HEADER HYDROLASE 26-JUN-00 1GFY
TITLE RESIDUE 259 IS A KEY DETERMINANT OF SUBSTRATE SPECIFICITY OF PROTEIN-
TITLE 2 TYROSINE PHOSPHATASE 1B AND ALPHA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (PROTEIN-TYROSINE PHOSPHATASE 1B);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN;
COMPND 5 SYNONYM: PTP1B;
COMPND 6 EC: 3.1.3.48;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: 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: 562
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.F.IVERSEN
REVDAT 6 27-DEC-23 1GFY 1 REMARK
REVDAT 5 03-NOV-21 1GFY 1 REMARK SEQADV
REVDAT 4 07-MAR-18 1GFY 1 REMARK
REVDAT 3 24-FEB-09 1GFY 1 VERSN
REVDAT 2 01-APR-03 1GFY 1 JRNL
REVDAT 1 04-JUL-00 1GFY 0
JRNL AUTH G.H.PETERS,L.F.IVERSEN,S.BRANNER,H.S.ANDERSEN,S.B.MORTENSEN,
JRNL AUTH 2 O.H.OLSEN,K.B.MOLLER,N.P.MOLLER
JRNL TITL RESIDUE 259 IS A KEY DETERMINANT OF SUBSTRATE SPECIFICITY OF
JRNL TITL 2 PROTEIN-TYROSINE PHOSPHATASES 1B AND ALPHA.
JRNL REF J.BIOL.CHEM. V. 275 18201 2000
JRNL REFN ISSN 0021-9258
JRNL PMID 10748206
JRNL DOI 10.1074/JBC.M910273199
REMARK 2
REMARK 2 RESOLUTION. 2.13 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.13
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 26558
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 SET) : 0.191
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 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 : 2417
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 18
REMARK 3 SOLVENT ATOMS : 209
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) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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) : 0.019
REMARK 3 BOND ANGLES (DEGREES) : 2.970
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 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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1GFY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JUN-00.
REMARK 100 THE DEPOSITION ID IS D_1000001478.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX II
REMARK 200 BEAMLINE : I711
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26558
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.130
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : 0.07300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.13
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.17
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.38700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.5
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 34.57600
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 69.15200
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 69.15200
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 34.57600
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 GLU A 2
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 GLN A 21 CG GLN A 21 CD 0.167
REMARK 500 HIS A 25 CG HIS A 25 CD2 0.085
REMARK 500 GLU A 186 CG GLU A 186 CD 0.109
REMARK 500 SER A 201 CB SER A 201 OG 0.078
REMARK 500 SER A 205 CB SER A 205 OG 0.187
REMARK 500 SER A 242 CB SER A 242 OG 0.093
REMARK 500 SER A 285 CB SER A 285 OG 0.112
REMARK 500 HIS A 296 CG HIS A 296 CD2 0.057
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 18 CB - CA - C ANGL. DEV. = -9.4 DEGREES
REMARK 500 HIS A 25 CA - CB - CG ANGL. DEV. = -11.4 DEGREES
REMARK 500 ARG A 33 NE - CZ - NH1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ARG A 45 NE - CZ - NH1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG A 45 NE - CZ - NH2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 VAL A 49 CA - CB - CG1 ANGL. DEV. = 11.3 DEGREES
REMARK 500 PHE A 52 CB - CG - CD1 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ARG A 56 NE - CZ - NH1 ANGL. DEV. = 10.1 DEGREES
REMARK 500 ARG A 56 NE - CZ - NH2 ANGL. DEV. = -10.2 DEGREES
REMARK 500 TYR A 66 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 TYR A 66 CB - CG - CD1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG A 79 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 79 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 TYR A 81 CB - CG - CD1 ANGL. DEV. = -4.6 DEGREES
REMARK 500 SER A 118 CA - CB - OG ANGL. DEV. = -16.3 DEGREES
REMARK 500 CYS A 121 CA - CB - SG ANGL. DEV. = 9.0 DEGREES
REMARK 500 LYS A 131 CD - CE - NZ ANGL. DEV. = 15.7 DEGREES
REMARK 500 THR A 151 CB - CA - C ANGL. DEV. = -17.8 DEGREES
REMARK 500 LEU A 160 CB - CG - CD2 ANGL. DEV. = 10.3 DEGREES
REMARK 500 ASN A 162 CB - CA - C ANGL. DEV. = 13.4 DEGREES
REMARK 500 ARG A 169 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG A 199 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 SER A 205 CB - CA - C ANGL. DEV. = 13.7 DEGREES
REMARK 500 LEU A 234 CB - CG - CD1 ANGL. DEV. = 14.5 DEGREES
REMARK 500 LYS A 237 CA - CB - CG ANGL. DEV. = 13.8 DEGREES
REMARK 500 ARG A 238 NE - CZ - NH1 ANGL. DEV. = 7.9 DEGREES
REMARK 500 ARG A 238 NE - CZ - NH2 ANGL. DEV. = -10.7 DEGREES
REMARK 500 SER A 243 CB - CA - C ANGL. DEV. = -12.3 DEGREES
REMARK 500 ASP A 252 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 MET A 253 CG - SD - CE ANGL. DEV. = -9.9 DEGREES
REMARK 500 ARG A 254 NE - CZ - NH2 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG A 257 CD - NE - CZ ANGL. DEV. = 12.0 DEGREES
REMARK 500 ARG A 268 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 268 NE - CZ - NH2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 LEU A 272 CB - CG - CD1 ANGL. DEV. = 10.4 DEGREES
REMARK 500 ASP A 289 CB - CA - C ANGL. DEV. = 12.5 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 ASP A 63 -74.32 -47.76
REMARK 500 LYS A 103 33.40 70.85
REMARK 500 CYS A 121 146.21 -170.14
REMARK 500 LYS A 131 73.74 -117.83
REMARK 500 SER A 146 178.04 179.14
REMARK 500 PHE A 182 16.61 58.82
REMARK 500 CYS A 215 -136.71 -123.79
REMARK 500 ILE A 219 -50.76 -132.82
REMARK 500 ILE A 261 117.37 77.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 33 0.11 SIDE CHAIN
REMARK 500 ARG A 105 0.15 SIDE CHAIN
REMARK 500 ARG A 112 0.14 SIDE CHAIN
REMARK 500 TYR A 153 0.08 SIDE CHAIN
REMARK 500 ARG A 254 0.15 SIDE CHAIN
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 COL A 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ECV RELATED DB: PDB
REMARK 900 PTP1B COMPLEXED WITH 5-IODO-2-(OXALYL-AMINO)-BENZOIC ACID
REMARK 900 RELATED ID: 1C83 RELATED DB: PDB
REMARK 900 PTP1B COMPLEXED WITH 6-(OXALYL-AMINO)-1H-INDOLE-5-CARBOXYLIC ACID
REMARK 900 RELATED ID: 1C84 RELATED DB: PDB
REMARK 900 PTP1B COMPLEXED WITH 3-(OXALYL-AMINO)-NAPHTHALENE-2-CARBOXLIC ACID
REMARK 900 RELATED ID: 1C85 RELATED DB: PDB
REMARK 900 PTP1B COMPLEXED WITH 2-(OXALYL-AMINO)-BENZOIC ACID
REMARK 900 RELATED ID: 1C86 RELATED DB: PDB
REMARK 900 PTP1B (R47V, D48N) COMPLEXED WITH 2-(OXALYL-AMINO)-4,7-DIHYDRO-5H-
REMARK 900 THIENO[2,3-C]PYRAN-3-CARBOXYLIC ACID
REMARK 900 RELATED ID: 1C87 RELATED DB: PDB
REMARK 900 PTP1B COMPLEXED WITH 2-(OXALYL-AMINO)-4,7-DIHYDRO-5H-THIENO[2,3-C]
REMARK 900 PYRAN-3-CARBOXYLIC ACID
REMARK 900 RELATED ID: 1C88 RELATED DB: PDB
REMARK 900 PTP1B COMPLEXED WITH 2-(OXALYL-AMINO)-4,5,6,7-TETRAHYDRO-THIENO[2,3-
REMARK 900 C]PYRIDINE-3-CARBOXYLIC ACID
DBREF 1GFY A 1 298 UNP P18031 PTN1_HUMAN 1 298
SEQADV 1GFY VAL A 47 UNP P18031 ARG 47 ENGINEERED MUTATION
SEQADV 1GFY ASN A 48 UNP P18031 ASP 48 ENGINEERED MUTATION
SEQADV 1GFY THR A 151 UNP P18031 SER 151 CONFLICT
SEQADV 1GFY ASP A 252 UNP P18031 GLU 252 CONFLICT
SEQADV 1GFY CYS A 258 UNP P18031 MET 258 ENGINEERED MUTATION
SEQADV 1GFY GLN A 259 UNP P18031 GLY 259 ENGINEERED MUTATION
SEQRES 1 A 298 MET GLU MET GLU LYS GLU PHE GLU GLN ILE ASP LYS SER
SEQRES 2 A 298 GLY SER TRP ALA ALA ILE TYR GLN ASP ILE ARG HIS GLU
SEQRES 3 A 298 ALA SER ASP PHE PRO CYS ARG VAL ALA LYS LEU PRO LYS
SEQRES 4 A 298 ASN LYS ASN ARG ASN ARG TYR VAL ASN VAL SER PRO PHE
SEQRES 5 A 298 ASP HIS SER ARG ILE LYS LEU HIS GLN GLU ASP ASN ASP
SEQRES 6 A 298 TYR ILE ASN ALA SER LEU ILE LYS MET GLU GLU ALA GLN
SEQRES 7 A 298 ARG SER TYR ILE LEU THR GLN GLY PRO LEU PRO ASN THR
SEQRES 8 A 298 CYS GLY HIS PHE TRP GLU MET VAL TRP GLU GLN LYS SER
SEQRES 9 A 298 ARG GLY VAL VAL MET LEU ASN ARG VAL MET GLU LYS GLY
SEQRES 10 A 298 SER LEU LYS CYS ALA GLN TYR TRP PRO GLN LYS GLU GLU
SEQRES 11 A 298 LYS GLU MET ILE PHE GLU ASP THR ASN LEU LYS LEU THR
SEQRES 12 A 298 LEU ILE SER GLU ASP ILE LYS THR TYR TYR THR VAL ARG
SEQRES 13 A 298 GLN LEU GLU LEU GLU ASN LEU THR THR GLN GLU THR ARG
SEQRES 14 A 298 GLU ILE LEU HIS PHE HIS TYR THR THR TRP PRO ASP PHE
SEQRES 15 A 298 GLY VAL PRO GLU SER PRO ALA SER PHE LEU ASN PHE LEU
SEQRES 16 A 298 PHE LYS VAL ARG GLU SER GLY SER LEU SER PRO GLU HIS
SEQRES 17 A 298 GLY PRO VAL VAL VAL HIS CYS SER ALA GLY ILE GLY ARG
SEQRES 18 A 298 SER GLY THR PHE CYS LEU ALA ASP THR CYS LEU LEU LEU
SEQRES 19 A 298 MET ASP LYS ARG LYS ASP PRO SER SER VAL ASP ILE LYS
SEQRES 20 A 298 LYS VAL LEU LEU ASP MET ARG LYS PHE ARG CYS GLN LEU
SEQRES 21 A 298 ILE GLN THR ALA ASP GLN LEU ARG PHE SER TYR LEU ALA
SEQRES 22 A 298 VAL ILE GLU GLY ALA LYS PHE ILE MET GLY ASP SER SER
SEQRES 23 A 298 VAL GLN ASP GLN TRP LYS GLU LEU SER HIS GLU ASP
HET COL A 301 18
HETNAM COL 2-(OXALYL-AMINO)-4,7-DIHYDRO-5H-THIENO[2,3-C]THIOPYRAN-
HETNAM 2 COL 3-CARBOXYLIC ACID
FORMUL 2 COL C10 H9 N O5 S2
FORMUL 3 HOH *209(H2 O)
HELIX 1 1 MET A 3 SER A 13 1 11
HELIX 2 2 SER A 15 ALA A 27 1 13
HELIX 3 3 LEU A 37 ASN A 44 5 8
HELIX 4 4 PHE A 52 HIS A 54 5 3
HELIX 5 5 THR A 91 LYS A 103 1 13
HELIX 6 6 SER A 187 SER A 201 1 15
HELIX 7 7 ILE A 219 LYS A 239 1 21
HELIX 8 8 ASP A 240 VAL A 244 5 5
HELIX 9 9 ASP A 245 LYS A 255 1 11
HELIX 10 10 THR A 263 MET A 282 1 20
HELIX 11 11 SER A 285 HIS A 296 1 12
SHEET 1 A 9 ARG A 56 LYS A 58 0
SHEET 2 A 9 TYR A 66 MET A 74 -1 N ILE A 67 O ILE A 57
SHEET 3 A 9 ARG A 79 THR A 84 -1 O ARG A 79 N MET A 74
SHEET 4 A 9 VAL A 211 HIS A 214 1 O VAL A 211 N ILE A 82
SHEET 5 A 9 GLY A 106 MET A 109 1 O GLY A 106 N VAL A 212
SHEET 6 A 9 THR A 168 TYR A 176 1 O LEU A 172 N VAL A 107
SHEET 7 A 9 TYR A 153 ASN A 162 -1 O THR A 154 N HIS A 175
SHEET 8 A 9 LEU A 140 ILE A 149 -1 O LYS A 141 N GLU A 161
SHEET 9 A 9 MET A 133 PHE A 135 -1 N MET A 133 O LEU A 142
SHEET 1 B 2 MET A 114 GLU A 115 0
SHEET 2 B 2 SER A 118 LEU A 119 -1 N SER A 118 O GLU A 115
SITE 1 AC1 15 TYR A 46 ASN A 48 LYS A 120 ASP A 181
SITE 2 AC1 15 PHE A 182 CYS A 215 SER A 216 ALA A 217
SITE 3 AC1 15 ILE A 219 GLY A 220 ARG A 221 GLN A 262
SITE 4 AC1 15 SER A 285 HOH A 322 HOH A 329
CRYST1 88.195 88.195 103.728 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 0.011338 0.006546 0.000000 0.00000
SCALE2 0.000000 0.013092 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009640 0.00000
(ATOM LINES ARE NOT SHOWN.)
END