HEADER HYDROLASE 04-MAY-06 2CM3
TITLE STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B (C2)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 2-298;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS POLYMORPHISM, PHOSPHORYLATION, PROTEIN PHOSPHATASE, ENDOPLASMIC
KEYWDS 2 RETICULUM, OXIDATION, HYDROLASE, ACETYLATION, PHOSPHATASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.J.ALA,L.GONNEVILLE,M.C.HILLMAN,M.BECKER-PASHA,M.WEI,B.G.REID,
AUTHOR 2 R.KLABE,E.W.YUE,B.WAYLAND,B.DOUTY,A.P.COMBS,P.POLAM,Z.WASSERMAN,
AUTHOR 3 M.BOWER,T.C.BURN,G.F.HOLLIS,R.WYNN
REVDAT 5 13-DEC-23 2CM3 1 LINK
REVDAT 4 05-JUL-17 2CM3 1 REMARK
REVDAT 3 24-FEB-09 2CM3 1 VERSN
REVDAT 2 25-OCT-06 2CM3 1 JRNL
REVDAT 1 17-AUG-06 2CM3 0
JRNL AUTH P.J.ALA,L.GONNEVILLE,M.C.HILLMAN,M.BECKER-PASHA,M.WEI,
JRNL AUTH 2 B.G.REID,R.KLABE,E.W.YUE,B.WAYLAND,B.DOUTY,P.POLAM,
JRNL AUTH 3 Z.WASSERMAN,M.BOWER,A.P.COMBS,T.C.BURN,G.F.HOLLIS,R.WYNN
JRNL TITL STRUCTURAL BASIS FOR INHIBITION OF PROTEIN-TYROSINE
JRNL TITL 2 PHOSPHATASE 1B BY ISOTHIAZOLIDINONE HETEROCYCLIC PHOSPHONATE
JRNL TITL 3 MIMETICS.
JRNL REF J.BIOL.CHEM. V. 281 32784 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16916797
JRNL DOI 10.1074/JBC.M606873200
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNX 2002
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 7.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 3.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 35681
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) : 0.233
REMARK 3 R VALUE (WORKING SET) : 0.233
REMARK 3 FREE R VALUE : 0.295
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.600
REMARK 3 FREE R VALUE TEST SET COUNT : 3649
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
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) : NULL
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) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4474
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 507
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.04900
REMARK 3 B22 (A**2) : -0.02100
REMARK 3 B33 (A**2) : -0.02900
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.24800
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.424
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : 0.80
REMARK 3 BSOL : 280.0
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : ION.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2CM3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-MAY-06.
REMARK 100 THE DEPOSITION ID IS D_1290028648.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 93.0
REMARK 200 PH : 7.00
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 MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : BLUE CONFOCAL MAX-FLUX MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR
REMARK 200 DATA SCALING SOFTWARE : CRYSTALCLEAR
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38991
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 27.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.75
REMARK 200 R MERGE FOR SHELL (I) : 0.14000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNX
REMARK 200 STARTING MODEL: PDB ENTRY 1EEO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12-16% PEG 3000, 100 MM HEPES PH 7.0
REMARK 280 -8.0, 200 MM MAGNESIUM ACETATE, 2 MM TCEP, PH 7.00
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 53.42500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.75000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 53.42500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 47.75000
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 400
REMARK 400 COMPOUND
REMARK 400 MAY PLAY AN IMPORTANT ROLE IN CKII- AND P60C-SRC-INDUCED
REMARK 400 SIGNAL TRANSDUCTION CASCADES (BY SIMILARITY).
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 -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 HIS A 1
REMARK 465 GLU A 2
REMARK 465 MET A 3
REMARK 465 GLU A 4
REMARK 465 LYS A 5
REMARK 465 GLU A 6
REMARK 465 MET A 282
REMARK 465 GLY A 283
REMARK 465 ASP A 284
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 MET B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 HIS B 1
REMARK 465 GLU B 2
REMARK 465 MET B 3
REMARK 465 GLU B 4
REMARK 465 LYS B 5
REMARK 465 GLU B 6
REMARK 465 MET B 282
REMARK 465 GLY B 283
REMARK 465 ASP B 284
REMARK 465 SER B 285
REMARK 465 SER B 286
REMARK 465 VAL B 287
REMARK 465 GLN B 288
REMARK 465 ASP B 289
REMARK 465 GLN B 290
REMARK 465 TRP B 291
REMARK 465 LYS B 292
REMARK 465 GLU B 293
REMARK 465 LEU B 294
REMARK 465 SER B 295
REMARK 465 HIS B 296
REMARK 465 GLU B 297
REMARK 465 ASP B 298
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 ILE A 281 CA C O CB CG1 CG2 CD1
REMARK 470 ILE B 281 CA C O CB CG1 CG2 CD1
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 PRO A 206 C - N - CA ANGL. DEV. = 11.2 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 LYS A 12 -71.79 -57.55
REMARK 500 SER A 13 7.97 -65.47
REMARK 500 VAL A 113 -8.32 -55.85
REMARK 500 LYS A 116 -133.40 84.14
REMARK 500 SER A 118 -135.10 -86.15
REMARK 500 LEU A 119 108.08 -171.79
REMARK 500 LYS A 131 71.62 -117.75
REMARK 500 GLN A 166 13.49 54.87
REMARK 500 ALA A 189 -72.55 -45.94
REMARK 500 CYS A 215 -128.73 -131.92
REMARK 500 ILE A 219 -32.52 -138.00
REMARK 500 MET A 235 -9.20 -57.75
REMARK 500 SER A 242 8.81 -153.16
REMARK 500 ILE A 261 100.81 74.17
REMARK 500 LYS A 279 30.65 -95.27
REMARK 500 ALA B 27 130.28 -39.32
REMARK 500 CYS B 121 134.97 -176.68
REMARK 500 CYS B 215 -139.98 -147.15
REMARK 500 ILE B 219 -31.70 -142.31
REMARK 500 VAL B 244 97.88 -67.08
REMARK 500 ILE B 261 100.28 76.96
REMARK 500 PHE B 280 -171.45 82.38
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 A2004 DISTANCE = 6.17 ANGSTROMS
REMARK 525 HOH A2055 DISTANCE = 6.42 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1282 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 54 O
REMARK 620 2 HOH A2070 O 72.1
REMARK 620 3 HOH A2071 O 92.0 80.2
REMARK 620 4 HOH A2072 O 79.7 71.6 151.7
REMARK 620 5 HOH B2149 O 144.6 73.4 89.9 82.1
REMARK 620 6 HOH B2152 O 75.9 136.4 72.2 130.1 137.6
REMARK 620 7 HOH B2154 O 146.0 134.1 75.7 124.9 68.2 70.2
REMARK 620 8 HOH B2155 O 93.0 141.7 136.8 71.1 109.4 67.6 76.5
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B1282 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A2148 O
REMARK 620 2 HOH A2152 O 76.2
REMARK 620 3 HIS B 54 O 101.8 150.9
REMARK 620 4 HOH B2077 O 150.8 87.3 81.1
REMARK 620 5 HOH B2079 O 126.1 135.9 68.9 82.4
REMARK 620 6 HOH B2080 O 59.3 117.7 83.6 148.8 66.8
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A1282
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B1282
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1A5Y RELATED DB: PDB
REMARK 900 PROTEIN TYROSINE PHOSPHATASE 1B CYSTEINYL- PHOSPHATEINTERMEDIATE
REMARK 900 RELATED ID: 1AAX RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1BCOMPLEXED WITH
REMARK 900 TWO BIS(PARA- PHOSPHOPHENYL)METHANE (BPPM)MOLECULES
REMARK 900 RELATED ID: 1BZC RELATED DB: PDB
REMARK 900 HUMAN PTP1B CATALYTIC DOMAIN COMPLEXED WITH TPI
REMARK 900 RELATED ID: 1BZH RELATED DB: PDB
REMARK 900 CYCLIC PEPTIDE INHIBITOR OF HUMAN PTP1B
REMARK 900 RELATED ID: 1BZJ RELATED DB: PDB
REMARK 900 HUMAN PTP1B COMPLEXED WITH TPICOOH
REMARK 900 RELATED ID: 1C83 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1BCOMPLEXED WITH
REMARK 900 6-(OXALYL-AMINO )-1H-INDOLE-5-CARBOXYLIC ACID
REMARK 900 RELATED ID: 1C84 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1BCOMPLEXED WITH
REMARK 900 3-(OXALYL-AMINO )-NAPHTHALENE-2-CARBOXLIC ACID
REMARK 900 RELATED ID: 1C85 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1BCOMPLEXED WITH
REMARK 900 2-(OXALYL-AMINO )-BENZOIC ACID
REMARK 900 RELATED ID: 1C86 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B (R47V,D48N)
REMARK 900 COMPLEXED WITH 2 -(OXALYL-AMINO-4,7-DIHYDRO-5H-THIENO[2, 3-C]PYRAN-
REMARK 900 3-CARBOXYLIC ACID
REMARK 900 RELATED ID: 1C87 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1BCOMPLEXED WITH
REMARK 900 2-(OXALYL-AMINO- 4,7-DIHYDRO-5H-THIENO[2,3-C]PYRAN-3- CARBOXYLIC
REMARK 900 ACID
REMARK 900 RELATED ID: 1C88 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1BCOMPLEXED WITH
REMARK 900 2-(OXALYL-AMINO )-4,5,6,7-TETRAHYDRO-THIENO[2,3-C] PYRIDINE-3-
REMARK 900 CARBOXYLIC ACID
REMARK 900 RELATED ID: 1ECV RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1BCOMPLEXED WITH
REMARK 900 5-IODO-2-( OXALYL-AMINO)-BENZOIC ACID
REMARK 900 RELATED ID: 1EEN RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1BCOMPLEXED WITH
REMARK 900 ACETYL-D-A-D- BPA-PTYR-L-I-P-Q-Q-G
REMARK 900 RELATED ID: 1EEO RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1BCOMPLEXED WITH
REMARK 900 ACETYL-E-L-E- F-PTYR-M-D-Y-E-NH2
REMARK 900 RELATED ID: 1G1F RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1BCOMPLEXED WITH
REMARK 900 A TRI- PHOSPHORYLATED PEPTIDE (RDI(PTR)ETD(PTR)(PTR )RK) FROM THE
REMARK 900 INSULIN RECEPTOR KINASE
REMARK 900 RELATED ID: 1G1G RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1BCOMPLEXED WITH
REMARK 900 A MONO- PHOSPHORYLATED PEPTIDE (ETDY(PTR)RKGGKGLL) FROM THE INSULIN
REMARK 900 RECEPTOR KINASE
REMARK 900 RELATED ID: 1G1H RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1BCOMPLEXED WITH
REMARK 900 A BIS- PHOSPHORYLATED PEPTIDE (ETD(PTR)(PTR)RKGGKGLL ) FROM THE
REMARK 900 INSULIN RECEPTOR KINASE
REMARK 900 RELATED ID: 1G7F RELATED DB: PDB
REMARK 900 HUMAN PTP1B CATALYTIC DOMAIN COMPLEXED WITH PNU177496
REMARK 900 RELATED ID: 1G7G RELATED DB: PDB
REMARK 900 HUMAN PTP1B CATALYTIC DOMAIN COMPLEXES WITH PNU179326
REMARK 900 RELATED ID: 1GFY RELATED DB: PDB
REMARK 900 RESIDUE 259 IS A KEY DETERMINANT OF SUBSTRATE SPECIFICITYOF PROTEIN-
REMARK 900 TYROSINE PHOSPHATASE 1B AND ALPHA
REMARK 900 RELATED ID: 1I57 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF APO HUMAN PTP1B (C215S ) MUTANT
REMARK 900 RELATED ID: 1JF7 RELATED DB: PDB
REMARK 900 HUMAN PTP1B CATALYTIC DOMAIN COMPLEXED WITH PNU177836
REMARK 900 RELATED ID: 1KAK RELATED DB: PDB
REMARK 900 HUMAN TYROSINE PHOSPHATASE 1B COMPLEXED WITH AN INHIBITOR
REMARK 900 RELATED ID: 1KAV RELATED DB: PDB
REMARK 900 HUMAN TYROSINE PHOSPHATASE 1B COMPLEXED WITH AN INHIBITOR
REMARK 900 RELATED ID: 1L8G RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PTP1B COMPLEXED WITH 7 -(1,1-DIOXO-1H-BENZO[D]
REMARK 900 ISOTHIAZOL-3- YLOXYMETHYL)-2-(OXALYL-AMINO)-4,7-DIHYDRO- 5H-
REMARK 900 THIENO[2,3-C]PYRAN-3-CARBOXYLIC ACID
REMARK 900 RELATED ID: 1LQF RELATED DB: PDB
REMARK 900 STRUCTURE OF PTP1B IN COMPLEX WITH A PEPTIDICBISPHOSPHONATE
REMARK 900 INHIBITOR
REMARK 900 RELATED ID: 1NL9 RELATED DB: PDB
REMARK 900 POTENT, SELECTIVE PROTEIN TYROSINE PHOSPHATASE 1B INHIBITORCOMPOUND
REMARK 900 12 USING A LINKED- FRAGMENT STRATEGY
REMARK 900 RELATED ID: 1NNY RELATED DB: PDB
REMARK 900 POTENT, SELECTIVE PROTEIN TYROSINE PHOSPHATASE 1B INHIBITORCOMPOUND
REMARK 900 23 USING A LINKED- FRAGMENT STRATEGY
REMARK 900 RELATED ID: 1NO6 RELATED DB: PDB
REMARK 900 POTENT, SELECTIVE PROTEIN TYROSINE PHOSPHATASE 1B INHIBITORCOMPOUND
REMARK 900 5 USING A LINKED- FRAGMENT STRATEGY
REMARK 900 RELATED ID: 1NWE RELATED DB: PDB
REMARK 900 PTP1B R47C MODIFIED AT C47 WITH N-[4-(2 -{2-[3-(2-BROMO-ACETYLAMINO)
REMARK 900 -PROPIONYLAMINO ]-3-HYDROXY-PROPIONYLAMINO}-ETHYL)-PHENYL]-
REMARK 900 OXALAMIC ACID
REMARK 900 RELATED ID: 1NWL RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE PTP1B COMPLEXED WITH SP7343-SP7964,A PTYR
REMARK 900 MIMETIC
REMARK 900 RELATED ID: 1NZ7 RELATED DB: PDB
REMARK 900 POTENT, SELECTIVE INHIBITORS OF PROTEIN TYROSINEPHOSPHATASE 1B
REMARK 900 USING A SECOND PHOSPHOTYROSINE BINDING SITE,COMPLEXED WITH COMPOUND
REMARK 900 19.
REMARK 900 RELATED ID: 1OEM RELATED DB: PDB
REMARK 900 PTP1B WITH THE CATALYTIC CYSTEINE OXIDIZED TO A SULFENYL-AMIDE BOND
REMARK 900 RELATED ID: 1OEO RELATED DB: PDB
REMARK 900 PTP1B WITH THE CATALYTIC CYSTEINE OXIDIZED TO SULFONIC ACID
REMARK 900 RELATED ID: 1OES RELATED DB: PDB
REMARK 900 OXIDATION STATE OF PROTEIN TYROSINE PHOSPHATASE 1B
REMARK 900 RELATED ID: 1OET RELATED DB: PDB
REMARK 900 OXIDATION STATE OF PROTEIN TYROSINE PHOSPHATASE 1B
REMARK 900 RELATED ID: 1OEU RELATED DB: PDB
REMARK 900 OXIDATION STATE OF PROTEIN TYROSINE PHOSPHATASE 1B
REMARK 900 RELATED ID: 1OEV RELATED DB: PDB
REMARK 900 OXIDATION STATE OF PROTEIN TYROSINE PHOSPHATASE 1B
REMARK 900 RELATED ID: 1ONY RELATED DB: PDB
REMARK 900 OXALYL-ARYL-AMINO BENZOIC ACID INHIBITORS OF PTP1B,COMPOUND 17
REMARK 900 RELATED ID: 1ONZ RELATED DB: PDB
REMARK 900 OXALYL-ARYL-AMINO BENZOIC ACID INHIBITORS OF PTP1B,COMPOUND 8B
REMARK 900 RELATED ID: 1PA1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE C215D MUTANT OF PROTEIN
REMARK 900 TYROSINEPHOSPHATASE 1B
REMARK 900 RELATED ID: 1PH0 RELATED DB: PDB
REMARK 900 NON-CARBOXYLIC ACID-CONTAINING INHIBITOR OF PTP1B TARGETINGTHE
REMARK 900 SECOND PHOSPHOTYROSINE SITE
REMARK 900 RELATED ID: 1PTT RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1BCOMPLEXED WITH
REMARK 900 PHOSPHOTYROSINE- CONTAINING TETRA-PEPTIDE(AC-DEPYL-NH2)
REMARK 900 RELATED ID: 1PTU RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1BCOMPLEXED WITH
REMARK 900 PHOSPHOTYROSINE- CONTAINING HEXA-PEPTIDE(DADEPYL-NH2)
REMARK 900 RELATED ID: 1PTV RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1BCOMPLEXED WITH
REMARK 900 PHOSPHOTYROSINE
REMARK 900 RELATED ID: 1PTY RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1BCOMPLEXED WITH
REMARK 900 TWO PHOSPHOTYROSINE MOLECULES
REMARK 900 RELATED ID: 1PXH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B WITHPOTENT AND
REMARK 900 SELECTIVE BIDENTATE INHIBITOR COMPOUND 2
REMARK 900 RELATED ID: 1PYN RELATED DB: PDB
REMARK 900 DUAL-SITE POTENT, SELECTIVE PROTEIN TYROSINE PHOSPHATASE
REMARK 900 1BINHIBITOR USING A LINKED FRAGMENT STRATEGY AND A MALONATEHEAD ON
REMARK 900 THE FIRST SITE
REMARK 900 RELATED ID: 1Q1M RELATED DB: PDB
REMARK 900 A HIGHLY EFFICIENT APPROACH TO A SELECTIVE AND CELL ACTIVEPTP1B
REMARK 900 INHIBITORS
REMARK 900 RELATED ID: 1Q6J RELATED DB: PDB
REMARK 900 THE STRUCTURE OF PHOSPHOTYROSINE PHOSPHATASE 1B IN COMPLEXWITH
REMARK 900 COMPOUND 2
REMARK 900 RELATED ID: 1Q6M RELATED DB: PDB
REMARK 900 THE STRUCTURE OF PHOSPHOTYROSINE PHOSPHATASE 1B IN COMPLEXWITH
REMARK 900 COMPOUND 3
REMARK 900 RELATED ID: 1Q6N RELATED DB: PDB
REMARK 900 THE STRUCTURE OF PHOSPHOTYROSINE PHOSPHATASE 1B IN COMPLEXWITH
REMARK 900 COMPOUND 4
REMARK 900 RELATED ID: 1Q6P RELATED DB: PDB
REMARK 900 THE STRUCTURE OF PHOSPHOTYROSINE PHOSPHATASE 1B IN COMPLEXWITH
REMARK 900 COMPOUND 6
REMARK 900 RELATED ID: 1Q6S RELATED DB: PDB
REMARK 900 THE STRUCTURE OF PHOSPHOTYROSINE PHOSPHATASE 1B IN COMPLEXWITH
REMARK 900 COMPOUND 9
REMARK 900 RELATED ID: 1Q6T RELATED DB: PDB
REMARK 900 THE STRUCTURE OF PHOSPHOTYROSINE PHOSPHATASE 1B IN COMPLEXWITH
REMARK 900 COMPOUND 11
REMARK 900 RELATED ID: 1QXK RELATED DB: PDB
REMARK 900 MONOACID-BASED, CELL PERMEABLE, SELECTIVE INHIBITORS OFPROTEIN
REMARK 900 TYROSINE PHOSPHATASE 1B
REMARK 900 RELATED ID: 1SUG RELATED DB: PDB
REMARK 900 1.95 A STRUCTURE OF APO PROTEIN TYROSINE PHOSPHATASE 1B
REMARK 900 RELATED ID: 1T48 RELATED DB: PDB
REMARK 900 ALLOSTERIC INHIBITION OF PROTEIN TYROSINE PHOSPHATASE 1B
REMARK 900 RELATED ID: 1T49 RELATED DB: PDB
REMARK 900 ALLOSTERIC INHIBITION OF PROTEIN TYROSINE PHOSPHATASE 1B
REMARK 900 RELATED ID: 1T4J RELATED DB: PDB
REMARK 900 ALLOSTERIC INHIBITION OF PROTEIN TYROSINE PHOSPHATASE 1B
REMARK 900 RELATED ID: 1WAX RELATED DB: PDB
REMARK 900 PROTEIN TYROSINE PHOSPHATASE 1B WITH ACTIVE SITE INHIBITOR
REMARK 900 RELATED ID: 1XBO RELATED DB: PDB
REMARK 900 PTP1B COMPLEXED WITH ISOXAZOLE CARBOXYLIC ACID
REMARK 900 RELATED ID: 2AZR RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PTP1B WITH BICYCLIC THIOPHENE INHIBITOR
REMARK 900 RELATED ID: 2B07 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PTP1B WITH TRICYCLIC THIOPHENEINHIBITOR.
REMARK 900 RELATED ID: 2B4S RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A COMPLEX BETWEEN PTP1B AND THEINSULIN
REMARK 900 RECEPTOR TYROSINE KINASE
REMARK 900 RELATED ID: 2BGD RELATED DB: PDB
REMARK 900 STRUCTURE-BASED DESIGN OF PROTEIN TYROSINE PHOSPHATASE-1B INHIBITORS
REMARK 900 RELATED ID: 2BGE RELATED DB: PDB
REMARK 900 STRUCTURE-BASED DESIGN OF PROTEIN TYROSINE PHOSPHATASE-1B INHIBITORS
REMARK 900 RELATED ID: 2CM2 RELATED DB: PDB
REMARK 900 STRUCTURAL OF PROTEIN TYROSINE PHOSPHATASE 1B (P212121)
REMARK 900 RELATED ID: 2CM7 RELATED DB: PDB
REMARK 900 STRUCTURAL BASIS FOR INHIBITION OF PROTEIN TYROSINE PHOSPHATASE 1B
REMARK 900 BY ISOTHIAZOLIDINONE HETEROCYCLIC PHOSPHONATE MIMETICS
REMARK 900 RELATED ID: 2CM8 RELATED DB: PDB
REMARK 900 STRUCTURAL BASIS FOR INHIBITION OF PROTEIN TYROSINE PHOSPHATASE 1B
REMARK 900 BY ISOTHIAZOLIDINONE HETEROCYCLIC PHOSPHONATE MIMETICS
REMARK 900 RELATED ID: 2CMA RELATED DB: PDB
REMARK 900 STRUCTURAL BASIS FOR INHIBITION OF PROTEIN TYROSINE PHOSPHATASE 1B
REMARK 900 BY ISOTHIAZOLIDINONE HETEROCYCLIC PHOSPHONATE MIMETICS
REMARK 900 RELATED ID: 2CMB RELATED DB: PDB
REMARK 900 STRUCTURAL BASIS FOR INHIBITION OF PROTEIN TYROSINE PHOSPHATASE 1B
REMARK 900 BY ISOTHIAZOLIDINONE HETEROCYCLIC PHOSPHONATE MIMETICS
REMARK 900 RELATED ID: 2CMC RELATED DB: PDB
REMARK 900 STRUCTURAL BASIS FOR INHIBITION OF PROTEIN TYROSINE PHOSPHATASE 1B
REMARK 900 BY ISOTHIAZOLIDINONE HETEROCYCLIC PHOSPHONATE MIMETICS
REMARK 900 RELATED ID: 2CNE RELATED DB: PDB
REMARK 900 STRUCTURAL INSIGHTS INTO THE DESIGN OF NONPEPTIDIC
REMARK 900 ISOTHIAZOLIDINONE-CONTAINING INHIBITORS OF PROTEIN TYROSINE
REMARK 900 PHOSPHATASE 1B
REMARK 900 RELATED ID: 2CNF RELATED DB: PDB
REMARK 900 STRUCTURAL INSIGHTS INTO THE DESIGN OF NONPEPTIDIC
REMARK 900 ISOTHIAZOLIDINONE-CONTAINING INHIBITORS OF PROTEIN TYROSINE
REMARK 900 PHOSPHATASE 1B
REMARK 900 RELATED ID: 2CNG RELATED DB: PDB
REMARK 900 STRUCTURAL INSIGHTS INTO THE DESIGN OF NONPEPTIDIC
REMARK 900 ISOTHIAZOLIDINONE-CONTAINING INHIBITORS OF PROTEIN TYROSINE
REMARK 900 PHOSPHATASE 1B
REMARK 900 RELATED ID: 2CNH RELATED DB: PDB
REMARK 900 STRUCTURAL INSIGHTS INTO THE DESIGN OF NONPEPTIDIC
REMARK 900 ISOTHIAZOLIDINONE-CONTAINING INHIBITORS OF PROTEIN TYROSINE
REMARK 900 PHOSPHATASE 1B
REMARK 900 RELATED ID: 2CNI RELATED DB: PDB
REMARK 900 STRUCTURAL INSIGHTS INTO THE DESIGN OF NONPEPTIDIC
REMARK 900 ISOTHIAZOLIDINONE-CONTAINING INHIBITORS OF PROTEIN TYROSINE
REMARK 900 PHOSPHATASE 1B
REMARK 900 RELATED ID: 2F6F RELATED DB: PDB
REMARK 900 THE STRUCTURE OF THE S295F MUTANT OF HUMAN PTP1B
REMARK 900 RELATED ID: 2F6T RELATED DB: PDB
REMARK 900 PROTEIN TYROSINE PHOSPHATASE 1B WITH SULFAMIC ACIDINHIBITORS
REMARK 900 RELATED ID: 2F6V RELATED DB: PDB
REMARK 900 PROTEIN TYROSINE PHOSPHATASE 1B WITH SULFAMIC ACIDINHIBITORS
REMARK 900 RELATED ID: 2F6W RELATED DB: PDB
REMARK 900 PROTEIN TYROSINE PHOSPHATASE 1B WITH SULFAMIC ACIDINHIBITORS
REMARK 900 RELATED ID: 2F6Y RELATED DB: PDB
REMARK 900 PROTEIN TYROSINE PHOSPHATASE 1B WITH SULFAMIC ACIDINHIBITORS
REMARK 900 RELATED ID: 2F6Z RELATED DB: PDB
REMARK 900 PROTEIN TYROSINE PHOSPHATASE 1B WITH SULFAMIC ACIDINHIBITORS
REMARK 900 RELATED ID: 2F70 RELATED DB: PDB
REMARK 900 PROTEIN TYROSINE PHOSPHATASE 1B WITH SULFAMIC ACIDINHIBITORS
REMARK 900 RELATED ID: 2F71 RELATED DB: PDB
REMARK 900 PROTEIN TYROSINE PHOSPHATASE 1B WITH SULFAMIC ACIDINHIBITORS
REMARK 900 RELATED ID: 2FJM RELATED DB: PDB
REMARK 900 THE STRUCTURE OF PHOSPHOTYROSINE PHOSPHATASE 1B IN COMPLEXWITH
REMARK 900 COMPOUND 2
REMARK 900 RELATED ID: 2FJN RELATED DB: PDB
REMARK 900 THE STRUCTURE OF PHOSPHOTYROSINE PHOSPHATASE 1B IN COMPLEXWITH
REMARK 900 COMPOUND 2
REMARK 900 RELATED ID: 2HNP RELATED DB: PDB
REMARK 900 RELATED ID: 2HNQ RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE USED IN THE CRYSTALLIZATION EXPERIMENTS WAS
REMARK 999 1-6XHIS-298. WHICH MEANS THAT THERE ARE SIX HISTIDINES
REMARK 999 INSERTED BETWEEN THE FIRST AND SECOND RESIDUES. THE STRUCTURE
REMARK 999 ONLY CONTAINS RESIDUES 7 TO 280
DBREF 2CM3 A -5 -5 UNP P18031 PTN1_HUMAN 1 1
DBREF 2CM3 A -4 1 PDB 2CM3 2CM3 -4 1
DBREF 2CM3 A 2 298 UNP P18031 PTN1_HUMAN 2 298
DBREF 2CM3 B -5 -5 UNP P18031 PTN1_HUMAN 1 1
DBREF 2CM3 B -4 1 PDB 2CM3 2CM3 -4 1
DBREF 2CM3 B 2 298 UNP P18031 PTN1_HUMAN 2 298
SEQRES 1 A 304 MET HIS HIS HIS HIS HIS HIS GLU MET GLU LYS GLU PHE
SEQRES 2 A 304 GLU GLN ILE ASP LYS SER GLY SER TRP ALA ALA ILE TYR
SEQRES 3 A 304 GLN ASP ILE ARG HIS GLU ALA SER ASP PHE PRO CYS ARG
SEQRES 4 A 304 VAL ALA LYS LEU PRO LYS ASN LYS ASN ARG ASN ARG TYR
SEQRES 5 A 304 ARG ASP VAL SER PRO PHE ASP HIS SER ARG ILE LYS LEU
SEQRES 6 A 304 HIS GLN GLU ASP ASN ASP TYR ILE ASN ALA SER LEU ILE
SEQRES 7 A 304 LYS MET GLU GLU ALA GLN ARG SER TYR ILE LEU THR GLN
SEQRES 8 A 304 GLY PRO LEU PRO ASN THR CYS GLY HIS PHE TRP GLU MET
SEQRES 9 A 304 VAL TRP GLU GLN LYS SER ARG GLY VAL VAL MET LEU ASN
SEQRES 10 A 304 ARG VAL MET GLU LYS GLY SER LEU LYS CYS ALA GLN TYR
SEQRES 11 A 304 TRP PRO GLN LYS GLU GLU LYS GLU MET ILE PHE GLU ASP
SEQRES 12 A 304 THR ASN LEU LYS LEU THR LEU ILE SER GLU ASP ILE LYS
SEQRES 13 A 304 SER TYR TYR THR VAL ARG GLN LEU GLU LEU GLU ASN LEU
SEQRES 14 A 304 THR THR GLN GLU THR ARG GLU ILE LEU HIS PHE HIS TYR
SEQRES 15 A 304 THR THR TRP PRO ASP PHE GLY VAL PRO GLU SER PRO ALA
SEQRES 16 A 304 SER PHE LEU ASN PHE LEU PHE LYS VAL ARG GLU SER GLY
SEQRES 17 A 304 SER LEU SER PRO GLU HIS GLY PRO VAL VAL VAL HIS CYS
SEQRES 18 A 304 SER ALA GLY ILE GLY ARG SER GLY THR PHE CYS LEU ALA
SEQRES 19 A 304 ASP THR CYS LEU LEU LEU MET ASP LYS ARG LYS ASP PRO
SEQRES 20 A 304 SER SER VAL ASP ILE LYS LYS VAL LEU LEU GLU MET ARG
SEQRES 21 A 304 LYS PHE ARG MET GLY LEU ILE GLN THR ALA ASP GLN LEU
SEQRES 22 A 304 ARG PHE SER TYR LEU ALA VAL ILE GLU GLY ALA LYS PHE
SEQRES 23 A 304 ILE MET GLY ASP SER SER VAL GLN ASP GLN TRP LYS GLU
SEQRES 24 A 304 LEU SER HIS GLU ASP
SEQRES 1 B 304 MET HIS HIS HIS HIS HIS HIS GLU MET GLU LYS GLU PHE
SEQRES 2 B 304 GLU GLN ILE ASP LYS SER GLY SER TRP ALA ALA ILE TYR
SEQRES 3 B 304 GLN ASP ILE ARG HIS GLU ALA SER ASP PHE PRO CYS ARG
SEQRES 4 B 304 VAL ALA LYS LEU PRO LYS ASN LYS ASN ARG ASN ARG TYR
SEQRES 5 B 304 ARG ASP VAL SER PRO PHE ASP HIS SER ARG ILE LYS LEU
SEQRES 6 B 304 HIS GLN GLU ASP ASN ASP TYR ILE ASN ALA SER LEU ILE
SEQRES 7 B 304 LYS MET GLU GLU ALA GLN ARG SER TYR ILE LEU THR GLN
SEQRES 8 B 304 GLY PRO LEU PRO ASN THR CYS GLY HIS PHE TRP GLU MET
SEQRES 9 B 304 VAL TRP GLU GLN LYS SER ARG GLY VAL VAL MET LEU ASN
SEQRES 10 B 304 ARG VAL MET GLU LYS GLY SER LEU LYS CYS ALA GLN TYR
SEQRES 11 B 304 TRP PRO GLN LYS GLU GLU LYS GLU MET ILE PHE GLU ASP
SEQRES 12 B 304 THR ASN LEU LYS LEU THR LEU ILE SER GLU ASP ILE LYS
SEQRES 13 B 304 SER TYR TYR THR VAL ARG GLN LEU GLU LEU GLU ASN LEU
SEQRES 14 B 304 THR THR GLN GLU THR ARG GLU ILE LEU HIS PHE HIS TYR
SEQRES 15 B 304 THR THR TRP PRO ASP PHE GLY VAL PRO GLU SER PRO ALA
SEQRES 16 B 304 SER PHE LEU ASN PHE LEU PHE LYS VAL ARG GLU SER GLY
SEQRES 17 B 304 SER LEU SER PRO GLU HIS GLY PRO VAL VAL VAL HIS CYS
SEQRES 18 B 304 SER ALA GLY ILE GLY ARG SER GLY THR PHE CYS LEU ALA
SEQRES 19 B 304 ASP THR CYS LEU LEU LEU MET ASP LYS ARG LYS ASP PRO
SEQRES 20 B 304 SER SER VAL ASP ILE LYS LYS VAL LEU LEU GLU MET ARG
SEQRES 21 B 304 LYS PHE ARG MET GLY LEU ILE GLN THR ALA ASP GLN LEU
SEQRES 22 B 304 ARG PHE SER TYR LEU ALA VAL ILE GLU GLY ALA LYS PHE
SEQRES 23 B 304 ILE MET GLY ASP SER SER VAL GLN ASP GLN TRP LYS GLU
SEQRES 24 B 304 LEU SER HIS GLU ASP
HET CA A1282 1
HET CA B1282 1
HETNAM CA CALCIUM ION
FORMUL 3 CA 2(CA 2+)
FORMUL 5 HOH *507(H2 O)
HELIX 1 1 PHE A 7 SER A 13 1 7
HELIX 2 2 SER A 15 ALA A 27 1 13
HELIX 3 3 ARG A 33 LEU A 37 5 5
HELIX 4 4 LEU A 37 ASN A 44 5 8
HELIX 5 5 THR A 91 GLN A 102 1 12
HELIX 6 6 PRO A 188 SER A 201 1 14
HELIX 7 7 GLY A 220 ARG A 238 1 19
HELIX 8 8 ASP A 245 LYS A 255 1 11
HELIX 9 9 THR A 263 LYS A 279 1 17
HELIX 10 10 PHE B 7 GLY B 14 1 8
HELIX 11 11 SER B 15 ALA B 27 1 13
HELIX 12 12 LEU B 37 ASN B 44 5 8
HELIX 13 13 THR B 91 GLN B 102 1 12
HELIX 14 14 PRO B 188 SER B 201 1 14
HELIX 15 15 GLY B 220 ARG B 238 1 19
HELIX 16 16 ASP B 245 ARG B 254 1 10
HELIX 17 17 THR B 263 LYS B 279 1 17
SHEET 1 AA 9 ARG A 56 LYS A 58 0
SHEET 2 AA 9 TYR A 66 MET A 74 -1 N ILE A 67 O ILE A 57
SHEET 3 AA 9 ARG A 79 THR A 84 -1 O ARG A 79 N MET A 74
SHEET 4 AA 9 VAL A 211 HIS A 214 1 O VAL A 211 N ILE A 82
SHEET 5 AA 9 GLY A 106 MET A 109 1 O GLY A 106 N VAL A 212
SHEET 6 AA 9 THR A 168 TYR A 176 1 O LEU A 172 N VAL A 107
SHEET 7 AA 9 TYR A 153 ASN A 162 -1 O THR A 154 N HIS A 175
SHEET 8 AA 9 LEU A 140 ILE A 149 -1 O LYS A 141 N GLU A 161
SHEET 9 AA 9 MET A 133 PHE A 135 -1 O MET A 133 N LEU A 142
SHEET 1 BA 9 ARG B 56 LYS B 58 0
SHEET 2 BA 9 TYR B 66 MET B 74 -1 N ILE B 67 O ILE B 57
SHEET 3 BA 9 ARG B 79 GLN B 85 -1 O ARG B 79 N MET B 74
SHEET 4 BA 9 VAL B 211 CYS B 215 1 O VAL B 211 N ILE B 82
SHEET 5 BA 9 GLY B 106 MET B 109 1 O GLY B 106 N VAL B 212
SHEET 6 BA 9 THR B 168 TYR B 176 1 O LEU B 172 N VAL B 107
SHEET 7 BA 9 TYR B 153 ASN B 162 -1 O THR B 154 N HIS B 175
SHEET 8 BA 9 LEU B 140 ILE B 149 -1 O LYS B 141 N GLU B 161
SHEET 9 BA 9 MET B 133 PHE B 135 -1 O MET B 133 N LEU B 142
SHEET 1 BB 2 MET B 114 GLU B 115 0
SHEET 2 BB 2 SER B 118 LEU B 119 -1 O SER B 118 N GLU B 115
LINK O HIS A 54 CA CA A1282 1555 1555 2.38
LINK CA CA A1282 O HOH A2070 1555 1555 2.64
LINK CA CA A1282 O HOH A2071 1555 1555 2.66
LINK CA CA A1282 O HOH A2072 1555 1555 2.54
LINK CA CA A1282 O HOH B2149 1555 1555 2.66
LINK CA CA A1282 O HOH B2152 1555 1555 2.75
LINK CA CA A1282 O HOH B2154 1555 1555 2.45
LINK CA CA A1282 O HOH B2155 1555 1555 2.65
LINK O HOH A2148 CA CA B1282 3454 1555 2.74
LINK O HOH A2152 CA CA B1282 3454 1555 2.83
LINK O HIS B 54 CA CA B1282 1555 1555 2.44
LINK CA CA B1282 O HOH B2077 1555 1555 2.78
LINK CA CA B1282 O HOH B2079 1555 1555 3.04
LINK CA CA B1282 O HOH B2080 1555 1555 2.82
SITE 1 AC1 9 HIS A 54 HOH A2070 HOH A2071 HOH A2072
SITE 2 AC1 9 LYS B 128 HOH B2149 HOH B2152 HOH B2154
SITE 3 AC1 9 HOH B2155
SITE 1 AC2 6 HOH A2148 HOH A2152 HIS B 54 HOH B2077
SITE 2 AC2 6 HOH B2079 HOH B2080
CRYST1 106.850 95.500 70.750 90.00 109.66 90.00 C 1 2 1 8
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 0.009359 0.000000 0.003344 0.00000
SCALE2 0.000000 0.010471 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015009 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
