THR A 341 N MSE A 342 1555 1555 1.34
LINK C MSE A 342 N LEU A 343 1555 1555 1.33
LINK C GLN A 472 N MSE A 473 1555 1555 1.32
LINK C MSE A 473 N ALA A 474 1555 1555 1.33
LINK C HIS A 530 N MSE A 531 1555 1555 1.33
LINK C MSE A 531 N MSE A 532 1555 1555 1.33
LINK C MSE A 532 N ALA A 533 1555 1555 1.34
LINK C ALA A 547 N MSE A 548 1555 1555 1.33
LINK C MSE A 548 N GLY A 549 1555 1555 1.33
LINK C GLN A 581 N MSE A 582 1555 1555 1.33
LINK C MSE A 582 N ASN A 583 1555 1555 1.33
LINK C THR B 42 N MSE B 43 1555 1555 1.33
LINK C MSE B 43 N HIS B 44 1555 1555 1.33
LINK C THR B 60 N MSE B 61 1555 1555 1.32
LINK C MSE B 61 N LYS B 62 1555 1555 1.33
LINK C ASP B 118 N MSE B 119 1555 1555 1.32
LINK C MSE B 119 N TYR B 120 1555 1555 1.33
LINK C PHE B 134 N MSE B 135 1555 1555 1.33
LINK C MSE B 135 N ALA B 136 1555 1555 1.33
LINK C ASP B 213 N MSE B 214 1555 1555 1.33
LINK C MSE B 214 N SER B 215 1555 1555 1.33
LINK C PRO B 331 N MSE B 332 1555 1555 1.33
LINK C MSE B 332 N LYS B 333 1555 1555 1.32
LINK C THR B 341 N MSE B 342 1555 1555 1.32
LINK C MSE B 342 N LEU B 343 1555 1555 1.32
LINK C GLN B 472 N MSE B 473 1555 1555 1.33
LINK C MSE B 473 N ALA B 474 1555 1555 1.33
LINK C HIS B 530 N MSE B 531 1555 1555 1.33
LINK C MSE B 531 N MSE B 532 1555 1555 1.33
LINK C MSE B 532 N ALA B 533 1555 1555 1.33
LINK C ALA B 547 N MSE B 548 1555 1555 1.33
LINK C MSE B 548 N GLY B 549 1555 1555 1.33
LINK C GLN B 581 N MSE B 582 1555 1555 1.33
LINK C MSE B 582 N ASN B 583 1555 1555 1.33
CRYST1 95.180 97.290 310.440 90.00 90.00 90.00 C 2 2 21 16
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 0.010506 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010279 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003221 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
