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PDBsum entry 2z72

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Hydrolase PDB id
2z72
Jmol
Contents
Protein chain
338 a.a.
Metals
_ZN ×2
Waters ×772
HEADER    HYDROLASE                               10-AUG-07   2Z72
TITLE     NEW STRUCTURE OF COLD-ACTIVE PROTEIN TYROSINE PHOSPHATASE
TITLE    2 AT 1.1 ANGSTROM
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROTEIN-TYROSINE-PHOSPHATASE;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: UNP RESIDUES 22-361;
COMPND   5 SYNONYM: COLD-ACTIVE PROTEIN TYROSINE PHOSPHTASE;
COMPND   6 EC: 3.1.3.48;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: SHEWANELLA SP.;
SOURCE   3 ORGANISM_TAXID: 50422;
SOURCE   4 GENE: PPI;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS    COLD-ACTIVE ENZYME, PSYCHROPHILE, PROTEIN TYROSINE
KEYWDS   2 PHOSPHATASE, SHEWANELLA SP., HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    H.TSURUTA,B.MIKAMI,C.YAMAMOTO,H.YAMAGATA
REVDAT   3   24-FEB-09 2Z72    1       VERSN
REVDAT   2   26-AUG-08 2Z72    1       JRNL
REVDAT   1   29-JUL-08 2Z72    0
JRNL        AUTH   H.TSURUTA,B.MIKAMI,C.YAMAMOTO,H.YAMAGATA
JRNL        TITL   THE ROLE OF GROUP BULKINESS IN THE CATALYTIC
JRNL        TITL 2 ACTIVITY OF PSYCHROPHILE COLD-ACTIVE PROTEIN
JRNL        TITL 3 TYROSINE PHOSPHATASE
JRNL        REF    FEBS J.                       V. 275  4317 2008
JRNL        REFN                   ISSN 1742-464X
JRNL        PMID   18647345
JRNL        DOI    10.1111/J.1742-4658.2008.06575.X
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    1.10 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : SHELXL-97
REMARK   3   AUTHORS     : G.M.SHELDRICK
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.10
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 84.7
REMARK   3   CROSS-VALIDATION METHOD           : FREE R
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.110
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.110
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.161
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.200
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 6225
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL
REMARK   3
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : NULL
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.097
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.142
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.200
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 4557
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 88224
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS      : 2883
REMARK   3   NUCLEIC ACID ATOMS : 0
REMARK   3   HETEROGEN ATOMS    : 2
REMARK   3   SOLVENT ATOMS      : 772
REMARK   3
REMARK   3  MODEL REFINEMENT.
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 3479.15
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 2670.00
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 39
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 32955
REMARK   3   NUMBER OF RESTRAINTS                     : 39804
REMARK   3
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK   3   BOND LENGTHS                         (A) : 0.017
REMARK   3   ANGLE DISTANCES                      (A) : 0.033
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.031
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.085
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.097
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.050
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.005
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.053
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.115
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED: NULL
REMARK   3
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER
REMARK   3   SPECIAL CASE: NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: ANISOTROPIC REFINEMENT REDUCED FREE
REMARK   3  R (NO CUTOFF) BY ?
REMARK   4
REMARK   4 2Z72 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-AUG-07.
REMARK 100 THE RCSB ID CODE IS RCSB027602.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 11-NOV-05
REMARK 200  TEMPERATURE           (KELVIN) : 103.0
REMARK 200  PH                             : 8.50
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SPRING-8
REMARK 200  BEAMLINE                       : BL38B1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.7
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU JUPITER 210
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 141407
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.100
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     (%) : 89.2
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) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
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: AB INITIO
REMARK 200 SOFTWARE USED: SHELX
REMARK 200 STARTING MODEL: PDB ENTRY 1V73
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 45.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% POLYETHYLENEGLYCOL, 0.1M
REMARK 280  AMMONIUM ACETATE, 50MM P-NITROPHENYLSULPHATE, 0.05M TRIS-HCL
REMARK 280  (PH8.5), PH8.50, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280  277.0K
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       27.78250
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       40.51450
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.65300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       40.51450
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       27.78250
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.65300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
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     MET A     1
REMARK 465     GLY A     2
REMARK 465     ASN A     3
REMARK 465     THR A     4
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    HIS A 163   ND1   HIS A 163   CE1    -0.106
REMARK 500    ARG A 332   CD    ARG A 332   NE      0.205
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    ASP A  28   CB  -  CG  -  OD2 ANGL. DEV. =  -6.4 DEGREES
REMARK 500    ARG A  30   CD  -  NE  -  CZ  ANGL. DEV. =   9.8 DEGREES
REMARK 500    ARG A  30   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES
REMARK 500    ARG A  43   CD  -  NE  -  CZ  ANGL. DEV. =  18.3 DEGREES
REMARK 500    ARG A  43   NE  -  CZ  -  NH1 ANGL. DEV. =   5.2 DEGREES
REMARK 500    HIS A  46   CA  -  CB  -  CG  ANGL. DEV. =  10.5 DEGREES
REMARK 500    CYS A  47   CA  -  CB  -  SG  ANGL. DEV. = -13.7 DEGREES
REMARK 500    GLU A  58   OE1 -  CD  -  OE2 ANGL. DEV. =  -9.7 DEGREES
REMARK 500    ASP A 138   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES
REMARK 500    HIS A 163   CG  -  ND1 -  CE1 ANGL. DEV. =   8.3 DEGREES
REMARK 500    GLN A 164   O   -  C   -  N   ANGL. DEV. = -11.8 DEGREES
REMARK 500    ARG A 258   CD  -  NE  -  CZ  ANGL. DEV. =  13.4 DEGREES
REMARK 500    ARG A 258   NH1 -  CZ  -  NH2 ANGL. DEV. =  -7.3 DEGREES
REMARK 500    ARG A 258   NE  -  CZ  -  NH1 ANGL. DEV. =  12.1 DEGREES
REMARK 500    ARG A 258   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.9 DEGREES
REMARK 500    GLU A 269   CB  -  CG  -  CD  ANGL. DEV. =  23.6 DEGREES
REMARK 500    ARG A 291   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES
REMARK 500    ARG A 325   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES
REMARK 500    ARG A 332   CG  -  CD  -  NE  ANGL. DEV. = -21.4 DEGREES
REMARK 500    ARG A 332   CD  -  NE  -  CZ  ANGL. DEV. =  -9.0 DEGREES
REMARK 500    ARG A 332   NE  -  CZ  -  NH2 ANGL. DEV. =   5.3 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    GLN A  82       77.43   -101.81
REMARK 500    THR A 112       47.25    -83.70
REMARK 500    ASP A 117      159.29     81.07
REMARK 500    ARG A 118      -54.38     72.19
REMARK 500    ASN A 201     -129.74     58.05
REMARK 500    ASP A 202       31.04    -99.59
REMARK 500    PHE A 250     -155.84   -119.89
REMARK 500    HIS A 286      -46.31     71.59
REMARK 500    ASN A 338      -91.61     45.64
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 A1378        DISTANCE =  6.76 ANGSTROMS
REMARK 525    HOH A1559        DISTANCE =  5.55 ANGSTROMS
REMARK 525    HOH A1654        DISTANCE =  6.92 ANGSTROMS
REMARK 525    HOH A1655        DISTANCE =  5.10 ANGSTROMS
REMARK 525    HOH A1663        DISTANCE =  8.47 ANGSTROMS
REMARK 525    HOH A1701        DISTANCE =  6.44 ANGSTROMS
REMARK 525    HOH A1753        DISTANCE =  6.55 ANGSTROMS
REMARK 525    HOH A1758        DISTANCE =  8.47 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                              ZN A 401  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A  78   OD1
REMARK 620 2 HIS A  80   NE2 116.7
REMARK 620 3 ASP A 114   OD1  88.3  95.4
REMARK 620 4 HOH A1267   O    90.0  94.0 170.2
REMARK 620 5 HOH A1269   O   104.7 137.5  75.6  95.5
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A 402  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 114   OD1
REMARK 620 2 ASN A 149   OD1  92.5
REMARK 620 3 HIS A 207   NE2  86.7  92.3
REMARK 620 4 HIS A 286   ND1 169.9  97.1  96.1
REMARK 620 5 HOH A1269   O    73.2 133.4 129.4  97.7
REMARK 620 N                    1     2     3     4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 401
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 402
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THERE ARE CONFLICTS BETWEEN SEQRES(SER)
REMARK 999 AND SEQUENCE DATABASE (GLY).
REMARK 999 THE AUTHORS BELIEVE THAT THE SEQRES IS CORRECT AND IS
REMARK 999 THE TRUE IDENTITY OF THESE RESIDUES AND IS NATURAL MUTANT.
DBREF  2Z72 A    3   342  UNP    Q9S427   Q9S427_9GAMM    22    361
SEQADV 2Z72 MET A    1  UNP  Q9S427              EXPRESSION TAG
SEQADV 2Z72 GLY A    2  UNP  Q9S427              EXPRESSION TAG
SEQADV 2Z72 SER A  182  UNP  Q9S427    GLY   201 SEE REMARK 999
SEQRES   1 A  342  MET GLY ASN THR ALA THR GLU PHE ASP GLY PRO TYR VAL
SEQRES   2 A  342  ILE THR PRO ILE SER GLY GLN SER THR ALA TYR TRP ILE
SEQRES   3 A  342  CYS ASP ASN ARG LEU LYS THR THR SER ILE GLU LYS LEU
SEQRES   4 A  342  GLN VAL ASN ARG PRO GLU HIS CYS GLY ASP LEU PRO GLU
SEQRES   5 A  342  THR LYS LEU SER SER GLU ILE LYS GLN ILE MET PRO ASP
SEQRES   6 A  342  THR TYR LEU GLY ILE LYS LYS VAL VAL ALA LEU SER ASP
SEQRES   7 A  342  VAL HIS GLY GLN TYR ASP VAL LEU LEU THR LEU LEU LYS
SEQRES   8 A  342  LYS GLN LYS ILE ILE ASP SER ASP GLY ASN TRP ALA PHE
SEQRES   9 A  342  GLY GLU GLY HIS MET VAL MET THR GLY ASP ILE PHE ASP
SEQRES  10 A  342  ARG GLY HIS GLN VAL ASN GLU VAL LEU TRP PHE MET TYR
SEQRES  11 A  342  GLN LEU ASP GLN GLN ALA ARG ASP ALA GLY GLY MET VAL
SEQRES  12 A  342  HIS LEU LEU MET GLY ASN HIS GLU GLN MET VAL LEU GLY
SEQRES  13 A  342  GLY ASP LEU ARG TYR VAL HIS GLN ARG TYR ASP ILE ALA
SEQRES  14 A  342  THR THR LEU ILE ASN ARG PRO TYR ASN LYS LEU TYR SER
SEQRES  15 A  342  ALA ASP THR GLU ILE GLY GLN TRP LEU ARG SER LYS ASN
SEQRES  16 A  342  THR ILE ILE LYS ILE ASN ASP VAL LEU TYR MET HIS GLY
SEQRES  17 A  342  GLY ILE SER SER GLU TRP ILE SER ARG GLU LEU THR LEU
SEQRES  18 A  342  ASP LYS ALA ASN ALA LEU TYR ARG ALA ASN VAL ASP ALA
SEQRES  19 A  342  SER LYS LYS SER LEU LYS ALA ASP ASP LEU LEU ASN PHE
SEQRES  20 A  342  LEU PHE PHE GLY ASN GLY PRO THR TRP TYR ARG GLY TYR
SEQRES  21 A  342  PHE SER GLU THR PHE THR GLU ALA GLU LEU ASP THR ILE
SEQRES  22 A  342  LEU GLN HIS PHE ASN VAL ASN HIS ILE VAL VAL GLY HIS
SEQRES  23 A  342  THR SER GLN GLU ARG VAL LEU GLY LEU PHE HIS ASN LYS
SEQRES  24 A  342  VAL ILE ALA VAL ASP SER SER ILE LYS VAL GLY LYS SER
SEQRES  25 A  342  GLY GLU LEU LEU LEU LEU GLU ASN ASN ARG LEU ILE ARG
SEQRES  26 A  342  GLY LEU TYR ASP GLY THR ARG GLU THR LEU GLN GLU ASN
SEQRES  27 A  342  SER LEU ASN GLN
HET     ZN  A 401       1
HET     ZN  A 402       1
HETNAM      ZN ZINC ION
FORMUL   2   ZN    2(ZN 2+)
FORMUL   4  HOH   *772(H2 O)
HELIX    1   1 GLN A   82  GLN A   93  1                                  12
HELIX    2   2 GLN A  121  ALA A  139  1                                  19
HELIX    3   3 GLY A  148  GLY A  157  1                                  10
HELIX    4   4 ARG A  165  ILE A  173  1                                   9
HELIX    5   5 PRO A  176  SER A  182  5                                   7
HELIX    6   6 THR A  185  SER A  193  1                                   9
HELIX    7   7 SER A  211  ARG A  217  1                                   7
HELIX    8   8 THR A  220  VAL A  232  1                                  13
HELIX    9   9 SER A  235  ASP A  242  1                                   8
HELIX   10  10 ASP A  242  PHE A  250  1                                   9
HELIX   11  11 ARG A  258  SER A  262  5                                   5
HELIX   12  12 THR A  266  ASN A  278  1                                  13
HELIX   13  13 SER A  306  GLY A  310  5                                   5
SHEET    1   A 3 PHE A   8  ILE A  14  0
SHEET    2   A 3 THR A  22  CYS A  27 -1  O  ILE A  26   N  ASP A   9
SHEET    3   A 3 ARG A  30  SER A  35 -1  O  LYS A  32   N  TRP A  25
SHEET    1   B 2 GLN A  40  VAL A  41  0
SHEET    2   B 2 THR A  53  LYS A  54 -1  O  THR A  53   N  VAL A  41
SHEET    1   C 6 THR A  66  TYR A  67  0
SHEET    2   C 6 ILE A 197  ILE A 200  1  O  LYS A 199   N  TYR A  67
SHEET    3   C 6 VAL A 203  MET A 206 -1  O  TYR A 205   N  ILE A 198
SHEET    4   C 6 HIS A 281  VAL A 284  1  O  VAL A 283   N  LEU A 204
SHEET    5   C 6 VAL A 300  ALA A 302  1  O  ILE A 301   N  ILE A 282
SHEET    6   C 6 LEU A 293  LEU A 295 -1  N  LEU A 293   O  ALA A 302
SHEET    1   D 7 MET A 142  LEU A 145  0
SHEET    2   D 7 HIS A 108  MET A 111  1  N  MET A 109   O  HIS A 144
SHEET    3   D 7 LYS A  72  LEU A  76  1  N  VAL A  74   O  VAL A 110
SHEET    4   D 7 LEU A 315  GLU A 319 -1  O  LEU A 318   N  VAL A  73
SHEET    5   D 7 ARG A 322  GLY A 326 -1  O  GLY A 326   N  LEU A 315
SHEET    6   D 7 ARG A 332  GLU A 337 -1  O  GLU A 333   N  ARG A 325
SHEET    7   D 7 LEU A 340  ASN A 341 -1  O  LEU A 340   N  GLU A 337
SSBOND   1 CYS A   27    CYS A   47                          1555   1555  1.94
LINK         OD1 ASP A  78                ZN    ZN A 401     1555   1555  1.99
LINK         NE2 HIS A  80                ZN    ZN A 401     1555   1555  2.01
LINK         OD1 ASP A 114                ZN    ZN A 401     1555   1555  2.17
LINK         OD1 ASP A 114                ZN    ZN A 402     1555   1555  2.29
LINK         OD1 ASN A 149                ZN    ZN A 402     1555   1555  2.07
LINK         NE2 HIS A 207                ZN    ZN A 402     1555   1555  2.01
LINK         ND1 HIS A 286                ZN    ZN A 402     1555   1555  2.13
LINK        ZN    ZN A 401                 O   HOH A1267     1555   1555  2.12
LINK        ZN    ZN A 401                 O   HOH A1269     1555   1555  1.98
LINK        ZN    ZN A 402                 O   HOH A1269     1555   1555  1.96
CISPEP   1 GLY A   10    PRO A   11          0         2.32
SITE     1 AC1  5 ASP A  78  HIS A  80  ASP A 114  HOH A1267
SITE     2 AC1  5 HOH A1269
SITE     1 AC2  5 ASP A 114  ASN A 149  HIS A 207  HIS A 286
SITE     2 AC2  5 HOH A1269
CRYST1   55.565   77.306   81.029  90.00  90.00  90.00 P 21 21 21    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      0.017997  0.000000  0.000000        0.00000
SCALE2      0.000000  0.012936  0.000000        0.00000
SCALE3      0.000000  0.000000  0.012341        0.00000
      
PROCHECK
Go to PROCHECK summary
 References