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PDBsum entry 1bxc

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Isomerase PDB id
1bxc
Jmol
Contents
Protein chains
387 a.a. *
Waters ×812
* Residue conservation analysis
HEADER    ISOMERASE                               02-OCT-98   1BXC
TITLE     XYLOSE ISOMERASE FROM THERMUS CALDOPHILUS
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: XYLOSE ISOMERASE;
COMPND   3 CHAIN: A, B, C, D;
COMPND   4 SYNONYM: XYLOSE (GLUCOSE) ISOMERASE;
COMPND   5 EC: 5.3.1.5;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: THERMUS CALDOPHILUS;
SOURCE   3 ORGANISM_TAXID: 272;
SOURCE   4 STRAIN: GK24;
SOURCE   5 GENE: XYLA;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PUC18
KEYWDS    ISOMERASE, XYLOSE METABOLISM
EXPDTA    X-RAY DIFFRACTION
AUTHOR    C.CHANG,B.C.PARK,D.-S.LEE,S.W.SUH
REVDAT   5   24-FEB-09 1BXC    1       VERSN
REVDAT   4   01-APR-03 1BXC    1       JRNL
REVDAT   3   02-DEC-99 1BXC    1       JRNL   REMARK
REVDAT   2   27-APR-99 1BXC    3       COMPND REMARK DBREF  SEQADV
REVDAT   2 2                   3       CRYST1 ATOM   SOURCE SEQRES
REVDAT   1   16-FEB-99 1BXC    0
JRNL        AUTH   C.CHANG,B.C.PARK,D.S.LEE,S.W.SUH
JRNL        TITL   CRYSTAL STRUCTURES OF THERMOSTABLE XYLOSE
JRNL        TITL 2 ISOMERASES FROM THERMUS CALDOPHILUS AND THERMUS
JRNL        TITL 3 THERMOPHILUS: POSSIBLE STRUCTURAL DETERMINANTS OF
JRNL        TITL 4 THERMOSTABILITY.
JRNL        REF    J.MOL.BIOL.                   V. 288   623 1999
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   10329168
JRNL        DOI    10.1006/JMBI.1999.2696
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000000.000
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 76.3
REMARK   3   NUMBER OF REFLECTIONS             : 48891
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) : 0.178
REMARK   3   FREE R VALUE                     : 0.264
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL
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) : 2.30
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.40
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3413
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2684
REMARK   3   BIN FREE R VALUE                    : 0.3923
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            : 13212
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 812
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) : 0.28
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) : 1.00
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.65
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.77
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 : RESTRAINTS
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  : PARHCSDX.PRO
REMARK   3  PARAMETER FILE  2  : NULL
REMARK   3  PARAMETER FILE  3  : NULL
REMARK   3  TOPOLOGY FILE  1   : TOPH19X.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 1BXC 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        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 287
REMARK 200  PH                             : 5.95
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY
REMARK 200  BEAMLINE                       : BL-6A
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : FUJI
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : WEIS
REMARK 200  DATA SCALING SOFTWARE          : CCP4
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 68336
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300
REMARK 200  RESOLUTION RANGE LOW       (A) : 8.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 76.0
REMARK 200  DATA REDUNDANCY                : 3.050
REMARK 200  R MERGE                    (I) : 0.10000
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: PDB ENTRY 5XIN
REMARK 200
REMARK 200 REMARK: DATA WERE COLLECTED USING THE WEISSENBERG METHOD
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 41.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 5.95
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       42.17500
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       70.12000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       61.80000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       70.12000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       42.17500
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       61.80000
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 30300 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 47590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -120.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 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     GLN A  65    CG   CD   OE1  NE2
REMARK 470     GLN B  65    CG   CD   OE1  NE2
REMARK 470     GLN C  65    CG   CD   OE1  NE2
REMARK 470     GLN D  65    CG   CD   OE1  NE2
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   N    ARG B   367     O    HOH A   568     1455     2.11
REMARK 500   O    ALA B   363     O    HOH A   568     1455     2.11
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    PRO A 137       54.90    -91.44
REMARK 500    GLU A 185      116.34     65.88
REMARK 500    ARG A 207       69.45   -116.56
REMARK 500    ASN A 214       78.20   -118.81
REMARK 500    ASN A 246     -168.11   -175.01
REMARK 500    PHE A 253      157.08    -43.95
REMARK 500    GLN A 334      119.07    -34.40
REMARK 500    ASP A 344     -156.87     69.44
REMARK 500    GLU B 185      115.39     67.94
REMARK 500    ARG B 207       69.13   -116.02
REMARK 500    ASN B 214       77.30   -117.96
REMARK 500    ASN B 246     -164.74   -169.50
REMARK 500    GLN B 248      135.94   -170.72
REMARK 500    ASN B 251       47.97     70.40
REMARK 500    PHE B 253      155.95    -41.22
REMARK 500    GLU B 262      -50.49   -120.92
REMARK 500    ASN B 263       79.90   -110.57
REMARK 500    GLN B 334      119.78    -34.13
REMARK 500    ASP B 344     -155.49     70.11
REMARK 500    GLU C 185      115.89     66.80
REMARK 500    ARG C 207       71.38   -115.98
REMARK 500    ASN C 214       79.93   -119.48
REMARK 500    ASN C 246     -166.86   -170.88
REMARK 500    PHE C 253      158.79    -47.66
REMARK 500    GLU C 262      -51.50   -120.99
REMARK 500    GLN C 334      117.53    -32.07
REMARK 500    ASP C 344     -156.27     68.89
REMARK 500    GLU D 185      116.44     67.77
REMARK 500    ARG D 207       69.20   -116.48
REMARK 500    ASN D 214       79.09   -118.47
REMARK 500    HIS D 242      148.77   -170.69
REMARK 500    ASN D 246     -166.41   -172.64
REMARK 500    GLN D 248      135.90   -170.68
REMARK 500    PHE D 253      159.39    -46.30
REMARK 500    ASN D 263       79.98   -110.03
REMARK 500    GLN D 334      117.19    -30.68
REMARK 500    ASP D 344     -156.76     68.72
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        RMS     TYPE
REMARK 500    PHE A 115         0.09    SIDE_CHAIN
REMARK 500    ARG A 258         0.12    SIDE_CHAIN
REMARK 500    PHE B 115         0.09    SIDE_CHAIN
REMARK 500    TYR B 191         0.06    SIDE_CHAIN
REMARK 500    ARG B 258         0.12    SIDE_CHAIN
REMARK 500    PHE C 115         0.10    SIDE_CHAIN
REMARK 500    ARG C 187         0.07    SIDE_CHAIN
REMARK 500    ARG C 258         0.11    SIDE_CHAIN
REMARK 500    PHE D 115         0.09    SIDE_CHAIN
REMARK 500    ARG D 258         0.12    SIDE_CHAIN
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 D 516        DISTANCE = 12.65 ANGSTROMS
REMARK 525    HOH A 526        DISTANCE = 23.17 ANGSTROMS
REMARK 525    HOH A 533        DISTANCE = 18.44 ANGSTROMS
REMARK 525    HOH A 535        DISTANCE = 22.82 ANGSTROMS
REMARK 525    HOH D 536        DISTANCE =  8.16 ANGSTROMS
REMARK 525    HOH C 535        DISTANCE = 10.63 ANGSTROMS
REMARK 525    HOH A 544        DISTANCE = 12.38 ANGSTROMS
REMARK 525    HOH C 538        DISTANCE =  7.96 ANGSTROMS
REMARK 525    HOH A 548        DISTANCE = 13.67 ANGSTROMS
REMARK 525    HOH A 550        DISTANCE = 16.19 ANGSTROMS
REMARK 525    HOH C 544        DISTANCE = 12.73 ANGSTROMS
REMARK 525    HOH A 552        DISTANCE = 10.70 ANGSTROMS
REMARK 525    HOH B 546        DISTANCE = 23.19 ANGSTROMS
REMARK 525    HOH A 558        DISTANCE = 15.33 ANGSTROMS
REMARK 525    HOH A 560        DISTANCE = 24.28 ANGSTROMS
REMARK 525    HOH A 561        DISTANCE = 23.39 ANGSTROMS
REMARK 525    HOH C 554        DISTANCE =  6.71 ANGSTROMS
REMARK 525    HOH B 553        DISTANCE = 18.49 ANGSTROMS
REMARK 525    HOH B 555        DISTANCE = 22.72 ANGSTROMS
REMARK 525    HOH A 568        DISTANCE = 18.42 ANGSTROMS
REMARK 525    HOH B 564        DISTANCE = 12.31 ANGSTROMS
REMARK 525    HOH C 567        DISTANCE = 12.49 ANGSTROMS
REMARK 525    HOH A 575        DISTANCE = 12.07 ANGSTROMS
REMARK 525    HOH A 577        DISTANCE = 13.59 ANGSTROMS
REMARK 525    HOH B 568        DISTANCE = 13.70 ANGSTROMS
REMARK 525    HOH B 570        DISTANCE = 16.32 ANGSTROMS
REMARK 525    HOH B 572        DISTANCE = 10.70 ANGSTROMS
REMARK 525    HOH B 577        DISTANCE = 15.38 ANGSTROMS
REMARK 525    HOH B 579        DISTANCE = 24.21 ANGSTROMS
REMARK 525    HOH B 580        DISTANCE = 23.60 ANGSTROMS
REMARK 525    HOH D 588        DISTANCE = 10.49 ANGSTROMS
REMARK 525    HOH C 587        DISTANCE =  8.20 ANGSTROMS
REMARK 525    HOH D 591        DISTANCE =  7.90 ANGSTROMS
REMARK 525    HOH B 587        DISTANCE = 18.46 ANGSTROMS
REMARK 525    HOH D 597        DISTANCE = 12.66 ANGSTROMS
REMARK 525    HOH B 594        DISTANCE = 12.15 ANGSTROMS
REMARK 525    HOH B 596        DISTANCE = 13.55 ANGSTROMS
REMARK 525    HOH D 607        DISTANCE =  6.73 ANGSTROMS
REMARK 525    HOH B 611        DISTANCE = 12.39 ANGSTROMS
REMARK 525    HOH C 621        DISTANCE = 23.15 ANGSTROMS
REMARK 525    HOH C 628        DISTANCE = 18.53 ANGSTROMS
REMARK 525    HOH C 630        DISTANCE = 22.75 ANGSTROMS
REMARK 525    HOH B 630        DISTANCE =  7.91 ANGSTROMS
REMARK 525    HOH A 643        DISTANCE = 10.62 ANGSTROMS
REMARK 525    HOH A 646        DISTANCE =  7.96 ANGSTROMS
REMARK 525    HOH C 639        DISTANCE = 12.34 ANGSTROMS
REMARK 525    HOH C 643        DISTANCE = 13.70 ANGSTROMS
REMARK 525    HOH A 652        DISTANCE = 12.56 ANGSTROMS
REMARK 525    HOH C 645        DISTANCE = 16.35 ANGSTROMS
REMARK 525    HOH C 647        DISTANCE = 10.73 ANGSTROMS
REMARK 525    HOH C 652        DISTANCE = 15.53 ANGSTROMS
REMARK 525    HOH D 655        DISTANCE = 23.17 ANGSTROMS
REMARK 525    HOH C 654        DISTANCE = 24.28 ANGSTROMS
REMARK 525    HOH A 662        DISTANCE =  6.68 ANGSTROMS
REMARK 525    HOH C 655        DISTANCE = 23.53 ANGSTROMS
REMARK 525    HOH D 662        DISTANCE = 18.49 ANGSTROMS
REMARK 525    HOH D 664        DISTANCE = 22.77 ANGSTROMS
REMARK 525    HOH C 662        DISTANCE = 18.43 ANGSTROMS
REMARK 525    HOH A 675        DISTANCE = 12.52 ANGSTROMS
REMARK 525    HOH C 669        DISTANCE = 12.12 ANGSTROMS
REMARK 525    HOH D 673        DISTANCE = 12.31 ANGSTROMS
REMARK 525    HOH C 671        DISTANCE = 13.70 ANGSTROMS
REMARK 525    HOH D 677        DISTANCE = 13.66 ANGSTROMS
REMARK 525    HOH D 679        DISTANCE = 16.45 ANGSTROMS
REMARK 525    HOH D 681        DISTANCE = 10.74 ANGSTROMS
REMARK 525    HOH D 686        DISTANCE = 15.42 ANGSTROMS
REMARK 525    HOH B 682        DISTANCE = 10.61 ANGSTROMS
REMARK 525    HOH D 688        DISTANCE = 24.28 ANGSTROMS
REMARK 525    HOH D 689        DISTANCE = 23.44 ANGSTROMS
REMARK 525    HOH A 695        DISTANCE =  8.00 ANGSTROMS
REMARK 525    HOH B 685        DISTANCE =  7.92 ANGSTROMS
REMARK 525    HOH D 696        DISTANCE = 18.39 ANGSTROMS
REMARK 525    HOH B 691        DISTANCE = 12.68 ANGSTROMS
REMARK 525    HOH D 703        DISTANCE = 12.09 ANGSTROMS
REMARK 525    HOH D 705        DISTANCE = 13.62 ANGSTROMS
REMARK 525    HOH B 701        DISTANCE =  6.69 ANGSTROMS
DBREF  1BXC A    1   387  UNP    P56681   XYLA_THECA       1    387
DBREF  1BXC B    1   387  UNP    P56681   XYLA_THECA       1    387
DBREF  1BXC C    1   387  UNP    P56681   XYLA_THECA       1    387
DBREF  1BXC D    1   387  UNP    P56681   XYLA_THECA       1    387
SEQADV 1BXC GLN A   65  UNP  P56681    ALA    65 CONFLICT
SEQADV 1BXC GLN B   65  UNP  P56681    ALA    65 CONFLICT
SEQADV 1BXC GLN C   65  UNP  P56681    ALA    65 CONFLICT
SEQADV 1BXC GLN D   65  UNP  P56681    ALA    65 CONFLICT
SEQRES   1 A  387  MET TYR GLU PRO LYS PRO GLU HIS ARG PHE THR PHE GLY
SEQRES   2 A  387  LEU TRP THR VAL GLY ASN VAL GLY ARG ASP PRO PHE GLY
SEQRES   3 A  387  ASP ALA VAL ARG GLU ARG LEU ASP PRO VAL TYR VAL GLY
SEQRES   4 A  387  HIS LYS LEU ALA GLU LEU GLY VAL HIS GLY VAL ASN LEU
SEQRES   5 A  387  HIS ASP GLU ASP LEU ILE PRO ARG GLY THR PRO PRO GLN
SEQRES   6 A  387  GLU ARG ASP GLN ILE VAL ARG ARG PHE LYS ARG ALA LEU
SEQRES   7 A  387  ASP GLU THR GLY LEU LYS VAL PRO MET VAL THR GLY ASN
SEQRES   8 A  387  LEU PHE SER ASP PRO GLY PHE LYS ASP GLY GLY PHE THR
SEQRES   9 A  387  SER ARG ASP PRO TRP VAL ARG ALA TYR ALA PHE ARG LYS
SEQRES  10 A  387  SER LEU GLU THR MET ASP LEU GLY ALA GLU LEU GLY ALA
SEQRES  11 A  387  GLU ILE TYR VAL VAL TRP PRO GLY ARG GLU GLY ALA GLU
SEQRES  12 A  387  VAL GLU ALA THR GLY LYS ALA ARG LYS VAL TRP ASP TRP
SEQRES  13 A  387  VAL ARG GLU PRO LEU ASN PHE MET ALA ALA TYR ALA GLU
SEQRES  14 A  387  ASP GLN GLY TYR GLY TYR ARG PHE ALA LEU GLU PRO LYS
SEQRES  15 A  387  PRO ASN GLU PRO ARG GLY ASP ILE TYR PHE ALA THR VAL
SEQRES  16 A  387  GLY SER MET LEU ALA LEU ILE HIS THR LEU GLU ARG PRO
SEQRES  17 A  387  GLU ARG PHE GLY LEU ASN PRO GLU PHE ALA HIS GLU THR
SEQRES  18 A  387  MET ALA GLY LEU ASN PHE VAL HIS ALA VAL ALA GLN ALA
SEQRES  19 A  387  LEU ASP ALA GLY LYS LEU LEU HIS ILE ASP LEU ASN GLY
SEQRES  20 A  387  GLN ARG MET ASN ARG PHE ASP GLN ASP LEU ARG PHE GLY
SEQRES  21 A  387  SER GLU ASN LEU LYS ALA ALA PHE LEU LEU VAL ASP LEU
SEQRES  22 A  387  LEU GLU SER SER GLY TYR GLN GLY PRO ARG HIS PHE ASP
SEQRES  23 A  387  ALA HIS ALA LEU ARG THR GLU ASP GLU GLU GLY VAL TRP
SEQRES  24 A  387  ALA PHE ALA ARG GLY CYS MET ARG THR TYR LEU ILE LEU
SEQRES  25 A  387  LYS GLU ARG ALA GLU ALA PHE ARG GLU ASP PRO GLU VAL
SEQRES  26 A  387  LYS GLU LEU LEU ALA ALA TYR TYR GLN GLU ASP PRO ALA
SEQRES  27 A  387  ALA LEU PRO LEU MET ASP PRO TYR SER HIS GLU LYS ALA
SEQRES  28 A  387  GLU ALA LEU LYS ARG ALA GLU LEU PRO LEU GLU ALA LYS
SEQRES  29 A  387  ARG HIS ARG GLY TYR ALA LEU GLU ARG LEU ASP GLN LEU
SEQRES  30 A  387  ALA VAL GLU TYR LEU LEU GLY VAL ARG GLY
SEQRES   1 B  387  MET TYR GLU PRO LYS PRO GLU HIS ARG PHE THR PHE GLY
SEQRES   2 B  387  LEU TRP THR VAL GLY ASN VAL GLY ARG ASP PRO PHE GLY
SEQRES   3 B  387  ASP ALA VAL ARG GLU ARG LEU ASP PRO VAL TYR VAL GLY
SEQRES   4 B  387  HIS LYS LEU ALA GLU LEU GLY VAL HIS GLY VAL ASN LEU
SEQRES   5 B  387  HIS ASP GLU ASP LEU ILE PRO ARG GLY THR PRO PRO GLN
SEQRES   6 B  387  GLU ARG ASP GLN ILE VAL ARG ARG PHE LYS ARG ALA LEU
SEQRES   7 B  387  ASP GLU THR GLY LEU LYS VAL PRO MET VAL THR GLY ASN
SEQRES   8 B  387  LEU PHE SER ASP PRO GLY PHE LYS ASP GLY GLY PHE THR
SEQRES   9 B  387  SER ARG ASP PRO TRP VAL ARG ALA TYR ALA PHE ARG LYS
SEQRES  10 B  387  SER LEU GLU THR MET ASP LEU GLY ALA GLU LEU GLY ALA
SEQRES  11 B  387  GLU ILE TYR VAL VAL TRP PRO GLY ARG GLU GLY ALA GLU
SEQRES  12 B  387  VAL GLU ALA THR GLY LYS ALA ARG LYS VAL TRP ASP TRP
SEQRES  13 B  387  VAL ARG GLU PRO LEU ASN PHE MET ALA ALA TYR ALA GLU
SEQRES  14 B  387  ASP GLN GLY TYR GLY TYR ARG PHE ALA LEU GLU PRO LYS
SEQRES  15 B  387  PRO ASN GLU PRO ARG GLY ASP ILE TYR PHE ALA THR VAL
SEQRES  16 B  387  GLY SER MET LEU ALA LEU ILE HIS THR LEU GLU ARG PRO
SEQRES  17 B  387  GLU ARG PHE GLY LEU ASN PRO GLU PHE ALA HIS GLU THR
SEQRES  18 B  387  MET ALA GLY LEU ASN PHE VAL HIS ALA VAL ALA GLN ALA
SEQRES  19 B  387  LEU ASP ALA GLY LYS LEU LEU HIS ILE ASP LEU ASN GLY
SEQRES  20 B  387  GLN ARG MET ASN ARG PHE ASP GLN ASP LEU ARG PHE GLY
SEQRES  21 B  387  SER GLU ASN LEU LYS ALA ALA PHE LEU LEU VAL ASP LEU
SEQRES  22 B  387  LEU GLU SER SER GLY TYR GLN GLY PRO ARG HIS PHE ASP
SEQRES  23 B  387  ALA HIS ALA LEU ARG THR GLU ASP GLU GLU GLY VAL TRP
SEQRES  24 B  387  ALA PHE ALA ARG GLY CYS MET ARG THR TYR LEU ILE LEU
SEQRES  25 B  387  LYS GLU ARG ALA GLU ALA PHE ARG GLU ASP PRO GLU VAL
SEQRES  26 B  387  LYS GLU LEU LEU ALA ALA TYR TYR GLN GLU ASP PRO ALA
SEQRES  27 B  387  ALA LEU PRO LEU MET ASP PRO TYR SER HIS GLU LYS ALA
SEQRES  28 B  387  GLU ALA LEU LYS ARG ALA GLU LEU PRO LEU GLU ALA LYS
SEQRES  29 B  387  ARG HIS ARG GLY TYR ALA LEU GLU ARG LEU ASP GLN LEU
SEQRES  30 B  387  ALA VAL GLU TYR LEU LEU GLY VAL ARG GLY
SEQRES   1 C  387  MET TYR GLU PRO LYS PRO GLU HIS ARG PHE THR PHE GLY
SEQRES   2 C  387  LEU TRP THR VAL GLY ASN VAL GLY ARG ASP PRO PHE GLY
SEQRES   3 C  387  ASP ALA VAL ARG GLU ARG LEU ASP PRO VAL TYR VAL GLY
SEQRES   4 C  387  HIS LYS LEU ALA GLU LEU GLY VAL HIS GLY VAL ASN LEU
SEQRES   5 C  387  HIS ASP GLU ASP LEU ILE PRO ARG GLY THR PRO PRO GLN
SEQRES   6 C  387  GLU ARG ASP GLN ILE VAL ARG ARG PHE LYS ARG ALA LEU
SEQRES   7 C  387  ASP GLU THR GLY LEU LYS VAL PRO MET VAL THR GLY ASN
SEQRES   8 C  387  LEU PHE SER ASP PRO GLY PHE LYS ASP GLY GLY PHE THR
SEQRES   9 C  387  SER ARG ASP PRO TRP VAL ARG ALA TYR ALA PHE ARG LYS
SEQRES  10 C  387  SER LEU GLU THR MET ASP LEU GLY ALA GLU LEU GLY ALA
SEQRES  11 C  387  GLU ILE TYR VAL VAL TRP PRO GLY ARG GLU GLY ALA GLU
SEQRES  12 C  387  VAL GLU ALA THR GLY LYS ALA ARG LYS VAL TRP ASP TRP
SEQRES  13 C  387  VAL ARG GLU PRO LEU ASN PHE MET ALA ALA TYR ALA GLU
SEQRES  14 C  387  ASP GLN GLY TYR GLY TYR ARG PHE ALA LEU GLU PRO LYS
SEQRES  15 C  387  PRO ASN GLU PRO ARG GLY ASP ILE TYR PHE ALA THR VAL
SEQRES  16 C  387  GLY SER MET LEU ALA LEU ILE HIS THR LEU GLU ARG PRO
SEQRES  17 C  387  GLU ARG PHE GLY LEU ASN PRO GLU PHE ALA HIS GLU THR
SEQRES  18 C  387  MET ALA GLY LEU ASN PHE VAL HIS ALA VAL ALA GLN ALA
SEQRES  19 C  387  LEU ASP ALA GLY LYS LEU LEU HIS ILE ASP LEU ASN GLY
SEQRES  20 C  387  GLN ARG MET ASN ARG PHE ASP GLN ASP LEU ARG PHE GLY
SEQRES  21 C  387  SER GLU ASN LEU LYS ALA ALA PHE LEU LEU VAL ASP LEU
SEQRES  22 C  387  LEU GLU SER SER GLY TYR GLN GLY PRO ARG HIS PHE ASP
SEQRES  23 C  387  ALA HIS ALA LEU ARG THR GLU ASP GLU GLU GLY VAL TRP
SEQRES  24 C  387  ALA PHE ALA ARG GLY CYS MET ARG THR TYR LEU ILE LEU
SEQRES  25 C  387  LYS GLU ARG ALA GLU ALA PHE ARG GLU ASP PRO GLU VAL
SEQRES  26 C  387  LYS GLU LEU LEU ALA ALA TYR TYR GLN GLU ASP PRO ALA
SEQRES  27 C  387  ALA LEU PRO LEU MET ASP PRO TYR SER HIS GLU LYS ALA
SEQRES  28 C  387  GLU ALA LEU LYS ARG ALA GLU LEU PRO LEU GLU ALA LYS
SEQRES  29 C  387  ARG HIS ARG GLY TYR ALA LEU GLU ARG LEU ASP GLN LEU
SEQRES  30 C  387  ALA VAL GLU TYR LEU LEU GLY VAL ARG GLY
SEQRES   1 D  387  MET TYR GLU PRO LYS PRO GLU HIS ARG PHE THR PHE GLY
SEQRES   2 D  387  LEU TRP THR VAL GLY ASN VAL GLY ARG ASP PRO PHE GLY
SEQRES   3 D  387  ASP ALA VAL ARG GLU ARG LEU ASP PRO VAL TYR VAL GLY
SEQRES   4 D  387  HIS LYS LEU ALA GLU LEU GLY VAL HIS GLY VAL ASN LEU
SEQRES   5 D  387  HIS ASP GLU ASP LEU ILE PRO ARG GLY THR PRO PRO GLN
SEQRES   6 D  387  GLU ARG ASP GLN ILE VAL ARG ARG PHE LYS ARG ALA LEU
SEQRES   7 D  387  ASP GLU THR GLY LEU LYS VAL PRO MET VAL THR GLY ASN
SEQRES   8 D  387  LEU PHE SER ASP PRO GLY PHE LYS ASP GLY GLY PHE THR
SEQRES   9 D  387  SER ARG ASP PRO TRP VAL ARG ALA TYR ALA PHE ARG LYS
SEQRES  10 D  387  SER LEU GLU THR MET ASP LEU GLY ALA GLU LEU GLY ALA
SEQRES  11 D  387  GLU ILE TYR VAL VAL TRP PRO GLY ARG GLU GLY ALA GLU
SEQRES  12 D  387  VAL GLU ALA THR GLY LYS ALA ARG LYS VAL TRP ASP TRP
SEQRES  13 D  387  VAL ARG GLU PRO LEU ASN PHE MET ALA ALA TYR ALA GLU
SEQRES  14 D  387  ASP GLN GLY TYR GLY TYR ARG PHE ALA LEU GLU PRO LYS
SEQRES  15 D  387  PRO ASN GLU PRO ARG GLY ASP ILE TYR PHE ALA THR VAL
SEQRES  16 D  387  GLY SER MET LEU ALA LEU ILE HIS THR LEU GLU ARG PRO
SEQRES  17 D  387  GLU ARG PHE GLY LEU ASN PRO GLU PHE ALA HIS GLU THR
SEQRES  18 D  387  MET ALA GLY LEU ASN PHE VAL HIS ALA VAL ALA GLN ALA
SEQRES  19 D  387  LEU ASP ALA GLY LYS LEU LEU HIS ILE ASP LEU ASN GLY
SEQRES  20 D  387  GLN ARG MET ASN ARG PHE ASP GLN ASP LEU ARG PHE GLY
SEQRES  21 D  387  SER GLU ASN LEU LYS ALA ALA PHE LEU LEU VAL ASP LEU
SEQRES  22 D  387  LEU GLU SER SER GLY TYR GLN GLY PRO ARG HIS PHE ASP
SEQRES  23 D  387  ALA HIS ALA LEU ARG THR GLU ASP GLU GLU GLY VAL TRP
SEQRES  24 D  387  ALA PHE ALA ARG GLY CYS MET ARG THR TYR LEU ILE LEU
SEQRES  25 D  387  LYS GLU ARG ALA GLU ALA PHE ARG GLU ASP PRO GLU VAL
SEQRES  26 D  387  LYS GLU LEU LEU ALA ALA TYR TYR GLN GLU ASP PRO ALA
SEQRES  27 D  387  ALA LEU PRO LEU MET ASP PRO TYR SER HIS GLU LYS ALA
SEQRES  28 D  387  GLU ALA LEU LYS ARG ALA GLU LEU PRO LEU GLU ALA LYS
SEQRES  29 D  387  ARG HIS ARG GLY TYR ALA LEU GLU ARG LEU ASP GLN LEU
SEQRES  30 D  387  ALA VAL GLU TYR LEU LEU GLY VAL ARG GLY
FORMUL   5  HOH   *812(H2 O)
HELIX    1   1 PRO A    6  HIS A    8  5                                   3
HELIX    2   2 LEU A   14  VAL A   17  1                                   4
HELIX    3   3 PRO A   35  LEU A   45  1                                  11
HELIX    4   4 ASP A   54  LEU A   57  1                                   4
HELIX    5   5 PRO A   64  THR A   81  1                                  18
HELIX    6   6 PRO A   96  PHE A   98  5                                   3
HELIX    7   7 PRO A  108  LEU A  128  1                                  21
HELIX    8   8 GLU A  145  THR A  147  5                                   3
HELIX    9   9 LYS A  149  ARG A  151  5                                   3
HELIX   10  10 VAL A  153  GLN A  171  1                                  19
HELIX   11  11 VAL A  195  THR A  204  1                                  10
HELIX   12  12 PRO A  208  ARG A  210  5                                   3
HELIX   13  13 PHE A  217  ALA A  223  1                                   7
HELIX   14  14 PHE A  227  ALA A  237  1                                  11
HELIX   15  15 LEU A  264  SER A  277  1                                  14
HELIX   16  16 GLU A  295  GLU A  321  1                                  27
HELIX   17  17 PRO A  323  TYR A  333  1                                  11
HELIX   18  18 PRO A  337  LEU A  342  1                                   6
HELIX   19  19 HIS A  348  ARG A  356  1                                   9
HELIX   20  20 LEU A  361  ARG A  365  1                                   5
HELIX   21  21 LEU A  371  LEU A  382  1                                  12
HELIX   22  22 PRO B    6  HIS B    8  5                                   3
HELIX   23  23 LEU B   14  VAL B   17  1                                   4
HELIX   24  24 PRO B   35  LEU B   45  1                                  11
HELIX   25  25 ASP B   54  LEU B   57  1                                   4
HELIX   26  26 PRO B   64  THR B   81  1                                  18
HELIX   27  27 PRO B   96  PHE B   98  5                                   3
HELIX   28  28 PRO B  108  LEU B  128  1                                  21
HELIX   29  29 GLU B  145  THR B  147  5                                   3
HELIX   30  30 LYS B  149  ARG B  151  5                                   3
HELIX   31  31 VAL B  153  GLN B  171  1                                  19
HELIX   32  32 VAL B  195  THR B  204  1                                  10
HELIX   33  33 PRO B  208  ARG B  210  5                                   3
HELIX   34  34 PHE B  217  ALA B  223  1                                   7
HELIX   35  35 PHE B  227  ASP B  236  1                                  10
HELIX   36  36 LEU B  264  SER B  277  1                                  14
HELIX   37  37 GLU B  295  GLU B  321  1                                  27
HELIX   38  38 PRO B  323  TYR B  333  1                                  11
HELIX   39  39 PRO B  337  LEU B  340  1                                   4
HELIX   40  40 HIS B  348  ARG B  356  1                                   9
HELIX   41  41 LEU B  361  ARG B  365  1                                   5
HELIX   42  42 LEU B  371  LEU B  382  1                                  12
HELIX   43  43 PRO C    6  HIS C    8  5                                   3
HELIX   44  44 LEU C   14  VAL C   17  1                                   4
HELIX   45  45 PRO C   35  LEU C   45  1                                  11
HELIX   46  46 ASP C   54  LEU C   57  1                                   4
HELIX   47  47 PRO C   64  THR C   81  1                                  18
HELIX   48  48 PRO C   96  PHE C   98  5                                   3
HELIX   49  49 PRO C  108  LEU C  128  1                                  21
HELIX   50  50 GLU C  145  THR C  147  5                                   3
HELIX   51  51 LYS C  149  ARG C  151  5                                   3
HELIX   52  52 VAL C  153  GLN C  171  1                                  19
HELIX   53  53 VAL C  195  THR C  204  1                                  10
HELIX   54  54 PRO C  208  ARG C  210  5                                   3
HELIX   55  55 PHE C  217  ALA C  223  1                                   7
HELIX   56  56 PHE C  227  ASP C  236  1                                  10
HELIX   57  57 LEU C  264  SER C  277  1                                  14
HELIX   58  58 GLU C  295  GLU C  321  1                                  27
HELIX   59  59 PRO C  323  TYR C  333  1                                  11
HELIX   60  60 PRO C  337  LEU C  342  1                                   6
HELIX   61  61 HIS C  348  ARG C  356  1                                   9
HELIX   62  62 LEU C  361  ARG C  365  1                                   5
HELIX   63  63 LEU C  371  LEU C  382  1                                  12
HELIX   64  64 PRO D    6  HIS D    8  5                                   3
HELIX   65  65 LEU D   14  VAL D   17  1                                   4
HELIX   66  66 PRO D   35  LEU D   45  1                                  11
HELIX   67  67 ASP D   54  LEU D   57  1                                   4
HELIX   68  68 PRO D   64  THR D   81  1                                  18
HELIX   69  69 PRO D   96  PHE D   98  5                                   3
HELIX   70  70 PRO D  108  LEU D  128  1                                  21
HELIX   71  71 GLU D  145  THR D  147  5                                   3
HELIX   72  72 LYS D  149  ARG D  151  5                                   3
HELIX   73  73 VAL D  153  GLN D  171  1                                  19
HELIX   74  74 VAL D  195  THR D  204  1                                  10
HELIX   75  75 PRO D  208  ARG D  210  5                                   3
HELIX   76  76 PHE D  217  ALA D  223  1                                   7
HELIX   77  77 PHE D  227  ASP D  236  1                                  10
HELIX   78  78 LEU D  264  SER D  277  1                                  14
HELIX   79  79 GLU D  295  GLU D  321  1                                  27
HELIX   80  80 PRO D  323  TYR D  333  1                                  11
HELIX   81  81 PRO D  337  LEU D  340  1                                   4
HELIX   82  82 HIS D  348  ARG D  356  1                                   9
HELIX   83  83 LEU D  361  ARG D  365  1                                   5
HELIX   84  84 LEU D  371  LEU D  382  1                                  12
SHEET    1   A 2 THR A  11  GLY A  13  0
SHEET    2   A 2 GLY A  49  ASN A  51  1  N  GLY A  49   O  PHE A  12
SHEET    1   B 5 ILE A 132  TRP A 136  0
SHEET    2   B 5 ARG A 176  GLU A 180  1  N  ARG A 176   O  TYR A 133
SHEET    3   B 5 PHE A 211  GLU A 216  1  N  GLY A 212   O  PHE A 177
SHEET    4   B 5 LEU A 240  LEU A 245  1  N  LEU A 241   O  LEU A 213
SHEET    5   B 5 ARG A 283  PHE A 285  1  N  HIS A 284   O  ILE A 243
SHEET    1   C 7 GLY B  49  ASN B  51  0
SHEET    2   C 7 PHE B  10  GLY B  13  1  N  PHE B  12   O  GLY B  49
SHEET    3   C 7 ARG B 283  PHE B 285  1  N  ARG B 283   O  THR B  11
SHEET    4   C 7 LEU B 240  LEU B 245  1  N  ILE B 243   O  HIS B 284
SHEET    5   C 7 PHE B 211  GLU B 216  1  N  LEU B 213   O  LEU B 241
SHEET    6   C 7 ARG B 176  GLU B 180  1  N  PHE B 177   O  GLY B 212
SHEET    7   C 7 ILE B 132  TRP B 136  1  N  TYR B 133   O  ARG B 176
SHEET    1   D 7 GLY C  49  ASN C  51  0
SHEET    2   D 7 PHE C  10  GLY C  13  1  N  PHE C  12   O  GLY C  49
SHEET    3   D 7 ARG C 283  PHE C 285  1  N  ARG C 283   O  THR C  11
SHEET    4   D 7 LEU C 240  LEU C 245  1  N  ILE C 243   O  HIS C 284
SHEET    5   D 7 PHE C 211  GLU C 216  1  N  LEU C 213   O  LEU C 241
SHEET    6   D 7 ARG C 176  GLU C 180  1  N  PHE C 177   O  GLY C 212
SHEET    7   D 7 ILE C 132  TRP C 136  1  N  TYR C 133   O  ARG C 176
SHEET    1   E 7 GLY D  49  ASN D  51  0
SHEET    2   E 7 PHE D  10  GLY D  13  1  N  PHE D  12   O  GLY D  49
SHEET    3   E 7 ARG D 283  PHE D 285  1  N  ARG D 283   O  THR D  11
SHEET    4   E 7 LEU D 240  LEU D 245  1  N  ILE D 243   O  HIS D 284
SHEET    5   E 7 PHE D 211  GLU D 216  1  N  LEU D 213   O  LEU D 241
SHEET    6   E 7 ARG D 176  GLU D 180  1  N  PHE D 177   O  GLY D 212
SHEET    7   E 7 ILE D 132  TRP D 136  1  N  TYR D 133   O  ARG D 176
CISPEP   1 GLU A  185    PRO A  186          0        11.46
CISPEP   2 GLU B  185    PRO B  186          0        12.20
CISPEP   3 GLU C  185    PRO C  186          0        12.15
CISPEP   4 GLU D  185    PRO D  186          0        12.24
CRYST1   84.350  123.600  140.240  90.00  90.00  90.00 P 21 21 21   16
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      0.011855  0.000000  0.000000        0.00000
SCALE2      0.000000  0.008091  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007131        0.00000
MTRIX1   1  0.900379 -0.427541 -0.080788      -37.13510    1
MTRIX2   1 -0.427630 -0.903793  0.017067     -237.11189    1
MTRIX3   1 -0.080313  0.019181 -0.996585      382.18439    1
MTRIX1   2 -0.951423  0.168886  0.257432      -13.13420    1
MTRIX2   2  0.170477 -0.407285  0.897249     -346.95200    1
MTRIX3   2  0.256382  0.897550  0.358709      231.63060    1
MTRIX1   3 -0.949684  0.257794 -0.177883       80.60450    1
MTRIX2   3  0.255996  0.311649 -0.915063       86.11540    1
MTRIX3   3 -0.180461 -0.914558 -0.361963      146.10001    1
      
PROCHECK
Go to PROCHECK summary
 References