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PDBsum entry 2hv6

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Top Page protein metals Protein-protein interface(s) links
Unknown function PDB id
2hv6
Jmol
Contents
Protein chain
301 a.a.
Metals
_MG
Waters ×205
HEADER    UNKNOWN FUNCTION                        27-JUL-06   2HV6
TITLE     CRYSTAL STRUCTURE OF THE PHOSPHOTYROSYL PHOSPHATASE
TITLE    2 ACTIVATOR
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROTEIN PHOSPHATASE 2A, REGULATORY SUBUNIT B;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: PR 53;
COMPND   5 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: PPP2R4;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-15B
KEYWDS    PHOSPHOTYROSYL PHOSPHATASE ACTIVATOR, PHOSPHATASE, PP2A,
KEYWDS   2 PHOSPHATASE SPECIFICITY, UNKNOWN FUNCTION
EXPDTA    X-RAY DIFFRACTION
AUTHOR    Y.CHAO,P.D.JEFFREY,Y.SHI
REVDAT   3   24-FEB-09 2HV6    1       VERSN
REVDAT   2   05-SEP-06 2HV6    1       JRNL
REVDAT   1   22-AUG-06 2HV6    0
JRNL        AUTH   Y.CHAO,Y.XING,Y.CHEN,Y.XU,Z.LIN,Z.LI,P.D.JEFFREY,
JRNL        AUTH 2 J.B.STOCK,Y.SHI
JRNL        TITL   STRUCTURE AND MECHANISM OF THE PHOSPHOTYROSYL
JRNL        TITL 2 PHOSPHATASE ACTIVATOR.
JRNL        REF    MOL.CELL                      V.  23   535 2006
JRNL        REFN                   ISSN 1097-2765
JRNL        PMID   16916641
JRNL        DOI    10.1016/J.MOLCEL.2006.07.027
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS
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) : 1.90
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00
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)   (%) : 92.2
REMARK   3   NUMBER OF REFLECTIONS             : 35226
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) : 0.183
REMARK   3   FREE R VALUE                     : 0.239
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 1726
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            : 4832
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 1
REMARK   3   SOLVENT ATOMS            : 205
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) : 0.008
REMARK   3   BOND ANGLES            (DEGREES) : 1.37
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 2HV6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JUL-06.
REMARK 100 THE RCSB ID CODE IS RCSB038800.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-06
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.8
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : NSLS
REMARK 200  BEAMLINE                       : X29A
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1
REMARK 200  MONOCHROMATOR                  : GRAPHITE
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36825
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900
REMARK 200  RESOLUTION RANGE LOW       (A) : 99.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.4
REMARK 200  DATA REDUNDANCY                : 3.000
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.05600
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) : 2.00
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.6
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.31300
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: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY: 2G62
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2MM MG FORMATE, 5% GLYCEROL,
REMARK 280  17.5% PEG3350 (W/V), 0.1 M BISTRIS, PH 6.8, VAPOR DIFFUSION,
REMARK 280  HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,Y,-Z
REMARK 290       3555   X+1/2,Y+1/2,Z
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        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       79.12500
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       21.39500
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       79.12500
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       21.39500
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 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 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     ALA A     2
REMARK 465     GLU A     3
REMARK 465     GLY A     4
REMARK 465     GLU A     5
REMARK 465     ARG A     6
REMARK 465     GLN A     7
REMARK 465     PRO A     8
REMARK 465     PRO A     9
REMARK 465     PRO A    10
REMARK 465     ASP A    11
REMARK 465     SER A    12
REMARK 465     SER A    13
REMARK 465     GLU A    14
REMARK 465     GLU A    15
REMARK 465     ALA A    16
REMARK 465     PRO A    17
REMARK 465     PRO A    18
REMARK 465     ALA A    19
REMARK 465     THR A    20
REMARK 465     GLN A    21
REMARK 465     GLY A   323
REMARK 465     MET B     1
REMARK 465     ALA B     2
REMARK 465     GLU B     3
REMARK 465     GLY B     4
REMARK 465     GLU B     5
REMARK 465     ARG B     6
REMARK 465     GLN B     7
REMARK 465     PRO B     8
REMARK 465     PRO B     9
REMARK 465     PRO B    10
REMARK 465     ASP B    11
REMARK 465     SER B    12
REMARK 465     SER B    13
REMARK 465     GLU B    14
REMARK 465     GLU B    15
REMARK 465     ALA B    16
REMARK 465     PRO B    17
REMARK 465     PRO B    18
REMARK 465     ALA B    19
REMARK 465     THR B    20
REMARK 465     GLN B    21
REMARK 465     GLY B   205
REMARK 465     SER B   206
REMARK 465     GLN B   207
REMARK 465     GLY B   208
REMARK 465     VAL B   209
REMARK 465     TRP B   210
REMARK 465     GLY B   323
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   O    PRO B    34     O    PRO B    34     2554     2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    PHE A 100     -143.80   -106.97
REMARK 500    ILE A 149       62.27     64.00
REMARK 500    PHE A 217      -55.98   -151.37
REMARK 500    TYR A 232      -53.48   -122.75
REMARK 500    SER A 272       55.78   -145.21
REMARK 500    CYS A 299      -70.30   -122.81
REMARK 500    ASP B  95       95.34    -68.34
REMARK 500    PRO B  97     -147.47    -96.21
REMARK 500    SER B  98       78.30    -17.48
REMARK 500    ARG B  99        4.82     51.76
REMARK 500    PHE B 100      108.83    -57.47
REMARK 500    PHE B 215      -71.55    -97.84
REMARK 500    PHE B 217      -49.00   -137.56
REMARK 500    LYS B 264       74.77    175.34
REMARK 500    THR B 265      104.82    -39.91
REMARK 500    PRO B 267     -122.33    -65.30
REMARK 500    PHE B 268      -84.88   -127.73
REMARK 500    ALA B 269      -64.27      3.52
REMARK 500    GLU B 270      -72.99    -74.92
REMARK 500    SER B 272       92.76   -165.22
REMARK 500    ALA B 297     -110.60    -70.90
REMARK 500    GLU B 298      -82.52    -18.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A 324  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 214   OD1
REMARK 620 2 HOH A 363   O    98.3
REMARK 620 3 HOH A 388   O    90.5 100.5
REMARK 620 4 HOH A 365   O   166.3  90.0  98.6
REMARK 620 5 GLY A 208   O    82.7 160.9  98.6  85.9
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 MG A 324
DBREF  2HV6 A    1   323  UNP    Q15257   PTPA_HUMAN       1    323
DBREF  2HV6 B    1   323  UNP    Q15257   PTPA_HUMAN       1    323
SEQRES   1 A  323  MET ALA GLU GLY GLU ARG GLN PRO PRO PRO ASP SER SER
SEQRES   2 A  323  GLU GLU ALA PRO PRO ALA THR GLN ASN PHE ILE ILE PRO
SEQRES   3 A  323  LYS LYS GLU ILE HIS THR VAL PRO ASP MET GLY LYS TRP
SEQRES   4 A  323  LYS ARG SER GLN ALA TYR ALA ASP TYR ILE GLY PHE ILE
SEQRES   5 A  323  LEU THR LEU ASN GLU GLY VAL LYS GLY LYS LYS LEU THR
SEQRES   6 A  323  PHE GLU TYR ARG VAL SER GLU ALA ILE GLU LYS LEU VAL
SEQRES   7 A  323  ALA LEU LEU ASN THR LEU ASP ARG TRP ILE ASP GLU THR
SEQRES   8 A  323  PRO PRO VAL ASP GLN PRO SER ARG PHE GLY ASN LYS ALA
SEQRES   9 A  323  TYR ARG THR TRP TYR ALA LYS LEU ASP GLU GLU ALA GLU
SEQRES  10 A  323  ASN LEU VAL ALA THR VAL VAL PRO THR HIS LEU ALA ALA
SEQRES  11 A  323  ALA VAL PRO GLU VAL ALA VAL TYR LEU LYS GLU SER VAL
SEQRES  12 A  323  GLY ASN SER THR ARG ILE ASP TYR GLY THR GLY HIS GLU
SEQRES  13 A  323  ALA ALA PHE ALA ALA PHE LEU CYS CYS LEU CYS LYS ILE
SEQRES  14 A  323  GLY VAL LEU ARG VAL ASP ASP GLN ILE ALA ILE VAL PHE
SEQRES  15 A  323  LYS VAL PHE ASN ARG TYR LEU GLU VAL MET ARG LYS LEU
SEQRES  16 A  323  GLN LYS THR TYR ARG MET GLU PRO ALA GLY SER GLN GLY
SEQRES  17 A  323  VAL TRP GLY LEU ASP ASP PHE GLN PHE LEU PRO PHE ILE
SEQRES  18 A  323  TRP GLY SER SER GLN LEU ILE ASP HIS PRO TYR LEU GLU
SEQRES  19 A  323  PRO ARG HIS PHE VAL ASP GLU LYS ALA VAL ASN GLU ASN
SEQRES  20 A  323  HIS LYS ASP TYR MET PHE LEU GLU CYS ILE LEU PHE ILE
SEQRES  21 A  323  THR GLU MET LYS THR GLY PRO PHE ALA GLU HIS SER ASN
SEQRES  22 A  323  GLN LEU TRP ASN ILE SER ALA VAL PRO SER TRP SER LYS
SEQRES  23 A  323  VAL ASN GLN GLY LEU ILE ARG MET TYR LYS ALA GLU CYS
SEQRES  24 A  323  LEU GLU LYS PHE PRO VAL ILE GLN HIS PHE LYS PHE GLY
SEQRES  25 A  323  SER LEU LEU PRO ILE HIS PRO VAL THR SER GLY
SEQRES   1 B  323  MET ALA GLU GLY GLU ARG GLN PRO PRO PRO ASP SER SER
SEQRES   2 B  323  GLU GLU ALA PRO PRO ALA THR GLN ASN PHE ILE ILE PRO
SEQRES   3 B  323  LYS LYS GLU ILE HIS THR VAL PRO ASP MET GLY LYS TRP
SEQRES   4 B  323  LYS ARG SER GLN ALA TYR ALA ASP TYR ILE GLY PHE ILE
SEQRES   5 B  323  LEU THR LEU ASN GLU GLY VAL LYS GLY LYS LYS LEU THR
SEQRES   6 B  323  PHE GLU TYR ARG VAL SER GLU ALA ILE GLU LYS LEU VAL
SEQRES   7 B  323  ALA LEU LEU ASN THR LEU ASP ARG TRP ILE ASP GLU THR
SEQRES   8 B  323  PRO PRO VAL ASP GLN PRO SER ARG PHE GLY ASN LYS ALA
SEQRES   9 B  323  TYR ARG THR TRP TYR ALA LYS LEU ASP GLU GLU ALA GLU
SEQRES  10 B  323  ASN LEU VAL ALA THR VAL VAL PRO THR HIS LEU ALA ALA
SEQRES  11 B  323  ALA VAL PRO GLU VAL ALA VAL TYR LEU LYS GLU SER VAL
SEQRES  12 B  323  GLY ASN SER THR ARG ILE ASP TYR GLY THR GLY HIS GLU
SEQRES  13 B  323  ALA ALA PHE ALA ALA PHE LEU CYS CYS LEU CYS LYS ILE
SEQRES  14 B  323  GLY VAL LEU ARG VAL ASP ASP GLN ILE ALA ILE VAL PHE
SEQRES  15 B  323  LYS VAL PHE ASN ARG TYR LEU GLU VAL MET ARG LYS LEU
SEQRES  16 B  323  GLN LYS THR TYR ARG MET GLU PRO ALA GLY SER GLN GLY
SEQRES  17 B  323  VAL TRP GLY LEU ASP ASP PHE GLN PHE LEU PRO PHE ILE
SEQRES  18 B  323  TRP GLY SER SER GLN LEU ILE ASP HIS PRO TYR LEU GLU
SEQRES  19 B  323  PRO ARG HIS PHE VAL ASP GLU LYS ALA VAL ASN GLU ASN
SEQRES  20 B  323  HIS LYS ASP TYR MET PHE LEU GLU CYS ILE LEU PHE ILE
SEQRES  21 B  323  THR GLU MET LYS THR GLY PRO PHE ALA GLU HIS SER ASN
SEQRES  22 B  323  GLN LEU TRP ASN ILE SER ALA VAL PRO SER TRP SER LYS
SEQRES  23 B  323  VAL ASN GLN GLY LEU ILE ARG MET TYR LYS ALA GLU CYS
SEQRES  24 B  323  LEU GLU LYS PHE PRO VAL ILE GLN HIS PHE LYS PHE GLY
SEQRES  25 B  323  SER LEU LEU PRO ILE HIS PRO VAL THR SER GLY
HET     MG  A 324       1
HETNAM      MG MAGNESIUM ION
FORMUL   3   MG    MG 2+
FORMUL   4  HOH   *205(H2 O)
HELIX    1   1 PRO A   34  SER A   42  1                                   9
HELIX    2   2 SER A   42  LYS A   60  1                                  19
HELIX    3   3 SER A   71  THR A   91  1                                  21
HELIX    4   4 LYS A  103  ALA A  121  1                                  19
HELIX    5   5 PRO A  125  ALA A  130  5                                   6
HELIX    6   6 ALA A  131  GLU A  141  1                                  11
HELIX    7   7 GLY A  152  ILE A  169  1                                  18
HELIX    8   8 ARG A  173  ASP A  175  5                                   3
HELIX    9   9 ASP A  176  LYS A  183  1                                   8
HELIX   10  10 LYS A  183  TYR A  199  1                                  17
HELIX   11  11 SER A  206  GLY A  211  1                                   6
HELIX   12  12 PHE A  217  ILE A  228  1                                  12
HELIX   13  13 GLU A  234  VAL A  239  5                                   6
HELIX   14  14 ASP A  240  HIS A  248  1                                   9
HELIX   15  15 TYR A  251  LYS A  264  1                                  14
HELIX   16  16 PRO A  267  SER A  272  1                                   6
HELIX   17  17 SER A  272  SER A  279  1                                   8
HELIX   18  18 SER A  283  CYS A  299  1                                  17
HELIX   19  19 LYS A  302  GLN A  307  1                                   6
HELIX   20  20 VAL B   33  TRP B   39  5                                   7
HELIX   21  21 SER B   42  LYS B   60  1                                  19
HELIX   22  22 ALA B   73  THR B   91  1                                  19
HELIX   23  23 LYS B  103  ALA B  121  1                                  19
HELIX   24  24 PRO B  125  ALA B  130  5                                   6
HELIX   25  25 ALA B  131  GLU B  141  1                                  11
HELIX   26  26 GLY B  152  ILE B  169  1                                  18
HELIX   27  27 ASP B  176  LYS B  183  1                                   8
HELIX   28  28 LYS B  183  ARG B  200  1                                  18
HELIX   29  29 GLY B  211  GLN B  216  1                                   6
HELIX   30  30 PHE B  217  ILE B  228  1                                  12
HELIX   31  31 GLU B  234  VAL B  239  5                                   6
HELIX   32  32 ASP B  240  HIS B  248  1                                   9
HELIX   33  33 TYR B  251  MET B  263  1                                  13
HELIX   34  34 ASN B  273  ALA B  280  1                                   8
HELIX   35  35 SER B  283  ALA B  297  1                                  15
HELIX   36  36 GLU B  298  GLU B  301  5                                   4
HELIX   37  37 LYS B  302  GLN B  307  1                                   6
SHEET    1   A 2 LYS A  27  LYS A  28  0
SHEET    2   A 2 LYS A 310  PHE A 311 -1  O  PHE A 311   N  LYS A  27
SHEET    1   B 2 ASP A 150  TYR A 151  0
SHEET    2   B 2 GLU A 202  PRO A 203  1  O  GLU A 202   N  TYR A 151
SHEET    1   C 2 LYS B  27  LYS B  28  0
SHEET    2   C 2 LYS B 310  PHE B 311 -1  O  PHE B 311   N  LYS B  27
SHEET    1   D 2 ASP B 150  TYR B 151  0
SHEET    2   D 2 GLU B 202  PRO B 203  1  O  GLU B 202   N  TYR B 151
LINK        MG    MG A 324                 OD1 ASP A 214     1555   1555  2.15
LINK        MG    MG A 324                 O   HOH A 363     1555   1555  1.93
LINK        MG    MG A 324                 O   HOH A 388     1555   1555  1.85
LINK        MG    MG A 324                 O   HOH A 365     1555   1555  2.07
LINK        MG    MG A 324                 O   GLY A 208     1555   1555  2.65
SITE     1 AC1  5 GLY A 208  ASP A 214  HOH A 363  HOH A 365
SITE     2 AC1  5 HOH A 388
CRYST1  158.250   42.790   75.570  90.00 108.83  90.00 C 1 2 1       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      0.006319  0.000000  0.002155        0.00000
SCALE2      0.000000  0.023370  0.000000        0.00000
SCALE3      0.000000  0.000000  0.013981        0.00000
      
PROCHECK
Go to PROCHECK summary
 References