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PDBsum entry 3f81

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Top Page protein ligands Protein-protein interface(s) links
Hydrolase PDB id
3f81
Jmol
Contents
Protein chains
179 a.a.
Ligands
STT ×2
Waters ×219
HEADER    HYDROLASE                               11-NOV-08   3F81
TITLE     INTERACTION OF VHR WITH SA3
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: DUAL SPECIFICITY PROTEIN PHOSPHATASE 3;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: UNP RESIDUES 3-185;
COMPND   5 SYNONYM: DUAL SPECIFICITY PROTEIN PHOSPHATASE VHR;
COMPND   6 EC: 3.1.3.48, 3.1.3.16;
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 GENE: DUSP3, VHR;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX-4T-1
KEYWDS    HYDROLASE, PROTEIN DUAL-SPECIFICITY PHOSPHATASE, INHIBITOR,
KEYWDS   2 PROTEIN PHOSPHATASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.WU,T.MUTELIN,L.TAUTZ
REVDAT   2   17-NOV-09 3F81    1       JRNL
REVDAT   1   10-NOV-09 3F81    0
JRNL        AUTH   S.WU,S.VOSSIUS,S.RAHMOUNI,A.V.MILETIC,T.VANG,
JRNL        AUTH 2 J.VAZQUEZ-RODRIGUEZ,F.CERIGNOLI,Y.ARIMURA,
JRNL        AUTH 3 S.WILLIAMS,T.HAYES,M.MOUTSCHEN,S.VASILE,
JRNL        AUTH 4 M.PELLECCHIA,T.MUSTELIN,L.TAUTZ
JRNL        TITL   MULTIDENTATE SMALL-MOLECULE INHIBITORS OF VACCINIA
JRNL        TITL 2 H1-RELATED (VHR) PHOSPHATASE DECREASE PROLIFERATION
JRNL        TITL 3 OF CERVIX CANCER CELLS.
JRNL        REF    J.MED.CHEM.                   V.  52  6716 2009
JRNL        REFN                   ISSN 0022-2623
JRNL        PMID   19888758
JRNL        DOI    10.1021/JM901016K
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    1.90 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) : 1.90
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1
REMARK   3   NUMBER OF REFLECTIONS             : 26330
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) : 0.180
REMARK   3   R VALUE            (WORKING SET) : 0.178
REMARK   3   FREE R VALUE                     : 0.219
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 1408
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) : 1.90
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1922
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.73
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1840
REMARK   3   BIN FREE R VALUE SET COUNT          : 106
REMARK   3   BIN FREE R VALUE                    : 0.2360
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2784
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 219
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.51
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.79000
REMARK   3    B22 (A**2) : -0.49000
REMARK   3    B33 (A**2) : -0.46000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : -0.58000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.160
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.144
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.087
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.807
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.946
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.918
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2856 ; 0.016 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3862 ; 1.724 ; 1.979
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   356 ; 9.920 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   136 ;38.973 ;24.706
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   500 ;15.395 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;17.852 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   428 ; 0.247 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2174 ; 0.006 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1405 ; 0.223 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1948 ; 0.303 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   214 ; 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):    52 ; 0.213 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    21 ; 0.273 ; 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):  1837 ; 0.912 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2854 ; 1.464 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1145 ; 2.541 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1008 ; 4.051 ; 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 : 1
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 1
REMARK   3     CHAIN NAMES                    : A B
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     A      7       A     185      4
REMARK   3           1     B      7       B     185      4
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1392 ;  0.57 ;  0.50
REMARK   3   MEDIUM THERMAL     1    A (A**2):   1392 ;  0.98 ;  2.00
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: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3F81 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-NOV-08.
REMARK 100 THE RCSB ID CODE IS RCSB050262.
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) : 140
REMARK 200  PH                             : 7.4
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 FR-E SUPERBRIGHT
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26330
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1
REMARK 200  DATA REDUNDANCY                : 6.800
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.05900
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.95
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CCP4
REMARK 200 STARTING MODEL: PDB ENTRY 1VHR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS  15% POLYETHYLENE
REMARK 280  GLYCOL 8000, 60 MM NAF, PH 7.4, VAPOR DIFFUSION, HANGING DROP,
REMARK 280  TEMPERATURE 297.0K
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       29.59300
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: DIMERIC
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   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000       29.59300
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
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 350   BIOMT1   2 -1.000000  0.000000  0.000000       41.58708
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000       29.59300
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       60.01147
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     GLY A     3
REMARK 465     SER A     4
REMARK 465     PHE A     5
REMARK 465     GLU A     6
REMARK 465     GLY B     3
REMARK 465     SER B     4
REMARK 465     PHE B     5
REMARK 465     GLU B     6
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    ARG A 104   CG    ARG A 104   CD      0.241
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 A 104   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES
REMARK 500    SER B   8   N   -  CA  -  C   ANGL. DEV. = -16.3 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    CYS A 124     -146.80   -137.25
REMARK 500    SER A 129      -57.05   -123.75
REMARK 500    CYS B 124     -143.29   -138.47
REMARK 500    SER B 129      -58.26   -122.50
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 ALA A  114     GLN A  115                  135.00
REMARK 500 LEU B    7     SER B    8                  -78.51
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    GLN A 115        22.0      L          L   OUTSIDE RANGE
REMARK 500    MET B  69        22.2      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 LIGAND STT IN THIS PDB FILE REFERS TO SA3 IN CITATION.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE STT A 1
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE STT B 1
DBREF  3F81 A    3   185  UNP    P51452   DUS3_HUMAN       3    185
DBREF  3F81 B    3   185  UNP    P51452   DUS3_HUMAN       3    185
SEQRES   1 A  183  GLY SER PHE GLU LEU SER VAL GLN ASP LEU ASN ASP LEU
SEQRES   2 A  183  LEU SER ASP GLY SER GLY CYS TYR SER LEU PRO SER GLN
SEQRES   3 A  183  PRO CYS ASN GLU VAL THR PRO ARG ILE TYR VAL GLY ASN
SEQRES   4 A  183  ALA SER VAL ALA GLN ASP ILE PRO LYS LEU GLN LYS LEU
SEQRES   5 A  183  GLY ILE THR HIS VAL LEU ASN ALA ALA GLU GLY ARG SER
SEQRES   6 A  183  PHE MET HIS VAL ASN THR ASN ALA ASN PHE TYR LYS ASP
SEQRES   7 A  183  SER GLY ILE THR TYR LEU GLY ILE LYS ALA ASN ASP THR
SEQRES   8 A  183  GLN GLU PHE ASN LEU SER ALA TYR PHE GLU ARG ALA ALA
SEQRES   9 A  183  ASP PHE ILE ASP GLN ALA LEU ALA GLN LYS ASN GLY ARG
SEQRES  10 A  183  VAL LEU VAL HIS CYS ARG GLU GLY TYR SER ARG SER PRO
SEQRES  11 A  183  THR LEU VAL ILE ALA TYR LEU MET MET ARG GLN LYS MET
SEQRES  12 A  183  ASP VAL LYS SER ALA LEU SER ILE VAL ARG GLN ASN ARG
SEQRES  13 A  183  GLU ILE GLY PRO ASN ASP GLY PHE LEU ALA GLN LEU CYS
SEQRES  14 A  183  GLN LEU ASN ASP ARG LEU ALA LYS GLU GLY LYS LEU LYS
SEQRES  15 A  183  PRO
SEQRES   1 B  183  GLY SER PHE GLU LEU SER VAL GLN ASP LEU ASN ASP LEU
SEQRES   2 B  183  LEU SER ASP GLY SER GLY CYS TYR SER LEU PRO SER GLN
SEQRES   3 B  183  PRO CYS ASN GLU VAL THR PRO ARG ILE TYR VAL GLY ASN
SEQRES   4 B  183  ALA SER VAL ALA GLN ASP ILE PRO LYS LEU GLN LYS LEU
SEQRES   5 B  183  GLY ILE THR HIS VAL LEU ASN ALA ALA GLU GLY ARG SER
SEQRES   6 B  183  PHE MET HIS VAL ASN THR ASN ALA ASN PHE TYR LYS ASP
SEQRES   7 B  183  SER GLY ILE THR TYR LEU GLY ILE LYS ALA ASN ASP THR
SEQRES   8 B  183  GLN GLU PHE ASN LEU SER ALA TYR PHE GLU ARG ALA ALA
SEQRES   9 B  183  ASP PHE ILE ASP GLN ALA LEU ALA GLN LYS ASN GLY ARG
SEQRES  10 B  183  VAL LEU VAL HIS CYS ARG GLU GLY TYR SER ARG SER PRO
SEQRES  11 B  183  THR LEU VAL ILE ALA TYR LEU MET MET ARG GLN LYS MET
SEQRES  12 B  183  ASP VAL LYS SER ALA LEU SER ILE VAL ARG GLN ASN ARG
SEQRES  13 B  183  GLU ILE GLY PRO ASN ASP GLY PHE LEU ALA GLN LEU CYS
SEQRES  14 B  183  GLN LEU ASN ASP ARG LEU ALA LYS GLU GLY LYS LEU LYS
SEQRES  15 B  183  PRO
HET    STT  A   1      14
HET    STT  B   1      14
HETNAM     STT 2-(5-METHYL-4-OXO-2-THIOXO-2,4-DIHYDRO-3H-1LAMBDA~4~,3-
HETNAM   2 STT  THIAZOL-3-YL)ETHANESULFONIC ACID
FORMUL   3  STT    2(C6 H9 N O4 S3)
FORMUL   5  HOH   *219(H2 O)
HELIX    1   1 LEU A    7  SER A   17  1                                  11
HELIX    2   2 ASN A   41  GLN A   46  1                                   6
HELIX    3   3 ASP A   47  GLY A   55  1                                   9
HELIX    4   4 ALA A   75  LYS A   79  5                                   5
HELIX    5   5 ASN A   97  ALA A  100  5                                   4
HELIX    6   6 TYR A  101  GLN A  115  1                                  15
HELIX    7   7 SER A  129  LYS A  144  1                                  16
HELIX    8   8 ASP A  146  ARG A  158  1                                  13
HELIX    9   9 ASN A  163  GLU A  180  1                                  18
HELIX   10  10 LEU B    7  SER B   17  1                                  11
HELIX   11  11 ASN B   41  GLN B   46  1                                   6
HELIX   12  12 ASP B   47  GLY B   55  1                                   9
HELIX   13  13 ALA B   75  LYS B   79  5                                   5
HELIX   14  14 ASN B   97  ALA B  100  5                                   4
HELIX   15  15 TYR B  101  GLN B  115  1                                  15
HELIX   16  16 SER B  129  GLN B  143  1                                  15
HELIX   17  17 ASP B  146  ARG B  158  1                                  13
HELIX   18  18 ASN B  163  GLY B  181  1                                  19
SHEET    1   A 5 CYS A  30  THR A  34  0
SHEET    2   A 5 ILE A  37  GLY A  40 -1  O  VAL A  39   N  ASN A  31
SHEET    3   A 5 VAL A 120  HIS A 123  1  O  VAL A 122   N  TYR A  38
SHEET    4   A 5 HIS A  58  ASN A  61  1  N  LEU A  60   O  LEU A 121
SHEET    5   A 5 THR A  84  GLY A  87  1  O  LEU A  86   N  ASN A  61
SHEET    1   B 5 CYS B  30  THR B  34  0
SHEET    2   B 5 ILE B  37  GLY B  40 -1  O  ILE B  37   N  THR B  34
SHEET    3   B 5 VAL B 120  HIS B 123  1  O  VAL B 120   N  TYR B  38
SHEET    4   B 5 HIS B  58  ASN B  61  1  N  LEU B  60   O  LEU B 121
SHEET    5   B 5 THR B  84  GLY B  87  1  O  THR B  84   N  VAL B  59
SITE     1 AC1  9 MET A  69  ASP A  92  CYS A 124  ARG A 125
SITE     2 AC1  9 GLU A 126  TYR A 128  SER A 129  ARG A 130
SITE     3 AC1  9 GLN B 115
SITE     1 AC2 11 ASN A 117  MET B  69  ASP B  92  CYS B 124
SITE     2 AC2 11 ARG B 125  GLU B 126  TYR B 128  SER B 129
SITE     3 AC2 11 ARG B 130  HOH B 240  HOH B 307
CRYST1   50.406   59.186   60.656  90.00  98.36  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      0.019839  0.000000  0.002917        0.00000
SCALE2      0.000000  0.016896  0.000000        0.00000
SCALE3      0.000000  0.000000  0.016664        0.00000
      
PROCHECK
Go to PROCHECK summary
 References