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PDBsum entry 1zcl

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Hydrolase PDB id
1zcl
Jmol
Contents
Protein chains
152 a.a.
Ligands
SO4 ×2
HEADER    HYDROLASE                               12-APR-05   1ZCL
TITLE     PRL-1 C104S MUTANT IN COMPLEX WITH SULFATE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROTEIN TYROSINE PHOSPHATASE 4A1;
COMPND   3 CHAIN: A, B;
COMPND   4 EC: 3.1.3.48;
COMPND   5 ENGINEERED: YES;
COMPND   6 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE   3 ORGANISM_COMMON: NORWAY RAT;
SOURCE   4 ORGANISM_TAXID: 10116;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PET15B
KEYWDS    PRL-1 PTP4A DUAL SPECIFIC PHOSPHATASE, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.P.SUN,W.Q.WANG,H.YANG,S.LIU,F.LIANG,A.A.FEDOROV,S.C.ALMO,
AUTHOR   2 Z.Y.ZHANG
REVDAT   2   24-FEB-09 1ZCL    1       VERSN
REVDAT   1   20-SEP-05 1ZCL    0
JRNL        AUTH   J.P.SUN,W.Q.WANG,H.YANG,S.LIU,F.LIANG,A.A.FEDOROV,
JRNL        AUTH 2 S.C.ALMO,Z.Y.ZHANG
JRNL        TITL   STRUCTURE AND BIOCHEMICAL PROPERTIES OF PRL-1, A
JRNL        TITL 2 PHOSPHATASE IMPLICATED IN CELL GROWTH,
JRNL        TITL 3 DIFFERENTIATION, AND TUMOR INVASION.
JRNL        REF    BIOCHEMISTRY                  V.  44 12009 2005
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   16142898
JRNL        DOI    10.1021/BI0509191
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.0
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
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             : 9778
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.261
REMARK   3   FREE R VALUE                     : 0.296
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 476
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 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            : 2451
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 10
REMARK   3   SOLVENT ATOMS            : 0
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) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
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) : NULL
REMARK   3   BOND ANGLES            (DEGREES) : NULL
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        : NULL
REMARK   3   BSOL        : NULL
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 1ZCL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-APR-05.
REMARK 100 THE RCSB ID CODE IS RCSB032570.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 20-NOV-04
REMARK 200  TEMPERATURE           (KELVIN) : 200
REMARK 200  PH                             : 4.8
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : CHESS
REMARK 200  BEAMLINE                       : F2
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU AFC-5
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10372
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900
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     (%) : 88.1
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4
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: CNS
REMARK 200 STARTING MODEL: 1RXD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 58.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, SODIUM ACETATE,
REMARK 280  PH 4.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 21 3
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       5555   Z,X,Y
REMARK 290       6555   Z+1/2,-X+1/2,-Y
REMARK 290       7555   -Z+1/2,-X,Y+1/2
REMARK 290       8555   -Z,X+1/2,-Y+1/2
REMARK 290       9555   Y,Z,X
REMARK 290      10555   -Y,Z+1/2,-X+1/2
REMARK 290      11555   Y+1/2,-Z+1/2,-X
REMARK 290      12555   -Y+1/2,-Z,X+1/2
REMARK 290      13555   X+1/2,Y+1/2,Z+1/2
REMARK 290      14555   -X,-Y+1/2,Z
REMARK 290      15555   -X+1/2,Y,-Z
REMARK 290      16555   X,-Y,-Z+1/2
REMARK 290      17555   Z+1/2,X+1/2,Y+1/2
REMARK 290      18555   Z,-X,-Y+1/2
REMARK 290      19555   -Z,-X+1/2,Y
REMARK 290      20555   -Z+1/2,X,-Y
REMARK 290      21555   Y+1/2,Z+1/2,X+1/2
REMARK 290      22555   -Y+1/2,Z,-X
REMARK 290      23555   Y,-Z,-X+1/2
REMARK 290      24555   -Y,-Z+1/2,X
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       73.34050
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       73.34050
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       73.34050
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       73.34050
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       73.34050
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       73.34050
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000       73.34050
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000       73.34050
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000       73.34050
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000       73.34050
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000       73.34050
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000       73.34050
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000       73.34050
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000       73.34050
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000       73.34050
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000       73.34050
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000       73.34050
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000       73.34050
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000       73.34050
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       73.34050
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000       73.34050
REMARK 290   SMTRY1  14 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       73.34050
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1  15 -1.000000  0.000000  0.000000       73.34050
REMARK 290   SMTRY2  15  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1  16  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  16  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       73.34050
REMARK 290   SMTRY1  17  0.000000  0.000000  1.000000       73.34050
REMARK 290   SMTRY2  17  1.000000  0.000000  0.000000       73.34050
REMARK 290   SMTRY3  17  0.000000  1.000000  0.000000       73.34050
REMARK 290   SMTRY1  18  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY2  18 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3  18  0.000000 -1.000000  0.000000       73.34050
REMARK 290   SMTRY1  19  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY2  19 -1.000000  0.000000  0.000000       73.34050
REMARK 290   SMTRY3  19  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY1  20  0.000000  0.000000 -1.000000       73.34050
REMARK 290   SMTRY2  20  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3  20  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY1  21  0.000000  1.000000  0.000000       73.34050
REMARK 290   SMTRY2  21  0.000000  0.000000  1.000000       73.34050
REMARK 290   SMTRY3  21  1.000000  0.000000  0.000000       73.34050
REMARK 290   SMTRY1  22  0.000000 -1.000000  0.000000       73.34050
REMARK 290   SMTRY2  22  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY3  22 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  23  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2  23  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY3  23 -1.000000  0.000000  0.000000       73.34050
REMARK 290   SMTRY1  24  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2  24  0.000000  0.000000 -1.000000       73.34050
REMARK 290   SMTRY3  24  1.000000  0.000000  0.000000        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: TRIMERIC
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  0.000000  0.000000  1.000000      -73.34050
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000      -73.34050
REMARK 350   BIOMT3   2  0.000000 -1.000000  0.000000        0.00000
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000      -73.34050
REMARK 350   BIOMT2   3  0.000000  0.000000 -1.000000        0.00000
REMARK 350   BIOMT3   3  1.000000  0.000000  0.000000       73.34050
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
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  0.000000  0.000000  1.000000      -73.34050
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000      -73.34050
REMARK 350   BIOMT3   2  0.000000 -1.000000  0.000000        0.00000
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000      -73.34050
REMARK 350   BIOMT2   3  0.000000  0.000000 -1.000000        0.00000
REMARK 350   BIOMT3   3  1.000000  0.000000  0.000000       73.34050
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   -19
REMARK 465     GLY A   -18
REMARK 465     SER A   -17
REMARK 465     SER A   -16
REMARK 465     HIS A   -15
REMARK 465     HIS A   -14
REMARK 465     HIS A   -13
REMARK 465     HIS A   -12
REMARK 465     HIS A   -11
REMARK 465     HIS A   -10
REMARK 465     SER A    -9
REMARK 465     SER A    -8
REMARK 465     GLY A    -7
REMARK 465     LEU A    -6
REMARK 465     VAL A    -5
REMARK 465     PRO A    -4
REMARK 465     ARG A    -3
REMARK 465     GLY A    -2
REMARK 465     SER A    -1
REMARK 465     HIS A     0
REMARK 465     MET A     1
REMARK 465     ALA A     2
REMARK 465     ARG A     3
REMARK 465     MET A     4
REMARK 465     ASN A     5
REMARK 465     ARG A     6
REMARK 465     PRO A     7
REMARK 465     ALA A     8
REMARK 465     MET B   -19
REMARK 465     GLY B   -18
REMARK 465     SER B   -17
REMARK 465     SER B   -16
REMARK 465     HIS B   -15
REMARK 465     HIS B   -14
REMARK 465     HIS B   -13
REMARK 465     HIS B   -12
REMARK 465     HIS B   -11
REMARK 465     HIS B   -10
REMARK 465     SER B    -9
REMARK 465     SER B    -8
REMARK 465     GLY B    -7
REMARK 465     LEU B    -6
REMARK 465     VAL B    -5
REMARK 465     PRO B    -4
REMARK 465     ARG B    -3
REMARK 465     GLY B    -2
REMARK 465     SER B    -1
REMARK 465     HIS B     0
REMARK 465     MET B     1
REMARK 465     ALA B     2
REMARK 465     ARG B     3
REMARK 465     MET B     4
REMARK 465     ASN B     5
REMARK 465     ARG B     6
REMARK 465     PRO B     7
REMARK 465     ALA B     8
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    LEU A   119     O    GLY A   123              2.17
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    LYS A  15     -114.95     59.73
REMARK 500    THR A  26     -113.43    -83.27
REMARK 500    ASN A  27       -2.45   -155.58
REMARK 500    LEU A  30      -89.03     -8.29
REMARK 500    ASN A  31      -34.53    -32.72
REMARK 500    LYS A  38      -32.60    -34.72
REMARK 500    LYS A  39       44.58   -103.82
REMARK 500    LYS A  60       10.20    -63.69
REMARK 500    PRO A  69      152.03    -39.73
REMARK 500    ASP A  71      109.73    -41.01
REMARK 500    ASP A  72       97.82    -62.55
REMARK 500    PRO A  76       86.52    -49.13
REMARK 500    SER A  77     -163.44     37.52
REMARK 500    ASN A  78      -37.27   -135.66
REMARK 500    ILE A  90      -92.26    -68.16
REMARK 500    LYS A  91      -62.01    -11.87
REMARK 500    CYS A  98     -138.39    -96.70
REMARK 500    CYS A  99      147.52    179.58
REMARK 500    MET A 124      122.62     77.28
REMARK 500    ARG A 137       46.77   -159.41
REMARK 500    ARG A 138      129.61    -28.52
REMARK 500    PHE A 141      138.42     85.75
REMARK 500    LYS B  15     -118.36     48.77
REMARK 500    ASN B  24       98.77    -25.94
REMARK 500    LEU B  30       -4.78    -53.99
REMARK 500    CYS B  49     -143.53    -98.77
REMARK 500    THR B  52       31.96   -146.76
REMARK 500    VAL B  58      -74.43    -80.83
REMARK 500    GLU B  59      -36.77    -31.12
REMARK 500    PRO B  69     -176.56    -68.76
REMARK 500    PHE B  70      136.68    159.83
REMARK 500    PRO B  76       27.22    -79.72
REMARK 500    SER B  77      152.65     53.46
REMARK 500    ILE B  90      -88.19    -71.90
REMARK 500    LYS B  91      -67.53    -22.14
REMARK 500    SER B 104     -154.86   -106.99
REMARK 500    ARG B 138      -67.34    -27.76
REMARK 500    ALA B 140      152.94    170.02
REMARK 500    PHE B 141      107.99     67.28
REMARK 500    SER B 143      -43.46    -23.77
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 4397
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 4398
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ZCK   RELATED DB: PDB
DBREF  1ZCL A    7   160  UNP    Q78EG7   TP4A1_RAT        7    160
DBREF  1ZCL B    7   160  UNP    Q78EG7   TP4A1_RAT        7    160
SEQADV 1ZCL MET A  -19  UNP  Q78EG7              CLONING ARTIFACT
SEQADV 1ZCL GLY A  -18  UNP  Q78EG7              CLONING ARTIFACT
SEQADV 1ZCL SER A  -17  UNP  Q78EG7              CLONING ARTIFACT
SEQADV 1ZCL SER A  -16  UNP  Q78EG7              CLONING ARTIFACT
SEQADV 1ZCL HIS A  -15  UNP  Q78EG7              CLONING ARTIFACT
SEQADV 1ZCL HIS A  -14  UNP  Q78EG7              CLONING ARTIFACT
SEQADV 1ZCL HIS A  -13  UNP  Q78EG7              CLONING ARTIFACT
SEQADV 1ZCL HIS A  -12  UNP  Q78EG7              CLONING ARTIFACT
SEQADV 1ZCL HIS A  -11  UNP  Q78EG7              CLONING ARTIFACT
SEQADV 1ZCL HIS A  -10  UNP  Q78EG7              CLONING ARTIFACT
SEQADV 1ZCL SER A   -9  UNP  Q78EG7              CLONING ARTIFACT
SEQADV 1ZCL SER A   -8  UNP  Q78EG7              CLONING ARTIFACT
SEQADV 1ZCL GLY A   -7  UNP  Q78EG7              CLONING ARTIFACT
SEQADV 1ZCL LEU A   -6  UNP  Q78EG7              CLONING ARTIFACT
SEQADV 1ZCL VAL A   -5  UNP  Q78EG7              CLONING ARTIFACT
SEQADV 1ZCL PRO A   -4  UNP  Q78EG7              CLONING ARTIFACT
SEQADV 1ZCL ARG A   -3  UNP  Q78EG7              CLONING ARTIFACT
SEQADV 1ZCL GLY A   -2  UNP  Q78EG7              CLONING ARTIFACT
SEQADV 1ZCL SER A   -1  UNP  Q78EG7              CLONING ARTIFACT
SEQADV 1ZCL HIS A    0  UNP  Q78EG7              CLONING ARTIFACT
SEQADV 1ZCL SER A  104  UNP  Q78EG7    CYS   104 ENGINEERED
SEQADV 1ZCL MET B  -19  UNP  Q78EG7              CLONING ARTIFACT
SEQADV 1ZCL GLY B  -18  UNP  Q78EG7              CLONING ARTIFACT
SEQADV 1ZCL SER B  -17  UNP  Q78EG7              CLONING ARTIFACT
SEQADV 1ZCL SER B  -16  UNP  Q78EG7              CLONING ARTIFACT
SEQADV 1ZCL HIS B  -15  UNP  Q78EG7              CLONING ARTIFACT
SEQADV 1ZCL HIS B  -14  UNP  Q78EG7              CLONING ARTIFACT
SEQADV 1ZCL HIS B  -13  UNP  Q78EG7              CLONING ARTIFACT
SEQADV 1ZCL HIS B  -12  UNP  Q78EG7              CLONING ARTIFACT
SEQADV 1ZCL HIS B  -11  UNP  Q78EG7              CLONING ARTIFACT
SEQADV 1ZCL HIS B  -10  UNP  Q78EG7              CLONING ARTIFACT
SEQADV 1ZCL SER B   -9  UNP  Q78EG7              CLONING ARTIFACT
SEQADV 1ZCL SER B   -8  UNP  Q78EG7              CLONING ARTIFACT
SEQADV 1ZCL GLY B   -7  UNP  Q78EG7              CLONING ARTIFACT
SEQADV 1ZCL LEU B   -6  UNP  Q78EG7              CLONING ARTIFACT
SEQADV 1ZCL VAL B   -5  UNP  Q78EG7              CLONING ARTIFACT
SEQADV 1ZCL PRO B   -4  UNP  Q78EG7              CLONING ARTIFACT
SEQADV 1ZCL ARG B   -3  UNP  Q78EG7              CLONING ARTIFACT
SEQADV 1ZCL GLY B   -2  UNP  Q78EG7              CLONING ARTIFACT
SEQADV 1ZCL SER B   -1  UNP  Q78EG7              CLONING ARTIFACT
SEQADV 1ZCL HIS B    0  UNP  Q78EG7              CLONING ARTIFACT
SEQADV 1ZCL SER B  104  UNP  Q78EG7    CYS   104 ENGINEERED
SEQRES   1 A  180  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES   2 A  180  LEU VAL PRO ARG GLY SER HIS MET ALA ARG MET ASN ARG
SEQRES   3 A  180  PRO ALA PRO VAL GLU VAL THR TYR LYS ASN MET ARG PHE
SEQRES   4 A  180  LEU ILE THR HIS ASN PRO THR ASN ALA THR LEU ASN LYS
SEQRES   5 A  180  PHE ILE GLU GLU LEU LYS LYS TYR GLY VAL THR THR ILE
SEQRES   6 A  180  VAL ARG VAL CYS GLU ALA THR TYR ASP THR THR LEU VAL
SEQRES   7 A  180  GLU LYS GLU GLY ILE HIS VAL LEU ASP TRP PRO PHE ASP
SEQRES   8 A  180  ASP GLY ALA PRO PRO SER ASN GLN ILE VAL ASP ASP TRP
SEQRES   9 A  180  LEU SER LEU VAL LYS ILE LYS PHE ARG GLU GLU PRO GLY
SEQRES  10 A  180  CYS CYS ILE ALA VAL HIS SER VAL ALA GLY LEU GLY ARG
SEQRES  11 A  180  ALA PRO VAL LEU VAL ALA LEU ALA LEU ILE GLU GLY GLY
SEQRES  12 A  180  MET LYS TYR GLU ASP ALA VAL GLN PHE ILE ARG GLN LYS
SEQRES  13 A  180  ARG ARG GLY ALA PHE ASN SER LYS GLN LEU LEU TYR LEU
SEQRES  14 A  180  GLU LYS TYR ARG PRO LYS MET ARG LEU ARG PHE
SEQRES   1 B  180  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES   2 B  180  LEU VAL PRO ARG GLY SER HIS MET ALA ARG MET ASN ARG
SEQRES   3 B  180  PRO ALA PRO VAL GLU VAL THR TYR LYS ASN MET ARG PHE
SEQRES   4 B  180  LEU ILE THR HIS ASN PRO THR ASN ALA THR LEU ASN LYS
SEQRES   5 B  180  PHE ILE GLU GLU LEU LYS LYS TYR GLY VAL THR THR ILE
SEQRES   6 B  180  VAL ARG VAL CYS GLU ALA THR TYR ASP THR THR LEU VAL
SEQRES   7 B  180  GLU LYS GLU GLY ILE HIS VAL LEU ASP TRP PRO PHE ASP
SEQRES   8 B  180  ASP GLY ALA PRO PRO SER ASN GLN ILE VAL ASP ASP TRP
SEQRES   9 B  180  LEU SER LEU VAL LYS ILE LYS PHE ARG GLU GLU PRO GLY
SEQRES  10 B  180  CYS CYS ILE ALA VAL HIS SER VAL ALA GLY LEU GLY ARG
SEQRES  11 B  180  ALA PRO VAL LEU VAL ALA LEU ALA LEU ILE GLU GLY GLY
SEQRES  12 B  180  MET LYS TYR GLU ASP ALA VAL GLN PHE ILE ARG GLN LYS
SEQRES  13 B  180  ARG ARG GLY ALA PHE ASN SER LYS GLN LEU LEU TYR LEU
SEQRES  14 B  180  GLU LYS TYR ARG PRO LYS MET ARG LEU ARG PHE
HET    SO4  B4397       5
HET    SO4  A4398       5
HETNAM     SO4 SULFATE ION
FORMUL   3  SO4    2(O4 S 2-)
HELIX    1   1 THR A   29  LYS A   39  1                                  11
HELIX    2   2 THR A   55  LYS A   60  1                                   6
HELIX    3   3 ASN A   78  GLU A   95  1                                  18
HELIX    4   4 GLY A  109  GLY A  122  1                                  14
HELIX    5   5 LYS A  125  LYS A  136  1                                  12
HELIX    6   6 ASN A  142  TYR A  152  1                                  11
HELIX    7   7 THR B   29  GLY B   41  1                                  13
HELIX    8   8 THR B   55  LYS B   60  1                                   6
HELIX    9   9 SER B   77  GLU B   95  1                                  19
HELIX   10  10 GLY B  109  GLU B  121  1                                  13
HELIX   11  11 LYS B  125  ARG B  137  1                                  13
HELIX   12  12 ASN B  142  TYR B  152  1                                  11
SHEET    1   A 4 PHE A  19  HIS A  23  0
SHEET    2   A 4 CYS A  99  SER A 104  1  O  ILE A 100   N  LEU A  20
SHEET    3   A 4 VAL A  42  ARG A  47  1  N  THR A  44   O  ALA A 101
SHEET    4   A 4 HIS A  64  ASP A  67  1  O  HIS A  64   N  ILE A  45
SHEET    1   B 5 VAL B  10  TYR B  14  0
SHEET    2   B 5 MET B  17  HIS B  23 -1  O  MET B  17   N  TYR B  14
SHEET    3   B 5 CYS B  99  SER B 104  1  O  ILE B 100   N  LEU B  20
SHEET    4   B 5 VAL B  42  ARG B  47  1  N  VAL B  46   O  ALA B 101
SHEET    5   B 5 HIS B  64  ASP B  67  1  O  HIS B  64   N  ILE B  45
SITE     1 AC1  7 ASP B  72  SER B 104  VAL B 105  ALA B 106
SITE     2 AC1  7 GLY B 107  GLY B 109  ARG B 110
SITE     1 AC2  8 ASP A  72  SER A 104  VAL A 105  ALA A 106
SITE     2 AC2  8 GLY A 107  LEU A 108  GLY A 109  ARG A 110
CRYST1  146.681  146.681  146.681  90.00  90.00  90.00 I 21 3       48
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      0.006818  0.000000  0.000000        0.00000
SCALE2      0.000000  0.006818  0.000000        0.00000
SCALE3      0.000000  0.000000  0.006818        0.00000
      
PROCHECK
Go to PROCHECK summary
 References