spacer
spacer

PDBsum entry 2h02

Go to PDB code: 
Top Page protein ligands Protein-protein interface(s) links
Hydrolase PDB id
2h02
Jmol
Contents
Protein chain
278 a.a.
Ligands
2UN ×2
Waters ×290
HEADER    HYDROLASE                               13-MAY-06   2H02
TITLE     STRUCTURAL STUDIES OF PROTEIN TYROSINE PHOSPHATASE BETA CATALYTIC
TITLE    2 DOMAIN IN COMPLEX WITH INHIBITORS
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROTEIN TYROSINE PHOSPHATASE, RECEPTOR TYPE, B,;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 1662-1973;
COMPND   5 EC: 3.1.3.48;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: PTPRB;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: TOP10;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PDEST-HISMBP
KEYWDS    PROTEIN TYROSINE PHOSPHATASE, WPD-LOOP, SULFAMIC ACID, PHOSPHATASE,
KEYWDS   2 INHIBITOR, DRUG DESIGN, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.G.EVDOKIMOV,M.E.POKROSS,R.L.WALTER,M.MEKEL,J.L.GRAY,K.G.PETERS,
AUTHOR   2 M.B.MAIER,K.D.AMARASINGHE,C.M.CLARK,R.NICHOLS
REVDAT   5   13-JUL-11 2H02    1       VERSN
REVDAT   4   24-FEB-09 2H02    1       VERSN
REVDAT   3   12-SEP-06 2H02    1       JRNL
REVDAT   2   08-AUG-06 2H02    1       JRNL
REVDAT   1   13-JUN-06 2H02    0
JRNL        AUTH   K.K.AMARASINGHE,A.G.EVDOKIMOV,K.XU,C.M.CLARK,M.B.MAIER,
JRNL        AUTH 2 A.SRIVASTAVA,A.O.COLSON,G.S.GERWE,G.E.STAKE,B.W.HOWARD,
JRNL        AUTH 3 M.E.POKROSS,J.L.GRAY,K.G.PETERS
JRNL        TITL   DESIGN AND SYNTHESIS OF POTENT, NON-PEPTIDIC INHIBITORS OF
JRNL        TITL 2 HPTPBETA.
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  16  4252 2006
JRNL        REFN                   ISSN 0960-894X
JRNL        PMID   16759857
JRNL        DOI    10.1016/J.BMCL.2006.05.074
REMARK   2
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0005
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2
REMARK   3   NUMBER OF REFLECTIONS             : 27353
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) : 0.190
REMARK   3   R VALUE            (WORKING SET) : 0.189
REMARK   3   FREE R VALUE                     : 0.244
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1379
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) : 2.30
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1846
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.96
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2060
REMARK   3   BIN FREE R VALUE SET COUNT          : 103
REMARK   3   BIN FREE R VALUE                    : 0.3560
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4584
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 56
REMARK   3   SOLVENT ATOMS            : 290
REMARK   3
REMARK   3  B VALUES.
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL
REMARK   3   FROM WILSON PLOT           (A**2) : 31.10
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.59
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 1.30000
REMARK   3    B22 (A**2) : -0.55000
REMARK   3    B33 (A**2) : -0.78000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : -0.21000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.402
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.251
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.159
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.085
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.909
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4814 ; 0.011 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6543 ; 2.162 ; 1.951
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   575 ; 8.779 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   252 ;35.432 ;23.492
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   818 ;19.167 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    42 ;21.923 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   700 ; 0.162 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3728 ; 0.006 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2265 ; 0.256 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3174 ; 0.327 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   330 ; 0.186 ; 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):    92 ; 0.448 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    17 ; 0.772 ; 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):  2879 ; 2.041 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4595 ; 3.114 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2187 ; 4.660 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1938 ; 6.507 ; 4.500
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  : 2
REMARK   3
REMARK   3   TLS GROUP : 1
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A  1678        A  1967
REMARK   3    ORIGIN FOR THE GROUP (A):  11.8875   0.6315  33.9886
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0443 T22:  -0.0337
REMARK   3      T33:  -0.0197 T12:  -0.0023
REMARK   3      T13:  -0.0082 T23:  -0.0023
REMARK   3    L TENSOR
REMARK   3      L11:   0.8166 L22:   0.6261
REMARK   3      L33:   0.7621 L12:   0.0852
REMARK   3      L13:   0.1764 L23:  -0.2857
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0433 S12:   0.0321 S13:   0.0480
REMARK   3      S21:   0.0288 S22:  -0.0089 S23:  -0.0223
REMARK   3      S31:  -0.0591 S32:   0.0605 S33:   0.0522
REMARK   3
REMARK   3   TLS GROUP : 2
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B  1679        B  1969
REMARK   3    ORIGIN FOR THE GROUP (A):  44.0433  24.8223  67.3304
REMARK   3    T TENSOR
REMARK   3      T11:   0.0034 T22:  -0.0379
REMARK   3      T33:  -0.0490 T12:  -0.0209
REMARK   3      T13:   0.0093 T23:   0.0049
REMARK   3    L TENSOR
REMARK   3      L11:   0.7512 L22:   0.4591
REMARK   3      L33:   1.1160 L12:   0.0355
REMARK   3      L13:  -0.3150 L23:   0.3542
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0539 S12:   0.0493 S13:  -0.0113
REMARK   3      S21:   0.0222 S22:  -0.0140 S23:   0.0138
REMARK   3      S31:   0.1042 S32:  -0.1320 S33:   0.0679
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
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 2H02 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAY-06.
REMARK 100 THE RCSB ID CODE IS RCSB037760.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-06
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 8.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 22-ID
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0
REMARK 200  MONOCHROMATOR                  : SI
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MAR
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32002
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.0
REMARK 200  DATA REDUNDANCY                : 2.300
REMARK 200  R MERGE                    (I) : 0.04500
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 15.6900
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) : 2.25
REMARK 200  COMPLETENESS FOR SHELL     (%) : 68.7
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.60
REMARK 200  R MERGE FOR SHELL          (I) : 0.28000
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 3.760
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 1RPM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 42.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 21% PEG 8000, 220 MM MGCL2, 1% BME,
REMARK 280  0.1% BOG, 5MM DTT, PH 8.0, VAPOR DIFFUSION, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,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       35.86200
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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     SER A  1661
REMARK 465     ASP A  1662
REMARK 465     ARG A  1663
REMARK 465     PRO A  1664
REMARK 465     LEU A  1665
REMARK 465     SER A  1666
REMARK 465     VAL A  1667
REMARK 465     HIS A  1668
REMARK 465     LEU A  1669
REMARK 465     ASN A  1670
REMARK 465     LEU A  1671
REMARK 465     GLY A  1672
REMARK 465     GLN A  1673
REMARK 465     LYS A  1674
REMARK 465     GLY A  1675
REMARK 465     ASN A  1676
REMARK 465     ARG A  1677
REMARK 465     ASN A  1748
REMARK 465     VAL A  1749
REMARK 465     ASP A  1750
REMARK 465     ASP A  1751
REMARK 465     ASP A  1752
REMARK 465     PRO A  1753
REMARK 465     CYS A  1754
REMARK 465     GLU A  1852
REMARK 465     GLN A  1853
REMARK 465     LEU A  1854
REMARK 465     ASP A  1855
REMARK 465     ALA A  1856
REMARK 465     LYS A  1968
REMARK 465     LEU A  1969
REMARK 465     ARG A  1970
REMARK 465     SER A  1971
REMARK 465     GLU A  1972
REMARK 465     GLN A  1973
REMARK 465     SER B  1661
REMARK 465     ASP B  1662
REMARK 465     ARG B  1663
REMARK 465     PRO B  1664
REMARK 465     LEU B  1665
REMARK 465     SER B  1666
REMARK 465     VAL B  1667
REMARK 465     HIS B  1668
REMARK 465     LEU B  1669
REMARK 465     ASN B  1670
REMARK 465     LEU B  1671
REMARK 465     GLY B  1672
REMARK 465     GLN B  1673
REMARK 465     LYS B  1674
REMARK 465     GLY B  1675
REMARK 465     ASN B  1676
REMARK 465     ARG B  1677
REMARK 465     LYS B  1678
REMARK 465     VAL B  1749
REMARK 465     ASP B  1750
REMARK 465     ASP B  1751
REMARK 465     ASP B  1752
REMARK 465     PRO B  1753
REMARK 465     GLN B  1853
REMARK 465     LEU B  1854
REMARK 465     ASP B  1855
REMARK 465     ARG B  1970
REMARK 465     SER B  1971
REMARK 465     GLU B  1972
REMARK 465     GLN B  1973
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    HOH A   150     O    HOH A   226              2.06
REMARK 500   O    HOH B    80     O    HOH B   256              2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   NH1  ARG B  1715     O    HOH B   132     2747     0.92
REMARK 500   CD   ARG A  1715     O    HOH A   215     2556     1.26
REMARK 500   NH1  ARG A  1715     O    HOH A   129     2556     1.28
REMARK 500   CZ   ARG B  1715     O    HOH B   132     2747     1.33
REMARK 500   CZ   ARG A  1715     O    HOH A   129     2556     1.51
REMARK 500   NH2  ARG A  1715     O    HOH A   129     2556     1.59
REMARK 500   NE   ARG A  1715     O    HOH A   215     2556     1.71
REMARK 500   NH2  ARG B  1715     O    HOH B   132     2747     2.01
REMARK 500   NH1  ARG A  1715     O    HOH A   215     2556     2.10
REMARK 500   CZ   ARG A  1715     O    HOH A   215     2556     2.11
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    ARG A1858   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.9 DEGREES
REMARK 500    ARG A1910   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.0 DEGREES
REMARK 500    ASP A1938   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES
REMARK 500    MET A1946   CG  -  SD  -  CE  ANGL. DEV. = -20.4 DEGREES
REMARK 500    CYS B1849   CA  -  CB  -  SG  ANGL. DEV. =   6.9 DEGREES
REMARK 500    ARG B1910   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.7 DEGREES
REMARK 500    ASP B1938   CB  -  CG  -  OD1 ANGL. DEV. =   7.0 DEGREES
REMARK 500    CYS B1951   CA  -  CB  -  SG  ANGL. DEV. =   6.8 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    THR A1679      137.39    163.17
REMARK 500    SER A1680      118.10     37.01
REMARK 500    LYS A1684      125.40    -29.53
REMARK 500    ARG A1770       58.88   -113.31
REMARK 500    LYS A1811      -31.23   -130.39
REMARK 500    ALA A1818      -37.41    -39.40
REMARK 500    ASP A1819     -156.99   -160.73
REMARK 500    HIS A1871       -2.31     63.10
REMARK 500    SER A1894       76.60   -118.92
REMARK 500    CYS A1904     -127.41   -132.00
REMARK 500    VAL A1908      -54.77   -133.94
REMARK 500    ASP A1931       74.95   -116.37
REMARK 500    HIS A1945       18.09     47.91
REMARK 500    VAL A1947       94.85     60.64
REMARK 500    SER B1680      137.80     34.31
REMARK 500    CYS B1681       71.16   -151.60
REMARK 500    SER B1699       78.13     33.79
REMARK 500    CYS B1719       39.76   -140.74
REMARK 500    ARG B1770       60.68   -115.03
REMARK 500    ASN B1794       34.45     70.31
REMARK 500    ASP B1819     -154.01   -152.50
REMARK 500    HIS B1857       74.55    116.84
REMARK 500    HIS B1871       11.00     48.74
REMARK 500    SER B1894       66.62   -107.17
REMARK 500    CYS B1904     -125.76   -134.23
REMARK 500    VAL B1908      -56.79   -135.36
REMARK 500    SER B1926        1.98   -160.74
REMARK 500    VAL B1947       85.00     64.22
REMARK 500    ARG B1965        4.05    -62.65
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 LYS A 1678     THR A 1679                 -141.36
REMARK 500 SER A 1926     LYS A 1927                 -147.13
REMARK 500 ASN B 1766     ASN B 1767                 -144.62
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    HIS A1942        24.4      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 329        DISTANCE =  7.36 ANGSTROMS
REMARK 525    HOH B 237        DISTANCE =  5.20 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2UN B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2UN A 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2HO3   RELATED DB: PDB
REMARK 900 STRUCTURAL STUDIES OF PROTEIN TYROSINE PHOSPHATASE BETA
REMARK 900 CATALYTIC DOMAIN IN COMPLEX WITH INHIBITORS
REMARK 900 RELATED ID: 2HO4   RELATED DB: PDB
REMARK 900 STRUCTURAL STUDIES OF PROTEIN TYROSINE PHOSPHATASE BETA
REMARK 900 CATALYTIC DOMAIN IN COMPLEX WITH INHIBITORS
DBREF  2H02 A 1662  1973  UNP    Q3MIV7   Q3MIV7_HUMAN  1662   1973
DBREF  2H02 B 1662  1973  UNP    Q3MIV7   Q3MIV7_HUMAN  1662   1973
SEQADV 2H02 SER A 1661  UNP  Q3MIV7              CLONING ARTIFACT
SEQADV 2H02 SER B 1661  UNP  Q3MIV7              CLONING ARTIFACT
SEQRES   1 A  313  SER ASP ARG PRO LEU SER VAL HIS LEU ASN LEU GLY GLN
SEQRES   2 A  313  LYS GLY ASN ARG LYS THR SER CYS PRO ILE LYS ILE ASN
SEQRES   3 A  313  GLN PHE GLU GLY HIS PHE MET LYS LEU GLN ALA ASP SER
SEQRES   4 A  313  ASN TYR LEU LEU SER LYS GLU TYR GLU GLU LEU LYS ASP
SEQRES   5 A  313  VAL GLY ARG ASN GLN SER CYS ASP ILE ALA LEU LEU PRO
SEQRES   6 A  313  GLU ASN ARG GLY LYS ASN ARG TYR ASN ASN ILE LEU PRO
SEQRES   7 A  313  TYR ASP ALA THR ARG VAL LYS LEU SER ASN VAL ASP ASP
SEQRES   8 A  313  ASP PRO CYS SER ASP TYR ILE ASN ALA SER TYR ILE PRO
SEQRES   9 A  313  GLY ASN ASN PHE ARG ARG GLU TYR ILE VAL THR GLN GLY
SEQRES  10 A  313  PRO LEU PRO GLY THR LYS ASP ASP PHE TRP LYS MET VAL
SEQRES  11 A  313  TRP GLU GLN ASN VAL HIS ASN ILE VAL MET VAL THR GLN
SEQRES  12 A  313  CYS VAL GLU LYS GLY ARG VAL LYS CYS ASP HIS TYR TRP
SEQRES  13 A  313  PRO ALA ASP GLN ASP SER LEU TYR TYR GLY ASP LEU ILE
SEQRES  14 A  313  LEU GLN MET LEU SER GLU SER VAL LEU PRO GLU TRP THR
SEQRES  15 A  313  ILE ARG GLU PHE LYS ILE CYS GLY GLU GLU GLN LEU ASP
SEQRES  16 A  313  ALA HIS ARG LEU ILE ARG HIS PHE HIS TYR THR VAL TRP
SEQRES  17 A  313  PRO ASP HIS GLY VAL PRO GLU THR THR GLN SER LEU ILE
SEQRES  18 A  313  GLN PHE VAL ARG THR VAL ARG ASP TYR ILE ASN ARG SER
SEQRES  19 A  313  PRO GLY ALA GLY PRO THR VAL VAL HIS CYS SER ALA GLY
SEQRES  20 A  313  VAL GLY ARG THR GLY THR PHE ILE ALA LEU ASP ARG ILE
SEQRES  21 A  313  LEU GLN GLN LEU ASP SER LYS ASP SER VAL ASP ILE TYR
SEQRES  22 A  313  GLY ALA VAL HIS ASP LEU ARG LEU HIS ARG VAL HIS MET
SEQRES  23 A  313  VAL GLN THR GLU CYS GLN TYR VAL TYR LEU HIS GLN CYS
SEQRES  24 A  313  VAL ARG ASP VAL LEU ARG ALA ARG LYS LEU ARG SER GLU
SEQRES  25 A  313  GLN
SEQRES   1 B  313  SER ASP ARG PRO LEU SER VAL HIS LEU ASN LEU GLY GLN
SEQRES   2 B  313  LYS GLY ASN ARG LYS THR SER CYS PRO ILE LYS ILE ASN
SEQRES   3 B  313  GLN PHE GLU GLY HIS PHE MET LYS LEU GLN ALA ASP SER
SEQRES   4 B  313  ASN TYR LEU LEU SER LYS GLU TYR GLU GLU LEU LYS ASP
SEQRES   5 B  313  VAL GLY ARG ASN GLN SER CYS ASP ILE ALA LEU LEU PRO
SEQRES   6 B  313  GLU ASN ARG GLY LYS ASN ARG TYR ASN ASN ILE LEU PRO
SEQRES   7 B  313  TYR ASP ALA THR ARG VAL LYS LEU SER ASN VAL ASP ASP
SEQRES   8 B  313  ASP PRO CYS SER ASP TYR ILE ASN ALA SER TYR ILE PRO
SEQRES   9 B  313  GLY ASN ASN PHE ARG ARG GLU TYR ILE VAL THR GLN GLY
SEQRES  10 B  313  PRO LEU PRO GLY THR LYS ASP ASP PHE TRP LYS MET VAL
SEQRES  11 B  313  TRP GLU GLN ASN VAL HIS ASN ILE VAL MET VAL THR GLN
SEQRES  12 B  313  CYS VAL GLU LYS GLY ARG VAL LYS CYS ASP HIS TYR TRP
SEQRES  13 B  313  PRO ALA ASP GLN ASP SER LEU TYR TYR GLY ASP LEU ILE
SEQRES  14 B  313  LEU GLN MET LEU SER GLU SER VAL LEU PRO GLU TRP THR
SEQRES  15 B  313  ILE ARG GLU PHE LYS ILE CYS GLY GLU GLU GLN LEU ASP
SEQRES  16 B  313  ALA HIS ARG LEU ILE ARG HIS PHE HIS TYR THR VAL TRP
SEQRES  17 B  313  PRO ASP HIS GLY VAL PRO GLU THR THR GLN SER LEU ILE
SEQRES  18 B  313  GLN PHE VAL ARG THR VAL ARG ASP TYR ILE ASN ARG SER
SEQRES  19 B  313  PRO GLY ALA GLY PRO THR VAL VAL HIS CYS SER ALA GLY
SEQRES  20 B  313  VAL GLY ARG THR GLY THR PHE ILE ALA LEU ASP ARG ILE
SEQRES  21 B  313  LEU GLN GLN LEU ASP SER LYS ASP SER VAL ASP ILE TYR
SEQRES  22 B  313  GLY ALA VAL HIS ASP LEU ARG LEU HIS ARG VAL HIS MET
SEQRES  23 B  313  VAL GLN THR GLU CYS GLN TYR VAL TYR LEU HIS GLN CYS
SEQRES  24 B  313  VAL ARG ASP VAL LEU ARG ALA ARG LYS LEU ARG SER GLU
SEQRES  25 B  313  GLN
HET    2UN  B 401      28
HET    2UN  A 402      28
HETNAM     2UN {4-[2-BENZYL-3-METHOXY-2-(METHOXYCARBONYL)-3-
HETNAM   2 2UN  OXOPROPYL]PHENYL}SULFAMIC ACID
FORMUL   3  2UN    2(C19 H21 N O7 S)
FORMUL   5  HOH   *290(H2 O)
HELIX    1   1 GLN A 1687  LEU A 1710  1                                  24
HELIX    2   2 LYS A 1711  VAL A 1713  5                                   3
HELIX    3   3 LEU A 1724  ASN A 1731  5                                   8
HELIX    4   4 TYR A 1739  ALA A 1741  5                                   3
HELIX    5   5 THR A 1782  GLN A 1793  1                                  12
HELIX    6   6 THR A 1876  ARG A 1893  1                                  18
HELIX    7   7 VAL A 1908  LYS A 1927  1                                  20
HELIX    8   8 ASP A 1931  ARG A 1943  1                                  13
HELIX    9   9 THR A 1949  ARG A 1967  1                                  19
HELIX   10  10 GLN B 1687  LEU B 1710  1                                  24
HELIX   11  11 LYS B 1711  VAL B 1713  5                                   3
HELIX   12  12 LEU B 1724  ASN B 1731  5                                   8
HELIX   13  13 THR B 1782  GLN B 1793  1                                  12
HELIX   14  14 THR B 1876  ARG B 1893  1                                  18
HELIX   15  15 VAL B 1908  ASP B 1925  1                                  18
HELIX   16  16 ASP B 1931  ARG B 1943  1                                  13
HELIX   17  17 THR B 1949  LYS B 1968  1                                  20
SHEET    1   A 2 ILE A1683  LYS A1684  0
SHEET    2   A 2 SER A1929  VAL A1930 -1  O  VAL A1930   N  ILE A1683
SHEET    1   B 9 ARG A1743  LYS A1745  0
SHEET    2   B 9 TYR A1757  ILE A1763 -1  O  ALA A1760   N  VAL A1744
SHEET    3   B 9 TYR A1772  THR A1775 -1  O  VAL A1774   N  SER A1761
SHEET    4   B 9 THR A1900  HIS A1903  1  O  THR A1900   N  ILE A1773
SHEET    5   B 9 ASN A1797  MET A1800  1  N  VAL A1799   O  VAL A1901
SHEET    6   B 9 ARG A1858  TYR A1865  1  O  PHE A1863   N  MET A1800
SHEET    7   B 9 TRP A1841  CYS A1849 -1  N  PHE A1846   O  ILE A1860
SHEET    8   B 9 LEU A1828  VAL A1837 -1  N  SER A1836   O  ILE A1843
SHEET    9   B 9 LEU A1823  TYR A1825 -1  N  LEU A1823   O  LEU A1830
SHEET    1   C 2 VAL A1805  GLU A1806  0
SHEET    2   C 2 ARG A1809  VAL A1810 -1  O  ARG A1809   N  GLU A1806
SHEET    1   D 2 ILE B1683  LYS B1684  0
SHEET    2   D 2 SER B1929  VAL B1930 -1  O  VAL B1930   N  ILE B1683
SHEET    1   E 9 ARG B1743  LYS B1745  0
SHEET    2   E 9 TYR B1757  ILE B1763 -1  O  ALA B1760   N  VAL B1744
SHEET    3   E 9 TYR B1772  THR B1775 -1  O  VAL B1774   N  SER B1761
SHEET    4   E 9 THR B1900  HIS B1903  1  O  VAL B1902   N  ILE B1773
SHEET    5   E 9 ASN B1797  MET B1800  1  N  VAL B1799   O  VAL B1901
SHEET    6   E 9 ARG B1858  TYR B1865  1  O  PHE B1863   N  MET B1800
SHEET    7   E 9 TRP B1841  CYS B1849 -1  N  THR B1842   O  HIS B1864
SHEET    8   E 9 LEU B1828  VAL B1837 -1  N  GLN B1831   O  LYS B1847
SHEET    9   E 9 LEU B1823  TYR B1825 -1  N  LEU B1823   O  LEU B1830
SHEET    1   F 2 VAL B1805  GLU B1806  0
SHEET    2   F 2 ARG B1809  VAL B1810 -1  O  ARG B1809   N  GLU B1806
SITE     1 AC1 11 TYR B1733  ASN B1735  ASP B1870  HIS B1871
SITE     2 AC1 11 CYS B1904  SER B1905  ALA B1906  VAL B1908
SITE     3 AC1 11 GLY B1909  ARG B1910  GLN B1948
SITE     1 AC2 12 TYR A1733  ASN A1735  ASP A1870  HIS A1871
SITE     2 AC2 12 CYS A1904  SER A1905  ALA A1906  GLY A1907
SITE     3 AC2 12 VAL A1908  GLY A1909  ARG A1910  GLN A1948
CRYST1   62.144   71.724   70.297  90.00  93.41  90.00 P 1 21 1      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      0.016092  0.000000  0.000959        0.00000
SCALE2      0.000000  0.013942  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014251        0.00000
      
PROCHECK
Go to PROCHECK summary
 References