HEADER HYDROLASE 06-JAN-03 1NL9
TITLE POTENT, SELECTIVE PROTEIN TYROSINE PHOSPHATASE 1B INHIBITOR
TITLE 2 COMPOUND 12 USING A LINKED-FRAGMENT STRATEGY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN-TYROSINE PHOSPHATASE, NON-RECEPTOR TYPE
COMPND 3 1;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: PTP1B CATALYTIC DOMAIN;
COMPND 6 SYNONYM: PROTEIN-TYROSINE PHOSPHATASE 1B, PTP-1B;
COMPND 7 EC: 3.1.3.48;
COMPND 8 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 BL21(DE3);
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: PT7-7
KEYWDS PROTEIN TYROSINE PHOSPHATASE FOLD, DUAL-SITE OXAMIC ACID
KEYWDS 2 INHIBITOR BOUND TO P-LOOP, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.G.SZCZEPANKIEWICZ,G.LIU,P.J.HAJDUK,C.ABAD-ZAPATERO,Z.PEI,
AUTHOR 2 Z.XIN,T.LUBBEN,J.M.TREVILLYAN,M.A.STASHKO,S.J.BALLARON,
AUTHOR 3 H.LIANG,F.HUANG,C.W.HUTCHINS,S.W.FESIK,M.R.JIROUSEK
REVDAT 2 24-FEB-09 1NL9 1 VERSN
REVDAT 1 08-APR-03 1NL9 0
JRNL AUTH B.G.SZCZEPANKIEWICZ,G.LIU,P.J.HAJDUK,
JRNL AUTH 2 C.ABAD-ZAPATERO,Z.PEI,Z.XIN,T.LUBBEN,
JRNL AUTH 3 J.M.TREVILLYAN,M.A.STASHKO,S.J.BALLARON,H.LIANG,
JRNL AUTH 4 F.HUANG,C.W.HUTCHINS,S.W.FESIK,M.R.JIROUSEK
JRNL TITL DISCOVERY OF A POTENT, SELECTIVE PROTEIN TYROSINE
JRNL TITL 2 PHOSPHATASE 1B INHIBITOR USING A LINKED-FRAGMENT
JRNL TITL 3 STRATEGY
JRNL REF J.AM.CHEM.SOC. V. 125 4087 2003
JRNL REFN ISSN 0002-7863
JRNL PMID 12670229
JRNL DOI 10.1021/JA0296733
REMARK 1
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
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.77
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) (%) : 84.6
REMARK 3 NUMBER OF REFLECTIONS : 16316
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) : 0.208
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1618
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
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) : 18704
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) (%) : 55.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 924
REMARK 3 BIN R VALUE (WORKING SET) : 0.2590
REMARK 3 BIN FREE R VALUE : 0.3440
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.60
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 110
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.033
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 : 39
REMARK 3 SOLVENT ATOMS : 285
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.90
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) : 0.00000
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) : 0.15
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) : 0.35
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.23
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.20
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.70
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) : 2.020 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.210 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.400 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 5.120 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 48.11
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : 989.PAR
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : 989.TOP
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RESIDUE CYS215, LISTED IN REMARK
REMARK 3 500, CORRESPONDS TO THE ACTIVE SITE CYS WHICH IS KNOWN TO BE
REMARK 3 IN A STRAINED CONFORMATION IN THIS CLASS OF ENZYMES.
REMARK 4
REMARK 4 1NL9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JAN-03.
REMARK 100 THE RCSB ID CODE IS RCSB017974.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-JUL-02
REMARK 200 TEMPERATURE (KELVIN) : 100.0
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 RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : MIRRORS
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 : 19212
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.1
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : 0.07000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 77.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.25800
REMARK 200 R SYM FOR SHELL (I) : 0.25800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.060
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
REMARK 200 REFINEMENT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.22
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 35.30333
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 70.60667
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 70.60667
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 35.30333
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 LYS A 12 45.05 -78.51
REMARK 500 SER A 13 3.13 -154.85
REMARK 500 CYS A 32 53.05 -117.29
REMARK 500 ASP A 63 -71.31 -61.12
REMARK 500 CYS A 121 138.94 -170.07
REMARK 500 SER A 146 163.60 179.18
REMARK 500 CYS A 215 -113.64 -131.10
REMARK 500 ILE A 219 -34.17 -141.85
REMARK 500 ILE A 261 101.20 82.35
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 A 476 DISTANCE = 9.56 ANGSTROMS
REMARK 525 HOH A 552 DISTANCE = 6.86 ANGSTROMS
REMARK 525 HOH A 555 DISTANCE = 9.41 ANGSTROMS
REMARK 525 HOH A 558 DISTANCE = 12.09 ANGSTROMS
REMARK 525 HOH A 568 DISTANCE = 12.43 ANGSTROMS
REMARK 525 HOH A 573 DISTANCE = 7.78 ANGSTROMS
REMARK 525 HOH A 579 DISTANCE = 5.55 ANGSTROMS
REMARK 525 HOH A 582 DISTANCE = 9.11 ANGSTROMS
REMARK 525 HOH A 583 DISTANCE = 11.53 ANGSTROMS
REMARK 525 HOH A 589 DISTANCE = 9.70 ANGSTROMS
REMARK 525 HOH A 612 DISTANCE = 5.01 ANGSTROMS
REMARK 525 HOH A 627 DISTANCE = 9.00 ANGSTROMS
REMARK 525 HOH A 662 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH A 665 DISTANCE = 5.33 ANGSTROMS
REMARK 525 HOH A 673 DISTANCE = 8.74 ANGSTROMS
REMARK 525 HOH A 679 DISTANCE = 5.14 ANGSTROMS
REMARK 525 HOH A 682 DISTANCE = 8.03 ANGSTROMS
REMARK 525 HOH A 683 DISTANCE = 7.55 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 989 A 322
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1NNY RELATED DB: PDB
REMARK 900 TYROSINE PHOSPHATASE 1B COMPLEXED WITH INHIBITOR COMPOUND 23
REMARK 900 RELATED ID: 1NO6 RELATED DB: PDB
REMARK 900 TYROSINE PHOSPHATASE 1B COMPLEXED WITH INHIBITOR COMPOUND 5
DBREF 1NL9 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 989 A 322 39
HETNAM 989 2-{[4-(2-ACETYLAMINO-2-PENTYLCARBAMOYL-ETHYL)-
HETNAM 2 989 NAPHTHALEN-1-YL]-OXALYL-AMINO}-BENZOIC ACID
HETSYN 989 COMPOUND 12, N-ACETYL-4-[(CARBOXYCARBONYL)(2-
HETSYN 2 989 CARBOXYPHENYL)AMINO]-N-PENTYL-1-NAPTHYLALANIAMIDE
FORMUL 2 989 C29 H31 N3 O7
FORMUL 3 HOH *285(H2 O)
HELIX 1 1 MET A 3 LYS A 12 1 10
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 GLN A 102 1 12
HELIX 7 7 PRO A 188 GLY A 202 1 15
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 GLY A 283 1 21
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 THR A 168 TYR A 176 1 O PHE A 174 N VAL A 107
SHEET 6 A 8 TYR A 153 ASN A 162 -1 N THR A 154 O HIS A 175
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 22 TYR A 46 ASP A 48 LYS A 120 TRP A 179
SITE 2 AC1 22 CYS A 215 SER A 216 ALA A 217 GLY A 218
SITE 3 AC1 22 ILE A 219 GLY A 220 ARG A 221 GLN A 262
SITE 4 AC1 22 THR A 263 GLN A 266 GLY A 283 HOH A 426
SITE 5 AC1 22 HOH A 451 HOH A 458 HOH A 525 HOH A 581
SITE 6 AC1 22 HOH A 601 HOH A 628
CRYST1 88.730 88.730 105.910 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 0.011270 0.006507 0.000000 0.00000
SCALE2 0.000000 0.013014 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009442 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
