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PDBsum entry 1gku

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Topoisomerase PDB id
1gku
Jmol
Contents
Protein chain
1011 a.a. *
Waters ×157
* Residue conservation analysis
HEADER    TOPOISOMERASE                           21-AUG-01   1GKU
TITLE     REVERSE GYRASE FROM ARCHAEOGLOBUS FULGIDUS
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: REVERSE GYRASE;
COMPND   3 CHAIN: B;
COMPND   4 SYNONYM: TOP-RG;
COMPND   5 ENGINEERED: YES;
COMPND   6 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ARCHAEOGLOBUS FULGIDUS;
SOURCE   3 ORGANISM_TAXID: 224325;
SOURCE   4 STRAIN: VC-16;
SOURCE   5 ATCC: 49558;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: C41(DE3);
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PRET3A;
SOURCE  10 OTHER_DETAILS: GERMAN COLLECTION OF MICROORGANISMS (DSMZ)
KEYWDS    TOPOISOMERASE, DNA SUPERCOILING, ARCHAEA, HELICASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.C.RODRIGUEZ,D.STOCK
REVDAT   2   24-FEB-09 1GKU    1       VERSN
REVDAT   1   11-FEB-02 1GKU    0
JRNL        AUTH   A.C.RODRIGUEZ,D.STOCK
JRNL        TITL   CRYSTAL STRUCTURE OF REVERSE GYRASE: INSIGHTS INTO
JRNL        TITL 2 THE POSITIVE SUPERCOILING OF DNA.
JRNL        REF    EMBO J.                       V.  21   418 2002
JRNL        REFN                   ISSN 0261-4189
JRNL        PMID   11823434
JRNL        DOI    10.1093/EMBOJ/21.3.418
REMARK   2
REMARK   2 RESOLUTION.    2.7  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 : MLF
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.7
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.3
REMARK   3   NUMBER OF REFLECTIONS             : 30333
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) : 0.226
REMARK   3   FREE R VALUE                     : 0.295
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.8
REMARK   3   FREE R VALUE TEST SET COUNT      : 1474
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           : 10
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.7
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.8
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.3
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2961
REMARK   3   BIN R VALUE           (WORKING SET) : 0.253
REMARK   3   BIN FREE R VALUE                    : 0.329
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 0.60
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 18
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            : 8151
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 157
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 67.6
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 55.4
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 7.130
REMARK   3    B22 (A**2) : -7.426
REMARK   3    B33 (A**2) : 0.296
REMARK   3    B12 (A**2) : 0.00
REMARK   3    B13 (A**2) : 0.438
REMARK   3    B23 (A**2) : 0.00
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.34
REMARK   3   ESD FROM SIGMAA              (A) : 0.23
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.0
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.49
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.45
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.007
REMARK   3   BOND ANGLES            (DEGREES) : 1.3
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) : 3.42  ; 3.00
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 5.77  ; 4.00
REMARK   3   SIDE-CHAIN BOND              (A**2) : 5.28  ; 4.00
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 8.11  ; 6.00
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : 0.35335
REMARK   3   BSOL        : 66.5478
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  : WATER_REP.PARAM
REMARK   3  PARAMETER FILE  2  : NULL
REMARK   3  TOPOLOGY FILE  1   : WATER.TOP
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NINETEEN RESIDUES N-TERMINAL TO
REMARK   3  SERINE 33 IN THE COORDINATES HAVE BEEN MODELLED AS THREE NON-
REMARK   3  CONTIGUOUS CHAINS OF POLYALANINE. AMINO ACID SEQUENCE AND
REMARK   3  NUMBERING FOR THESE RESIDUES HAS BEEN ASSIGNED AS 1-21. THEIR
REMARK   3  ACTUAL POSITION IN THE PROTEIN SEQUENCE IS UNCLEAR DUE TO POOR
REMARK   3  ELECTRON DENSITY.
REMARK   4
REMARK   4 1GKU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-AUG-01.
REMARK 100 THE PDBE ID CODE IS EBI-8476.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 15-FEB-01
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 6.00
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : ID14-4
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9686
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : NULL
REMARK 200  DETECTOR MANUFACTURER          : ADSC
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28735
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700
REMARK 200  RESOLUTION RANGE LOW       (A) : 41.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3
REMARK 200  DATA REDUNDANCY                : 3.200
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.06200
REMARK 200   FOR THE DATA SET  : 8.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.78
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.28800
REMARK 200   FOR SHELL         : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE/RESOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS  (%): 52.0
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 1000,
REMARK 280  15% ETHYLENE GLYCOL, 100 MM CACODYLATE (PH 6)
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       33.99250
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 GENERATING THE BIOMOLECULE
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: PQS
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 400
REMARK 400 COMPOUND
REMARK 400  CHAIN B ENGINEERED MUTATION PRO719LEU, LEU1046MET.
REMARK 400  NINETEEN RESIDUES N-TERMINAL TO SERINE 33 IN THE
REMARK 400  COORDINATES HAVE BEEN MODELLED AS THREE NON-CONTIGUOUS
REMARK 400  CHAINS OF POLYALANINE.  AMINO ACID SEQUENCE AND NUMBERING
REMARK 400  FOR THESE RESIDUES HAS BEEN ASSIGNED AS 1-21. THEIR ACTUAL
REMARK 400  POSITION IN THE PROTEIN SEQUENCE IS UNCLEAR DUE TO POOR
REMARK 400  ELECTRON DENSITY.
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     ALA B     7
REMARK 465     ALA B    13
REMARK 465     ALA B    22
REMARK 465     ALA B    23
REMARK 465     ALA B    24
REMARK 465     ALA B    25
REMARK 465     ALA B    26
REMARK 465     ALA B    27
REMARK 465     ALA B    28
REMARK 465     ALA B    29
REMARK 465     ALA B    30
REMARK 465     ALA B    31
REMARK 465     ALA B    32
REMARK 465     TYR B   329
REMARK 465     TYR B   330
REMARK 465     GLY B   331
REMARK 465     THR B   332
REMARK 465     LEU B   333
REMARK 465     VAL B   334
REMARK 465     ARG B   583
REMARK 465     CYS B   584
REMARK 465     ARG B   585
REMARK 465     ASP B   586
REMARK 465     CYS B   587
REMARK 465     GLY B   588
REMARK 465     TYR B   589
REMARK 465     GLN B   590
REMARK 465     PHE B   591
REMARK 465     THR B   592
REMARK 465     GLU B   593
REMARK 465     ASP B   594
REMARK 465     ARG B   595
REMARK 465     GLU B   596
REMARK 465     SER B   597
REMARK 465     CYS B   598
REMARK 465     PRO B   599
REMARK 465     LYS B   600
REMARK 465     CYS B   601
REMARK 465     GLY B   602
REMARK 465     SER B   603
REMARK 465     GLU B   604
REMARK 465     ASN B   605
REMARK 465     VAL B   606
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 B   532  -  N    GLY B   534              2.20
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 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    ALA B   3     -141.09   -130.47
REMARK 500    ALA B   5       98.06    -63.43
REMARK 500    ALA B   9      104.64     88.26
REMARK 500    ALA B  16      -44.27    177.84
REMARK 500    CYS B  35       63.47   -115.34
REMARK 500    GLU B  56      114.28     62.98
REMARK 500    LYS B  84      -62.43   -109.02
REMARK 500    ARG B 101       95.44     63.96
REMARK 500    GLU B 124       36.64    -64.90
REMARK 500    LYS B 125       30.35   -154.52
REMARK 500    THR B 130     -161.43     65.30
REMARK 500    PRO B 142        1.05    -69.62
REMARK 500    LYS B 143      -55.66     62.25
REMARK 500    LEU B 153      -75.57    -43.99
REMARK 500    GLU B 172      -29.43     73.63
REMARK 500    SER B 191      -48.14    -22.95
REMARK 500    LYS B 208      -72.21    -61.26
REMARK 500    THR B 224      154.51     47.72
REMARK 500    THR B 226     -168.35    -57.74
REMARK 500    ALA B 227        5.53    -61.26
REMARK 500    LYS B 228       75.27    -62.09
REMARK 500    ASN B 241       67.96     35.03
REMARK 500    ASP B 261       99.14    179.38
REMARK 500    GLU B 262       36.44    -97.74
REMARK 500    ILE B 264       52.74    -63.56
REMARK 500    SER B 265     -121.29   -148.23
REMARK 500    THR B 266        0.70    -52.02
REMARK 500    LEU B 295      -14.16   -156.40
REMARK 500    PHE B 299      144.44     60.43
REMARK 500    ALA B 306       19.28     98.69
REMARK 500    LYS B 308      -78.70    -58.16
REMARK 500    LEU B 337       50.56   -109.90
REMARK 500    ASP B 362        0.29    -66.01
REMARK 500    LEU B 375      -17.05     94.74
REMARK 500    ARG B 384       28.39    -66.29
REMARK 500    LEU B 386       72.12     19.34
REMARK 500    ARG B 391       96.65     58.89
REMARK 500    ILE B 393      -35.60    -34.94
REMARK 500    LYS B 406       -9.86   -171.56
REMARK 500    GLU B 420      132.51   -172.21
REMARK 500    ASP B 470      -59.65     50.19
REMARK 500    ILE B 471     -154.14    -64.88
REMARK 500    ARG B 498      -15.89    -46.42
REMARK 500    ASP B 502       75.23   -159.49
REMARK 500    ALA B 535      149.32   -170.42
REMARK 500    PHE B 565       78.83    -64.56
REMARK 500    LEU B 569       85.56     54.63
REMARK 500    VAL B 570     -151.38    -91.37
REMARK 500    ARG B 573      -49.07   -160.03
REMARK 500    PHE B 574       99.49     60.80
REMARK 500    TRP B 693      -80.10    -72.58
REMARK 500    ASN B 707       99.80    -15.46
REMARK 500    ASN B 708      130.24    179.21
REMARK 500    ARG B 709     -144.40    -73.98
REMARK 500    ASN B 710       -7.10     59.46
REMARK 500    ALA B 716      -39.09    169.25
REMARK 500    ASP B 726       42.35    -67.70
REMARK 500    ARG B 727      -35.55   -153.01
REMARK 500    ASP B 742        1.90     86.70
REMARK 500    ASP B 750      -68.29   -106.80
REMARK 500    GLU B 751      164.35    -46.47
REMARK 500    LEU B 760      175.55    -58.34
REMARK 500    VAL B 761      -22.97   -162.43
REMARK 500    GLU B 762      152.25    171.08
REMARK 500    LYS B 788       40.43    -90.58
REMARK 500    ASP B 831      -46.47     92.64
REMARK 500    ARG B 836      101.33     67.24
REMARK 500    THR B 854     -174.21    -67.51
REMARK 500    GLU B 913      118.52   -161.54
REMARK 500    ARG B 915      115.18   -168.06
REMARK 500    ILE B 916      109.19    -52.00
REMARK 500    ARG B 928       88.06    -67.09
REMARK 500    VAL B 947      112.67     57.97
REMARK 500    TYR B1013      106.78     80.09
REMARK 500    PHE B1016       41.25    -95.81
REMARK 500    VAL B1017       14.52   -157.53
REMARK 500    GLU B1036      -76.86    -80.65
REMARK 500    SER B1052       11.08    -69.70
REMARK 500    ILE B1053     -139.68   -165.31
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 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
DBREF  1GKU B    1    32  PDB    1GKU     1GKU             1     32
DBREF  1GKU B   33  1054  UNP    O29238   O29238          33   1054
SEQADV 1GKU LEU B  719  UNP  O29238    PRO   719 ENGINEERED MUTATION
SEQADV 1GKU MET B 1046  UNP  O29238    LEU  1046 ENGINEERED MUTATION
SEQRES   1 B 1054  ALA ALA ALA ALA ALA ALA ALA ALA ALA ALA ALA ALA ALA
SEQRES   2 B 1054  ALA ALA ALA ALA ALA ALA ALA ALA ALA ALA ALA ALA ALA
SEQRES   3 B 1054  ALA ALA ALA ALA ALA ALA SER LEU CYS LEU PHE PRO GLU
SEQRES   4 B 1054  ASP PHE LEU LEU LYS GLU PHE VAL GLU PHE PHE ARG LYS
SEQRES   5 B 1054  CYS VAL GLY GLU PRO ARG ALA ILE GLN LYS MET TRP ALA
SEQRES   6 B 1054  LYS ARG ILE LEU ARG LYS GLU SER PHE ALA ALA THR ALA
SEQRES   7 B 1054  PRO THR GLY VAL GLY LYS THR SER PHE GLY LEU ALA MET
SEQRES   8 B 1054  SER LEU PHE LEU ALA LEU LYS GLY LYS ARG CYS TYR VAL
SEQRES   9 B 1054  ILE PHE PRO THR SER LEU LEU VAL ILE GLN ALA ALA GLU
SEQRES  10 B 1054  THR ILE ARG LYS TYR ALA GLU LYS ALA GLY VAL GLY THR
SEQRES  11 B 1054  GLU ASN LEU ILE GLY TYR TYR HIS GLY ARG ILE PRO LYS
SEQRES  12 B 1054  ARG GLU LYS GLU ASN PHE MET GLN ASN LEU ARG ASN PHE
SEQRES  13 B 1054  LYS ILE VAL ILE THR THR THR GLN PHE LEU SER LYS HIS
SEQRES  14 B 1054  TYR ARG GLU LEU GLY HIS PHE ASP PHE ILE PHE VAL ASP
SEQRES  15 B 1054  ASP VAL ASP ALA ILE LEU LYS ALA SER LYS ASN VAL ASP
SEQRES  16 B 1054  LYS LEU LEU HIS LEU LEU GLY PHE HIS TYR ASP LEU LYS
SEQRES  17 B 1054  THR LYS SER TRP VAL GLY GLU ALA ARG GLY CYS LEU MET
SEQRES  18 B 1054  VAL SER THR ALA THR ALA LYS LYS GLY LYS LYS ALA GLU
SEQRES  19 B 1054  LEU PHE ARG GLN LEU LEU ASN PHE ASP ILE GLY SER SER
SEQRES  20 B 1054  ARG ILE THR VAL ARG ASN VAL GLU ASP VAL ALA VAL ASN
SEQRES  21 B 1054  ASP GLU SER ILE SER THR LEU SER SER ILE LEU GLU LYS
SEQRES  22 B 1054  LEU GLY THR GLY GLY ILE ILE TYR ALA ARG THR GLY GLU
SEQRES  23 B 1054  GLU ALA GLU GLU ILE TYR GLU SER LEU LYS ASN LYS PHE
SEQRES  24 B 1054  ARG ILE GLY ILE VAL THR ALA THR LYS LYS GLY ASP TYR
SEQRES  25 B 1054  GLU LYS PHE VAL GLU GLY GLU ILE ASP HIS LEU ILE GLY
SEQRES  26 B 1054  THR ALA HIS TYR TYR GLY THR LEU VAL ARG GLY LEU ASP
SEQRES  27 B 1054  LEU PRO GLU ARG ILE ARG PHE ALA VAL PHE VAL GLY CYS
SEQRES  28 B 1054  PRO SER PHE ARG VAL THR ILE GLU ASP ILE ASP SER LEU
SEQRES  29 B 1054  SER PRO GLN MET VAL LYS LEU LEU ALA TYR LEU TYR ARG
SEQRES  30 B 1054  ASN VAL ASP GLU ILE GLU ARG LEU LEU PRO ALA VAL GLU
SEQRES  31 B 1054  ARG HIS ILE ASP GLU VAL ARG GLU ILE LEU LYS LYS VAL
SEQRES  32 B 1054  MET GLY LYS GLU ARG PRO GLN ALA LYS ASP VAL VAL VAL
SEQRES  33 B 1054  ARG GLU GLY GLU VAL ILE PHE PRO ASP LEU ARG THR TYR
SEQRES  34 B 1054  ILE GLN GLY SER GLY ARG THR SER ARG LEU PHE ALA GLY
SEQRES  35 B 1054  GLY LEU THR LYS GLY ALA SER PHE LEU LEU GLU ASP ASP
SEQRES  36 B 1054  SER GLU LEU LEU SER ALA PHE ILE GLU ARG ALA LYS LEU
SEQRES  37 B 1054  TYR ASP ILE GLU PHE LYS SER ILE ASP GLU VAL ASP PHE
SEQRES  38 B 1054  GLU LYS LEU SER ARG GLU LEU ASP GLU SER ARG ASP ARG
SEQRES  39 B 1054  TYR ARG ARG ARG GLN GLU PHE ASP LEU ILE LYS PRO ALA
SEQRES  40 B 1054  LEU PHE ILE VAL GLU SER PRO THR LYS ALA ARG GLN ILE
SEQRES  41 B 1054  SER ARG PHE PHE GLY LYS PRO SER VAL LYS VAL LEU ASP
SEQRES  42 B 1054  GLY ALA VAL VAL TYR GLU ILE PRO MET GLN LYS TYR VAL
SEQRES  43 B 1054  LEU MET VAL THR ALA SER ILE GLY HIS VAL VAL ASP LEU
SEQRES  44 B 1054  ILE THR ASN ARG GLY PHE HIS GLY VAL LEU VAL ASN GLY
SEQRES  45 B 1054  ARG PHE VAL PRO VAL TYR ALA SER ILE LYS ARG CYS ARG
SEQRES  46 B 1054  ASP CYS GLY TYR GLN PHE THR GLU ASP ARG GLU SER CYS
SEQRES  47 B 1054  PRO LYS CYS GLY SER GLU ASN VAL ASP ASN SER ARG SER
SEQRES  48 B 1054  ARG ILE GLU ALA LEU ARG LYS LEU ALA HIS ASP ALA GLU
SEQRES  49 B 1054  PHE VAL ILE VAL GLY THR ASP PRO ASP THR GLU GLY GLU
SEQRES  50 B 1054  LYS ILE ALA TRP ASP LEU LYS ASN LEU LEU SER GLY CYS
SEQRES  51 B 1054  GLY ALA VAL LYS ARG ALA GLU PHE HIS GLU VAL THR ARG
SEQRES  52 B 1054  ARG ALA ILE LEU GLU ALA LEU GLU SER LEU ARG ASP VAL
SEQRES  53 B 1054  ASP GLU ASN LEU VAL LYS ALA GLN VAL VAL ARG ARG ILE
SEQRES  54 B 1054  GLU ASP ARG TRP ILE GLY PHE VAL LEU SER GLN LYS LEU
SEQRES  55 B 1054  TRP GLU ARG PHE ASN ASN ARG ASN LEU SER ALA GLY ARG
SEQRES  56 B 1054  ALA GLN THR LEU VAL LEU GLY TRP ILE ILE ASP ARG PHE
SEQRES  57 B 1054  GLN GLU SER ARG GLU ARG ARG LYS ILE ALA ILE VAL ARG
SEQRES  58 B 1054  ASP PHE ASP LEU VAL LEU GLU HIS ASP GLU GLU GLU PHE
SEQRES  59 B 1054  ASP LEU THR ILE LYS LEU VAL GLU GLU ARG GLU GLU LEU
SEQRES  60 B 1054  ARG THR PRO LEU PRO PRO TYR THR THR GLU THR MET LEU
SEQRES  61 B 1054  SER ASP ALA ASN ARG ILE LEU LYS PHE SER VAL LYS GLN
SEQRES  62 B 1054  THR MET GLN ILE ALA GLN GLU LEU PHE GLU ASN GLY LEU
SEQRES  63 B 1054  ILE THR TYR HIS ARG THR ASP SER THR ARG VAL SER ASP
SEQRES  64 B 1054  VAL GLY GLN ARG ILE ALA LYS GLU TYR LEU GLY ASP ASP
SEQRES  65 B 1054  PHE VAL GLY ARG GLU TRP GLY GLU SER GLY ALA HIS GLU
SEQRES  66 B 1054  CYS ILE ARG PRO THR ARG PRO LEU THR ARG ASP ASP VAL
SEQRES  67 B 1054  GLN ARG LEU ILE GLN GLU GLY VAL LEU VAL VAL GLU GLY
SEQRES  68 B 1054  LEU ARG TRP GLU HIS PHE ALA LEU TYR ASP LEU ILE PHE
SEQRES  69 B 1054  ARG ARG PHE MET ALA SER GLN CYS ARG PRO PHE LYS VAL
SEQRES  70 B 1054  VAL VAL LYS LYS TYR SER ILE GLU PHE ASP GLY LYS THR
SEQRES  71 B 1054  ALA GLU GLU GLU ARG ILE VAL ARG ALA GLU GLY ARG ALA
SEQRES  72 B 1054  TYR GLU LEU TYR ARG ALA VAL TRP VAL LYS ASN GLU LEU
SEQRES  73 B 1054  PRO THR GLY THR PHE ARG VAL LYS ALA GLU VAL LYS SER
SEQRES  74 B 1054  VAL PRO LYS VAL LEU PRO PHE THR GLN SER GLU ILE ILE
SEQRES  75 B 1054  GLN MET MET LYS GLU ARG GLY ILE GLY ARG PRO SER THR
SEQRES  76 B 1054  TYR ALA THR ILE VAL ASP ARG LEU PHE MET ARG ASN TYR
SEQRES  77 B 1054  VAL VAL GLU LYS TYR GLY ARG MET ILE PRO THR LYS LEU
SEQRES  78 B 1054  GLY ILE ASP VAL PHE ARG PHE LEU VAL ARG ARG TYR ALA
SEQRES  79 B 1054  LYS PHE VAL SER GLU ASP ARG THR ARG ASP LEU GLU SER
SEQRES  80 B 1054  ARG MET ASP ALA ILE GLU ARG GLY GLU LEU ASP TYR LEU
SEQRES  81 B 1054  LYS ALA LEU GLU ASP MET TYR ALA GLU ILE LYS SER ILE
SEQRES  82 B 1054  ASP
FORMUL   2  HOH   *157(H2 O1)
HELIX    1   1 GLU B   39  LYS B   52  1                                  14
HELIX    2   2 ARG B   58  ARG B   70  1                                  13
HELIX    3   3 LYS B   84  LEU B   97  1                                  14
HELIX    4   4 THR B  108  GLU B  124  1                                  17
HELIX    5   5 GLY B  129  ASN B  132  5                                   4
HELIX    6   6 LYS B  143  ASN B  152  1                                  10
HELIX    7   7 LEU B  153  PHE B  156  5                                   4
HELIX    8   8 THR B  163  HIS B  169  1                                   7
HELIX    9   9 ASP B  183  LYS B  189  1                                   7
HELIX   10  10 SER B  191  LEU B  201  1                                  11
HELIX   11  11 LYS B  232  ASN B  241  1                                  10
HELIX   12  12 LEU B  267  GLU B  272  1                                   6
HELIX   13  13 THR B  284  SER B  294  1                                  11
HELIX   14  14 LYS B  309  GLU B  317  1                                   9
HELIX   15  15 ASP B  360  LEU B  364  5                                   5
HELIX   16  16 SER B  365  TYR B  374  1                                  10
HELIX   17  17 ASN B  378  ARG B  384  1                                   7
HELIX   18  18 HIS B  392  GLY B  405  1                                  14
HELIX   19  19 ASP B  425  ARG B  435  1                                  11
HELIX   20  20 ASP B  455  LEU B  468  1                                  14
HELIX   21  21 ASP B  480  ARG B  497  1                                  18
HELIX   22  22 ARG B  498  PHE B  501  5                                   4
HELIX   23  23 SER B  513  ARG B  522  1                                  10
HELIX   24  24 ASN B  608  GLU B  624  1                                  17
HELIX   25  25 ASP B  633  SER B  648  1                                  16
HELIX   26  26 THR B  662  GLU B  671  1                                  10
HELIX   27  27 ASP B  677  ARG B  705  1                                  29
HELIX   28  28 ALA B  716  GLN B  729  1                                  14
HELIX   29  29 GLU B  730  ARG B  732  5                                   3
HELIX   30  30 THR B  775  ILE B  786  1                                  12
HELIX   31  31 SER B  790  ASN B  804  1                                  15
HELIX   32  32 SER B  818  GLY B  830  1                                  13
HELIX   33  33 THR B  854  GLY B  865  1                                  12
HELIX   34  34 ARG B  873  SER B  890  1                                  18
HELIX   35  35 GLY B  921  TYR B  927  1                                   7
HELIX   36  36 THR B  957  GLY B  969  1                                  13
HELIX   37  37 THR B  975  ARG B  986  1                                  12
HELIX   38  38 THR B  999  ARG B 1012  1                                  14
HELIX   39  39 ALA B 1014  VAL B 1017  5                                   4
HELIX   40  40 SER B 1018  GLY B 1035  1                                  18
HELIX   41  41 ASP B 1038  SER B 1052  1                                  15
SHEET    1  BA 4 ALA B  10  ALA B  11  0
SHEET    2  BA 4 ALA B  18  ALA B  19  1  N  ALA B  19   O  ALA B  10
SHEET    3  BA 4 VAL B 577  SER B 580 -1  O  TYR B 578   N  ALA B  18
SHEET    4  BA 4 VAL B 557  LEU B 559 -1  O  ASP B 558   N  ALA B 579
SHEET    1  BB 6 PHE B  74  ALA B  75  0
SHEET    2  BB 6 CYS B 219  VAL B 222  1  O  LEU B 220   N  PHE B  74
SHEET    3  BB 6 PHE B 178  VAL B 181  1  O  ILE B 179   N  MET B 221
SHEET    4  BB 6 CYS B 102  PHE B 106  1  O  TYR B 103   N  PHE B 180
SHEET    5  BB 6 ILE B 158  THR B 162  1  O  VAL B 159   N  VAL B 104
SHEET    6  BB 6 ILE B 134  TYR B 136  1  O  GLY B 135   N  ILE B 160
SHEET    1  BC 2 PHE B 203  ASP B 206  0
SHEET    2  BC 2 SER B 211  GLY B 214 -1  O  SER B 211   N  ASP B 206
SHEET    1  BD 2 ARG B 248  ILE B 249  0
SHEET    2  BD 2 GLY B 525  LYS B 526 -1  O  LYS B 526   N  ARG B 248
SHEET    1  BE 6 VAL B 254  VAL B 259  0
SHEET    2  BE 6 GLY B 447  LEU B 452  1  O  GLY B 447   N  GLU B 255
SHEET    3  BE 6 PHE B 345  VAL B 349  1  O  ALA B 346   N  PHE B 450
SHEET    4  BE 6 GLY B 278  ALA B 282  1  O  ILE B 279   N  VAL B 347
SHEET    5  BE 6 HIS B 322  THR B 326  1  O  LEU B 323   N  ILE B 280
SHEET    6  BE 6 ILE B 301  ILE B 303  1  O  GLY B 302   N  ILE B 324
SHEET    1  BF 3 SER B 353  THR B 357  0
SHEET    2  BF 3 GLU B 420  PRO B 424 -1  O  VAL B 421   N  VAL B 356
SHEET    3  BF 3 VAL B 415  ARG B 417 -1  O  VAL B 415   N  ILE B 422
SHEET    1  BG 2 LEU B 439  PHE B 440  0
SHEET    2  BG 2 GLY B 443  LEU B 444 -1  O  GLY B 443   N  PHE B 440
SHEET    1  BH 6 SER B 528  LEU B 532  0
SHEET    2  BH 6 ALA B 535  PRO B 541 -1  O  ALA B 535   N  LEU B 532
SHEET    3  BH 6 TYR B 545  ALA B 551 -1  O  LEU B 547   N  ILE B 540
SHEET    4  BH 6 LYS B 505  VAL B 511  1  O  LYS B 505   N  VAL B 546
SHEET    5  BH 6 PHE B 625  VAL B 628  1  O  PHE B 625   N  LEU B 508
SHEET    6  BH 6 ALA B 652  ARG B 655  1  O  ALA B 652   N  VAL B 626
SHEET    1  BI 3 LEU B 745  LEU B 747  0
SHEET    2  BI 3 ARG B 734  VAL B 740 -1  O  ALA B 738   N  LEU B 747
SHEET    3  BI 3 LYS B 948  PRO B 951 -1  N  LYS B 948   O  ILE B 737
SHEET    1  BJ 4 LYS B 909  GLU B 913  0
SHEET    2  BJ 4 PHE B 895  PHE B 906 -1  O  TYR B 902   N  GLU B 913
SHEET    3  BJ 4 GLU B 753  ARG B 768 -1  O  THR B 757   N  GLU B 905
SHEET    4  BJ 4 GLY B 939  LYS B 944 -1  O  GLY B 939   N  ILE B 758
SHEET    1  BK 3 LYS B 909  GLU B 913  0
SHEET    2  BK 3 PHE B 895  PHE B 906 -1  O  TYR B 902   N  GLU B 913
SHEET    3  BK 3 ILE B 916  GLU B 920 -1  N  VAL B 917   O  VAL B 898
SHEET    1  BL 2 VAL B 989  LYS B 992  0
SHEET    2  BL 2 ARG B 995  PRO B 998 -1  O  ARG B 995   N  LYS B 992
SSBOND   1 CYS B   35    CYS B  650                          1555   1555  2.03
CRYST1   65.198   67.985  129.728  90.00 104.01  90.00 P 1 21 1      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      0.015338  0.000000  0.003827        0.00000
SCALE2      0.000000  0.014709  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007945        0.00000
      
PROCHECK
Go to PROCHECK summary
 References