HEADER LIPID BINDING PROTEIN 11-OCT-10 3P6H
TITLE HUMAN ADIPOCYTE LIPID-BINDING PROTEIN FABP4 IN COMPLEX WITH (S)-
TITLE 2 IBUPROFEN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FATTY ACID-BINDING PROTEIN, ADIPOCYTE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ADIPOCYTE LIPID-BINDING PROTEIN, ALBP, ADIPOCYTE-TYPE FATTY
COMPND 5 ACID-BINDING PROTEIN, A-FABP, AFABP, FATTY ACID-BINDING PROTEIN 4;
COMPND 6 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: FABP4;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS LIPOCALIN, BETA BARREL, FATTY ACID BINDING PROTEIN, DRUG,
KEYWDS 2 NONSTEROIDAL ANTI-INFLAMMATORY DRUG, LIPID BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.M.GONZALEZ,E.POZHARSKI
REVDAT 5 21-FEB-24 3P6H 1 REMARK SEQADV
REVDAT 4 25-FEB-15 3P6H 1 JRNL
REVDAT 3 11-FEB-15 3P6H 1 JRNL
REVDAT 2 20-APR-11 3P6H 1 KEYWDS REMARK
REVDAT 1 13-APR-11 3P6H 0
JRNL AUTH J.M.GONZALEZ,S.Z.FISHER
JRNL TITL STRUCTURAL ANALYSIS OF IBUPROFEN BINDING TO HUMAN ADIPOCYTE
JRNL TITL 2 FATTY-ACID BINDING PROTEIN (FABP4).
JRNL REF ACTA CRYSTALLOGR F STRUCT V. 71 163 2015
JRNL REF 2 BIOL COMMUN
JRNL REFN
JRNL PMID 25664790
JRNL DOI 10.1107/S2053230X14027897
REMARK 2
REMARK 2 RESOLUTION. 1.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 1.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.50
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 46490
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.160
REMARK 3 R VALUE (WORKING SET) : 0.158
REMARK 3 FREE R VALUE : 0.191
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2355
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.18
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3144
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.63
REMARK 3 BIN R VALUE (WORKING SET) : 0.2410
REMARK 3 BIN FREE R VALUE SET COUNT : 157
REMARK 3 BIN FREE R VALUE : 0.2590
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1072
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 15
REMARK 3 SOLVENT ATOMS : 172
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.03
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.60000
REMARK 3 B22 (A**2) : -0.13000
REMARK 3 B33 (A**2) : -1.47000
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): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.033
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.636
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.971
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.963
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1227 ; 0.021 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 854 ; 0.014 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1663 ; 2.010 ; 1.972
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2098 ; 1.021 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 166 ; 6.316 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 49 ;34.384 ;24.898
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 247 ;15.520 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;19.104 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 188 ; 0.112 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1394 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 239 ; 0.005 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 761 ; 2.197 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 317 ; 0.734 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1246 ; 3.355 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 466 ; 4.824 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 412 ; 6.770 ; 4.500
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): 2081 ; 2.040 ; 3.000
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 : NULL
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 4
REMARK 4 3P6H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-OCT-10.
REMARK 100 THE DEPOSITION ID IS D_1000062016.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-FEB-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.16
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58556
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.060
REMARK 200 RESOLUTION RANGE LOW (A) : 43.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.12400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.06
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.72500
REMARK 200 R SYM FOR SHELL (I) : 0.72500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6 M SODIUM CITRATE, PH 6.5, VAPOR
REMARK 280 DIFFUSION, TEMPERATURE 293K
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 16.16400
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 37.51550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.69000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 37.51550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 16.16400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 26.69000
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLN A -7 CG CD OE1 NE2
REMARK 470 GLN A -6 CG CD OE1 NE2
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 14 O HOH A 206 2.03
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 MET A 0 CG - SD - CE ANGL. DEV. = -13.5 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 PHE A 57 -71.11 -78.04
REMARK 500 PHE A 57 -78.70 -78.04
REMARK 500 ASP A 77 31.32 75.14
REMARK 500 ASP A 110 -134.62 53.94
REMARK 500 LYS A 120 -122.97 56.03
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 IBP A 133
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3P6C RELATED DB: PDB
REMARK 900 RELATED ID: 3P6D RELATED DB: PDB
REMARK 900 RELATED ID: 3P6E RELATED DB: PDB
REMARK 900 RELATED ID: 3P6F RELATED DB: PDB
REMARK 900 RELATED ID: 3P6G RELATED DB: PDB
DBREF 3P6H A 0 131 UNP P15090 FABP4_HUMAN 1 132
SEQADV 3P6H GLN A -7 UNP P15090 EXPRESSION TAG
SEQADV 3P6H GLN A -6 UNP P15090 EXPRESSION TAG
SEQADV 3P6H MET A -5 UNP P15090 EXPRESSION TAG
SEQADV 3P6H GLY A -4 UNP P15090 EXPRESSION TAG
SEQADV 3P6H ARG A -3 UNP P15090 EXPRESSION TAG
SEQADV 3P6H GLY A -2 UNP P15090 EXPRESSION TAG
SEQADV 3P6H SER A -1 UNP P15090 EXPRESSION TAG
SEQRES 1 A 139 GLN GLN MET GLY ARG GLY SER MET CYS ASP ALA PHE VAL
SEQRES 2 A 139 GLY THR TRP LYS LEU VAL SER SER GLU ASN PHE ASP ASP
SEQRES 3 A 139 TYR MET LYS GLU VAL GLY VAL GLY PHE ALA THR ARG LYS
SEQRES 4 A 139 VAL ALA GLY MET ALA LYS PRO ASN MET ILE ILE SER VAL
SEQRES 5 A 139 ASN GLY ASP VAL ILE THR ILE LYS SER GLU SER THR PHE
SEQRES 6 A 139 LYS ASN THR GLU ILE SER PHE ILE LEU GLY GLN GLU PHE
SEQRES 7 A 139 ASP GLU VAL THR ALA ASP ASP ARG LYS VAL LYS SER THR
SEQRES 8 A 139 ILE THR LEU ASP GLY GLY VAL LEU VAL HIS VAL GLN LYS
SEQRES 9 A 139 TRP ASP GLY LYS SER THR THR ILE LYS ARG LYS ARG GLU
SEQRES 10 A 139 ASP ASP LYS LEU VAL VAL GLU CYS VAL MET LYS GLY VAL
SEQRES 11 A 139 THR SER THR ARG VAL TYR GLU ARG ALA
HET IBP A 133 15
HETNAM IBP IBUPROFEN
HETSYN IBP 2-(4-ISOBUTYLPHENYL)PROPIONIC ACID
FORMUL 2 IBP C13 H18 O2
FORMUL 3 HOH *172(H2 O)
HELIX 1 1 SER A -1 VAL A 5 5 7
HELIX 2 2 ASN A 15 GLY A 24 1 10
HELIX 3 3 GLY A 26 ALA A 36 1 11
SHEET 1 A10 ASN A 59 PHE A 64 0
SHEET 2 A10 VAL A 48 GLU A 54 -1 N ILE A 49 O PHE A 64
SHEET 3 A10 ASN A 39 ASN A 45 -1 N ASN A 39 O GLU A 54
SHEET 4 A10 GLY A 6 GLU A 14 -1 N TRP A 8 O MET A 40
SHEET 5 A10 VAL A 122 ARG A 130 -1 O VAL A 127 N VAL A 11
SHEET 6 A10 LYS A 112 MET A 119 -1 N VAL A 115 O ARG A 126
SHEET 7 A10 LYS A 100 GLU A 109 -1 N LYS A 107 O VAL A 114
SHEET 8 A10 VAL A 90 TRP A 97 -1 N TRP A 97 O LYS A 100
SHEET 9 A10 LYS A 79 ASP A 87 -1 N THR A 85 O VAL A 92
SHEET 10 A10 PHE A 70 VAL A 73 -1 N PHE A 70 O SER A 82
SITE 1 AC1 5 ASP A 76 ARG A 126 TYR A 128 HOH A 210
SITE 2 AC1 5 HOH A 279
CRYST1 32.328 53.380 75.031 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 0.030933 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018734 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013328 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
