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HEADER TRANSFERASE 14-MAY-07 2PX6
TITLE CRYSTAL STRUCTURE OF THE THIOESTERASE DOMAIN OF HUMAN FATTY
TITLE 2 ACID SYNTHASE INHIBITED BY ORLISTAT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THIOESTERASE DOMAIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 2200-2511;
COMPND 5 EC: 2.3.1.85;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 GENE: FAS;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: C41(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS THIOESATERSE DOMAIN, ORLISTAT, FATTY ACID SYNTHASE, DRUG
KEYWDS 2 COMPLEX, TETRAHYDROLIPSTATIN
EXPDTA X-RAY DIFFRACTION
AUTHOR C.W.PEMBLE IV,L.C.JOHNSON,S.J.KRIDEL,T.W.LOWTHER
REVDAT 1 10-JUL-07 2PX6 0
JRNL AUTH C.W.PEMBLE IV,L.C.JOHNSON,S.J.KRIDEL,T.W.LOWTHER
JRNL TITL CRYSTAL STRUCTURE OF THE THIOESTERASE DOMAIN OF
JRNL TITL 2 HUMAN FATTY ACID SYNTHASE INHIBITED BY ORLISTAT
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.01
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 3 NUMBER OF REFLECTIONS : 21850
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) : 0.228
REMARK 3 R VALUE (WORKING SET) : 0.225
REMARK 3 FREE R VALUE : 0.273
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1184
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1207
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 73.01
REMARK 3 BIN R VALUE (WORKING SET) : 0.2310
REMARK 3 BIN FREE R VALUE SET COUNT : 70
REMARK 3 BIN FREE R VALUE : 0.3740
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 4143
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.96
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.01000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.474
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.282
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.196
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.796
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.927
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.900
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4176 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5641 ; 1.273 ; 1.984
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 507 ; 5.557 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 185 ;35.008 ;23.622
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 673 ;17.322 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 27 ;19.884 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 640 ; 0.084 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3123 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1914 ; 0.205 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2844 ; 0.303 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 169 ; 0.166 ; 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): 63 ; 0.202 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 5 ; 0.120 ; 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): 2646 ; 0.661 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4123 ; 1.093 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1707 ; 1.475 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1518 ; 2.370 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 0
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 0
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 2PX6 COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006
REMARK 4
REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY.
REMARK 4 REMEDIATED DATA FILE REVISION 3.100 (2007-07-02)
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE RCSB ID CODE IS RCSB042877.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 4.30
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X12C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200 DATA SCALING SOFTWARE : D*TREK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21850
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 39.010
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 76.2
REMARK 200 DATA REDUNDANCY IN SHELL : 6.20
REMARK 200 R MERGE FOR SHELL (I) : 0.23000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 6.200
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: PDB ENTRY 1XKT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM SODIUM DIHYDROGEN PHOSPHATE,
REMARK 280 30-35% PEG 3350, 30MM DITHIOTHREITOL, PH 4.3, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,1/2+Y,-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 47.16000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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 BIOMOLECULE: 2
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 GLY A 2196
REMARK 465 SER A 2197
REMARK 465 HIS A 2198
REMARK 465 ASN A 2199
REMARK 465 LEU A 2200
REMARK 465 ALA A 2201
REMARK 465 CYS A 2202
REMARK 465 PRO A 2203
REMARK 465 THR A 2204
REMARK 465 PRO A 2205
REMARK 465 LYS A 2206
REMARK 465 GLU A 2207
REMARK 465 ASP A 2208
REMARK 465 GLY A 2209
REMARK 465 LEU A 2210
REMARK 465 ALA A 2211
REMARK 465 GLN A 2212
REMARK 465 GLN A 2213
REMARK 465 GLN A 2214
REMARK 465 THR A 2215
REMARK 465 GLN A 2216
REMARK 465 LEU A 2217
REMARK 465 ASN A 2218
REMARK 465 LEU A 2219
REMARK 465 ARG A 2220
REMARK 465 SER A 2326
REMARK 465 PRO A 2327
REMARK 465 ALA A 2328
REMARK 465 VAL A 2344
REMARK 465 LEU A 2345
REMARK 465 ALA A 2346
REMARK 465 TYR A 2347
REMARK 465 THR A 2348
REMARK 465 GLN A 2349
REMARK 465 SER A 2350
REMARK 465 TYR A 2351
REMARK 465 ARG A 2352
REMARK 465 ALA A 2353
REMARK 465 LYS A 2354
REMARK 465 LEU A 2355
REMARK 465 THR A 2356
REMARK 465 PRO A 2357
REMARK 465 GLY A 2358
REMARK 465 CYS A 2359
REMARK 465 GLU A 2360
REMARK 465 GLY A 2451
REMARK 465 GLY A 2452
REMARK 465 ALA A 2453
REMARK 465 TYR A 2454
REMARK 465 GLY A 2455
REMARK 465 GLU A 2456
REMARK 465 ASP A 2457
REMARK 465 LEU A 2458
REMARK 465 ALA A 2502
REMARK 465 GLU A 2503
REMARK 465 PRO A 2504
REMARK 465 ARG A 2505
REMARK 465 VAL A 2506
REMARK 465 SER A 2507
REMARK 465 VAL A 2508
REMARK 465 ARG A 2509
REMARK 465 GLU A 2510
REMARK 465 GLY A 2511
REMARK 465 GLY B 2196
REMARK 465 SER B 2197
REMARK 465 HIS B 2198
REMARK 465 ASN B 2199
REMARK 465 LEU B 2200
REMARK 465 ALA B 2201
REMARK 465 CYS B 2202
REMARK 465 PRO B 2203
REMARK 465 THR B 2204
REMARK 465 PRO B 2205
REMARK 465 LYS B 2206
REMARK 465 GLU B 2207
REMARK 465 ASP B 2208
REMARK 465 GLY B 2209
REMARK 465 LEU B 2210
REMARK 465 ALA B 2211
REMARK 465 GLN B 2212
REMARK 465 GLN B 2213
REMARK 465 GLN B 2214
REMARK 465 THR B 2215
REMARK 465 GLN B 2216
REMARK 465 LEU B 2217
REMARK 465 ASN B 2218
REMARK 465 LEU B 2219
REMARK 465 ARG B 2220
REMARK 465 VAL B 2344
REMARK 465 LEU B 2345
REMARK 465 ALA B 2346
REMARK 465 TYR B 2347
REMARK 465 THR B 2348
REMARK 465 GLN B 2349
REMARK 465 SER B 2350
REMARK 465 TYR B 2351
REMARK 465 ARG B 2352
REMARK 465 ALA B 2353
REMARK 465 LYS B 2354
REMARK 465 LEU B 2355
REMARK 465 THR B 2356
REMARK 465 PRO B 2357
REMARK 465 GLY B 2358
REMARK 465 CYS B 2359
REMARK 465 ALA B 2453
REMARK 465 TYR B 2454
REMARK 465 GLY B 2455
REMARK 465 GLU B 2456
REMARK 465 ASP B 2457
REMARK 465 LEU B 2458
REMARK 465 GLY B 2459
REMARK 465 ALA B 2460
REMARK 465 VAL B 2508
REMARK 465 ARG B 2509
REMARK 465 GLU B 2510
REMARK 465 GLY B 2511
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
REMARK 500 NH1 ARG A 2428 OD1 ASP B 2291 2.13
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),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 TYR A2439 C HIS A2440 N -0.110
REMARK 500 HIS A2440 C GLY A2441 N -0.392
REMARK 500 HIS B2440 CA HIS B2440 CB -0.186
REMARK 500 HIS B2440 CA HIS B2440 C -0.148
REMARK 500 HIS B2440 C HIS B2440 O -0.163
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 TYR A2307 CA - C - N ANGL. DEV. = 17.4 DEGREES
REMARK 500 TYR A2307 O - C - N ANGL. DEV. =-17.8 DEGREES
REMARK 500 SER A2308 C - N - CA ANGL. DEV. = 26.2 DEGREES
REMARK 500 SER A2308 CA - C - N ANGL. DEV. = 11.1 DEGREES
REMARK 500 SER A2308 O - C - N ANGL. DEV. =-12.1 DEGREES
REMARK 500 HIS A2440 CA - C - N ANGL. DEV. = 8.5 DEGREES
REMARK 500 HIS A2440 O - C - N ANGL. DEV. = -9.0 DEGREES
REMARK 500 LEU B2260 CA - CB - CG ANGL. DEV. = 9.7 DEGREES
REMARK 500 HIS B2440 N - CA - C ANGL. DEV. = 13.0 DEGREES
REMARK 500 GLY B2441 C - N - CA ANGL. DEV. = 8.5 DEGREES
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 M RES CSSEQI PSI PHI
REMARK 500 SER A2308 -94.32 60.89
REMARK 500 SER B2308 -111.26 60.78
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 DH9 3000 FORMS AN ADDUCT WITH SER 2308 AND IS MISSING
REMARK 600 THE O2* ATOM
DBREF 2PX6 A 2200 2511 UNP P49327 FAS_HUMAN 2200 2511
DBREF 2PX6 B 2200 2511 UNP P49327 FAS_HUMAN 2200 2511
SEQADV 2PX6 GLY A 2196 UNP P49327 CLONING ARTIFACT
SEQADV 2PX6 SER A 2197 UNP P49327 CLONING ARTIFACT
SEQADV 2PX6 HIS A 2198 UNP P49327 CLONING ARTIFACT
SEQADV 2PX6 ASN A 2199 UNP P49327 CLONING ARTIFACT
SEQADV 2PX6 GLY B 2196 UNP P49327 CLONING ARTIFACT
SEQADV 2PX6 SER B 2197 UNP P49327 CLONING ARTIFACT
SEQADV 2PX6 HIS B 2198 UNP P49327 CLONING ARTIFACT
SEQADV 2PX6 ASN B 2199 UNP P49327 CLONING ARTIFACT
SEQRES 1 A 316 GLY SER HIS ASN LEU ALA CYS PRO THR PRO LYS GLU ASP
SEQRES 2 A 316 GLY LEU ALA GLN GLN GLN THR GLN LEU ASN LEU ARG SER
SEQRES 3 A 316 LEU LEU VAL ASN PRO GLU GLY PRO THR LEU MET ARG LEU
SEQRES 4 A 316 ASN SER VAL GLN SER SER GLU ARG PRO LEU PHE LEU VAL
SEQRES 5 A 316 HIS PRO ILE GLU GLY SER THR THR VAL PHE HIS SER LEU
SEQRES 6 A 316 ALA SER ARG LEU SER ILE PRO THR TYR GLY LEU GLN CYS
SEQRES 7 A 316 THR ARG ALA ALA PRO LEU ASP SER ILE HIS SER LEU ALA
SEQRES 8 A 316 ALA TYR TYR ILE ASP CYS ILE ARG GLN VAL GLN PRO GLU
SEQRES 9 A 316 GLY PRO TYR ARG VAL ALA GLY TYR SER TYR GLY ALA CYS
SEQRES 10 A 316 VAL ALA PHE GLU MET CYS SER GLN LEU GLN ALA GLN GLN
SEQRES 11 A 316 SER PRO ALA PRO THR HIS ASN SER LEU PHE LEU PHE ASP
SEQRES 12 A 316 GLY SER PRO THR TYR VAL LEU ALA TYR THR GLN SER TYR
SEQRES 13 A 316 ARG ALA LYS LEU THR PRO GLY CYS GLU ALA GLU ALA GLU
SEQRES 14 A 316 THR GLU ALA ILE CYS PHE PHE VAL GLN GLN PHE THR ASP
SEQRES 15 A 316 MET GLU HIS ASN ARG VAL LEU GLU ALA LEU LEU PRO LEU
SEQRES 16 A 316 LYS GLY LEU GLU GLU ARG VAL ALA ALA ALA VAL ASP LEU
SEQRES 17 A 316 ILE ILE LYS SER HIS GLN GLY LEU ASP ARG GLN GLU LEU
SEQRES 18 A 316 SER PHE ALA ALA ARG SER PHE TYR TYR LYS LEU ARG ALA
SEQRES 19 A 316 ALA GLU GLN TYR THR PRO LYS ALA LYS TYR HIS GLY ASN
SEQRES 20 A 316 VAL MET LEU LEU ARG ALA LYS THR GLY GLY ALA TYR GLY
SEQRES 21 A 316 GLU ASP LEU GLY ALA ASP TYR ASN LEU SER GLN VAL CYS
SEQRES 22 A 316 ASP GLY LYS VAL SER VAL HIS VAL ILE GLU GLY ASP HIS
SEQRES 23 A 316 ARG THR LEU LEU GLU GLY SER GLY LEU GLU SER ILE ILE
SEQRES 24 A 316 SER ILE ILE HIS SER SER LEU ALA GLU PRO ARG VAL SER
SEQRES 25 A 316 VAL ARG GLU GLY
SEQRES 1 B 316 GLY SER HIS ASN LEU ALA CYS PRO THR PRO LYS GLU ASP
SEQRES 2 B 316 GLY LEU ALA GLN GLN GLN THR GLN LEU ASN LEU ARG SER
SEQRES 3 B 316 LEU LEU VAL ASN PRO GLU GLY PRO THR LEU MET ARG LEU
SEQRES 4 B 316 ASN SER VAL GLN SER SER GLU ARG PRO LEU PHE LEU VAL
SEQRES 5 B 316 HIS PRO ILE GLU GLY SER THR THR VAL PHE HIS SER LEU
SEQRES 6 B 316 ALA SER ARG LEU SER ILE PRO THR TYR GLY LEU GLN CYS
SEQRES 7 B 316 THR ARG ALA ALA PRO LEU ASP SER ILE HIS SER LEU ALA
SEQRES 8 B 316 ALA TYR TYR ILE ASP CYS ILE ARG GLN VAL GLN PRO GLU
SEQRES 9 B 316 GLY PRO TYR ARG VAL ALA GLY TYR SER TYR GLY ALA CYS
SEQRES 10 B 316 VAL ALA PHE GLU MET CYS SER GLN LEU GLN ALA GLN GLN
SEQRES 11 B 316 SER PRO ALA PRO THR HIS ASN SER LEU PHE LEU PHE ASP
SEQRES 12 B 316 GLY SER PRO THR TYR VAL LEU ALA TYR THR GLN SER TYR
SEQRES 13 B 316 ARG ALA LYS LEU THR PRO GLY CYS GLU ALA GLU ALA GLU
SEQRES 14 B 316 THR GLU ALA ILE CYS PHE PHE VAL GLN GLN PHE THR ASP
SEQRES 15 B 316 MET GLU HIS ASN ARG VAL LEU GLU ALA LEU LEU PRO LEU
SEQRES 16 B 316 LYS GLY LEU GLU GLU ARG VAL ALA ALA ALA VAL ASP LEU
SEQRES 17 B 316 ILE ILE LYS SER HIS GLN GLY LEU ASP ARG GLN GLU LEU
SEQRES 18 B 316 SER PHE ALA ALA ARG SER PHE TYR TYR LYS LEU ARG ALA
SEQRES 19 B 316 ALA GLU GLN TYR THR PRO LYS ALA LYS TYR HIS GLY ASN
SEQRES 20 B 316 VAL MET LEU LEU ARG ALA LYS THR GLY GLY ALA TYR GLY
SEQRES 21 B 316 GLU ASP LEU GLY ALA ASP TYR ASN LEU SER GLN VAL CYS
SEQRES 22 B 316 ASP GLY LYS VAL SER VAL HIS VAL ILE GLU GLY ASP HIS
SEQRES 23 B 316 ARG THR LEU LEU GLU GLY SER GLY LEU GLU SER ILE ILE
SEQRES 24 B 316 SER ILE ILE HIS SER SER LEU ALA GLU PRO ARG VAL SER
SEQRES 25 B 316 VAL ARG GLU GLY
HET DH9 A3000 35
HET DH9 61 36
HET DTT 71 8
HETNAM DH9 (2S,3S,5S)-5-[(N-FORMYL-L-LEUCYL)OXY]-2-HEXYL-3-
HETNAM 2 DH9 HYDROXYHEXADECANOIC ACID
HETNAM DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE
HETSYN DTT 1,4-DITHIOTHREITOL
FORMUL 3 DH9 2(C29 H55 N O6)
FORMUL 5 DTT C4 H10 O2 S2
FORMUL 6 HOH *53(H2 O)
HELIX 1 1 THR A 2254 VAL A 2256 5 3
HELIX 2 2 PHE A 2257 LEU A 2264 1 8
HELIX 3 3 SER A 2281 ARG A 2294 1 14
HELIX 4 4 SER A 2308 GLN A 2325 1 18
HELIX 5 5 ALA A 2361 THR A 2376 1 16
HELIX 6 6 GLU A 2379 LEU A 2388 1 10
HELIX 7 7 GLY A 2392 HIS A 2408 1 17
HELIX 8 8 ASP A 2412 GLN A 2432 1 21
HELIX 9 9 ARG A 2482 LEU A 2485 5 4
HELIX 10 10 GLU A 2486 LEU A 2501 1 16
HELIX 11 11 THR B 2254 VAL B 2256 5 3
HELIX 12 12 PHE B 2257 LEU B 2264 1 8
HELIX 13 13 SER B 2281 ARG B 2294 1 14
HELIX 14 14 SER B 2308 SER B 2326 1 19
HELIX 15 15 GLU B 2360 THR B 2376 1 17
HELIX 16 16 GLU B 2379 LEU B 2388 1 10
HELIX 17 17 GLY B 2392 LYS B 2406 1 15
HELIX 18 18 ASP B 2412 GLN B 2432 1 21
HELIX 19 19 ARG B 2482 LEU B 2485 5 4
HELIX 20 20 GLU B 2486 ALA B 2502 1 17
SHEET 1 A 7 LEU A2231 ARG A2233 0
SHEET 2 A 7 THR A2268 LEU A2271 -1 O GLY A2270 N MET A2232
SHEET 3 A 7 LEU A2244 VAL A2247 1 N LEU A2244 O TYR A2269
SHEET 4 A 7 ARG A2303 TYR A2307 1 O ARG A2303 N PHE A2245
SHEET 5 A 7 SER A2333 PHE A2337 1 O PHE A2337 N GLY A2306
SHEET 6 A 7 VAL A2443 ALA A2448 1 O MET A2444 N LEU A2336
SHEET 7 A 7 VAL A2472 ILE A2477 1 O HIS A2475 N LEU A2445
SHEET 1 B 7 LEU B2231 ARG B2233 0
SHEET 2 B 7 THR B2268 LEU B2271 -1 O GLY B2270 N MET B2232
SHEET 3 B 7 LEU B2244 VAL B2247 1 N LEU B2246 O LEU B2271
SHEET 4 B 7 ARG B2303 TYR B2307 1 O ARG B2303 N PHE B2245
SHEET 5 B 7 SER B2333 PHE B2337 1 O SER B2333 N VAL B2304
SHEET 6 B 7 VAL B2443 ALA B2448 1 O MET B2444 N LEU B2336
SHEET 7 B 7 VAL B2472 ILE B2477 1 O ILE B2477 N ARG B2447
LINK OG SER A2308 C1' DH9 A3000
CISPEP 1 GLY A 2300 PRO A 2301 0 5.09
CISPEP 2 THR A 2342 TYR A 2343 0 21.35
CISPEP 3 GLY B 2300 PRO B 2301 0 -2.10
CISPEP 4 SER B 2326 PRO B 2327 0 8.41
CRYST1 41.860 94.320 69.720 90.00 95.82 90.00 P 1 21 1 4
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 0.023889 0.000000 0.002435 0.00000
SCALE2 0.000000 0.010602 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014417 0.00000
TER 1971 LEU A2501
TER 4013 SER B2507
MASTER 419 0 3 20 14 0 0 6 4143 2 80 50
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