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HEADER HYDROLASE/HYDROLASE INHIBITOR 24-AUG-11 3TJM
TITLE CRYSTAL STRUCTURE OF THE HUMAN FATTY ACID SYNTHASE THIOESTERASE DOMAIN
TITLE 2 WITH AN ACTIVATE SITE-SPECIFIC POLYUNSATURATED FATTY ACYL ADDUCT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FATTY ACID SYNTHASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 2218-2500;
COMPND 5 SYNONYM: [ACYL-CARRIER-PROTEIN] S-ACETYLTRANSFERASE, [ACYL-CARRIER-
COMPND 6 PROTEIN] S-MALONYLTRANSFERASE, 3-OXOACYL-[ACYL-CARRIER-PROTEIN]
COMPND 7 SYNTHASE, 3-OXOACYL-[ACYL-CARRIER-PROTEIN] REDUCTASE, 3-
COMPND 8 HYDROXYPALMITOYL-[ACYL-CARRIER-PROTEIN] DEHYDRATASE, ENOYL-[ACYL-
COMPND 9 CARRIER-PROTEIN] REDUCTASE, OLEOYL-[ACYL-CARRIER-PROTEIN] HYDROLASE;
COMPND 10 EC: 2.3.1.85, 2.3.1.38, 2.3.1.39, 2.3.1.41, 1.1.1.100, 4.2.1.61,
COMPND 11 1.3.1.10, 3.1.2.14;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: FAS, FASN;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PROEX
KEYWDS THIOESTERASE DOMAIN, FATTY ACID SYNTHESIS, HYDROLASE-HYDROLASE
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR W.ZHANG,F.ZHENG,A.Q.FLORANTE
REVDAT 1 28-SEP-11 3TJM 0
JRNL AUTH W.ZHANG,B.CHAKRAVARTY,F.ZHENG,Z.GU,H.WU,J.MAO,S.J.WAKIL,
JRNL AUTH 2 F.A.QUIOCHO
JRNL TITL CRYSTAL STRUCTURE OF FAS THIOESTERASE DOMAIN WITH
JRNL TITL 2 POLYUNSATURATED FATTY ACYL ADDUCT AND INHIBITION BY
JRNL TITL 3 DIHOMO-{GAMMA}-LINOLENIC ACID.
JRNL REF PROC.NATL.ACAD.SCI.USA 2011
JRNL REFN ESSN 1091-6490
JRNL PMID 21908709
JRNL DOI 10.1073/PNAS.1112334108
REMARK 2
REMARK 2 RESOLUTION. 1.48 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) : 1.48
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.56
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 38459
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) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2033
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) : 1.48
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.52
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2736
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.55
REMARK 3 BIN R VALUE (WORKING SET) : 0.1890
REMARK 3 BIN FREE R VALUE SET COUNT : 149
REMARK 3 BIN FREE R VALUE : 0.2650
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2123
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 22
REMARK 3 SOLVENT ATOMS : 251
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.07
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.23000
REMARK 3 B22 (A**2) : -0.10000
REMARK 3 B33 (A**2) : -0.14000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.087
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.046
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.564
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.941
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2335 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3174 ; 1.358 ; 1.977
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 277 ; 4.974 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 106 ;35.377 ;23.396
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 414 ;14.548 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;13.788 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 380 ; 0.097 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1720 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1197 ; 0.235 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1633 ; 0.310 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 184 ; 0.140 ; 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): 85 ; 0.321 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 29 ; 0.134 ; 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): 1443 ; 1.254 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2316 ; 1.890 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 982 ; 3.921 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 856 ; 3.873 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 2425 ; 3.886 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 251 ; 4.808 ; 3.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 2286 ; 3.677 ; 3.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3TJM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-SEP-11.
REMARK 100 THE RCSB ID CODE IS RCSB067558.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-JUL-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97948
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38459
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.480
REMARK 200 RESOLUTION RANGE LOW (A) : 23.560
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1XKT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18-23% PEG 3350, 0.1M BIS-TRIS BUFFER,
REMARK 280 PH 5.5, VAPOR DIFFUSION, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 25.45750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 38.25550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.04850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 38.25550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.45750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 31.04850
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 LYS A 2449
REMARK 465 THR A 2450
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 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLN A 2325 CG CD OE1 NE2
REMARK 480 ARG A 2447 CZ NH1 NH2
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 OE1 GLU A 2395 O HOH A 1133 1.96
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 GLN A2325 CB GLN A2325 CG -0.290
REMARK 500 ARG A2447 NE ARG A2447 CZ -0.145
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 HIS A2248 152.11 -49.59
REMARK 500 SER A2308 -121.19 58.47
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1146 DISTANCE = 6.13 ANGSTROMS
REMARK 525 HOH A1161 DISTANCE = 5.98 ANGSTROMS
REMARK 525 HOH A1169 DISTANCE = 6.22 ANGSTROMS
REMARK 525 HOH A1170 DISTANCE = 7.14 ANGSTROMS
REMARK 525 HOH A1213 DISTANCE = 6.75 ANGSTROMS
REMARK 525 HOH A1216 DISTANCE = 8.90 ANGSTROMS
REMARK 525 HOH A1218 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH A1240 DISTANCE = 5.33 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 7FA A 500
DBREF 3TJM A 2218 2500 UNP P49327 FAS_HUMAN 2218 2500
SEQADV 3TJM GLY A 2349 UNP P49327 GLN 2349 CONFLICT
SEQADV 3TJM ALA A 2457 UNP P49327 ASP 2457 CONFLICT
SEQADV 3TJM ALA A 2458 UNP P49327 LEU 2458 CONFLICT
SEQADV 3TJM ALA A 2482 UNP P49327 ARG 2482 CONFLICT
SEQRES 1 A 283 ASN LEU ARG SER LEU LEU VAL ASN PRO GLU GLY PRO THR
SEQRES 2 A 283 LEU MET ARG LEU ASN SER VAL GLN SER SER GLU ARG PRO
SEQRES 3 A 283 LEU PHE LEU VAL HIS PRO ILE GLU GLY SER THR THR VAL
SEQRES 4 A 283 PHE HIS SER LEU ALA SER ARG LEU SER ILE PRO THR TYR
SEQRES 5 A 283 GLY LEU GLN CYS THR ARG ALA ALA PRO LEU ASP SER ILE
SEQRES 6 A 283 HIS SER LEU ALA ALA TYR TYR ILE ASP CYS ILE ARG GLN
SEQRES 7 A 283 VAL GLN PRO GLU GLY PRO TYR ARG VAL ALA GLY TYR SER
SEQRES 8 A 283 TYR GLY ALA CYS VAL ALA PHE GLU MET CYS SER GLN LEU
SEQRES 9 A 283 GLN ALA GLN GLN SER PRO ALA PRO THR HIS ASN SER LEU
SEQRES 10 A 283 PHE LEU PHE ASP GLY SER PRO THR TYR VAL LEU ALA TYR
SEQRES 11 A 283 THR GLY SER TYR ARG ALA LYS LEU THR PRO GLY CYS GLU
SEQRES 12 A 283 ALA GLU ALA GLU THR GLU ALA ILE CYS PHE PHE VAL GLN
SEQRES 13 A 283 GLN PHE THR ASP MET GLU HIS ASN ARG VAL LEU GLU ALA
SEQRES 14 A 283 LEU LEU PRO LEU LYS GLY LEU GLU GLU ARG VAL ALA ALA
SEQRES 15 A 283 ALA VAL ASP LEU ILE ILE LYS SER HIS GLN GLY LEU ASP
SEQRES 16 A 283 ARG GLN GLU LEU SER PHE ALA ALA ARG SER PHE TYR TYR
SEQRES 17 A 283 LYS LEU ARG ALA ALA GLU GLN TYR THR PRO LYS ALA LYS
SEQRES 18 A 283 TYR HIS GLY ASN VAL MET LEU LEU ARG ALA LYS THR GLY
SEQRES 19 A 283 GLY ALA TYR GLY GLU ALA ALA GLY ALA ASP TYR ASN LEU
SEQRES 20 A 283 SER GLN VAL CYS ASP GLY LYS VAL SER VAL HIS VAL ILE
SEQRES 21 A 283 GLU GLY ASP HIS ALA THR LEU LEU GLU GLY SER GLY LEU
SEQRES 22 A 283 GLU SER ILE ILE SER ILE ILE HIS SER SER
HET 7FA A 500 22
HETNAM 7FA METHYL (S)-(6Z,9Z)-OCTADECA-6,9,12-TRIEN-1-
HETNAM 2 7FA YLPHOSPHONOFLUORIDATE
FORMUL 2 7FA C19 H34 F O2 P
FORMUL 3 HOH *251(H2 O)
HELIX 1 1 ASN A 2218 LEU A 2223 5 6
HELIX 2 2 THR A 2254 VAL A 2256 5 3
HELIX 3 3 PHE A 2257 LEU A 2264 1 8
HELIX 4 4 SER A 2281 ARG A 2294 1 14
HELIX 5 5 SER A 2308 SER A 2326 1 19
HELIX 6 6 THR A 2342 ALA A 2353 1 12
HELIX 7 7 CYS A 2359 THR A 2376 1 18
HELIX 8 8 GLU A 2379 LEU A 2388 1 10
HELIX 9 9 GLY A 2392 HIS A 2408 1 17
HELIX 10 10 ASP A 2412 TYR A 2433 1 22
HELIX 11 11 ASN A 2463 VAL A 2467 5 5
HELIX 12 12 ALA A 2482 LEU A 2485 5 4
HELIX 13 13 GLU A 2486 SER A 2500 1 15
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 ALA A2305 N PHE A2245
SHEET 5 A 7 SER A2333 PHE A2337 1 O PHE A2337 N GLY A2306
SHEET 6 A 7 VAL A2443 ARG A2447 1 O MET A2444 N LEU A2336
SHEET 7 A 7 VAL A2472 VAL A2476 1 O SER A2473 N LEU A2445
LINK OG SER A2308 P1 7FA A 500 1555 1555 1.66
CISPEP 1 GLY A 2300 PRO A 2301 0 -0.84
CISPEP 2 SER A 2326 PRO A 2327 0 1.85
SITE 1 AC1 11 PRO A2249 ILE A2250 GLU A2251 SER A2308
SITE 2 AC1 11 TYR A2309 TYR A2347 TYR A2351 PHE A2370
SITE 3 AC1 11 LEU A2427 ARG A2428 GLU A2431
CRYST1 50.915 62.097 76.511 90.00 90.00 90.00 P 21 21 21 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 0.019641 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016104 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013070 0.00000
TER 2272 SER A2500
MASTER 327 0 1 13 7 0 3 6 2396 1 23 22
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