HEADER OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 03-OCT-11 3U2C
TITLE ALDOSE REDUCTASE IN COMPLEX WITH NSAID-TYPE INHIBITOR AT 1.0 A
TITLE 2 RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALDOSE REDUCTASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: AR, ALDEHYDE REDUCTASE, ALDO-KETO REDUCTASE FAMILY 1 MEMBER
COMPND 5 B1;
COMPND 6 EC: 1.1.1.21;
COMPND 7 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: AKR1B1, ALDOSE REDUCTASE, ALDR1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 GOLD;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS TIM BARREL, OXIDOREDUCTASE, OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.STEUBER
REVDAT 3 13-SEP-23 3U2C 1 REMARK SEQADV
REVDAT 2 03-JUL-13 3U2C 1 JRNL
REVDAT 1 02-NOV-11 3U2C 0
JRNL AUTH H.STEUBER
JRNL TITL AN OLD NSAID REVISITED: CRYSTAL STRUCTURE OF ALDOSE
JRNL TITL 2 REDUCTASE IN COMPLEX WITH SULINDAC AT 1.0 A SUPPORTS A NOVEL
JRNL TITL 3 MECHANISM FOR ITS ANTICANCER AND ANTIPROLIFERATIVE EFFECTS.
JRNL REF CHEMMEDCHEM V. 6 2155 2011
JRNL REFN ISSN 1860-7179
JRNL PMID 21997888
JRNL DOI 10.1002/CMDC.201100374
REMARK 2
REMARK 2 RESOLUTION. 1.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.5
REMARK 3 CROSS-VALIDATION METHOD : FREE R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.113
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.114
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.138
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 7789
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 155786
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.106
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE (F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 123451
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2517
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 137
REMARK 3 SOLVENT ATOMS : 309
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 2979.2
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 2525.1
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 14
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 27544
REMARK 3 NUMBER OF RESTRAINTS : 32479
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.016
REMARK 3 ANGLE DISTANCES (A) : 2.300
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.029
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.099
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.102
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.086
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.006
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.054
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.000
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3U2C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-OCT-11.
REMARK 100 THE DEPOSITION ID IS D_1000068217.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JUN-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.88561
REMARK 200 MONOCHROMATOR : NI FILTER
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 155837
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : 0.05000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.7200
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 <I/SIGMA(I)> 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: MOLREP
REMARK 200 STARTING MODEL: 1EL3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM CITRATE, PEG4000, PH 5, VAPOR
REMARK 280 DIFFUSION, TEMPERATURE 278K
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,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 33.60350
REMARK 290 SMTRY3 2 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 MET A 0
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 HIS A 187 NE2 HIS A 187 CD2 -0.067
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 ALA A 1 CB - CA - C ANGL. DEV. = 10.3 DEGREES
REMARK 500 ALA A 1 O - C - N ANGL. DEV. = -14.7 DEGREES
REMARK 500 SER A 2 N - CA - CB ANGL. DEV. = 9.9 DEGREES
REMARK 500 ARG A 3 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG A 3 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 GLU A 60 OE1 - CD - OE2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 PHE A 115 CB - CG - CD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 PHE A 115 CB - CG - CD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP A 125 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ASP A 125 CA - C - N ANGL. DEV. = 13.4 DEGREES
REMARK 500 GLU A 126 C - N - CA ANGL. DEV. = 17.2 DEGREES
REMARK 500 ASP A 134 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 GLU A 146 OE1 - CD - OE2 ANGL. DEV. = -7.8 DEGREES
REMARK 500 GLU A 193 OE1 - CD - OE2 ANGL. DEV. = 10.1 DEGREES
REMARK 500 ARG A 250 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ASP A 284 CA - CB - CG ANGL. DEV. = 20.4 DEGREES
REMARK 500 ASP A 284 CB - CG - OD2 ANGL. DEV. = 12.3 DEGREES
REMARK 500 ARG A 293 NE - CZ - NH1 ANGL. DEV. = 10.1 DEGREES
REMARK 500 ARG A 293 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 HIS A 306 CG - ND1 - CE1 ANGL. DEV. = 12.0 DEGREES
REMARK 500 HIS A 306 ND1 - CE1 - NE2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 ASP A 308 C - N - CA 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 ASP A 125 -137.92 -94.59
REMARK 500 ASP A 134 47.77 -77.89
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 NAP A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 1800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG5 A 1803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG5 A 1805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT A 2000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SUZ A 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 2010
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 2011
DBREF 3U2C A 0 315 UNP P15121 ALDR_HUMAN 1 316
SEQADV 3U2C ILE A 4 UNP P15121 LEU 5 CONFLICT
SEQRES 1 A 316 MET ALA SER ARG ILE LEU LEU ASN ASN GLY ALA LYS MET
SEQRES 2 A 316 PRO ILE LEU GLY LEU GLY THR TRP LYS SER PRO PRO GLY
SEQRES 3 A 316 GLN VAL THR GLU ALA VAL LYS VAL ALA ILE ASP VAL GLY
SEQRES 4 A 316 TYR ARG HIS ILE ASP CYS ALA HIS VAL TYR GLN ASN GLU
SEQRES 5 A 316 ASN GLU VAL GLY VAL ALA ILE GLN GLU LYS LEU ARG GLU
SEQRES 6 A 316 GLN VAL VAL LYS ARG GLU GLU LEU PHE ILE VAL SER LYS
SEQRES 7 A 316 LEU TRP CYS THR TYR HIS GLU LYS GLY LEU VAL LYS GLY
SEQRES 8 A 316 ALA CYS GLN LYS THR LEU SER ASP LEU LYS LEU ASP TYR
SEQRES 9 A 316 LEU ASP LEU TYR LEU ILE HIS TRP PRO THR GLY PHE LYS
SEQRES 10 A 316 PRO GLY LYS GLU PHE PHE PRO LEU ASP GLU SER GLY ASN
SEQRES 11 A 316 VAL VAL PRO SER ASP THR ASN ILE LEU ASP THR TRP ALA
SEQRES 12 A 316 ALA MET GLU GLU LEU VAL ASP GLU GLY LEU VAL LYS ALA
SEQRES 13 A 316 ILE GLY ILE SER ASN PHE ASN HIS LEU GLN VAL GLU MET
SEQRES 14 A 316 ILE LEU ASN LYS PRO GLY LEU LYS TYR LYS PRO ALA VAL
SEQRES 15 A 316 ASN GLN ILE GLU CYS HIS PRO TYR LEU THR GLN GLU LYS
SEQRES 16 A 316 LEU ILE GLN TYR CYS GLN SER LYS GLY ILE VAL VAL THR
SEQRES 17 A 316 ALA TYR SER PRO LEU GLY SER PRO ASP ARG PRO TRP ALA
SEQRES 18 A 316 LYS PRO GLU ASP PRO SER LEU LEU GLU ASP PRO ARG ILE
SEQRES 19 A 316 LYS ALA ILE ALA ALA LYS HIS ASN LYS THR THR ALA GLN
SEQRES 20 A 316 VAL LEU ILE ARG PHE PRO MET GLN ARG ASN LEU VAL VAL
SEQRES 21 A 316 ILE PRO LYS SER VAL THR PRO GLU ARG ILE ALA GLU ASN
SEQRES 22 A 316 PHE LYS VAL PHE ASP PHE GLU LEU SER SER GLN ASP MET
SEQRES 23 A 316 THR THR LEU LEU SER TYR ASN ARG ASN TRP ARG VAL CYS
SEQRES 24 A 316 ALA LEU LEU SER CYS THR SER HIS LYS ASP TYR PRO PHE
SEQRES 25 A 316 HIS GLU GLU PHE
HET NAP A 400 48
HET PEG A1800 7
HET PG5 A1803 12
HET PG5 A1805 12
HET CIT A2000 13
HET SUZ A2001 25
HET PEG A2010 7
HET PG4 A2011 13
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM PG5 1-METHOXY-2-[2-(2-METHOXY-ETHOXY]-ETHANE
HETNAM CIT CITRIC ACID
HETNAM SUZ [(1Z)-5-FLUORO-2-METHYL-1-{4-
HETNAM 2 SUZ [METHYLSULFINYL]BENZYLIDENE}-1H-INDEN-3-YL]ACETIC ACID
HETNAM PG4 TETRAETHYLENE GLYCOL
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
HETSYN SUZ SULINDAC
FORMUL 2 NAP C21 H28 N7 O17 P3
FORMUL 3 PEG 2(C4 H10 O3)
FORMUL 4 PG5 2(C8 H18 O4)
FORMUL 6 CIT C6 H8 O7
FORMUL 7 SUZ C20 H17 F O3 S
FORMUL 9 PG4 C8 H18 O5
FORMUL 10 HOH *309(H2 O)
HELIX 1 1 PRO A 23 GLY A 38 1 16
HELIX 2 2 ALA A 45 GLN A 49 5 5
HELIX 3 3 ASN A 50 GLU A 64 1 15
HELIX 4 4 LYS A 68 LEU A 72 5 5
HELIX 5 5 TRP A 79 HIS A 83 5 5
HELIX 6 6 GLU A 84 GLY A 86 5 3
HELIX 7 7 LEU A 87 LYS A 100 1 14
HELIX 8 8 ASN A 136 GLU A 150 1 15
HELIX 9 9 ASN A 162 ASN A 171 1 10
HELIX 10 10 GLN A 192 LYS A 202 1 11
HELIX 11 11 SER A 226 GLU A 229 5 4
HELIX 12 12 ASP A 230 ASN A 241 1 12
HELIX 13 13 THR A 243 GLN A 254 1 12
HELIX 14 14 THR A 265 LYS A 274 1 10
HELIX 15 15 SER A 281 SER A 290 1 10
HELIX 16 16 LEU A 300 THR A 304 5 5
SHEET 1 A 2 ARG A 3 LEU A 5 0
SHEET 2 A 2 LYS A 11 PRO A 13 -1 O MET A 12 N ILE A 4
SHEET 1 B 8 LEU A 17 GLY A 18 0
SHEET 2 B 8 HIS A 41 ASP A 43 1 O ASP A 43 N LEU A 17
SHEET 3 B 8 PHE A 73 LEU A 78 1 O VAL A 75 N ILE A 42
SHEET 4 B 8 LEU A 106 ILE A 109 1 O LEU A 108 N LEU A 78
SHEET 5 B 8 ILE A 156 SER A 159 1 O GLY A 157 N ILE A 109
SHEET 6 B 8 VAL A 181 GLU A 185 1 O VAL A 181 N ILE A 158
SHEET 7 B 8 VAL A 205 TYR A 209 1 O THR A 207 N ILE A 184
SHEET 8 B 8 VAL A 258 VAL A 259 1 O VAL A 258 N ALA A 208
SITE 1 AC1 32 GLY A 18 THR A 19 TRP A 20 LYS A 21
SITE 2 AC1 32 ASP A 43 TYR A 48 LYS A 77 HIS A 110
SITE 3 AC1 32 SER A 159 ASN A 160 GLN A 183 TYR A 209
SITE 4 AC1 32 SER A 210 PRO A 211 LEU A 212 GLY A 213
SITE 5 AC1 32 SER A 214 PRO A 215 ASP A 216 ALA A 245
SITE 6 AC1 32 ILE A 260 PRO A 261 LYS A 262 SER A 263
SITE 7 AC1 32 VAL A 264 THR A 265 ARG A 268 GLU A 271
SITE 8 AC1 32 ASN A 272 HOH A1182 HOH A1193 SUZ A2001
SITE 1 AC2 2 GLN A 200 HOH A1260
SITE 1 AC3 6 ASN A 8 TYR A 103 GLY A 151 VAL A 153
SITE 2 AC3 6 LYS A 154 ARG A 232
SITE 1 AC4 8 GLN A 49 ASN A 52 LYS A 94 ASP A 98
SITE 2 AC4 8 HOH A1029 HOH A1030 HOH A1305 HOH A1318
SITE 1 AC5 7 TRP A 219 ALA A 299 LEU A 300 LEU A 301
SITE 2 AC5 7 SER A 302 HOH A1337 SUZ A2001
SITE 1 AC6 11 TRP A 20 VAL A 47 TYR A 48 HIS A 110
SITE 2 AC6 11 PHE A 122 TRP A 219 CYS A 298 SER A 302
SITE 3 AC6 11 NAP A 400 HOH A1338 CIT A2000
SITE 1 AC7 5 ALA A 1 ARG A 250 MET A 253 ASN A 256
SITE 2 AC7 5 PHE A 276
SITE 1 AC8 3 GLN A 59 LYS A 100 HOH A1334
CRYST1 47.095 67.207 49.419 90.00 92.38 90.00 P 1 21 1 2
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 0.021234 0.000000 0.000883 0.00000
SCALE2 0.000000 0.014879 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020253 0.00000
(ATOM LINES ARE NOT SHOWN.)
END