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PDBsum entry 3cwe

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Hydrolase PDB id
3cwe
Jmol
Contents
Protein chain
285 a.a.
Ligands
825
Metals
_MG ×3
Waters ×318
HEADER    HYDROLASE                               21-APR-08   3CWE
TITLE     PTP1B IN COMPLEX WITH A PHOSPHONIC ACID INHIBITOR
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 1;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: TYROSINE-PROTEIN PHOSPHATASE DOMAIN;
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 GENE: PTPN1, PTP1B;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET
KEYWDS    PHOSPHATASE, PHOSPHONATES, DIABETES, INHIBITOR, ACETYLATION,
KEYWDS   2 ENDOPLASMIC RETICULUM, HYDROLASE, MEMBRANE, OXIDATION,
KEYWDS   3 PHOSPHOPROTEIN, POLYMORPHISM, PROTEIN PHOSPHATASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    G.SCAPIN,Y.HAN,B.P.KENNEDY
REVDAT   2   24-FEB-09 3CWE    1       VERSN
REVDAT   1   10-JUN-08 3CWE    0
JRNL        AUTH   Y.HAN,M.BELLEY,C.I.BAYLY,J.COLUCCI,C.DUFRESNE,
JRNL        AUTH 2 A.GIROUX,C.K.LAU,Y.LEBLANC,D.MCKAY,M.THERIEN,
JRNL        AUTH 3 M.C.WILSON,K.SKOREY,C.C.CHAN,G.SCAPIN,B.P.KENNEDY
JRNL        TITL   DISCOVERY OF
JRNL        TITL 2 [(3-BROMO-7-CYANO-2-NAPHTHYL)(DIFLUORO)
JRNL        TITL 3 METHYL]PHOSPHONIC ACID, A POTENT AND ORALLY ACTIVE
JRNL        TITL 4 SMALL MOLECULE PTP1B INHIBITOR
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  18  3200 2008
JRNL        REFN                   ISSN 0960-894X
JRNL        PMID   18477508
JRNL        DOI    10.1016/J.BMCL.2008.04.064
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
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) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.39
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.7
REMARK   3   NUMBER OF REFLECTIONS             : 61668
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) : 0.177
REMARK   3   R VALUE            (WORKING SET) : 0.176
REMARK   3   FREE R VALUE                     : 0.193
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 3090
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 10
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.69
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 8203
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.90
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2040
REMARK   3   BIN FREE R VALUE SET COUNT          : 446
REMARK   3   BIN FREE R VALUE                    : 0.2540
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2334
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 33
REMARK   3   SOLVENT ATOMS            : 318
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 16.30
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.50
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.18000
REMARK   3    B22 (A**2) : -0.18000
REMARK   3    B33 (A**2) : 0.26000
REMARK   3    B12 (A**2) : -0.09000
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): 0.081
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.068
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.037
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.252
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2418 ; 0.009 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3260 ; 1.249 ; 1.970
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   283 ; 5.201 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   118 ;32.461 ;23.983
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   447 ;13.340 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    17 ;20.092 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   345 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1823 ; 0.005 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1220 ; 0.199 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1672 ; 0.313 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   265 ; 0.153 ; 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):    35 ; 0.160 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    27 ; 0.270 ; 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):  1457 ; 1.011 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2304 ; 1.455 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1087 ; 2.539 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   956 ; 3.535 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2544 ; 1.899 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   321 ; 4.100 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2364 ; 2.493 ; 3.000
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 : 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 3CWE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-APR-08.
REMARK 100 THE RCSB ID CODE IS RCSB047293.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 10-DEC-99
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 17-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                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 63877
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9
REMARK 200  DATA REDUNDANCY                : 5.300
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.05200
REMARK 200   FOR THE DATA SET  : 12.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.70
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.30
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.24200
REMARK 200   FOR SHELL         : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 65.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, MGCL2, HEPES, PH 7.0,
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 284K
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       34.80867
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       69.61733
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       69.61733
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       34.80867
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: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLU A   615
REMARK 465     LYS A   616
REMARK 465     GLY A   617
REMARK 465     SER A   618
REMARK 465     LEU A   619
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 A 614    CG   SD   CE
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  1012     O    HOH A  1043              1.96
REMARK 500   OE2  GLU A   659     O    HOH A   793              2.12
REMARK 500   OD1  ASP A   681     O    HOH A  1101              2.16
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   O    HOH A  1098     O    HOH A  1098     4555     2.03
REMARK 500   O    HOH A  1056     O    HOH A  1098     4555     2.07
REMARK 500   O    HOH A  1055     O    HOH A  1055     4555     2.14
REMARK 500   O    HOH A  1097     O    HOH A  1097     4555     2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    ASP A 563      -73.76    -59.94
REMARK 500    CYS A 621      132.47   -179.84
REMARK 500    PHE A 682       19.65     59.18
REMARK 500    CYS A 715     -129.00   -136.61
REMARK 500    ILE A 719      -44.77   -132.59
REMARK 500    ILE A 761      119.79     73.67
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 879        DISTANCE =  6.10 ANGSTROMS
REMARK 525    HOH A1015        DISTANCE =  5.90 ANGSTROMS
REMARK 525    HOH A1064        DISTANCE =  6.72 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A   1  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 787   O
REMARK 620 2 HOH A 790   O    92.8
REMARK 620 3 HOH A 785   O    92.8  87.8
REMARK 620 4 HOH A 789   O    92.7  87.6 172.9
REMARK 620 5 HOH A 786   O    81.6 171.8  98.4  86.7
REMARK 620 6 HOH A 788   O   164.0 102.2  82.3  93.5  84.1
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A   2  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 796   O
REMARK 620 2 HOH A1073   O    69.9
REMARK 620 3 HOH A 794   O    88.3  91.1
REMARK 620 4 HOH A 795   O    83.5 153.0  93.1
REMARK 620 5 HOH A 791   O   172.7 115.9  95.9  90.3
REMARK 620 6 HOH A 792   O    92.0  83.7 174.3  92.6  84.4
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A   3  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 797   O
REMARK 620 2 HOH A 800   O    96.4
REMARK 620 3 HOH A 799   O   123.5  69.3
REMARK 620 N                    1     2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 2
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 825 A 784
DBREF  3CWE A  501   783  UNP    P18031   PTN1_HUMAN       1    283
SEQADV 3CWE ALA A  494  UNP  P18031              EXPRESSION TAG
SEQADV 3CWE ALA A  495  UNP  P18031              EXPRESSION TAG
SEQADV 3CWE ASP A  496  UNP  P18031              EXPRESSION TAG
SEQADV 3CWE LYS A  497  UNP  P18031              EXPRESSION TAG
SEQADV 3CWE LEU A  498  UNP  P18031              EXPRESSION TAG
SEQADV 3CWE GLU A  499  UNP  P18031              EXPRESSION TAG
SEQADV 3CWE PHE A  500  UNP  P18031              EXPRESSION TAG
SEQRES   1 A  290  ALA ALA ASP LYS LEU GLU PHE MET GLU MET GLU LYS GLU
SEQRES   2 A  290  PHE GLU GLN ILE ASP LYS SER GLY SER TRP ALA ALA ILE
SEQRES   3 A  290  TYR GLN ASP ILE ARG HIS GLU ALA SER ASP PHE PRO CYS
SEQRES   4 A  290  ARG VAL ALA LYS LEU PRO LYS ASN LYS ASN ARG ASN ARG
SEQRES   5 A  290  TYR ARG ASP VAL SER PRO PHE ASP HIS SER ARG ILE LYS
SEQRES   6 A  290  LEU HIS GLN GLU ASP ASN ASP TYR ILE ASN ALA SER LEU
SEQRES   7 A  290  ILE LYS MET GLU GLU ALA GLN ARG SER TYR ILE LEU THR
SEQRES   8 A  290  GLN GLY PRO LEU PRO ASN THR CYS GLY HIS PHE TRP GLU
SEQRES   9 A  290  MET VAL TRP GLU GLN LYS SER ARG GLY VAL VAL MET LEU
SEQRES  10 A  290  ASN ARG VAL MET GLU LYS GLY SER LEU LYS CYS ALA GLN
SEQRES  11 A  290  TYR TRP PRO GLN LYS GLU GLU LYS GLU MET ILE PHE GLU
SEQRES  12 A  290  ASP THR ASN LEU LYS LEU THR LEU ILE SER GLU ASP ILE
SEQRES  13 A  290  LYS SER TYR TYR THR VAL ARG GLN LEU GLU LEU GLU ASN
SEQRES  14 A  290  LEU THR THR GLN GLU THR ARG GLU ILE LEU HIS PHE HIS
SEQRES  15 A  290  TYR THR THR TRP PRO ASP PHE GLY VAL PRO GLU SER PRO
SEQRES  16 A  290  ALA SER PHE LEU ASN PHE LEU PHE LYS VAL ARG GLU SER
SEQRES  17 A  290  GLY SER LEU SER PRO GLU HIS GLY PRO VAL VAL VAL HIS
SEQRES  18 A  290  CYS SER ALA GLY ILE GLY ARG SER GLY THR PHE CYS LEU
SEQRES  19 A  290  ALA ASP THR CYS LEU LEU LEU MET ASP LYS ARG LYS ASP
SEQRES  20 A  290  PRO SER SER VAL ASP ILE LYS LYS VAL LEU LEU GLU MET
SEQRES  21 A  290  ARG LYS PHE ARG MET GLY LEU ILE GLN THR ALA ASP GLN
SEQRES  22 A  290  LEU ARG PHE SER TYR LEU ALA VAL ILE GLU GLY ALA LYS
SEQRES  23 A  290  PHE ILE MET GLY
HET     MG  A   1       1
HET     MG  A   2       1
HET     MG  A   3       1
HET    825  A 784      30
HETNAM      MG MAGNESIUM ION
HETNAM     825 [{2-BROMO-4-[(2R)-3-OXO-2,3-
HETNAM   2 825  DIPHENYLPROPYL]PHENYL}(DIFLUORO)METHYL]PHOSPHONIC ACID
FORMUL   2   MG    3(MG 2+)
FORMUL   5  825    C22 H18 BR F2 O4 P
FORMUL   6  HOH   *318(H2 O)
HELIX    1   1 ALA A  495  GLY A  514  1                                  20
HELIX    2   2 SER A  515  ALA A  527  1                                  13
HELIX    3   3 LEU A  537  ASN A  544  5                                   8
HELIX    4   4 PHE A  552  HIS A  554  5                                   3
HELIX    5   5 THR A  591  LYS A  603  1                                  13
HELIX    6   6 SER A  687  SER A  701  1                                  15
HELIX    7   7 ILE A  719  ARG A  738  1                                  20
HELIX    8   8 ASP A  740  VAL A  744  5                                   5
HELIX    9   9 ASP A  745  ARG A  754  1                                  10
HELIX   10  10 THR A  763  GLY A  783  1                                  21
SHEET    1   A 9 ARG A 556  LYS A 558  0
SHEET    2   A 9 TYR A 566  MET A 574 -1  O  ALA A 569   N  ILE A 557
SHEET    3   A 9 ARG A 579  THR A 584 -1  O  TYR A 581   N  ILE A 572
SHEET    4   A 9 VAL A 711  HIS A 714  1  O  VAL A 713   N  ILE A 582
SHEET    5   A 9 GLY A 606  MET A 609  1  N  VAL A 608   O  VAL A 712
SHEET    6   A 9 THR A 668  TYR A 676  1  O  PHE A 674   N  VAL A 607
SHEET    7   A 9 TYR A 653  ASN A 662 -1  N  THR A 654   O  HIS A 675
SHEET    8   A 9 LEU A 640  ILE A 649 -1  N  LYS A 641   O  GLU A 661
SHEET    9   A 9 MET A 633  PHE A 635 -1  N  PHE A 635   O  LEU A 640
LINK        MG    MG A   1                 O   HOH A 787     1555   1555  2.07
LINK        MG    MG A   1                 O   HOH A 790     1555   1555  2.06
LINK        MG    MG A   1                 O   HOH A 785     1555   1555  2.18
LINK        MG    MG A   1                 O   HOH A 789     1555   1555  2.06
LINK        MG    MG A   1                 O   HOH A 786     1555   1555  2.04
LINK        MG    MG A   1                 O   HOH A 788     1555   1555  2.04
LINK        MG    MG A   2                 O   HOH A 796     1555   1555  2.40
LINK        MG    MG A   2                 O   HOH A1073     1555   1555  2.03
LINK        MG    MG A   2                 O   HOH A 794     1555   1555  2.09
LINK        MG    MG A   2                 O   HOH A 795     1555   1555  2.02
LINK        MG    MG A   2                 O   HOH A 791     1555   1555  2.25
LINK        MG    MG A   2                 O   HOH A 792     1555   1555  2.09
LINK        MG    MG A   3                 O   HOH A 797     1555   1555  2.13
LINK        MG    MG A   3                 O   HOH A 800     1555   1555  2.05
LINK        MG    MG A   3                 O   HOH A 799     1555   1555  2.24
SITE     1 AC1  6 HOH A 785  HOH A 786  HOH A 787  HOH A 788
SITE     2 AC1  6 HOH A 789  HOH A 790
SITE     1 AC2  6 HOH A 791  HOH A 792  HOH A 794  HOH A 795
SITE     2 AC2  6 HOH A 796  HOH A1073
SITE     1 AC3  4 HOH A 797  HOH A 798  HOH A 799  HOH A 800
SITE     1 AC4 18 GLN A 521  ASP A 522  ARG A 524  HIS A 525
SITE     2 AC4 18 TYR A 546  ASP A 548  ASP A 681  PHE A 682
SITE     3 AC4 18 CYS A 715  SER A 716  ALA A 717  GLY A 718
SITE     4 AC4 18 ILE A 719  GLY A 720  ARG A 721  GLN A 762
SITE     5 AC4 18 HOH A 820  HOH A 953
CRYST1   88.747   88.747  104.426  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      0.011268  0.006506  0.000000        0.00000
SCALE2      0.000000  0.013011  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009576        0.00000
      
PROCHECK
Go to PROCHECK summary
 References