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PDBsum entry 2cnh

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Hydrolase PDB id
2cnh
Jmol
Contents
Protein chain
297 a.a.
Ligands
IZB
Metals
_CA
Waters ×275
HEADER    HYDROLASE                               21-MAY-06   2CNH
TITLE     STRUCTURAL INSIGHTS INTO THE DESIGN OF NONPEPTIDIC
TITLE    2 ISOTHIAZOLIDINONE-CONTAINING INHIBITORS OF PROTEIN
TITLE    3 TYROSINE PHOSPHATASE 1B
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 1;
COMPND   3 CHAIN: A;
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
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,
KEYWDS   2 ENDOPLASMIC RETICULUM, OXIDATION, HYDROLASE, ACETYLATION,
KEYWDS   3 PHOSPHATASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    P.J.ALA,L.GONNEVILLE,M.HILLMAN,M.BECKER-PASHA,E.W.YUE,
AUTHOR   2 B.DOUTY,B.WAYLAND,P.POLAM,M.L.CRAWLEY,E.MCLAUGHLIN,
AUTHOR   3 R.B.SPARKS,B.GLASS,A.TAKVORIAN,A.P.COMBS,T.C.BURN,
AUTHOR   4 G.F.HOLLIS,R.WYNN
REVDAT   3   24-FEB-09 2CNH    1       VERSN
REVDAT   2   06-DEC-06 2CNH    1       JRNL
REVDAT   1   27-SEP-06 2CNH    0
JRNL        AUTH   P.J.ALA,L.GONNEVILLE,M.HILLMAN,M.BECKER-PASHA,
JRNL        AUTH 2 E.W.YUE,B.DOUTY,B.WAYLAND,P.POLAM,M.L.CRAWLEY,
JRNL        AUTH 3 E.MCLAUGHLIN,R.B.SPARKS,B.GLASS,A.TAKVORIAN,
JRNL        AUTH 4 A.P.COMBS,T.C.BURN,G.F.HOLLIS,R.WYNN
JRNL        TITL   STRUCTURAL INSIGHTS INTO THE DESIGN OF NONPEPTIDIC
JRNL        TITL 2 ISOTHIAZOLIDINONE-CONTAINING INHIBITORS OF
JRNL        TITL 3 PROTEIN- TYROSINE PHOSPHATASE 1B.
JRNL        REF    J.BIOL.CHEM.                  V. 281 38013 2006
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   17028182
JRNL        DOI    10.1074/JBC.M607913200
REMARK   2
REMARK   2 RESOLUTION.    1.8  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) : 1.8
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.0
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.0
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             : 37427
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) : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.2080
REMARK   3   FREE R VALUE                     : 0.2403
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.6
REMARK   3   FREE R VALUE TEST SET COUNT      : 3766
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            : 2420
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 41
REMARK   3   SOLVENT ATOMS            : 275
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) : 0.010
REMARK   3    B22 (A**2) : -0.119
REMARK   3    B33 (A**2) : 0.109
REMARK   3    B12 (A**2) : 0.000
REMARK   3    B13 (A**2) : 0.000
REMARK   3    B23 (A**2) : 0.000
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) : 0.009665
REMARK   3   BOND ANGLES            (DEGREES) : 1.60719
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        : 0.8
REMARK   3   BSOL        : 280
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 2CNH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-MAY-06.
REMARK 100 THE PDBE ID CODE IS EBI-28825.
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                             : 7.30
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 MSC MICROMAXTM-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 (RAXIS IV)
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU MSC
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR
REMARK 200  DATA SCALING SOFTWARE          : CRYSTALCLEAR
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38984
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.900
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6
REMARK 200  DATA REDUNDANCY                : 3.500
REMARK 200  R MERGE                    (I) : 0.04000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 15.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.2
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50
REMARK 200  R MERGE FOR SHELL          (I) : 0.28000
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 4.000
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   (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA):NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 160 MM CALCIUM ACETATE,
REMARK 280  PH 7.3, 16% PEG 3350
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
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       33.45000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       43.79000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.70500
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       43.79000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       33.45000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.70500
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 GENERATING THE BIOMOLECULE
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: 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 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     1
REMARK 465     GLU A     2
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     LEU A 299    CA   C    O    CB   CG   CD1  CD2
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 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      -82.89    -46.25
REMARK 500    CYS A 215     -133.62   -135.91
REMARK 500    ILE A 261      107.97     81.28
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 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 A1299  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A2079   O
REMARK 620 2 HOH A2164   O    73.1
REMARK 620 3 HOH A2161   O   143.2  99.6
REMARK 620 4 HOH A2165   O    71.4  73.3  71.9
REMARK 620 5 HOH A2078   O    75.4 147.4 100.7  89.1
REMARK 620 6 HIS A  54   O    77.2  97.6 139.4 148.6  83.1
REMARK 620 7 HOH A2080   O   138.3  74.0  67.5 121.5 137.8  82.6
REMARK 620 8 HOH A2081   O   134.1 145.5  70.7 129.5  66.2  74.3  71.7
REMARK 620 N                    1     2     3     4     5     6     7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A1299
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IZB A1300
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1A5Y   RELATED DB: PDB
REMARK 900  PROTEIN TYROSINE PHOSPHATASE 1B CYSTEINYL-
REMARK 900  PHOSPHATEINTERMEDIATE
REMARK 900 RELATED ID: 1AAX   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF PROTEIN TYROSINE
REMARK 900  PHOSPHATASE 1BCOMPLEXED WITH TWO BIS(PARA-
REMARK 900  PHOSPHOPHENYL)METHANE (BPPM)MOLECULES
REMARK 900 RELATED ID: 1BZC   RELATED DB: PDB
REMARK 900  HUMAN PTP1B CATALYTIC DOMAIN COMPLEXED WITH
REMARK 900  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
REMARK 900  PHOSPHATASE 1BCOMPLEXED WITH 6-(OXALYL-AMINO
REMARK 900  )-1H-INDOLE-5-CARBOXYLIC ACID
REMARK 900 RELATED ID: 1C84   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF PROTEIN TYROSINE
REMARK 900  PHOSPHATASE 1BCOMPLEXED WITH 3-(OXALYL-AMINO
REMARK 900  )-NAPHTHALENE-2-CARBOXLIC ACID
REMARK 900 RELATED ID: 1C85   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF PROTEIN TYROSINE
REMARK 900  PHOSPHATASE 1BCOMPLEXED WITH 2-(OXALYL-AMINO
REMARK 900  )-BENZOIC ACID
REMARK 900 RELATED ID: 1C86   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF PROTEIN TYROSINE
REMARK 900  PHOSPHATASE 1B (R47V,D48N) COMPLEXED WITH 2
REMARK 900  -(OXALYL-AMINO-4,7-DIHYDRO-5H-THIENO[2,
REMARK 900  3-C]PYRAN-3-CARBOXYLIC ACID
REMARK 900 RELATED ID: 1C87   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF PROTEIN TYROSINE
REMARK 900  PHOSPHATASE 1BCOMPLEXED WITH 2-(OXALYL-AMINO-
REMARK 900  4,7-DIHYDRO-5H-THIENO[2,3-C]PYRAN-3-
REMARK 900  CARBOXYLIC ACID
REMARK 900 RELATED ID: 1C88   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF PROTEIN TYROSINE
REMARK 900  PHOSPHATASE 1BCOMPLEXED WITH 2-(OXALYL-AMINO
REMARK 900  )-4,5,6,7-TETRAHYDRO-THIENO[2,3-C]
REMARK 900  PYRIDINE-3-CARBOXYLIC ACID
REMARK 900 RELATED ID: 1ECV   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF PROTEIN TYROSINE
REMARK 900  PHOSPHATASE 1BCOMPLEXED WITH 5-IODO-2-(
REMARK 900  OXALYL-AMINO)-BENZOIC ACID
REMARK 900 RELATED ID: 1EEN   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF PROTEIN TYROSINE
REMARK 900  PHOSPHATASE 1BCOMPLEXED WITH ACETYL-D-A-D-
REMARK 900  BPA-PTYR-L-I-P-Q-Q-G
REMARK 900 RELATED ID: 1EEO   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF PROTEIN TYROSINE
REMARK 900  PHOSPHATASE 1BCOMPLEXED WITH ACETYL-E-L-E-
REMARK 900  F-PTYR-M-D-Y-E-NH2
REMARK 900 RELATED ID: 1G1F   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF PROTEIN TYROSINE
REMARK 900  PHOSPHATASE 1BCOMPLEXED WITH A TRI-
REMARK 900  PHOSPHORYLATED PEPTIDE (RDI(PTR)ETD(PTR)(PTR
REMARK 900  )RK) FROM THE INSULIN RECEPTOR KINASE
REMARK 900 RELATED ID: 1G1G   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF PROTEIN TYROSINE
REMARK 900  PHOSPHATASE 1BCOMPLEXED WITH A MONO-
REMARK 900  PHOSPHORYLATED PEPTIDE (ETDY(PTR)RKGGKGLL)
REMARK 900  FROM THE INSULIN RECEPTOR KINASE
REMARK 900 RELATED ID: 1G1H   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF PROTEIN TYROSINE
REMARK 900  PHOSPHATASE 1BCOMPLEXED WITH A BIS-
REMARK 900  PHOSPHORYLATED PEPTIDE (ETD(PTR)(PTR)RKGGKGLL
REMARK 900  ) FROM THE INSULIN RECEPTOR KINASE
REMARK 900 RELATED ID: 1G7F   RELATED DB: PDB
REMARK 900  HUMAN PTP1B CATALYTIC DOMAIN COMPLEXED WITH
REMARK 900  PNU177496
REMARK 900 RELATED ID: 1G7G   RELATED DB: PDB
REMARK 900  HUMAN PTP1B CATALYTIC DOMAIN COMPLEXES WITH
REMARK 900  PNU179326
REMARK 900 RELATED ID: 1GFY   RELATED DB: PDB
REMARK 900  RESIDUE 259 IS A KEY DETERMINANT OF
REMARK 900  SUBSTRATE SPECIFICITYOF PROTEIN-TYROSINE
REMARK 900  PHOSPHATASE 1B AND ALPHA
REMARK 900 RELATED ID: 1I57   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF APO HUMAN PTP1B (C215S
REMARK 900  ) MUTANT
REMARK 900 RELATED ID: 1JF7   RELATED DB: PDB
REMARK 900  HUMAN PTP1B CATALYTIC DOMAIN COMPLEXED WITH
REMARK 900  PNU177836
REMARK 900 RELATED ID: 1KAK   RELATED DB: PDB
REMARK 900  HUMAN TYROSINE PHOSPHATASE 1B COMPLEXED WITH
REMARK 900  AN INHIBITOR
REMARK 900 RELATED ID: 1KAV   RELATED DB: PDB
REMARK 900  HUMAN TYROSINE PHOSPHATASE 1B COMPLEXED WITH
REMARK 900  AN INHIBITOR
REMARK 900 RELATED ID: 1L8G   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF PTP1B COMPLEXED WITH 7
REMARK 900  -(1,1-DIOXO-1H-BENZO[D]ISOTHIAZOL-3-
REMARK 900  YLOXYMETHYL)-2-(OXALYL-AMINO)-4,7-DIHYDRO-
REMARK 900  5H-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
REMARK 900  PEPTIDICBISPHOSPHONATE INHIBITOR
REMARK 900 RELATED ID: 1NL9   RELATED DB: PDB
REMARK 900  POTENT, SELECTIVE PROTEIN TYROSINE PHOSPHATASE
REMARK 900  1B INHIBITORCOMPOUND 12 USING A LINKED-
REMARK 900  FRAGMENT STRATEGY
REMARK 900 RELATED ID: 1NNY   RELATED DB: PDB
REMARK 900  POTENT, SELECTIVE PROTEIN TYROSINE PHOSPHATASE
REMARK 900  1B INHIBITORCOMPOUND 23 USING A LINKED-
REMARK 900  FRAGMENT STRATEGY
REMARK 900 RELATED ID: 1NO6   RELATED DB: PDB
REMARK 900  POTENT, SELECTIVE PROTEIN TYROSINE PHOSPHATASE
REMARK 900  1B INHIBITORCOMPOUND 5 USING A LINKED-
REMARK 900  FRAGMENT STRATEGY
REMARK 900 RELATED ID: 1NWE   RELATED DB: PDB
REMARK 900  PTP1B R47C MODIFIED AT C47 WITH N-[4-(2
REMARK 900  -{2-[3-(2-BROMO-ACETYLAMINO)-PROPIONYLAMINO
REMARK 900  ]-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
REMARK 900  WITH SP7343-SP7964,A PTYR MIMETIC
REMARK 900 RELATED ID: 1NZ7   RELATED DB: PDB
REMARK 900  POTENT, SELECTIVE INHIBITORS OF PROTEIN
REMARK 900  TYROSINEPHOSPHATASE 1B USING A SECOND
REMARK 900  PHOSPHOTYROSINE BINDING SITE,COMPLEXED WITH
REMARK 900  COMPOUND 19.
REMARK 900 RELATED ID: 1OEM   RELATED DB: PDB
REMARK 900  PTP1B WITH THE CATALYTIC CYSTEINE OXIDIZED
REMARK 900  TO A SULFENYL-AMIDE BOND
REMARK 900 RELATED ID: 1OEO   RELATED DB: PDB
REMARK 900  PTP1B WITH THE CATALYTIC CYSTEINE OXIDIZED
REMARK 900  TO SULFONIC ACID
REMARK 900 RELATED ID: 1OES   RELATED DB: PDB
REMARK 900  OXIDATION STATE OF PROTEIN TYROSINE
REMARK 900  PHOSPHATASE 1B
REMARK 900 RELATED ID: 1OET   RELATED DB: PDB
REMARK 900  OXIDATION STATE OF PROTEIN TYROSINE
REMARK 900  PHOSPHATASE 1B
REMARK 900 RELATED ID: 1OEU   RELATED DB: PDB
REMARK 900  OXIDATION STATE OF PROTEIN TYROSINE
REMARK 900  PHOSPHATASE 1B
REMARK 900 RELATED ID: 1OEV   RELATED DB: PDB
REMARK 900  OXIDATION STATE OF PROTEIN TYROSINE
REMARK 900  PHOSPHATASE 1B
REMARK 900 RELATED ID: 1ONY   RELATED DB: PDB
REMARK 900  OXALYL-ARYL-AMINO BENZOIC ACID INHIBITORS OF
REMARK 900   PTP1B,COMPOUND 17
REMARK 900 RELATED ID: 1ONZ   RELATED DB: PDB
REMARK 900  OXALYL-ARYL-AMINO BENZOIC ACID INHIBITORS OF
REMARK 900   PTP1B,COMPOUND 8B
REMARK 900 RELATED ID: 1PA1   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF THE C215D MUTANT OF
REMARK 900  PROTEIN TYROSINEPHOSPHATASE 1B
REMARK 900 RELATED ID: 1PH0   RELATED DB: PDB
REMARK 900  NON-CARBOXYLIC ACID-CONTAINING INHIBITOR OF
REMARK 900  PTP1B TARGETINGTHE SECOND PHOSPHOTYROSINE SITE
REMARK 900 RELATED ID: 1PTT   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF PROTEIN TYROSINE
REMARK 900  PHOSPHATASE 1BCOMPLEXED WITH PHOSPHOTYROSINE-
REMARK 900  CONTAINING TETRA-PEPTIDE(AC-DEPYL-NH2)
REMARK 900 RELATED ID: 1PTU   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF PROTEIN TYROSINE
REMARK 900  PHOSPHATASE 1BCOMPLEXED WITH PHOSPHOTYROSINE-
REMARK 900  CONTAINING HEXA-PEPTIDE(DADEPYL-NH2)
REMARK 900 RELATED ID: 1PTV   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF PROTEIN TYROSINE
REMARK 900  PHOSPHATASE 1BCOMPLEXED WITH PHOSPHOTYROSINE
REMARK 900 RELATED ID: 1PTY   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF PROTEIN TYROSINE
REMARK 900  PHOSPHATASE 1BCOMPLEXED WITH TWO PHOSPHOTYROSINE
REMARK 900   MOLECULES
REMARK 900 RELATED ID: 1PXH   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF PROTEIN TYROSINE
REMARK 900  PHOSPHATASE 1B WITHPOTENT AND SELECTIVE
REMARK 900  BIDENTATE INHIBITOR COMPOUND 2
REMARK 900 RELATED ID: 1PYN   RELATED DB: PDB
REMARK 900  DUAL-SITE POTENT, SELECTIVE PROTEIN TYROSINE
REMARK 900  PHOSPHATASE 1BINHIBITOR USING A LINKED
REMARK 900  FRAGMENT STRATEGY AND A MALONATEHEAD ON THE
REMARK 900   FIRST SITE
REMARK 900 RELATED ID: 1Q1M   RELATED DB: PDB
REMARK 900  A HIGHLY EFFICIENT APPROACH TO A SELECTIVE
REMARK 900  AND CELL ACTIVEPTP1B INHIBITORS
REMARK 900 RELATED ID: 1Q6J   RELATED DB: PDB
REMARK 900  THE STRUCTURE OF PHOSPHOTYROSINE PHOSPHATASE
REMARK 900  1B IN COMPLEXWITH COMPOUND 2
REMARK 900 RELATED ID: 1Q6M   RELATED DB: PDB
REMARK 900  THE STRUCTURE OF PHOSPHOTYROSINE PHOSPHATASE
REMARK 900  1B IN COMPLEXWITH COMPOUND 3
REMARK 900 RELATED ID: 1Q6N   RELATED DB: PDB
REMARK 900  THE STRUCTURE OF PHOSPHOTYROSINE PHOSPHATASE
REMARK 900  1B IN COMPLEXWITH COMPOUND 4
REMARK 900 RELATED ID: 1Q6P   RELATED DB: PDB
REMARK 900  THE STRUCTURE OF PHOSPHOTYROSINE PHOSPHATASE
REMARK 900  1B IN COMPLEXWITH COMPOUND 6
REMARK 900 RELATED ID: 1Q6S   RELATED DB: PDB
REMARK 900  THE STRUCTURE OF PHOSPHOTYROSINE PHOSPHATASE
REMARK 900  1B IN COMPLEXWITH COMPOUND 9
REMARK 900 RELATED ID: 1Q6T   RELATED DB: PDB
REMARK 900  THE STRUCTURE OF PHOSPHOTYROSINE PHOSPHATASE
REMARK 900  1B IN COMPLEXWITH COMPOUND 11
REMARK 900 RELATED ID: 1QXK   RELATED DB: PDB
REMARK 900  MONOACID-BASED, CELL PERMEABLE, SELECTIVE
REMARK 900  INHIBITORS OFPROTEIN TYROSINE PHOSPHATASE 1B
REMARK 900 RELATED ID: 1SUG   RELATED DB: PDB
REMARK 900  1.95 A STRUCTURE OF APO PROTEIN TYROSINE
REMARK 900  PHOSPHATASE 1B
REMARK 900 RELATED ID: 1T48   RELATED DB: PDB
REMARK 900  ALLOSTERIC INHIBITION OF PROTEIN TYROSINE
REMARK 900  PHOSPHATASE 1B
REMARK 900 RELATED ID: 1T49   RELATED DB: PDB
REMARK 900  ALLOSTERIC INHIBITION OF PROTEIN TYROSINE
REMARK 900  PHOSPHATASE 1B
REMARK 900 RELATED ID: 1T4J   RELATED DB: PDB
REMARK 900  ALLOSTERIC INHIBITION OF PROTEIN TYROSINE
REMARK 900  PHOSPHATASE 1B
REMARK 900 RELATED ID: 1WAX   RELATED DB: PDB
REMARK 900  PROTEIN TYROSINE PHOSPHATASE 1B WITH ACTIVE
REMARK 900  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
REMARK 900  THIOPHENE INHIBITOR
REMARK 900 RELATED ID: 2B07   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF PTP1B WITH TRICYCLIC
REMARK 900  THIOPHENEINHIBITOR.
REMARK 900 RELATED ID: 2B4S   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF A COMPLEX BETWEEN PTP1B
REMARK 900   AND THEINSULIN RECEPTOR TYROSINE KINASE
REMARK 900 RELATED ID: 2BGD   RELATED DB: PDB
REMARK 900  STRUCTURE-BASED DESIGN OF PROTEIN TYROSINE
REMARK 900  PHOSPHATASE-1B INHIBITORS
REMARK 900 RELATED ID: 2BGE   RELATED DB: PDB
REMARK 900  STRUCTURE-BASED DESIGN OF PROTEIN TYROSINE
REMARK 900  PHOSPHATASE-1B INHIBITORS
REMARK 900 RELATED ID: 2CM2   RELATED DB: PDB
REMARK 900  STRUCTURAL OF PROTEIN TYROSINE PHOSPHATASE 1B
REMARK 900   (P212121)
REMARK 900 RELATED ID: 2CM3   RELATED DB: PDB
REMARK 900  STRUCTURAL OF PROTEIN TYROSINE PHOSPHATASE 1B
REMARK 900   (C2)
REMARK 900 RELATED ID: 2CM7   RELATED DB: PDB
REMARK 900  STRUCTURAL BASIS FOR INHIBITION OF PROTEIN
REMARK 900  TYROSINE PHOSPHATASE 1B BY ISOTHIAZOLIDINONE
REMARK 900  HETEROCYCLIC PHOSPHONATE MIMETICS
REMARK 900 RELATED ID: 2CM8   RELATED DB: PDB
REMARK 900  STRUCTURAL BASIS FOR INHIBITION OF PROTEIN
REMARK 900  TYROSINE PHOSPHATASE 1B BY ISOTHIAZOLIDINONE
REMARK 900  HETEROCYCLIC PHOSPHONATE MIMETICS
REMARK 900 RELATED ID: 2CMA   RELATED DB: PDB
REMARK 900  STRUCTURAL BASIS FOR INHIBITION OF PROTEIN
REMARK 900  TYROSINE PHOSPHATASE 1B BY ISOTHIAZOLIDINONE
REMARK 900  HETEROCYCLIC PHOSPHONATE MIMETICS
REMARK 900 RELATED ID: 2CMB   RELATED DB: PDB
REMARK 900  STRUCTURAL BASIS FOR INHIBITION OF PROTEIN
REMARK 900  TYROSINE PHOSPHATASE 1B BY ISOTHIAZOLIDINONE
REMARK 900  HETEROCYCLIC PHOSPHONATE MIMETICS
REMARK 900 RELATED ID: 2CMC   RELATED DB: PDB
REMARK 900  STRUCTURAL BASIS FOR INHIBITION OF PROTEIN
REMARK 900  TYROSINE PHOSPHATASE 1B BY ISOTHIAZOLIDINONE
REMARK 900  HETEROCYCLIC PHOSPHONATE MIMETICS
REMARK 900 RELATED ID: 2F6F   RELATED DB: PDB
REMARK 900  THE STRUCTURE OF THE S295F MUTANT OF HUMAN
REMARK 900   PTP1B
REMARK 900 RELATED ID: 2F6T   RELATED DB: PDB
REMARK 900  PROTEIN TYROSINE PHOSPHATASE 1B WITH SULFAMIC
REMARK 900   ACIDINHIBITORS
REMARK 900 RELATED ID: 2F6V   RELATED DB: PDB
REMARK 900  PROTEIN TYROSINE PHOSPHATASE 1B WITH SULFAMIC
REMARK 900   ACIDINHIBITORS
REMARK 900 RELATED ID: 2F6W   RELATED DB: PDB
REMARK 900  PROTEIN TYROSINE PHOSPHATASE 1B WITH SULFAMIC
REMARK 900   ACIDINHIBITORS
REMARK 900 RELATED ID: 2F6Y   RELATED DB: PDB
REMARK 900  PROTEIN TYROSINE PHOSPHATASE 1B WITH SULFAMIC
REMARK 900   ACIDINHIBITORS
REMARK 900 RELATED ID: 2F6Z   RELATED DB: PDB
REMARK 900  PROTEIN TYROSINE PHOSPHATASE 1B WITH SULFAMIC
REMARK 900   ACIDINHIBITORS
REMARK 900 RELATED ID: 2F70   RELATED DB: PDB
REMARK 900  PROTEIN TYROSINE PHOSPHATASE 1B WITH SULFAMIC
REMARK 900   ACIDINHIBITORS
REMARK 900 RELATED ID: 2F71   RELATED DB: PDB
REMARK 900  PROTEIN TYROSINE PHOSPHATASE 1B WITH SULFAMIC
REMARK 900   ACIDINHIBITORS
REMARK 900 RELATED ID: 2FJM   RELATED DB: PDB
REMARK 900  THE STRUCTURE OF PHOSPHOTYROSINE PHOSPHATASE
REMARK 900  1B IN COMPLEXWITH COMPOUND 2
REMARK 900 RELATED ID: 2FJN   RELATED DB: PDB
REMARK 900  THE STRUCTURE OF PHOSPHOTYROSINE PHOSPHATASE
REMARK 900  1B IN COMPLEXWITH COMPOUND 2
REMARK 900 RELATED ID: 2HNP   RELATED DB: PDB
REMARK 900 RELATED ID: 2HNQ   RELATED DB: PDB
REMARK 900 RELATED ID: 2CNE   RELATED DB: PDB
REMARK 900  STRUCTURAL INSIGHTS INTO THE DESIGN OF
REMARK 900  NONPEPTIDIC ISOTHIAZOLIDINONE-CONTAINING
REMARK 900  INHIBITORS OF PROTEIN TYROSINE PHOSPHATASE 1B
REMARK 900 RELATED ID: 2CNF   RELATED DB: PDB
REMARK 900  STRUCTURAL INSIGHTS INTO THE DESIGN OF
REMARK 900  NONPEPTIDIC ISOTHIAZOLIDINONE-CONTAINING
REMARK 900  INHIBITORS OF PROTEIN TYROSINE PHOSPHATASE 1B
REMARK 900 RELATED ID: 2CNG   RELATED DB: PDB
REMARK 900  STRUCTURAL INSIGHTS INTO THE DESIGN OF
REMARK 900  NONPEPTIDIC ISOTHIAZOLIDINONE-CONTAINING
REMARK 900  INHIBITORS OF PROTEIN TYROSINE PHOSPHATASE 1B
REMARK 900 RELATED ID: 2CNI   RELATED DB: PDB
REMARK 900  STRUCTURAL INSIGHTS INTO THE DESIGN OF
REMARK 900  NONPEPTIDIC ISOTHIAZOLIDINONE-CONTAINING
REMARK 900  INHIBITORS OF PROTEIN TYROSINE PHOSPHATASE 1B
DBREF  2CNH 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     CA  A1299       1
HET    IZB  A1300      40
HETNAM      CA CALCIUM ION
HETNAM     IZB N-[(1S)-1-(1H-BENZIMIDAZOL-2-YL)-2-{4-[(5S)-
HETNAM   2 IZB  1,1-DIOXIDO-3-OXOISOTHIAZOLIDIN-5-YL]PHENYL}
HETNAM   3 IZB  ETHYL]-4-METHYL-3,4-DIHYDRO-2H-1,4-BENZOXAZINE-
HETNAM   4 IZB  7-SULFONAMIDE
HETSYN     IZB ISOTHIAZOLIDINONE ANALOG
FORMUL   2   CA    CA 2+
FORMUL   3  IZB    C27 H27 N5 O6 S2
FORMUL   4  HOH   *275(H2 O1)
HELIX    1   1 MET A    3  GLY A   14  1                                  12
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  SER A   55  5                                   4
HELIX    5   5 THR A   91  GLN A  102  1                                  12
HELIX    6   6 SER A  187  SER A  201  1                                  15
HELIX    7   7 GLY A  220  ARG A  238  1                                  19
HELIX    8   8 ASP A  240  VAL A  244  5                                   5
HELIX    9   9 ASP A  245  ARG A  254  1                                  10
HELIX   10  10 THR A  263  MET A  282  1                                  20
HELIX   11  11 SER A  286  HIS A  296  1                                  11
SHEET    1  AA 8 ALA A  69  MET A  74  0
SHEET    2  AA 8 ARG A  79  THR A  84 -1  O  ARG A  79   N  MET A  74
SHEET    3  AA 8 VAL A 211  HIS A 214  1  O  VAL A 211   N  ILE A  82
SHEET    4  AA 8 GLY A 106  MET A 109  1  O  GLY A 106   N  VAL A 212
SHEET    5  AA 8 THR A 168  TYR A 176  1  O  LEU A 172   N  VAL A 107
SHEET    6  AA 8 TYR A 153  ASN A 162 -1  O  THR A 154   N  HIS A 175
SHEET    7  AA 8 LEU A 140  ILE A 149 -1  O  LYS A 141   N  GLU A 161
SHEET    8  AA 8 MET A 133  PHE A 135 -1  O  MET A 133   N  LEU A 142
SHEET    1  AB 2 MET A 114  GLU A 115  0
SHEET    2  AB 2 SER A 118  LEU A 119 -1  O  SER A 118   N  GLU A 115
LINK        CA    CA A1299                 O   HOH A2079     1555   2555  2.63
LINK        CA    CA A1299                 O   HOH A2164     1555   1555  2.78
LINK        CA    CA A1299                 O   HOH A2161     1555   1555  2.67
LINK        CA    CA A1299                 O   HOH A2165     1555   1555  2.61
LINK        CA    CA A1299                 O   HOH A2078     1555   2555  2.70
LINK        CA    CA A1299                 O   HIS A  54     1555   2555  2.43
LINK        CA    CA A1299                 O   HOH A2080     1555   2555  2.64
LINK        CA    CA A1299                 O   HOH A2081     1555   2555  2.69
SITE     1 AC1  8 HIS A  54  HOH A2078  HOH A2079  HOH A2080
SITE     2 AC1  8 HOH A2081  HOH A2161  HOH A2164  HOH A2165
SITE     1 AC2 20 TYR A  46  ASP A  48  VAL A  49  ASP A 181
SITE     2 AC2 20 PHE A 182  CYS A 215  SER A 216  ALA A 217
SITE     3 AC2 20 GLY A 218  ILE A 219  GLY A 220  ARG A 221
SITE     4 AC2 20 GLN A 262  GLN A 266  GLU A 293  LEU A 294
SITE     5 AC2 20 HOH A2272  HOH A2273  HOH A2274  HOH A2275
CRYST1   66.900   71.410   87.580  90.00  90.00  90.00 P 21 21 21    4
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      0.014948  0.000000  0.000000        0.00000
SCALE2      0.000000  0.014004  0.000000        0.00000
SCALE3      0.000000  0.000000  0.011418        0.00000
      
PROCHECK
Go to PROCHECK summary
 References