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PDBsum entry 3m4u

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Top Page protein ligands Protein-protein interface(s) links
Hydrolase PDB id
3m4u
Jmol
Contents
Protein chains
285 a.a.
Ligands
PO4 ×2
Waters ×192
HEADER    HYDROLASE                               12-MAR-10   3M4U
TITLE     CRYSTAL STRUCTURE OF TRYPANOSOMA BRUCEI PROTEIN TYROSINE PHOSPHATASE
TITLE    2 TBPTP1
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE SPECIFIC PROTEIN PHOSPHATASE, PUTATIVE;
COMPND   3 CHAIN: A, B;
COMPND   4 EC: 3.1.3.48;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: TRYPANOSOMA BRUCEI;
SOURCE   3 ORGANISM_TAXID: 5691;
SOURCE   4 GENE: TB10.70.0070;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28B
KEYWDS    PROTEIN TYROSINE PHOSPHATASE, HYDROLASE, PROTEIN PHOSPHATASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.CHOU,T.ALBER,C.GRUNDNER
REVDAT   2   01-SEP-10 3M4U    1       JRNL
REVDAT   1   05-MAY-10 3M4U    0
JRNL        AUTH   S.CHOU,B.C.JENSEN,M.PARSONS,T.ALBER,C.GRUNDNER
JRNL        TITL   THE TRYPANOSOMA BRUCEI LIFE CYCLE SWITCH TBPTP1 IS
JRNL        TITL 2 STRUCTURALLY CONSERVED AND DEPHOSPHORYLATES THE NUCLEOLAR
JRNL        TITL 3 PROTEIN NOPP44/46.
JRNL        REF    J.BIOL.CHEM.                  V. 285 22075 2010
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   20444707
JRNL        DOI    10.1074/JBC.M110.108860
REMARK   2
REMARK   2 RESOLUTION.    2.39 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.5_2)
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK   3               : ZWART
REMARK   3
REMARK   3    REFINEMENT TARGET : ML
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.39
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.71
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.890
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5
REMARK   3   NUMBER OF REFLECTIONS             : 28040
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.201
REMARK   3   R VALUE            (WORKING SET) : 0.199
REMARK   3   FREE R VALUE                     : 0.256
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.040
REMARK   3   FREE R VALUE TEST SET COUNT      : 1412
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE
REMARK   3     1 46.7227 -  5.1514    0.99     2838   132  0.2148 0.2280
REMARK   3     2  5.1514 -  4.0896    1.00     2688   161  0.1558 0.1959
REMARK   3     3  4.0896 -  3.5728    1.00     2702   134  0.1685 0.2454
REMARK   3     4  3.5728 -  3.2463    1.00     2660   136  0.1862 0.2663
REMARK   3     5  3.2463 -  3.0136    1.00     2654   143  0.2014 0.2450
REMARK   3     6  3.0136 -  2.8360    1.00     2648   146  0.2056 0.3092
REMARK   3     7  2.8360 -  2.6940    1.00     2641   144  0.2178 0.2840
REMARK   3     8  2.6940 -  2.5767    1.00     2623   136  0.2263 0.3238
REMARK   3     9  2.5767 -  2.4775    1.00     2641   139  0.2324 0.3357
REMARK   3    10  2.4775 -  2.3920    0.97     2533   141  0.2320 0.2969
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.11
REMARK   3   SHRINKAGE RADIUS   : 0.90
REMARK   3   K_SOL              : 0.33
REMARK   3   B_SOL              : 36.59
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.300
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.940
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 43.94
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 5.52140
REMARK   3    B22 (A**2) : -3.74772
REMARK   3    B33 (A**2) : -1.77370
REMARK   3    B12 (A**2) : -0.00000
REMARK   3    B13 (A**2) : -0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  TWINNING INFORMATION.
REMARK   3   FRACTION: NULL
REMARK   3   OPERATOR: NULL
REMARK   3
REMARK   3  DEVIATIONS FROM IDEAL VALUES.
REMARK   3                 RMSD          COUNT
REMARK   3   BOND      :  0.008           4523
REMARK   3   ANGLE     :  1.065           6146
REMARK   3   CHIRALITY :  0.065            714
REMARK   3   PLANARITY :  0.004            788
REMARK   3   DIHEDRAL  : 16.159           1653
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  NCS DETAILS
REMARK   3   NUMBER OF NCS GROUPS : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 3M4U COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAR-10.
REMARK 100 THE RCSB ID CODE IS RCSB058109.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 19-JAN-09
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 9.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ALS
REMARK 200  BEAMLINE                       : 8.3.1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.158
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200  DATA SCALING SOFTWARE          : HKL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28099
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8
REMARK 200  DATA REDUNDANCY                : 5.000
REMARK 200  R MERGE                    (I) : 0.10000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 11.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.44
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.90
REMARK 200  R MERGE FOR SHELL          (I) : 0.65600
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: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 51.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 3000  0.1 M CHES PH 9.5, VAPOR
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       38.31600
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       58.59750
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.68850
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       58.59750
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       38.31600
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.68850
REMARK 290   SMTRY3   4  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 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 350
REMARK 350 BIOMOLECULE: 2
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: 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     MET A     1
REMARK 465     SER A     2
REMARK 465     THR A     3
REMARK 465     ALA A     4
REMARK 465     LYS A     5
REMARK 465     LEU A    66
REMARK 465     LYS A    67
REMARK 465     ALA A    68
REMARK 465     VAL A    69
REMARK 465     GLY A    70
REMARK 465     ALA A    71
REMARK 465     GLN A    72
REMARK 465     PRO A    73
REMARK 465     ALA A   160
REMARK 465     GLU A   161
REMARK 465     ALA A   162
REMARK 465     LEU A   302
REMARK 465     ASN A   303
REMARK 465     LEU A   304
REMARK 465     LYS A   305
REMARK 465     ALA A   306
REMARK 465     LYS B    67
REMARK 465     ALA B    68
REMARK 465     VAL B    69
REMARK 465     GLY B    70
REMARK 465     ALA B    71
REMARK 465     GLN B    72
REMARK 465     PRO B    73
REMARK 465     GLY B    74
REMARK 465     ARG B    75
REMARK 465     GLU B   140
REMARK 465     PRO B   147
REMARK 465     GLU B   148
REMARK 465     SER B   149
REMARK 465     GLY B   150
REMARK 465     HIS B   151
REMARK 465     VAL B   299
REMARK 465     SER B   300
REMARK 465     THR B   301
REMARK 465     LEU B   302
REMARK 465     ASN B   303
REMARK 465     LEU B   304
REMARK 465     LYS B   305
REMARK 465     ALA B   306
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     ARG A  35    CG   CD   NE   CZ   NH1  NH2
REMARK 470     TYR A  76    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     GLU A 138    CG   CD   OE1  OE2
REMARK 470     GLU A 139    CG   CD   OE1  OE2
REMARK 470     GLU A 140    CG   CD   OE1  OE2
REMARK 470     GLU A 148    CG   CD   OE1  OE2
REMARK 470     SER A 149    OG
REMARK 470     HIS A 151    CG   ND1  CD2  CE1  NE2
REMARK 470     ASP A 152    CG   OD1  OD2
REMARK 470     CYS A 229    SG
REMARK 470     LEU A 254    CG   CD1  CD2
REMARK 470     VAL B  26    CG2
REMARK 470     ARG B  35    CG   CD   NE   CZ   NH1  NH2
REMARK 470     TYR B  76    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     GLU B 138    CG   CD   OE1  OE2
REMARK 470     GLU B 139    CG   CD   OE1  OE2
REMARK 470     ASP B 142    CG   OD1  OD2
REMARK 470     CYS B 229    SG
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    ASP B   159     O    ALA B   162              2.17
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    GLU A 148   CB  -  CA  -  C   ANGL. DEV. = -27.0 DEGREES
REMARK 500    GLU A 148   N   -  CA  -  C   ANGL. DEV. =  18.4 DEGREES
REMARK 500    HIS A 151   CB  -  CA  -  C   ANGL. DEV. = -12.6 DEGREES
REMARK 500    HIS A 151   N   -  CA  -  C   ANGL. DEV. =  17.9 DEGREES
REMARK 500    CYS A 229   N   -  CA  -  C   ANGL. DEV. = -17.4 DEGREES
REMARK 500    ALA B 162   CB  -  CA  -  C   ANGL. DEV. =   9.6 DEGREES
REMARK 500    VAL B 274   N   -  CA  -  C   ANGL. DEV. =  19.8 DEGREES
REMARK 500    GLN B 275   N   -  CA  -  C   ANGL. DEV. =  17.0 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    ASN A  45       40.65   -108.83
REMARK 500    ILE A 233      -54.45   -142.43
REMARK 500    VAL A 274      102.55     74.77
REMARK 500    SER A 300       71.71    -65.63
REMARK 500    ARG B  46      -39.10    -39.62
REMARK 500    ALA B 162      136.65   -171.29
REMARK 500    ILE B 233      -37.94   -136.52
REMARK 500    ARG B 251        4.31    -67.72
REMARK 500    VAL B 274       63.44     64.49
REMARK 500    SER B 296      130.39    -37.52
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 A 151        24.3      L          L   OUTSIDE RANGE
REMARK 500    VAL B 274        15.5      L          L   OUTSIDE RANGE
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 PO4 A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 307
DBREF  3M4U A    1   306  UNP    Q38AT7   Q38AT7_9TRYP     1    306
DBREF  3M4U B    1   306  UNP    Q38AT7   Q38AT7_9TRYP     1    306
SEQRES   1 A  306  MET SER THR ALA LYS SER PHE PRO MET ALA GLN LEU SER
SEQRES   2 A  306  THR ARG ALA GLN TYR SER ARG MET GLN ARG GLU PHE VAL
SEQRES   3 A  306  GLN LEU GLN ARG GLN GLU ASN PRO ARG ASN ILE ASN PHE
SEQRES   4 A  306  THR THR SER LEU LYS ASN ARG HIS LYS ASN ARG TYR LEU
SEQRES   5 A  306  ASP ILE LEU ALA ASN GLU GLU THR ILE TYR PRO PRO VAL
SEQRES   6 A  306  LEU LYS ALA VAL GLY ALA GLN PRO GLY ARG TYR PRO TYR
SEQRES   7 A  306  ILE ASN GLY ASN LEU ILE ASP LEU ASP LEU PRO HIS THR
SEQRES   8 A  306  PHE VAL ALA CYS GLN ALA PRO VAL PRO GLN GLY VAL PRO
SEQRES   9 A  306  ASP PHE LEU GLU THR LEU SER GLU LYS LYS VAL ASP LEU
SEQRES  10 A  306  VAL VAL MET LEU THR LYS LEU ARG GLU GLY GLY VAL LEU
SEQRES  11 A  306  LYS ALA GLU ARG TYR TRP PRO GLU GLU GLU GLU ASP SER
SEQRES  12 A  306  LEU SER PHE PRO GLU SER GLY HIS ASP ALA ILE LYS VAL
SEQRES  13 A  306  THR ARG ASP ALA GLU ALA SER TYR GLU VAL ASP ALA GLU
SEQRES  14 A  306  LEU ASP ILE VAL ARG ARG PRO LEU VAL ILE HIS VAL PRO
SEQRES  15 A  306  GLY LYS PRO MET HIS ARG VAL LEU GLN VAL GLN TYR VAL
SEQRES  16 A  306  GLY TRP PRO ASP HIS GLY VAL PRO GLU SER ALA ALA SER
SEQRES  17 A  306  PHE ASP GLU LEU LEU SER VAL ILE LYS ASN CYS VAL THR
SEQRES  18 A  306  THR SER PRO ILE LEU VAL HIS CYS SER ALA GLY ILE GLY
SEQRES  19 A  306  ARG THR GLY THR LEU ILE GLY ALA TYR ALA ALA LEU LEU
SEQRES  20 A  306  HIS ILE GLU ARG GLY ILE LEU THR ASP SER THR VAL TYR
SEQRES  21 A  306  SER ILE VAL ALA ALA MET LYS GLN LYS ARG PHE GLY MET
SEQRES  22 A  306  VAL GLN ARG LEU GLU GLN TYR ALA VAL ILE TYR MET THR
SEQRES  23 A  306  VAL LEU GLY ARG LEU GLY VAL ASP ILE SER GLY LEU VAL
SEQRES  24 A  306  SER THR LEU ASN LEU LYS ALA
SEQRES   1 B  306  MET SER THR ALA LYS SER PHE PRO MET ALA GLN LEU SER
SEQRES   2 B  306  THR ARG ALA GLN TYR SER ARG MET GLN ARG GLU PHE VAL
SEQRES   3 B  306  GLN LEU GLN ARG GLN GLU ASN PRO ARG ASN ILE ASN PHE
SEQRES   4 B  306  THR THR SER LEU LYS ASN ARG HIS LYS ASN ARG TYR LEU
SEQRES   5 B  306  ASP ILE LEU ALA ASN GLU GLU THR ILE TYR PRO PRO VAL
SEQRES   6 B  306  LEU LYS ALA VAL GLY ALA GLN PRO GLY ARG TYR PRO TYR
SEQRES   7 B  306  ILE ASN GLY ASN LEU ILE ASP LEU ASP LEU PRO HIS THR
SEQRES   8 B  306  PHE VAL ALA CYS GLN ALA PRO VAL PRO GLN GLY VAL PRO
SEQRES   9 B  306  ASP PHE LEU GLU THR LEU SER GLU LYS LYS VAL ASP LEU
SEQRES  10 B  306  VAL VAL MET LEU THR LYS LEU ARG GLU GLY GLY VAL LEU
SEQRES  11 B  306  LYS ALA GLU ARG TYR TRP PRO GLU GLU GLU GLU ASP SER
SEQRES  12 B  306  LEU SER PHE PRO GLU SER GLY HIS ASP ALA ILE LYS VAL
SEQRES  13 B  306  THR ARG ASP ALA GLU ALA SER TYR GLU VAL ASP ALA GLU
SEQRES  14 B  306  LEU ASP ILE VAL ARG ARG PRO LEU VAL ILE HIS VAL PRO
SEQRES  15 B  306  GLY LYS PRO MET HIS ARG VAL LEU GLN VAL GLN TYR VAL
SEQRES  16 B  306  GLY TRP PRO ASP HIS GLY VAL PRO GLU SER ALA ALA SER
SEQRES  17 B  306  PHE ASP GLU LEU LEU SER VAL ILE LYS ASN CYS VAL THR
SEQRES  18 B  306  THR SER PRO ILE LEU VAL HIS CYS SER ALA GLY ILE GLY
SEQRES  19 B  306  ARG THR GLY THR LEU ILE GLY ALA TYR ALA ALA LEU LEU
SEQRES  20 B  306  HIS ILE GLU ARG GLY ILE LEU THR ASP SER THR VAL TYR
SEQRES  21 B  306  SER ILE VAL ALA ALA MET LYS GLN LYS ARG PHE GLY MET
SEQRES  22 B  306  VAL GLN ARG LEU GLU GLN TYR ALA VAL ILE TYR MET THR
SEQRES  23 B  306  VAL LEU GLY ARG LEU GLY VAL ASP ILE SER GLY LEU VAL
SEQRES  24 B  306  SER THR LEU ASN LEU LYS ALA
HET    PO4  A 307       5
HET    PO4  B 307       5
HETNAM     PO4 PHOSPHATE ION
FORMUL   3  PO4    2(O4 P 3-)
FORMUL   5  HOH   *192(H2 O)
HELIX    1   1 PHE A    7  GLN A   11  5                                   5
HELIX    2   2 SER A   13  GLU A   32  1                                  20
HELIX    3   3 ASN A   33  ILE A   37  5                                   5
HELIX    4   4 PHE A   39  ASN A   45  1                                   7
HELIX    5   5 ARG A   46  ASN A   49  5                                   4
HELIX    6   6 VAL A   99  GLN A  101  5                                   3
HELIX    7   7 GLY A  102  LYS A  113  1                                  12
HELIX    8   8 SER A  205  ASN A  218  1                                  14
HELIX    9   9 ILE A  233  ARG A  251  1                                  19
HELIX   10  10 SER A  257  ARG A  270  1                                  14
HELIX   11  11 ARG A  276  LEU A  291  1                                  16
HELIX   12  12 ILE A  295  SER A  300  1                                   6
HELIX   13  13 THR B    3  LEU B   12  5                                  10
HELIX   14  14 SER B   13  ARG B   30  1                                  18
HELIX   15  15 ASN B   33  ILE B   37  5                                   5
HELIX   16  16 PHE B   39  ASN B   45  1                                   7
HELIX   17  17 ARG B   46  ASN B   49  5                                   4
HELIX   18  18 VAL B   99  GLN B  101  5                                   3
HELIX   19  19 GLY B  102  LYS B  113  1                                  12
HELIX   20  20 SER B  205  ASN B  218  1                                  14
HELIX   21  21 ILE B  233  ARG B  251  1                                  19
HELIX   22  22 SER B  257  ARG B  270  1                                  14
HELIX   23  23 ARG B  276  LEU B  291  1                                  16
SHEET    1   A 9 ILE A  61  TYR A  62  0
SHEET    2   A 9 GLY A  81  ILE A  84 -1  O  GLY A  81   N  TYR A  62
SHEET    3   A 9 PHE A  92  CYS A  95 -1  O  PHE A  92   N  ILE A  84
SHEET    4   A 9 ILE A 225  HIS A 228  1  O  VAL A 227   N  VAL A  93
SHEET    5   A 9 LEU A 117  MET A 120  1  N  VAL A 119   O  LEU A 226
SHEET    6   A 9 HIS A 187  TYR A 194  1  O  VAL A 192   N  MET A 120
SHEET    7   A 9 ILE A 172  HIS A 180 -1  N  ARG A 175   O  GLN A 191
SHEET    8   A 9 ILE A 154  ARG A 158 -1  N  LYS A 155   O  HIS A 180
SHEET    9   A 9 SER A 143  PHE A 146 -1  N  LEU A 144   O  VAL A 156
SHEET    1   B 8 ILE A  61  TYR A  62  0
SHEET    2   B 8 GLY A  81  ILE A  84 -1  O  GLY A  81   N  TYR A  62
SHEET    3   B 8 PHE A  92  CYS A  95 -1  O  PHE A  92   N  ILE A  84
SHEET    4   B 8 ILE A 225  HIS A 228  1  O  VAL A 227   N  VAL A  93
SHEET    5   B 8 LEU A 117  MET A 120  1  N  VAL A 119   O  LEU A 226
SHEET    6   B 8 HIS A 187  TYR A 194  1  O  VAL A 192   N  MET A 120
SHEET    7   B 8 ILE A 172  HIS A 180 -1  N  ARG A 175   O  GLN A 191
SHEET    8   B 8 GLU A 165  ASP A 167 -1  N  ASP A 167   O  ILE A 172
SHEET    1   C 2 ARG A 125  GLU A 126  0
SHEET    2   C 2 VAL A 129  LEU A 130 -1  O  VAL A 129   N  GLU A 126
SHEET    1   D 9 ILE B  61  TYR B  62  0
SHEET    2   D 9 GLY B  81  ILE B  84 -1  O  GLY B  81   N  TYR B  62
SHEET    3   D 9 PHE B  92  CYS B  95 -1  O  PHE B  92   N  ILE B  84
SHEET    4   D 9 ILE B 225  HIS B 228  1  O  VAL B 227   N  VAL B  93
SHEET    5   D 9 LEU B 117  MET B 120  1  N  VAL B 119   O  LEU B 226
SHEET    6   D 9 HIS B 187  TYR B 194  1  O  VAL B 192   N  MET B 120
SHEET    7   D 9 ILE B 172  HIS B 180 -1  N  ARG B 175   O  GLN B 191
SHEET    8   D 9 LYS B 155  ARG B 158 -1  N  LYS B 155   O  HIS B 180
SHEET    9   D 9 SER B 143  SER B 145 -1  N  LEU B 144   O  VAL B 156
SHEET    1   E 8 ILE B  61  TYR B  62  0
SHEET    2   E 8 GLY B  81  ILE B  84 -1  O  GLY B  81   N  TYR B  62
SHEET    3   E 8 PHE B  92  CYS B  95 -1  O  PHE B  92   N  ILE B  84
SHEET    4   E 8 ILE B 225  HIS B 228  1  O  VAL B 227   N  VAL B  93
SHEET    5   E 8 LEU B 117  MET B 120  1  N  VAL B 119   O  LEU B 226
SHEET    6   E 8 HIS B 187  TYR B 194  1  O  VAL B 192   N  MET B 120
SHEET    7   E 8 ILE B 172  HIS B 180 -1  N  ARG B 175   O  GLN B 191
SHEET    8   E 8 GLU B 165  ASP B 167 -1  N  ASP B 167   O  ILE B 172
SHEET    1   F 2 ARG B 125  GLU B 126  0
SHEET    2   F 2 VAL B 129  LEU B 130 -1  O  VAL B 129   N  GLU B 126
CISPEP   1 TYR A   62    PRO A   63          0        -7.35
CISPEP   2 GLU A  139    GLU A  140          0        -0.34
CISPEP   3 PHE A  146    PRO A  147          0         6.25
CISPEP   4 TYR B   62    PRO B   63          0        -3.12
SITE     1 AC1 10 ASP A 199  CYS A 229  SER A 230  ALA A 231
SITE     2 AC1 10 GLY A 232  ILE A 233  GLY A 234  ARG A 235
SITE     3 AC1 10 THR A 236  HOH A 319
SITE     1 AC2 10 CYS B 229  SER B 230  ALA B 231  GLY B 232
SITE     2 AC2 10 ILE B 233  GLY B 234  ARG B 235  THR B 236
SITE     3 AC2 10 HOH B 308  HOH B 385
CRYST1   76.632   77.377  117.195  90.00  90.00  90.00 P 21 21 21    8
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      0.013049  0.000000  0.000000        0.00000
SCALE2      0.000000  0.012924  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008533        0.00000
      
PROCHECK
Go to PROCHECK summary
 References