HEADER HYDROLASE 02-MAR-03 1ONZ
TITLE OXALYL-ARYL-AMINO BENZOIC ACID INHIBITORS OF PTP1B, COMPOUND 8B
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN-TYROSINE PHOSPHATASE, NON-RECEPTOR TYPE 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PTP1B CATALYTIC DOMAIN;
COMPND 5 SYNONYM: PROTEIN-TYROSINE PHOSPHATASE 1B, PTP-1B;
COMPND 6 EC: 3.1.3.48;
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: PTPN1 OR PTP1B;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(D33)PTPASE 1B;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PT7-7
KEYWDS PROTEIN TYROSINE PHOSPHATASE, OXALYL-ARYL-BENZOIC ACID COMPOUND WITH
KEYWDS 2 NAPTHYL MOIETY ANCHOR INHIBITOR, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.LIU,B.G.SZCZEPANKIEWICZ,Z.PEI,D.A.JANOWICH,Z.XIN,P.J.HADJUK,C.ABAD-
AUTHOR 2 ZAPATERO,H.LIANG,C.W.HUTCHINS,S.W.FESIK,S.J.BALLARON,M.A.STASHKO,
AUTHOR 3 T.LUBBEN,A.K.MIKA,B.A.ZINKER,J.M.TREVILLYAN,M.R.JIROUSEK
REVDAT 4 16-AUG-23 1ONZ 1 REMARK
REVDAT 3 11-OCT-17 1ONZ 1 REMARK
REVDAT 2 24-FEB-09 1ONZ 1 VERSN
REVDAT 1 20-MAY-03 1ONZ 0
JRNL AUTH G.LIU,B.G.SZCZEPANKIEWICZ,Z.PEI,D.A.JANOWICH,Z.XIN,
JRNL AUTH 2 P.J.HADJUK,C.ABAD-ZAPATERO,H.LIANG,C.W.HUTCHINS,S.W.FESIK,
JRNL AUTH 3 S.J.BALLARON,M.A.STASHKO,T.LUBBEN,A.K.MIKA,B.A.ZINKER,
JRNL AUTH 4 J.M.TREVILLYAN,M.R.JIROUSEK
JRNL TITL DISCOVERY AND STRUCTURE-ACTIVITY RELATIONSHIP OF
JRNL TITL 2 OXALYLARYLAMINOBENZOIC ACIDS AS INHIBITORS OF PROTEIN
JRNL TITL 3 TYROSINE PHOSPHATASE 1B
JRNL REF J.MED.CHEM. V. 46 2093 2003
JRNL REFN ISSN 0022-2623
JRNL PMID 12747781
JRNL DOI 10.1021/JM0205696
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH Z.XIN,T.K.OOST,C.ABAD-ZAPATERO,P.J.HAJDUK,Z.PEI,
REMARK 1 AUTH 2 B.G.SZCZEPANKIEWICZ,C.W.HUTCHINS,S.J.BALLARON,M.A.STASHKO,
REMARK 1 AUTH 3 T.LUBBEN,J.M.TREVILLYAN,M.R.JIROUSEK,G.LIU
REMARK 1 TITL POTENT, SELECTIVE INHIBITORS OF PROTEIN TYROSINE PHOSPHATASE
REMARK 1 TITL 2 1B
REMARK 1 REF BIOORG.MED.CHEM.LETT. V. 13 1887 2003
REMARK 1 REFN ISSN 0960-894X
REMARK 1 DOI 10.1016/S0960-894X(03)00302-0
REMARK 1 REFERENCE 2
REMARK 1 AUTH B.G.SZCZEPANKIEWICZ,G.LIU,P.J.HAJDUK,C.ABAD-ZAPATERO,Z.PEI,
REMARK 1 AUTH 2 Z.XIN,T.LUBBEN,J.M.TREVILLYAN,M.A.STASHKO,S.J.BALLARON,
REMARK 1 AUTH 3 H.LIANG,F.HUANG,C.W.HUTCHINS,S.W.FESIK,M.R.JIROUSEK
REMARK 1 TITL POTENT, SELECTIVE PROTEIN TYROSINE PHOSPHATASE 1B INHIBITOR
REMARK 1 TITL 2 USING A LINKED-FRAGMENT STRATEGY
REMARK 1 REF J.AM.CHEM.SOC. V. 125 4087 2003
REMARK 1 REFN ISSN 0002-7863
REMARK 1 DOI 10.1021/JA0296733
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNX 2000
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN,ACCELRYS
REMARK 3 : SOFTWARE INC.(BADGER,BERARD,KUMAR,SZALMA,
REMARK 3 : YIP,DZAKULA)
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.73
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 86.4
REMARK 3 NUMBER OF REFLECTIONS : 16513
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) : 0.226
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1651
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 18495
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.49
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 66.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1123
REMARK 3 BIN R VALUE (WORKING SET) : 0.2260
REMARK 3 BIN FREE R VALUE : 0.2610
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 127
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.023
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2301
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 26
REMARK 3 SOLVENT ATOMS : 279
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 42.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.96000
REMARK 3 B22 (A**2) : 4.96000
REMARK 3 B33 (A**2) : -9.91000
REMARK 3 B12 (A**2) : 6.81000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.26
REMARK 3 ESD FROM SIGMAA (A) : 0.24
REMARK 3 LOW RESOLUTION CUTOFF (A) : 6.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.32
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.30
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.880
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 3.850 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 5.600 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 6.350 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 8.550 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 45.32
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : 968.PAR
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : 968.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RESIDUE CYS215, LISTED IN REMARK 500,
REMARK 3 CORRESPONDS TO THE ACTIVE SITE CYS WHICH IS KNOWN TO BE IN A
REMARK 3 STRAINED CONFORMATION IN THIS CLASS OF ENZYMES.
REMARK 4
REMARK 4 1ONZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAR-03.
REMARK 100 THE DEPOSITION ID IS D_1000018486.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-MAR-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.1
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MAR
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23620
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.8
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : 0.04600
REMARK 200 R SYM (I) : 0.04600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.2
REMARK 200 DATA REDUNDANCY IN SHELL : 4.50
REMARK 200 R MERGE FOR SHELL (I) : 0.26600
REMARK 200 R SYM FOR SHELL (I) : 0.26600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNX 2000
REMARK 200 STARTING MODEL: PDB ENTRY 1TYR AND INITIAL INTERNAL REFINEMENT OF
REMARK 200 OTHER COMPLEXES
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PRECIPITATION BUFFER: 100 MM HEPES,
REMARK 280 0.2 M MAGNESIUM ACETATE, 14% PEG8000, PH 7.1, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 35.05567
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 70.11133
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 70.11133
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 35.05567
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 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 1
REMARK 465 SER A 285
REMARK 465 SER A 286
REMARK 465 VAL A 287
REMARK 465 GLN A 288
REMARK 465 ASP A 289
REMARK 465 GLN A 290
REMARK 465 TRP A 291
REMARK 465 LYS A 292
REMARK 465 GLU A 293
REMARK 465 LEU A 294
REMARK 465 SER A 295
REMARK 465 HIS A 296
REMARK 465 GLU A 297
REMARK 465 ASP A 298
REMARK 465 LEU A 299
REMARK 465 GLU A 300
REMARK 465 PRO A 301
REMARK 465 PRO A 302
REMARK 465 PRO A 303
REMARK 465 GLU A 304
REMARK 465 HIS A 305
REMARK 465 ILE A 306
REMARK 465 PRO A 307
REMARK 465 PRO A 308
REMARK 465 PRO A 309
REMARK 465 PRO A 310
REMARK 465 ARG A 311
REMARK 465 PRO A 312
REMARK 465 PRO A 313
REMARK 465 LYS A 314
REMARK 465 ARG A 315
REMARK 465 ILE A 316
REMARK 465 LEU A 317
REMARK 465 GLU A 318
REMARK 465 PRO A 319
REMARK 465 HIS A 320
REMARK 465 ASN A 321
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 ASP A 284 CA C O CB CG OD1 OD2
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 63 -96.68 -63.24
REMARK 500 PRO A 87 153.24 -49.07
REMARK 500 CYS A 121 142.84 -177.29
REMARK 500 LYS A 131 77.68 -112.21
REMARK 500 GLN A 166 5.00 82.50
REMARK 500 CYS A 215 -116.75 -137.51
REMARK 500 ILE A 219 -36.07 -140.49
REMARK 500 ILE A 261 99.58 73.06
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 968 A 322
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1NL9 RELATED DB: PDB
REMARK 900 POTENT, SELECTIVE PROTEIN TYROSINE PHOSPHATASE INHIBITORS USING A
REMARK 900 LINKED-FRAGMENT STRATEGY COMPLEXED WITH COMPOUND 12
REMARK 900 RELATED ID: 1NNY RELATED DB: PDB
REMARK 900 POTENT, SELECTIVE PROTEIN TYROSINE PHOSPHATASE INHIBITORS USING A
REMARK 900 LINKED-FRAGMENT STRATEGY COMPLEXED WITH COMPOUND 23
REMARK 900 RELATED ID: 1NO6 RELATED DB: PDB
REMARK 900 POTENT, SELECTIVE PROTEIN TYROSINE PHOSPHATASE INHIBITORS USING A
REMARK 900 LINKED-FRAGMENT STRATEGY COMPLEXED WITH COMPOUND 5
REMARK 900 RELATED ID: 1NZ7 RELATED DB: PDB
REMARK 900 POTENT, SELECTIVE INHIBITORS OF PROTEIN TYROSINE PHOSPHATASE 1B
REMARK 900 COMPLEXED WITH COMPOUND 19
REMARK 900 RELATED ID: 1ONY RELATED DB: PDB
REMARK 900 DISCOVERY AND SAR OF OXALYL-ARYL-AMINO BENZOIC ACIDS AS INHBITORS
REMARK 900 OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH COMPOUND 17
DBREF 1ONZ A 1 321 UNP P18031 PTN1_HUMAN 1 321
SEQRES 1 A 321 MET GLU MET GLU LYS GLU PHE GLU GLN ILE ASP LYS SER
SEQRES 2 A 321 GLY SER TRP ALA ALA ILE TYR GLN ASP ILE ARG HIS GLU
SEQRES 3 A 321 ALA SER ASP PHE PRO CYS ARG VAL ALA LYS LEU PRO LYS
SEQRES 4 A 321 ASN LYS ASN ARG ASN ARG TYR ARG ASP VAL SER PRO PHE
SEQRES 5 A 321 ASP HIS SER ARG ILE LYS LEU HIS GLN GLU ASP ASN ASP
SEQRES 6 A 321 TYR ILE ASN ALA SER LEU ILE LYS MET GLU GLU ALA GLN
SEQRES 7 A 321 ARG SER TYR ILE LEU THR GLN GLY PRO LEU PRO ASN THR
SEQRES 8 A 321 CYS GLY HIS PHE TRP GLU MET VAL TRP GLU GLN LYS SER
SEQRES 9 A 321 ARG GLY VAL VAL MET LEU ASN ARG VAL MET GLU LYS GLY
SEQRES 10 A 321 SER LEU LYS CYS ALA GLN TYR TRP PRO GLN LYS GLU GLU
SEQRES 11 A 321 LYS GLU MET ILE PHE GLU ASP THR ASN LEU LYS LEU THR
SEQRES 12 A 321 LEU ILE SER GLU ASP ILE LYS SER TYR TYR THR VAL ARG
SEQRES 13 A 321 GLN LEU GLU LEU GLU ASN LEU THR THR GLN GLU THR ARG
SEQRES 14 A 321 GLU ILE LEU HIS PHE HIS TYR THR THR TRP PRO ASP PHE
SEQRES 15 A 321 GLY VAL PRO GLU SER PRO ALA SER PHE LEU ASN PHE LEU
SEQRES 16 A 321 PHE LYS VAL ARG GLU SER GLY SER LEU SER PRO GLU HIS
SEQRES 17 A 321 GLY PRO VAL VAL VAL HIS CYS SER ALA GLY ILE GLY ARG
SEQRES 18 A 321 SER GLY THR PHE CYS LEU ALA ASP THR CYS LEU LEU LEU
SEQRES 19 A 321 MET ASP LYS ARG LYS ASP PRO SER SER VAL ASP ILE LYS
SEQRES 20 A 321 LYS VAL LEU LEU GLU MET ARG LYS PHE ARG MET GLY LEU
SEQRES 21 A 321 ILE GLN THR ALA ASP GLN LEU ARG PHE SER TYR LEU ALA
SEQRES 22 A 321 VAL ILE GLU GLY ALA LYS PHE ILE MET GLY ASP SER SER
SEQRES 23 A 321 VAL GLN ASP GLN TRP LYS GLU LEU SER HIS GLU ASP LEU
SEQRES 24 A 321 GLU PRO PRO PRO GLU HIS ILE PRO PRO PRO PRO ARG PRO
SEQRES 25 A 321 PRO LYS ARG ILE LEU GLU PRO HIS ASN
HET 968 A 322 26
HETNAM 968 2-[(7-HYDROXY-NAPHTHALEN-1-YL)-OXALYL-AMINO]-BENZOIC
HETNAM 2 968 ACID
HETSYN 968 COMPOUND 8B
FORMUL 2 968 C19 H13 N O6
FORMUL 3 HOH *279(H2 O)
HELIX 1 1 GLU A 2 SER A 13 1 12
HELIX 2 2 SER A 15 ALA A 27 1 13
HELIX 3 3 CYS A 32 LEU A 37 1 6
HELIX 4 4 PRO A 38 ASN A 44 5 7
HELIX 5 5 PHE A 52 ARG A 56 5 5
HELIX 6 6 THR A 91 LYS A 103 1 13
HELIX 7 7 PRO A 188 SER A 201 1 14
HELIX 8 8 GLY A 220 ARG A 238 1 19
HELIX 9 9 ASP A 240 VAL A 244 5 5
HELIX 10 10 ASP A 245 ARG A 254 1 10
HELIX 11 11 THR A 263 MET A 282 1 20
SHEET 1 A 8 ALA A 69 MET A 74 0
SHEET 2 A 8 ARG A 79 THR A 84 -1 O TYR A 81 N ILE A 72
SHEET 3 A 8 VAL A 211 HIS A 214 1 O VAL A 213 N ILE A 82
SHEET 4 A 8 GLY A 106 MET A 109 1 N VAL A 108 O VAL A 212
SHEET 5 A 8 GLU A 167 TYR A 176 1 O PHE A 174 N VAL A 107
SHEET 6 A 8 TYR A 153 ASN A 162 -1 N ARG A 156 O HIS A 173
SHEET 7 A 8 LEU A 140 ILE A 149 -1 N SER A 146 O GLN A 157
SHEET 8 A 8 MET A 133 PHE A 135 -1 N PHE A 135 O LEU A 140
SHEET 1 B 2 MET A 114 GLU A 115 0
SHEET 2 B 2 SER A 118 LEU A 119 -1 O SER A 118 N GLU A 115
SITE 1 AC1 15 TYR A 46 LYS A 120 TRP A 179 CYS A 215
SITE 2 AC1 15 SER A 216 ALA A 217 GLY A 218 ILE A 219
SITE 3 AC1 15 GLY A 220 ARG A 221 GLN A 262 THR A 263
SITE 4 AC1 15 GLN A 266 HOH A 556 HOH A 661
CRYST1 88.614 88.614 105.167 90.00 90.00 120.00 P 31 2 1 6
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 0.011285 0.006515 0.000000 0.00000
SCALE2 0.000000 0.013031 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009509 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
