HEADER HYDROLASE 28-MAR-03 1OEO
TITLE PTP1B WITH THE CATALYTIC CYSTEINE OXIDIZED TO SULFONIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN-TYROSINE PHOSPHATASE, NON-RECEPTOR TYPE 1;
COMPND 3 CHAIN: X;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 1-321;
COMPND 5 SYNONYM: PROTEIN-TYROSINE PHOSPHATASE 1B, PTP-1B;
COMPND 6 EC: 3.1.3.48;
COMPND 7 ENGINEERED: YES;
COMPND 8 OTHER_DETAILS: CATALYTIC CYSTEINE X215 IS OXIDIZED TO A SULFONIC ACID
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, PHOSPHORYLATION, CYSTEINE SULFONIC ACID
EXPDTA X-RAY DIFFRACTION
AUTHOR A.SALMEEN,J.N.ANDERSEN,M.P.MYERS,T.C.MENG,J.A.HINKS,N.K.TONKS,
AUTHOR 2 D.BARFORD
REVDAT 3 13-DEC-23 1OEO 1 LINK
REVDAT 2 24-FEB-09 1OEO 1 VERSN
REVDAT 1 12-JUN-03 1OEO 0
JRNL AUTH A.SALMEEN,J.N.ANDERSEN,M.P.MYERS,T.C.MENG,J.A.HINKS,
JRNL AUTH 2 N.K.TONKS,D.BARFORD
JRNL TITL REDOX REGULATION OF PROTEIN TYROSINE PHOSPHATASE INVOLVES A
JRNL TITL 2 SULFENYL-AMIDE INTERMEDIATE
JRNL REF NATURE V. 423 769 2003
JRNL REFN ISSN 0028-0836
JRNL PMID 12802338
JRNL DOI 10.1038/NATURE01680
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 76.70
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 24459
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) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1305
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.21
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1757
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2020
REMARK 3 BIN FREE R VALUE SET COUNT : 107
REMARK 3 BIN FREE R VALUE : 0.2510
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2292
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 153
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.43000
REMARK 3 B22 (A**2) : 0.43000
REMARK 3 B33 (A**2) : -0.64000
REMARK 3 B12 (A**2) : 0.21000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.163
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.151
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.098
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.676
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.934
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2342 ; 0.025 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3155 ; 1.989 ; 1.951
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 277 ; 6.141 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 337 ; 0.154 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1761 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1036 ; 0.239 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 158 ; 0.137 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 26 ; 0.236 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 6 ; 0.131 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1397 ; 1.313 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2260 ; 2.458 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 945 ; 3.883 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 895 ; 6.311 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1OEO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-MAR-03.
REMARK 100 THE DEPOSITION ID IS D_1290012467.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-OCT-02
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.50
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 : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.541
REMARK 200 MONOCHROMATOR : YALE MIRRORS
REMARK 200 OPTICS : YALE MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26299
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 6.980
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.6800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.33200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.970
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 2HNP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH 7.5, 12%PEG, 0.2M
REMARK 280 MGCL2,CRYSTALS WERE SOAKED OVERNIGHT IN 100 MICROMOLAR
REMARK 280 PERVANADATE PRIOR TO DATA COLLECTION, PH 7.50
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 34.92133
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 69.84267
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 69.84267
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 34.92133
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: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: X
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 400
REMARK 400 COMPOUND
REMARK 400 CATALYSES HYDROLYSIS OF PROTEIN TYROSINE PHOSPHATE TO
REMARK 400 PROTEIN TYROSINE ANDPHOSPHATE.
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 X 1
REMARK 465 GLY X 283
REMARK 465 ASP X 284
REMARK 465 SER X 285
REMARK 465 SER X 286
REMARK 465 VAL X 287
REMARK 465 GLN X 288
REMARK 465 ASP X 289
REMARK 465 GLN X 290
REMARK 465 TRP X 291
REMARK 465 LYS X 292
REMARK 465 GLU X 293
REMARK 465 LEU X 294
REMARK 465 SER X 295
REMARK 465 HIS X 296
REMARK 465 GLU X 297
REMARK 465 ASP X 298
REMARK 465 LEU X 299
REMARK 465 GLU X 300
REMARK 465 PRO X 301
REMARK 465 PRO X 302
REMARK 465 PRO X 303
REMARK 465 GLU X 304
REMARK 465 HIS X 305
REMARK 465 ILE X 306
REMARK 465 PRO X 307
REMARK 465 PRO X 308
REMARK 465 PRO X 309
REMARK 465 PRO X 310
REMARK 465 ARG X 311
REMARK 465 PRO X 312
REMARK 465 PRO X 313
REMARK 465 LYS X 314
REMARK 465 ARG X 315
REMARK 465 ILE X 316
REMARK 465 LEU X 317
REMARK 465 GLU X 318
REMARK 465 PRO X 319
REMARK 465 HIS X 320
REMARK 465 ASN X 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 MET X 282 CA C O CB CG SD CE
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 X 214 C OCS X 215 N 0.182
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 ASP X 22 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 LEU X 37 CA - CB - CG ANGL. DEV. = 14.4 DEGREES
REMARK 500 LEU X 37 CB - CG - CD1 ANGL. DEV. = 10.6 DEGREES
REMARK 500 ARG X 45 NE - CZ - NH1 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG X 56 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ASP X 65 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 GLU X 129 CA - CB - CG ANGL. DEV. = 15.3 DEGREES
REMARK 500 ASP X 137 CB - CG - OD2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 OCS X 215 O - C - N ANGL. DEV. = -11.3 DEGREES
REMARK 500 ARG X 238 NE - CZ - NH1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG X 238 NE - CZ - NH2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 ARG X 254 CD - NE - CZ ANGL. DEV. = 10.3 DEGREES
REMARK 500 ARG X 254 NE - CZ - NH1 ANGL. DEV. = 8.9 DEGREES
REMARK 500 ARG X 254 NE - CZ - NH2 ANGL. DEV. = -10.8 DEGREES
REMARK 500 ARG X 257 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ILE X 281 O - C - N ANGL. DEV. = -11.0 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 X 63 -79.11 -70.77
REMARK 500 OCS X 215 -132.63 -129.07
REMARK 500 ILE X 219 -31.39 -138.79
REMARK 500 ILE X 261 110.99 71.77
REMARK 500 ILE X 281 -83.77 -67.82
REMARK 500
REMARK 500 REMARK: NULL
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: 1N6W 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: 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: 1NWL RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE PTP1B COMPLEXED WITH SP7343-SP7964,A PTYR
REMARK 900 MIMETIC
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: 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: 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: 2HNP RELATED DB: PDB
REMARK 900 RELATED ID: 2HNQ RELATED DB: PDB
DBREF 1OEO X 1 321 UNP P18031 PTN1_HUMAN 1 321
SEQRES 1 X 321 MET GLU MET GLU LYS GLU PHE GLU GLN ILE ASP LYS SER
SEQRES 2 X 321 GLY SER TRP ALA ALA ILE TYR GLN ASP ILE ARG HIS GLU
SEQRES 3 X 321 ALA SER ASP PHE PRO CYS ARG VAL ALA LYS LEU PRO LYS
SEQRES 4 X 321 ASN LYS ASN ARG ASN ARG TYR ARG ASP VAL SER PRO PHE
SEQRES 5 X 321 ASP HIS SER ARG ILE LYS LEU HIS GLN GLU ASP ASN ASP
SEQRES 6 X 321 TYR ILE ASN ALA SER LEU ILE LYS MET GLU GLU ALA GLN
SEQRES 7 X 321 ARG SER TYR ILE LEU THR GLN GLY PRO LEU PRO ASN THR
SEQRES 8 X 321 CYS GLY HIS PHE TRP GLU MET VAL TRP GLU GLN LYS SER
SEQRES 9 X 321 ARG GLY VAL VAL MET LEU ASN ARG VAL MET GLU LYS GLY
SEQRES 10 X 321 SER LEU LYS CYS ALA GLN TYR TRP PRO GLN LYS GLU GLU
SEQRES 11 X 321 LYS GLU MET ILE PHE GLU ASP THR ASN LEU LYS LEU THR
SEQRES 12 X 321 LEU ILE SER GLU ASP ILE LYS SER TYR TYR THR VAL ARG
SEQRES 13 X 321 GLN LEU GLU LEU GLU ASN LEU THR THR GLN GLU THR ARG
SEQRES 14 X 321 GLU ILE LEU HIS PHE HIS TYR THR THR TRP PRO ASP PHE
SEQRES 15 X 321 GLY VAL PRO GLU SER PRO ALA SER PHE LEU ASN PHE LEU
SEQRES 16 X 321 PHE LYS VAL ARG GLU SER GLY SER LEU SER PRO GLU HIS
SEQRES 17 X 321 GLY PRO VAL VAL VAL HIS OCS SER ALA GLY ILE GLY ARG
SEQRES 18 X 321 SER GLY THR PHE CYS LEU ALA ASP THR CYS LEU LEU LEU
SEQRES 19 X 321 MET ASP LYS ARG LYS ASP PRO SER SER VAL ASP ILE LYS
SEQRES 20 X 321 LYS VAL LEU LEU GLU MET ARG LYS PHE ARG MET GLY LEU
SEQRES 21 X 321 ILE GLN THR ALA ASP GLN LEU ARG PHE SER TYR LEU ALA
SEQRES 22 X 321 VAL ILE GLU GLY ALA LYS PHE ILE MET GLY ASP SER SER
SEQRES 23 X 321 VAL GLN ASP GLN TRP LYS GLU LEU SER HIS GLU ASP LEU
SEQRES 24 X 321 GLU PRO PRO PRO GLU HIS ILE PRO PRO PRO PRO ARG PRO
SEQRES 25 X 321 PRO LYS ARG ILE LEU GLU PRO HIS ASN
MODRES 1OEO OCS X 215 CYS CYSTEINESULFONIC ACID
HET OCS X 215 9
HETNAM OCS CYSTEINESULFONIC ACID
FORMUL 1 OCS C3 H7 N O5 S
FORMUL 2 HOH *153(H2 O)
HELIX 1 1 GLU X 2 GLY X 14 1 13
HELIX 2 2 SER X 15 ALA X 27 1 13
HELIX 3 3 CYS X 32 LEU X 37 1 6
HELIX 4 4 PRO X 38 ASN X 44 5 7
HELIX 5 5 PHE X 52 HIS X 54 5 3
HELIX 6 6 THR X 91 LYS X 103 1 13
HELIX 7 7 PRO X 188 SER X 201 1 14
HELIX 8 8 GLY X 220 ARG X 238 1 19
HELIX 9 9 ASP X 240 VAL X 244 5 5
HELIX 10 10 ASP X 245 ARG X 254 1 10
HELIX 11 11 THR X 263 PHE X 280 1 18
SHEET 1 XA 9 ARG X 56 LYS X 58 0
SHEET 2 XA 9 TYR X 66 MET X 74 -1 N ILE X 67 O ILE X 57
SHEET 3 XA 9 ARG X 79 GLN X 85 -1 O ARG X 79 N MET X 74
SHEET 4 XA 9 VAL X 211 OCS X 215 1 O VAL X 211 N ILE X 82
SHEET 5 XA 9 GLY X 106 MET X 109 1 O GLY X 106 N VAL X 212
SHEET 6 XA 9 GLU X 167 TYR X 176 1 O LEU X 172 N VAL X 107
SHEET 7 XA 9 TYR X 153 ASN X 162 -1 O THR X 154 N HIS X 175
SHEET 8 XA 9 LEU X 140 ILE X 149 -1 O LYS X 141 N GLU X 161
SHEET 9 XA 9 MET X 133 PHE X 135 -1 O MET X 133 N LEU X 142
SHEET 1 XB 2 MET X 114 GLU X 115 0
SHEET 2 XB 2 SER X 118 LEU X 119 -1 O SER X 118 N GLU X 115
LINK C HIS X 214 N OCS X 215 1555 1555 1.52
LINK C OCS X 215 N SER X 216 1555 1555 1.37
CRYST1 88.365 88.365 104.764 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 0.011317 0.006534 0.000000 0.00000
SCALE2 0.000000 0.013067 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009545 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
