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PDBsum entry 1gwz

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Hydrolase PDB id
1gwz
Jmol
Contents
Protein chain
280 a.a.
HEADER    HYDROLASE                               22-AUG-98   1GWZ
TITLE     CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF THE PROTEIN
TITLE    2 TYROSINE PHOSPHATASE SHP-1
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: SHP-1;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: CATALYTIC DOMAIN;
COMPND   5 SYNONYM: PROTEIN-TYROSINE PHOSPHATASE;
COMPND   6 EC: 3.1.3.48;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PT7-PTP1C
KEYWDS    HYDROLASE, PROTEIN TYROSINE PHOSPHATASE, CATALYTIC DOMAIN,
KEYWDS   2 WPD LOOP, SH2 DOMAIN
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.YANG,X.LIANG,T.NIU,W.MENG,Z.ZHAO,G.W.ZHOU
REVDAT   2   24-FEB-09 1GWZ    1       VERSN
REVDAT   1   22-AUG-99 1GWZ    0
JRNL        AUTH   J.YANG,X.LIANG,T.NIU,W.MENG,Z.ZHAO,G.W.ZHOU
JRNL        TITL   CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF
JRNL        TITL 2 PROTEIN-TYROSINE PHOSPHATASE SHP-1.
JRNL        REF    J.BIOL.CHEM.                  V. 273 28199 1998
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   9774441
JRNL        DOI    10.1074/JBC.273.43.28199
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   X.LIANG,W.MENG,T.NIU,Z.ZHAO,G.W.ZHOU
REMARK   1  TITL   EXPRESSION, PURIFICATION, AND CRYSTALLIZATION OF
REMARK   1  TITL 2 THE CATALYTIC DOMAIN OF PROTEIN TYROSINE
REMARK   1  TITL 3 PHOSPHATASE SHP-1
REMARK   1  REF    J.STRUCT.BIOL.                V. 120   201 1997
REMARK   1  REFN                   ISSN 1047-8477
REMARK   2
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.85
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1000000.000
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.7
REMARK   3   NUMBER OF REFLECTIONS             : 7392
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.209
REMARK   3   FREE R VALUE                     : 0.293
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 366
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           : 8
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.60
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            : 2207
REMARK   3   NUCLEIC ACID ATOMS       : NULL
REMARK   3   HETEROGEN ATOMS          : NULL
REMARK   3   SOLVENT ATOMS            : NULL
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) : 0.30
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.30
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.014
REMARK   3   BOND ANGLES            (DEGREES) : 2.10
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 28.40
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.90
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  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  : PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : NULL
REMARK   3  PARAMETER FILE  3  : NULL
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3  TOPOLOGY FILE  3   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1GWZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : MAY-97
REMARK 200  TEMPERATURE           (KELVIN) : 85
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RUH3R
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NI FILTER
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 8779
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7
REMARK 200  DATA REDUNDANCY                : 3.200
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.08200
REMARK 200   FOR THE DATA SET  : 9.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.57
REMARK 200  COMPLETENESS FOR SHELL     (%) : 71.8
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         : 4.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PTP-1B
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 39.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       43.89000
REMARK 290   SMTRY3   2  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 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     GLY A   245
REMARK 465     PHE A   246
REMARK 465     TRP A   247
REMARK 465     GLU A   248
REMARK 465     GLU A   249
REMARK 465     LEU A   402
REMARK 465     ASP A   403
REMARK 465     ASN A   404
REMARK 465     GLY A   533
REMARK 465     GLN A   534
REMARK 465     GLU A   535
REMARK 465     SER A   536
REMARK 465     GLU A   537
REMARK 465     TYR A   538
REMARK 465     GLY A   539
REMARK 465     ASN A   540
REMARK 465     ILE A   541
REMARK 465     THR A   542
REMARK 465     TYR A   543
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     PHE A 250    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     VAL A 258    CG1  CG2
REMARK 470     LEU A 261    CG   CD1  CD2
REMARK 470     LEU A 314    CG   CD1  CD2
REMARK 470     ASP A 317    CG   OD1  OD2
REMARK 470     LYS A 362    CG   CD   CE   NZ
REMARK 470     ASP A 436    CG   OD1  OD2
REMARK 470     ASP A 481    CG   OD1  OD2
REMARK 470     GLU A 504    CG   CD   OE1  OE2
REMARK 470     LYS A 508    CG   CD   CE   NZ
REMARK 470     GLU A 519    CG   CD   OE1  OE2
REMARK 470     GLN A 529    CG   CD   OE1  NE2
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    PHE A   517     OG1  THR A   521              2.10
REMARK 500   O    GLY A   460     OG1  THR A   464              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    GLU A 251     -163.46    172.40
REMARK 500    LEU A 253       94.21    -68.05
REMARK 500    LYS A 255       87.53    -59.76
REMARK 500    GLN A 256       91.97    -53.94
REMARK 500    LYS A 259       76.01     44.28
REMARK 500    ARG A 264       44.19   -159.67
REMARK 500    ARG A 294      160.76    -43.48
REMARK 500    PRO A 299      -91.99     -8.75
REMARK 500    ASN A 311      -83.11    -34.39
REMARK 500    PRO A 316      157.22    -32.91
REMARK 500    ASP A 317     -151.72     45.42
REMARK 500    GLU A 318     -165.03    -73.18
REMARK 500    ALA A 320      160.66    -26.80
REMARK 500    TRP A 342      -72.75    -58.41
REMARK 500    ASN A 345       23.07     48.96
REMARK 500    GLU A 355      -52.24    -22.67
REMARK 500    ASN A 361      151.17    -47.00
REMARK 500    LYS A 362      -54.04   -127.58
REMARK 500    TYR A 366       36.54   -144.26
REMARK 500    TYR A 376       79.11   -112.61
REMARK 500    PRO A 378       36.80    -88.72
REMARK 500    ASP A 406       94.77    -35.92
REMARK 500    SER A 426     -112.99    -73.15
REMARK 500    CYS A 455      -84.32   -127.21
REMARK 500    SER A 456      -60.49   -148.33
REMARK 500    ILE A 459       33.09   -159.47
REMARK 500    THR A 462      -78.12    -60.73
REMARK 500    MET A 500      -66.13     -7.61
REMARK 500    GLU A 504      -67.52    -27.19
REMARK 500    THR A 521        6.33    -63.28
REMARK 500    GLN A 531       36.77    -97.43
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: WPD
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: INVOLVED IN SUBSTRATE BINDING
DBREF  1GWZ A  245   543  UNP    P29350   PTN6_HUMAN     243    541
SEQRES   1 A  299  GLY PHE TRP GLU GLU PHE GLU SER LEU GLN LYS GLN GLU
SEQRES   2 A  299  VAL LYS ASN LEU HIS GLN ARG LEU GLU GLY GLN ARG PRO
SEQRES   3 A  299  GLU ASN LYS GLY LYS ASN ARG TYR LYS ASN ILE LEU PRO
SEQRES   4 A  299  PHE ASP HIS SER ARG VAL ILE LEU GLN GLY ARG ASP SER
SEQRES   5 A  299  ASN ILE PRO GLY SER ASP TYR ILE ASN ALA ASN TYR ILE
SEQRES   6 A  299  LYS ASN GLN LEU LEU GLY PRO ASP GLU ASN ALA LYS THR
SEQRES   7 A  299  TYR ILE ALA SER GLN GLY CYS LEU GLU ALA THR VAL ASN
SEQRES   8 A  299  ASP PHE TRP GLN MET ALA TRP GLN GLU ASN SER ARG VAL
SEQRES   9 A  299  ILE VAL MET THR THR ARG GLU VAL GLU LYS GLY ARG ASN
SEQRES  10 A  299  LYS CYS VAL PRO TYR TRP PRO GLU VAL GLY MET GLN ARG
SEQRES  11 A  299  ALA TYR GLY PRO TYR SER VAL THR ASN CYS GLY GLU HIS
SEQRES  12 A  299  ASP THR THR GLU TYR LYS LEU ARG THR LEU GLN VAL SER
SEQRES  13 A  299  PRO LEU ASP ASN GLY ASP LEU ILE ARG GLU ILE TRP HIS
SEQRES  14 A  299  TYR GLN TYR LEU SER TRP PRO ASP HIS GLY VAL PRO SER
SEQRES  15 A  299  GLU PRO GLY GLY VAL LEU SER PHE LEU ASP GLN ILE ASN
SEQRES  16 A  299  GLN ARG GLN GLU SER LEU PRO HIS ALA GLY PRO ILE ILE
SEQRES  17 A  299  VAL HIS CYS SER ALA GLY ILE GLY ARG THR GLY THR ILE
SEQRES  18 A  299  ILE VAL ILE ASP MET LEU MET GLU ASN ILE SER THR LYS
SEQRES  19 A  299  GLY LEU ASP CYS ASP ILE ASP ILE GLN LYS THR ILE GLN
SEQRES  20 A  299  MET VAL ARG ALA GLN ARG SER GLY MET VAL GLN THR GLU
SEQRES  21 A  299  ALA GLN TYR LYS PHE ILE TYR VAL ALA ILE ALA GLN PHE
SEQRES  22 A  299  ILE GLU THR THR LYS LYS LYS LEU GLU VAL LEU GLN SER
SEQRES  23 A  299  GLN LYS GLY GLN GLU SER GLU TYR GLY ASN ILE THR TYR
HELIX    1  A1 GLU A  266  LYS A  275  1                                  10
HELIX    2  A2 GLU A  331  GLN A  343  1                                  13
HELIX    3  A3 LEU A  432  GLN A  442  1                                  11
HELIX    4  A4 ARG A  461  LYS A  478  1                                  18
HELIX    5  A5 ILE A  486  ARG A  494  1                                   9
HELIX    6  A6 GLU A  504  LYS A  523  1                                  20
SHEET    1  S110 SER A 287  VAL A 289  0
SHEET    2  S110 ALA A 306  LYS A 310 -1
SHEET    3  S110 LYS A 321  GLN A 327 -1
SHEET    4  S110 ILE A 451  HIS A 454  1
SHEET    5  S110 ARG A 347  THR A 353  1
SHEET    6  S110 ARG A 409  LEU A 417  1
SHEET    7  S110 TYR A 392  VAL A 399 -1
SHEET    8  S110 GLY A 385  THR A 389 -1
SHEET    9  S110 SER A 380  ASN A 383  1
SHEET   10  S110 MET A 372  ALA A 375 -1
SHEET    1  S2 2 VAL A 356  GLU A 357  0
SHEET    2  S2 2 ARG A 360  LYS A 362 -1
SITE     1 WPD  2 TRP A 419  PRO A 428
CRYST1   41.820   87.780   43.000  90.00 117.40  90.00 P 1 21 1      2
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      0.023912  0.000000  0.012395        0.00000
SCALE2      0.000000  0.011392  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026194        0.00000
      
PROCHECK
Go to PROCHECK summary
 References