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PDBsum entry 1a0d

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Top Page protein metals Protein-protein interface(s) links
Ketolisomerase PDB id
1a0d
Jmol
Contents
Protein chains
437 a.a. *
Metals
_MN ×8
Waters ×240
* Residue conservation analysis
HEADER    KETOLISOMERASE                          28-NOV-97   1A0D
TITLE     XYLOSE ISOMERASE FROM BACILLUS STEAROTHERMOPHILUS
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: XYLOSE ISOMERASE;
COMPND   3 CHAIN: A, B, C, D;
COMPND   4 SYNONYM: GLUCOSE ISOMERASE;
COMPND   5 EC: 5.3.1.5
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: GEOBACILLUS STEAROTHERMOPHILUS;
SOURCE   3 ORGANISM_TAXID: 1422;
SOURCE   4 STRAIN: LLD-R;
SOURCE   5 CELLULAR_LOCATION: CYTOPLASM
KEYWDS    KETOLISOMERASE, XYLOSE METABOLISM, GLUCOSE-FRUCTOSE
KEYWDS   2 INTERCONVERSION, HYDRIDE TRANSFER, ALPHA-BETA BARREL,
KEYWDS   3 METALLOENZYME, THERMOPHILE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    O.GALLAY,R.CHOPRA,E.CONTI,P.BRICK,D.BLOW
REVDAT   2   24-FEB-09 1A0D    1       VERSN
REVDAT   1   03-JUN-98 1A0D    0
JRNL        AUTH   O.GALLAY,R.CHOPRA,E.CONTI,P.BRICK,R.JACKSON,
JRNL        AUTH 2 B.HARTLEY,C.VIEILLE,J.G.ZEIKUS,D.BLOW
JRNL        TITL   CRYSTAL STRUCTURES OF CLASS II XYLOSE ISOMERASES
JRNL        TITL 2 FROM TWO THERMOPHILES AND A HYPERTHERMOPHILE
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   L.WUXIANG,K.JEYASEELAN
REMARK   1  TITL   HIGH LEVEL EXPRESSION OF A THERMOSTABLE BACILLUS
REMARK   1  TITL 2 XYLOSE (GLUCOSE) ISOMERASE IN ESCHERICHIA COLI
REMARK   1  REF    BIOTECHNOL.LETT.              V.  15  1101 1993
REMARK   1  REFN                   ISSN 0141-5492
REMARK   2
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.1
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 89.3
REMARK   3   NUMBER OF REFLECTIONS             : 35802
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : A POSTERIORI
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.209
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1775
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005
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) : 3.00
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.14
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 57.90
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2734
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3030
REMARK   3   BIN FREE R VALUE                    : 0.2820
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 124
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.025
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3481
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 2
REMARK   3   SOLVENT ATOMS            : 2
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 49.80
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.10
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) : 0.009
REMARK   3   BOND ANGLES            (DEGREES) : 1.60
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.30
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.26
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  : PARHCSDX.PRO
REMARK   3  PARAMETER FILE  2  : PARAM19.SOL
REMARK   3  PARAMETER FILE  3  : PARAM.ION
REMARK   3  PARAMETER FILE  4  : NULL
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO
REMARK   3  TOPOLOGY FILE  2   : TOPH19.SOL
REMARK   3  TOPOLOGY FILE  3   : TOPH.ION
REMARK   3  TOPOLOGY FILE  4   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS:  OCCUPANCIES OF THE MN CATIONS AND
REMARK   3  WATER HOH 501 WERE REFINED, SIMULTANEOUSLY WITH TEMPERATURE
REMARK   3  FACTORS FOR ALL ATOMS, USING THE GROUP B COMMAND IN X-PLOR.
REMARK   3  THESE OCCUPANCIES WERE THEN FIXED AT ROUNDED VALUES FOR THE
REMARK   3  SUBSEQUENT REFINEMENT PROTOCOL. DISORDERED SIDE CHAINS WERE
REMARK   3  NOT INCLUDED IN REFINEMENT.
REMARK   4
REMARK   4 1A0D 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        : FEB-93
REMARK 200  TEMPERATURE           (KELVIN) : 293
REMARK 200  PH                             : 6.3 - 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          : ELLIOTT GX-21
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : GRAPHITE(002)
REMARK 200  OPTICS                         : DUAL SLITS, COLLIMATOR
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : ENRAF-NONIUS FAST
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MADNES
REMARK 200  DATA SCALING SOFTWARE          : CCP4
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35985
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 33.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.6
REMARK 200  DATA REDUNDANCY                : 1.700
REMARK 200  R MERGE                    (I) : 0.10000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 7.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.16
REMARK 200  COMPLETENESS FOR SHELL     (%) : 62.2
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.50
REMARK 200  R MERGE FOR SHELL          (I) : 0.23000
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: PDB ENTRY 6XIA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 45.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION FROM HANGING DROPS
REMARK 280  (18 DEG C): PROTEIN (A280 22) WAS IN 50 MM TRIS, 10 MM MNCL2,
REMARK 280  PH 7.5; RESERVOIR SOLUTION WAS 10% PEG, 100 MM LICL, 100 MM
REMARK 280  MES, PH 6.3; DROPS WERE FORMED FROM EQUAL PARTS OF PROTEIN AND
REMARK 280  RESERVOIR SOLUTIONS., PH 6.5, VAPOR DIFFUSION - HANGING DROP
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       43.14500
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       80.33000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       70.92500
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       80.33000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       43.14500
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       70.92500
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: 29880 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 54930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -206.0 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 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 A   438
REMARK 465     ALA A   439
REMARK 465     ARG A   440
REMARK 465     ALA B   438
REMARK 465     ALA B   439
REMARK 465     ARG B   440
REMARK 465     ALA C   438
REMARK 465     ALA C   439
REMARK 465     ARG C   440
REMARK 465     ALA D   438
REMARK 465     ALA D   439
REMARK 465     ARG D   440
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     LYS A  17    CG   CD   CE   NZ
REMARK 470     LYS A 110    CG   CD   CE   NZ
REMARK 470     LYS A 114    CG   CD   CE   NZ
REMARK 470     LYS A 365    CG   CD   CE   NZ
REMARK 470     GLU A 414    CG   CD   OE1  OE2
REMARK 470     LYS B  17    CG   CD   CE   NZ
REMARK 470     LYS B 110    CG   CD   CE   NZ
REMARK 470     LYS B 114    CG   CD   CE   NZ
REMARK 470     LYS B 365    CG   CD   CE   NZ
REMARK 470     GLU B 414    CG   CD   OE1  OE2
REMARK 470     LYS C  17    CG   CD   CE   NZ
REMARK 470     LYS C 110    CG   CD   CE   NZ
REMARK 470     LYS C 114    CG   CD   CE   NZ
REMARK 470     LYS C 365    CG   CD   CE   NZ
REMARK 470     GLU C 414    CG   CD   OE1  OE2
REMARK 470     LYS D  17    CG   CD   CE   NZ
REMARK 470     LYS D 110    CG   CD   CE   NZ
REMARK 470     LYS D 114    CG   CD   CE   NZ
REMARK 470     LYS D 365    CG   CD   CE   NZ
REMARK 470     GLU D 414    CG   CD   OE1  OE2
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   CG2  THR B   129     CE   LYS D    69     4455     2.16
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    LEU A  20       55.04   -100.70
REMARK 500    ARG A  41       56.26     36.94
REMARK 500    ASN A  91       44.34     74.56
REMARK 500    TYR A 126      -42.21   -174.26
REMARK 500    LEU A 141       40.19   -108.18
REMARK 500    PHE A 142      -28.25   -141.83
REMARK 500    ALA A 151      -82.10   -115.76
REMARK 500    LYS A 233     -177.37   -172.06
REMARK 500    GLU A 234      108.66     69.12
REMARK 500    ASN A 295     -155.23   -132.68
REMARK 500    LEU B  20       55.04   -100.70
REMARK 500    ARG B  41       56.32     36.83
REMARK 500    ASN B  91       44.39     74.54
REMARK 500    TYR B 126      -42.21   -174.30
REMARK 500    LEU B 141       40.21   -108.17
REMARK 500    PHE B 142      -28.22   -141.85
REMARK 500    ALA B 151      -82.13   -115.75
REMARK 500    LYS B 233     -177.38   -172.07
REMARK 500    GLU B 234      108.69     69.10
REMARK 500    ASN B 295     -155.25   -132.68
REMARK 500    LEU C  20       55.02   -100.69
REMARK 500    ARG C  41       56.20     36.98
REMARK 500    ASN C  91       44.32     74.59
REMARK 500    TYR C 126      -42.21   -174.23
REMARK 500    LEU C 141       40.22   -108.23
REMARK 500    PHE C 142      -28.27   -141.85
REMARK 500    ALA C 151      -82.10   -115.74
REMARK 500    LYS C 233     -177.34   -172.03
REMARK 500    GLU C 234      108.59     69.17
REMARK 500    ASN C 295     -155.20   -132.68
REMARK 500    LEU D  20       55.07   -100.65
REMARK 500    ARG D  41       56.25     36.90
REMARK 500    ASN D  91       44.36     74.50
REMARK 500    TYR D 126      -42.20   -174.23
REMARK 500    LEU D 141       40.27   -108.17
REMARK 500    PHE D 142      -28.25   -141.88
REMARK 500    ALA D 151      -82.07   -115.72
REMARK 500    LYS D 233     -177.42   -172.09
REMARK 500    GLU D 234      108.65     69.12
REMARK 500    ASN D 295     -155.23   -132.64
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                              MN A 491  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 229   OE2
REMARK 620 2 GLU A 265   OE1  80.6
REMARK 620 3 ASP A 336   OD2 162.3  90.1
REMARK 620 4 ASP A 293   OD2  87.2  86.6  77.2
REMARK 620 5 HOH A 538   O   100.8 177.1  89.2  96.0
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN A 492  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 265   OE2
REMARK 620 2 ASP A 304   OD2  90.2
REMARK 620 3 HOH A 544   O   112.4 104.2
REMARK 620 4 ASP A 306   OD1  86.9  74.4 160.7
REMARK 620 5 HOH A 493   O   141.0 127.7  71.2  94.1
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN B 491  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 229   OE2
REMARK 620 2 GLU B 265   OE1  80.6
REMARK 620 3 ASP B 336   OD2 162.2  90.1
REMARK 620 4 ASP B 293   OD2  87.2  86.6  77.1
REMARK 620 5 HOH B 542   O   100.8 177.1  89.2  96.0
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN B 492  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 265   OE2
REMARK 620 2 ASP B 304   OD2  90.2
REMARK 620 3 ASP B 306   OD1  86.9  74.4
REMARK 620 4 HOH B 496   O   141.0 127.7  94.1
REMARK 620 5 HOH B 548   O   112.5 104.2 160.6  71.2
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN C 491  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 229   OE2
REMARK 620 2 GLU C 265   OE1  80.5
REMARK 620 3 ASP C 336   OD2 162.3  90.1
REMARK 620 4 ASP C 293   OD2  87.2  86.6  77.1
REMARK 620 5 HOH C 541   O   100.9 177.1  89.2  96.0
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN C 492  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 265   OE2
REMARK 620 2 ASP C 304   OD2  90.2
REMARK 620 3 HOH C 497   O   141.0 127.7
REMARK 620 4 HOH C 547   O   112.4 104.2  71.3
REMARK 620 5 ASP C 306   OD1  86.9  74.4  94.1 160.7
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN D 491  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 229   OE2
REMARK 620 2 GLU D 265   OE1  80.6
REMARK 620 3 ASP D 336   OD2 162.3  90.1
REMARK 620 4 HOH D 544   O   100.8 177.1  89.2
REMARK 620 5 ASP D 293   OD2  87.2  86.6  77.2  96.0
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN D 492  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 265   OE2
REMARK 620 2 ASP D 304   OD2  90.2
REMARK 620 3 HOH D 499   O   141.0 127.7
REMARK 620 4 HOH D 550   O   112.4 104.2  71.2
REMARK 620 5 ASP D 306   OD1  86.9  74.4  94.1 160.7
REMARK 620 N                    1     2     3     4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: MN1
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: MN BINDING SITE 1 OF MOLECULE A
REMARK 800 SITE_IDENTIFIER: MN2
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: MN BINDING SITE 2 OF MOLECULE A
REMARK 800 SITE_IDENTIFIER: MN3
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: MN BINDING SITE 1 OF MOLECULE B
REMARK 800 SITE_IDENTIFIER: MN4
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: MN BINDING SITE 2 OF MOLECULE B
REMARK 800 SITE_IDENTIFIER: MN5
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: MN BINDING SITE 1 OF MOLECULE C
REMARK 800 SITE_IDENTIFIER: MN6
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: MN BINDING SITE 2 OF MOLECULE C
REMARK 800 SITE_IDENTIFIER: MN7
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: MN BINDING SITE 1 OF MOLECULE D
REMARK 800 SITE_IDENTIFIER: MN8
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: MN BINDING SITE 2 OF MOLECULE D
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 491
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 492
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 491
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 492
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 491
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 492
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN D 491
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN D 492
DBREF  1A0D A    1   440  UNP    P54273   XYLA_BACST       2    441
DBREF  1A0D B    1   440  UNP    P54273   XYLA_BACST       2    441
DBREF  1A0D C    1   440  UNP    P54273   XYLA_BACST       2    441
DBREF  1A0D D    1   440  UNP    P54273   XYLA_BACST       2    441
SEQRES   1 A  440  PRO TYR PHE ASP ASN ILE SER THR ILE ALA TYR GLU GLY
SEQRES   2 A  440  PRO ALA SER LYS ASN PRO LEU ALA PHE LYS PHE TYR ASN
SEQRES   3 A  440  PRO GLU GLU LYS VAL GLY ASP LYS THR MET GLU GLU HIS
SEQRES   4 A  440  LEU ARG PHE SER VAL ALA TYR TRP HIS THR PHE THR GLY
SEQRES   5 A  440  ASP GLY SER ASP PRO PHE GLY ALA GLY ASN MET ILE ARG
SEQRES   6 A  440  PRO TRP ASN LYS TYR SER GLY MET ASP LEU ALA LYS ALA
SEQRES   7 A  440  ARG VAL GLU ALA ALA PHE GLU PHE PHE GLU LYS LEU ASN
SEQRES   8 A  440  ILE PRO PHE PHE CYS PHE HIS ASP VAL ASP ILE ALA PRO
SEQRES   9 A  440  GLU GLY GLU THR LEU LYS GLU THR TYR LYS ASN LEU ASP
SEQRES  10 A  440  ILE ILE VAL ASP MET ILE GLU GLU TYR MET LYS THR SER
SEQRES  11 A  440  LYS THR LYS LEU LEU TRP ASN THR ALA ASN LEU PHE THR
SEQRES  12 A  440  HIS PRO ARG PHE VAL HIS GLY ALA ALA THR SER CYS ASN
SEQRES  13 A  440  ALA ASP VAL PHE ALA TYR ALA ALA ALA LYS VAL LYS LYS
SEQRES  14 A  440  GLY LEU GLU ILE ALA LYS ARG LEU GLY ALA GLU ASN TYR
SEQRES  15 A  440  VAL PHE TRP GLY GLY ARG GLU GLY TYR GLU THR LEU LEU
SEQRES  16 A  440  ASN THR ASP MET LYS LEU GLU LEU ASP ASN LEU ALA ARG
SEQRES  17 A  440  PHE LEU HIS MET ALA VAL ASP TYR ALA LYS GLU ILE GLY
SEQRES  18 A  440  PHE ASP GLY GLN PHE LEU ILE GLU PRO LYS PRO LYS GLU
SEQRES  19 A  440  PRO THR LYS HIS GLN TYR ASP PHE ASP VAL ALA THR ALA
SEQRES  20 A  440  LEU ALA PHE LEU GLN THR TYR GLY LEU LYS ASP TYR PHE
SEQRES  21 A  440  LYS PHE ASN ILE GLU ALA ASN HIS ALA THR LEU ALA GLY
SEQRES  22 A  440  HIS THR PHE GLU HIS GLU LEU ARG VAL ALA ARG ILE HIS
SEQRES  23 A  440  GLY MET LEU GLY SER VAL ASP ALA ASN GLN GLY ASP MET
SEQRES  24 A  440  LEU LEU GLY TRP ASP THR ASP GLU PHE PRO THR ASP LEU
SEQRES  25 A  440  TYR SER THR THR LEU ALA MET TYR GLU ILE LEU LYS ASN
SEQRES  26 A  440  GLY GLY LEU GLY ARG GLY GLY LEU ASN PHE ASP ALA LYS
SEQRES  27 A  440  VAL ARG ARG GLY SER PHE GLU PRO GLU ASP LEU PHE TYR
SEQRES  28 A  440  ALA HIS ILE ALA GLY MET ASP SER PHE ALA VAL GLY LEU
SEQRES  29 A  440  LYS VAL ALA HIS ARG LEU ILE GLU ASP ARG VAL PHE ASP
SEQRES  30 A  440  GLU PHE ILE GLU GLU ARG TYR LYS SER TYR THR GLU GLY
SEQRES  31 A  440  ILE GLY ARG GLU ILE VAL GLU GLY THR ALA ASP PHE HIS
SEQRES  32 A  440  LYS LEU GLU ALA HIS ALA LEU GLN LEU GLY GLU ILE GLN
SEQRES  33 A  440  ASN GLN SER GLY ARG GLN GLU ARG LEU LYS THR LEU LEU
SEQRES  34 A  440  ASN GLN TYR LEU LEU GLU VAL CYS ALA ALA ARG
SEQRES   1 B  440  PRO TYR PHE ASP ASN ILE SER THR ILE ALA TYR GLU GLY
SEQRES   2 B  440  PRO ALA SER LYS ASN PRO LEU ALA PHE LYS PHE TYR ASN
SEQRES   3 B  440  PRO GLU GLU LYS VAL GLY ASP LYS THR MET GLU GLU HIS
SEQRES   4 B  440  LEU ARG PHE SER VAL ALA TYR TRP HIS THR PHE THR GLY
SEQRES   5 B  440  ASP GLY SER ASP PRO PHE GLY ALA GLY ASN MET ILE ARG
SEQRES   6 B  440  PRO TRP ASN LYS TYR SER GLY MET ASP LEU ALA LYS ALA
SEQRES   7 B  440  ARG VAL GLU ALA ALA PHE GLU PHE PHE GLU LYS LEU ASN
SEQRES   8 B  440  ILE PRO PHE PHE CYS PHE HIS ASP VAL ASP ILE ALA PRO
SEQRES   9 B  440  GLU GLY GLU THR LEU LYS GLU THR TYR LYS ASN LEU ASP
SEQRES  10 B  440  ILE ILE VAL ASP MET ILE GLU GLU TYR MET LYS THR SER
SEQRES  11 B  440  LYS THR LYS LEU LEU TRP ASN THR ALA ASN LEU PHE THR
SEQRES  12 B  440  HIS PRO ARG PHE VAL HIS GLY ALA ALA THR SER CYS ASN
SEQRES  13 B  440  ALA ASP VAL PHE ALA TYR ALA ALA ALA LYS VAL LYS LYS
SEQRES  14 B  440  GLY LEU GLU ILE ALA LYS ARG LEU GLY ALA GLU ASN TYR
SEQRES  15 B  440  VAL PHE TRP GLY GLY ARG GLU GLY TYR GLU THR LEU LEU
SEQRES  16 B  440  ASN THR ASP MET LYS LEU GLU LEU ASP ASN LEU ALA ARG
SEQRES  17 B  440  PHE LEU HIS MET ALA VAL ASP TYR ALA LYS GLU ILE GLY
SEQRES  18 B  440  PHE ASP GLY GLN PHE LEU ILE GLU PRO LYS PRO LYS GLU
SEQRES  19 B  440  PRO THR LYS HIS GLN TYR ASP PHE ASP VAL ALA THR ALA
SEQRES  20 B  440  LEU ALA PHE LEU GLN THR TYR GLY LEU LYS ASP TYR PHE
SEQRES  21 B  440  LYS PHE ASN ILE GLU ALA ASN HIS ALA THR LEU ALA GLY
SEQRES  22 B  440  HIS THR PHE GLU HIS GLU LEU ARG VAL ALA ARG ILE HIS
SEQRES  23 B  440  GLY MET LEU GLY SER VAL ASP ALA ASN GLN GLY ASP MET
SEQRES  24 B  440  LEU LEU GLY TRP ASP THR ASP GLU PHE PRO THR ASP LEU
SEQRES  25 B  440  TYR SER THR THR LEU ALA MET TYR GLU ILE LEU LYS ASN
SEQRES  26 B  440  GLY GLY LEU GLY ARG GLY GLY LEU ASN PHE ASP ALA LYS
SEQRES  27 B  440  VAL ARG ARG GLY SER PHE GLU PRO GLU ASP LEU PHE TYR
SEQRES  28 B  440  ALA HIS ILE ALA GLY MET ASP SER PHE ALA VAL GLY LEU
SEQRES  29 B  440  LYS VAL ALA HIS ARG LEU ILE GLU ASP ARG VAL PHE ASP
SEQRES  30 B  440  GLU PHE ILE GLU GLU ARG TYR LYS SER TYR THR GLU GLY
SEQRES  31 B  440  ILE GLY ARG GLU ILE VAL GLU GLY THR ALA ASP PHE HIS
SEQRES  32 B  440  LYS LEU GLU ALA HIS ALA LEU GLN LEU GLY GLU ILE GLN
SEQRES  33 B  440  ASN GLN SER GLY ARG GLN GLU ARG LEU LYS THR LEU LEU
SEQRES  34 B  440  ASN GLN TYR LEU LEU GLU VAL CYS ALA ALA ARG
SEQRES   1 C  440  PRO TYR PHE ASP ASN ILE SER THR ILE ALA TYR GLU GLY
SEQRES   2 C  440  PRO ALA SER LYS ASN PRO LEU ALA PHE LYS PHE TYR ASN
SEQRES   3 C  440  PRO GLU GLU LYS VAL GLY ASP LYS THR MET GLU GLU HIS
SEQRES   4 C  440  LEU ARG PHE SER VAL ALA TYR TRP HIS THR PHE THR GLY
SEQRES   5 C  440  ASP GLY SER ASP PRO PHE GLY ALA GLY ASN MET ILE ARG
SEQRES   6 C  440  PRO TRP ASN LYS TYR SER GLY MET ASP LEU ALA LYS ALA
SEQRES   7 C  440  ARG VAL GLU ALA ALA PHE GLU PHE PHE GLU LYS LEU ASN
SEQRES   8 C  440  ILE PRO PHE PHE CYS PHE HIS ASP VAL ASP ILE ALA PRO
SEQRES   9 C  440  GLU GLY GLU THR LEU LYS GLU THR TYR LYS ASN LEU ASP
SEQRES  10 C  440  ILE ILE VAL ASP MET ILE GLU GLU TYR MET LYS THR SER
SEQRES  11 C  440  LYS THR LYS LEU LEU TRP ASN THR ALA ASN LEU PHE THR
SEQRES  12 C  440  HIS PRO ARG PHE VAL HIS GLY ALA ALA THR SER CYS ASN
SEQRES  13 C  440  ALA ASP VAL PHE ALA TYR ALA ALA ALA LYS VAL LYS LYS
SEQRES  14 C  440  GLY LEU GLU ILE ALA LYS ARG LEU GLY ALA GLU ASN TYR
SEQRES  15 C  440  VAL PHE TRP GLY GLY ARG GLU GLY TYR GLU THR LEU LEU
SEQRES  16 C  440  ASN THR ASP MET LYS LEU GLU LEU ASP ASN LEU ALA ARG
SEQRES  17 C  440  PHE LEU HIS MET ALA VAL ASP TYR ALA LYS GLU ILE GLY
SEQRES  18 C  440  PHE ASP GLY GLN PHE LEU ILE GLU PRO LYS PRO LYS GLU
SEQRES  19 C  440  PRO THR LYS HIS GLN TYR ASP PHE ASP VAL ALA THR ALA
SEQRES  20 C  440  LEU ALA PHE LEU GLN THR TYR GLY LEU LYS ASP TYR PHE
SEQRES  21 C  440  LYS PHE ASN ILE GLU ALA ASN HIS ALA THR LEU ALA GLY
SEQRES  22 C  440  HIS THR PHE GLU HIS GLU LEU ARG VAL ALA ARG ILE HIS
SEQRES  23 C  440  GLY MET LEU GLY SER VAL ASP ALA ASN GLN GLY ASP MET
SEQRES  24 C  440  LEU LEU GLY TRP ASP THR ASP GLU PHE PRO THR ASP LEU
SEQRES  25 C  440  TYR SER THR THR LEU ALA MET TYR GLU ILE LEU LYS ASN
SEQRES  26 C  440  GLY GLY LEU GLY ARG GLY GLY LEU ASN PHE ASP ALA LYS
SEQRES  27 C  440  VAL ARG ARG GLY SER PHE GLU PRO GLU ASP LEU PHE TYR
SEQRES  28 C  440  ALA HIS ILE ALA GLY MET ASP SER PHE ALA VAL GLY LEU
SEQRES  29 C  440  LYS VAL ALA HIS ARG LEU ILE GLU ASP ARG VAL PHE ASP
SEQRES  30 C  440  GLU PHE ILE GLU GLU ARG TYR LYS SER TYR THR GLU GLY
SEQRES  31 C  440  ILE GLY ARG GLU ILE VAL GLU GLY THR ALA ASP PHE HIS
SEQRES  32 C  440  LYS LEU GLU ALA HIS ALA LEU GLN LEU GLY GLU ILE GLN
SEQRES  33 C  440  ASN GLN SER GLY ARG GLN GLU ARG LEU LYS THR LEU LEU
SEQRES  34 C  440  ASN GLN TYR LEU LEU GLU VAL CYS ALA ALA ARG
SEQRES   1 D  440  PRO TYR PHE ASP ASN ILE SER THR ILE ALA TYR GLU GLY
SEQRES   2 D  440  PRO ALA SER LYS ASN PRO LEU ALA PHE LYS PHE TYR ASN
SEQRES   3 D  440  PRO GLU GLU LYS VAL GLY ASP LYS THR MET GLU GLU HIS
SEQRES   4 D  440  LEU ARG PHE SER VAL ALA TYR TRP HIS THR PHE THR GLY
SEQRES   5 D  440  ASP GLY SER ASP PRO PHE GLY ALA GLY ASN MET ILE ARG
SEQRES   6 D  440  PRO TRP ASN LYS TYR SER GLY MET ASP LEU ALA LYS ALA
SEQRES   7 D  440  ARG VAL GLU ALA ALA PHE GLU PHE PHE GLU LYS LEU ASN
SEQRES   8 D  440  ILE PRO PHE PHE CYS PHE HIS ASP VAL ASP ILE ALA PRO
SEQRES   9 D  440  GLU GLY GLU THR LEU LYS GLU THR TYR LYS ASN LEU ASP
SEQRES  10 D  440  ILE ILE VAL ASP MET ILE GLU GLU TYR MET LYS THR SER
SEQRES  11 D  440  LYS THR LYS LEU LEU TRP ASN THR ALA ASN LEU PHE THR
SEQRES  12 D  440  HIS PRO ARG PHE VAL HIS GLY ALA ALA THR SER CYS ASN
SEQRES  13 D  440  ALA ASP VAL PHE ALA TYR ALA ALA ALA LYS VAL LYS LYS
SEQRES  14 D  440  GLY LEU GLU ILE ALA LYS ARG LEU GLY ALA GLU ASN TYR
SEQRES  15 D  440  VAL PHE TRP GLY GLY ARG GLU GLY TYR GLU THR LEU LEU
SEQRES  16 D  440  ASN THR ASP MET LYS LEU GLU LEU ASP ASN LEU ALA ARG
SEQRES  17 D  440  PHE LEU HIS MET ALA VAL ASP TYR ALA LYS GLU ILE GLY
SEQRES  18 D  440  PHE ASP GLY GLN PHE LEU ILE GLU PRO LYS PRO LYS GLU
SEQRES  19 D  440  PRO THR LYS HIS GLN TYR ASP PHE ASP VAL ALA THR ALA
SEQRES  20 D  440  LEU ALA PHE LEU GLN THR TYR GLY LEU LYS ASP TYR PHE
SEQRES  21 D  440  LYS PHE ASN ILE GLU ALA ASN HIS ALA THR LEU ALA GLY
SEQRES  22 D  440  HIS THR PHE GLU HIS GLU LEU ARG VAL ALA ARG ILE HIS
SEQRES  23 D  440  GLY MET LEU GLY SER VAL ASP ALA ASN GLN GLY ASP MET
SEQRES  24 D  440  LEU LEU GLY TRP ASP THR ASP GLU PHE PRO THR ASP LEU
SEQRES  25 D  440  TYR SER THR THR LEU ALA MET TYR GLU ILE LEU LYS ASN
SEQRES  26 D  440  GLY GLY LEU GLY ARG GLY GLY LEU ASN PHE ASP ALA LYS
SEQRES  27 D  440  VAL ARG ARG GLY SER PHE GLU PRO GLU ASP LEU PHE TYR
SEQRES  28 D  440  ALA HIS ILE ALA GLY MET ASP SER PHE ALA VAL GLY LEU
SEQRES  29 D  440  LYS VAL ALA HIS ARG LEU ILE GLU ASP ARG VAL PHE ASP
SEQRES  30 D  440  GLU PHE ILE GLU GLU ARG TYR LYS SER TYR THR GLU GLY
SEQRES  31 D  440  ILE GLY ARG GLU ILE VAL GLU GLY THR ALA ASP PHE HIS
SEQRES  32 D  440  LYS LEU GLU ALA HIS ALA LEU GLN LEU GLY GLU ILE GLN
SEQRES  33 D  440  ASN GLN SER GLY ARG GLN GLU ARG LEU LYS THR LEU LEU
SEQRES  34 D  440  ASN GLN TYR LEU LEU GLU VAL CYS ALA ALA ARG
HET     MN  A 491       1
HET     MN  A 492       1
HET     MN  B 491       1
HET     MN  B 492       1
HET     MN  C 491       1
HET     MN  C 492       1
HET     MN  D 491       1
HET     MN  D 492       1
HETNAM      MN MANGANESE (II) ION
FORMUL   5   MN    8(MN 2+)
FORMUL  13  HOH   *240(H2 O)
HELIX    1   1 MET A   36  LEU A   40  1                                   5
HELIX    2   2 TYR A   46  THR A   51  1                                   6
HELIX    3   3 PRO A   66  LYS A   69  5                                   4
HELIX    4   4 GLY A   72  LEU A   90  1                                  19
HELIX    5   5 ASP A   99  ILE A  102  1                                   4
HELIX    6   6 LEU A  109  THR A  129  1                                  21
HELIX    7   7 PRO A  145  PHE A  147  5                                   3
HELIX    8   8 ALA A  157  LEU A  177  1                                  21
HELIX    9   9 LEU A  194  ASN A  196  5                                   3
HELIX   10  10 MET A  199  GLU A  219  1                                  21
HELIX   11  11 VAL A  244  THR A  253  1                                  10
HELIX   12  12 LYS A  257  TYR A  259  5                                   3
HELIX   13  13 ALA A  266  LEU A  271  1                                   6
HELIX   14  14 PHE A  276  HIS A  286  1                                  11
HELIX   15  15 LEU A  312  LYS A  324  1                                  13
HELIX   16  16 PRO A  346  GLU A  372  5                                  27
HELIX   17  17 VAL A  375  ARG A  383  1                                   9
HELIX   18  18 LYS A  385  THR A  388  5                                   4
HELIX   19  19 GLY A  390  GLU A  397  1                                   8
HELIX   20  20 PHE A  402  GLN A  411  1                                  10
HELIX   21  21 GLN A  422  LEU A  434  1                                  13
HELIX   22  22 MET B   36  LEU B   40  1                                   5
HELIX   23  23 TYR B   46  THR B   51  1                                   6
HELIX   24  24 PRO B   66  LYS B   69  5                                   4
HELIX   25  25 GLY B   72  LEU B   90  1                                  19
HELIX   26  26 ASP B   99  ILE B  102  1                                   4
HELIX   27  27 LEU B  109  THR B  129  1                                  21
HELIX   28  28 PRO B  145  PHE B  147  5                                   3
HELIX   29  29 ALA B  157  LEU B  177  1                                  21
HELIX   30  30 LEU B  194  ASN B  196  5                                   3
HELIX   31  31 MET B  199  GLU B  219  1                                  21
HELIX   32  32 VAL B  244  THR B  253  1                                  10
HELIX   33  33 LYS B  257  TYR B  259  5                                   3
HELIX   34  34 ALA B  266  LEU B  271  1                                   6
HELIX   35  35 PHE B  276  HIS B  286  1                                  11
HELIX   36  36 LEU B  312  LYS B  324  1                                  13
HELIX   37  37 PRO B  346  GLU B  372  5                                  27
HELIX   38  38 VAL B  375  ARG B  383  1                                   9
HELIX   39  39 LYS B  385  THR B  388  5                                   4
HELIX   40  40 GLY B  390  GLU B  397  1                                   8
HELIX   41  41 PHE B  402  GLN B  411  1                                  10
HELIX   42  42 GLN B  422  LEU B  434  1                                  13
HELIX   43  43 MET C   36  LEU C   40  1                                   5
HELIX   44  44 TYR C   46  THR C   51  1                                   6
HELIX   45  45 PRO C   66  LYS C   69  5                                   4
HELIX   46  46 GLY C   72  LEU C   90  1                                  19
HELIX   47  47 ASP C   99  ILE C  102  1                                   4
HELIX   48  48 LEU C  109  THR C  129  1                                  21
HELIX   49  49 PRO C  145  PHE C  147  5                                   3
HELIX   50  50 ALA C  157  LEU C  177  1                                  21
HELIX   51  51 LEU C  194  ASN C  196  5                                   3
HELIX   52  52 MET C  199  GLU C  219  1                                  21
HELIX   53  53 VAL C  244  THR C  253  1                                  10
HELIX   54  54 LYS C  257  TYR C  259  5                                   3
HELIX   55  55 ALA C  266  LEU C  271  1                                   6
HELIX   56  56 PHE C  276  HIS C  286  1                                  11
HELIX   57  57 LEU C  312  LYS C  324  1                                  13
HELIX   58  58 PRO C  346  GLU C  372  5                                  27
HELIX   59  59 VAL C  375  ARG C  383  1                                   9
HELIX   60  60 LYS C  385  THR C  388  5                                   4
HELIX   61  61 GLY C  390  GLU C  397  1                                   8
HELIX   62  62 PHE C  402  GLN C  411  1                                  10
HELIX   63  63 GLN C  422  LEU C  434  1                                  13
HELIX   64  64 MET D   36  LEU D   40  1                                   5
HELIX   65  65 TYR D   46  THR D   51  1                                   6
HELIX   66  66 PRO D   66  LYS D   69  5                                   4
HELIX   67  67 GLY D   72  LEU D   90  1                                  19
HELIX   68  68 ASP D   99  ILE D  102  1                                   4
HELIX   69  69 LEU D  109  THR D  129  1                                  21
HELIX   70  70 PRO D  145  PHE D  147  5                                   3
HELIX   71  71 ALA D  157  LEU D  177  1                                  21
HELIX   72  72 LEU D  194  ASN D  196  5                                   3
HELIX   73  73 MET D  199  GLU D  219  1                                  21
HELIX   74  74 VAL D  244  THR D  253  1                                  10
HELIX   75  75 LYS D  257  TYR D  259  5                                   3
HELIX   76  76 ALA D  266  LEU D  271  1                                   6
HELIX   77  77 PHE D  276  HIS D  286  1                                  11
HELIX   78  78 LEU D  312  LYS D  324  1                                  13
HELIX   79  79 PRO D  346  GLU D  372  5                                  27
HELIX   80  80 VAL D  375  ARG D  383  1                                   9
HELIX   81  81 LYS D  385  THR D  388  5                                   4
HELIX   82  82 GLY D  390  GLU D  397  1                                   8
HELIX   83  83 PHE D  402  GLN D  411  1                                  10
HELIX   84  84 GLN D  422  LEU D  434  1                                  13
SHEET    1   A 8 LEU A 333  PHE A 335  0
SHEET    2   A 8 PHE A  42  ALA A  45  1  N  SER A  43   O  LEU A 333
SHEET    3   A 8 PHE A  94  HIS A  98  1  N  PHE A  94   O  VAL A  44
SHEET    4   A 8 LYS A 133  THR A 138  1  N  LYS A 133   O  PHE A  95
SHEET    5   A 8 ASN A 181  PHE A 184  1  N  ASN A 181   O  ASN A 137
SHEET    6   A 8 GLN A 225  ILE A 228  1  N  GLN A 225   O  TYR A 182
SHEET    7   A 8 PHE A 260  GLU A 265  1  N  LYS A 261   O  PHE A 226
SHEET    8   A 8 LEU A 289  ASP A 293  1  N  GLY A 290   O  PHE A 262
SHEET    1   B 8 LEU B 333  PHE B 335  0
SHEET    2   B 8 PHE B  42  ALA B  45  1  N  SER B  43   O  LEU B 333
SHEET    3   B 8 PHE B  94  HIS B  98  1  N  PHE B  94   O  VAL B  44
SHEET    4   B 8 LYS B 133  THR B 138  1  N  LYS B 133   O  PHE B  95
SHEET    5   B 8 ASN B 181  PHE B 184  1  N  ASN B 181   O  ASN B 137
SHEET    6   B 8 GLN B 225  ILE B 228  1  N  GLN B 225   O  TYR B 182
SHEET    7   B 8 PHE B 260  GLU B 265  1  N  LYS B 261   O  PHE B 226
SHEET    8   B 8 LEU B 289  ASP B 293  1  N  GLY B 290   O  PHE B 262
SHEET    1   C 8 LEU C 333  PHE C 335  0
SHEET    2   C 8 PHE C  42  ALA C  45  1  N  SER C  43   O  LEU C 333
SHEET    3   C 8 PHE C  94  HIS C  98  1  N  PHE C  94   O  VAL C  44
SHEET    4   C 8 LYS C 133  THR C 138  1  N  LYS C 133   O  PHE C  95
SHEET    5   C 8 ASN C 181  PHE C 184  1  N  ASN C 181   O  ASN C 137
SHEET    6   C 8 GLN C 225  ILE C 228  1  N  GLN C 225   O  TYR C 182
SHEET    7   C 8 PHE C 260  GLU C 265  1  N  LYS C 261   O  PHE C 226
SHEET    8   C 8 LEU C 289  ASP C 293  1  N  GLY C 290   O  PHE C 262
SHEET    1   D 8 LEU D 333  PHE D 335  0
SHEET    2   D 8 PHE D  42  ALA D  45  1  N  SER D  43   O  LEU D 333
SHEET    3   D 8 PHE D  94  HIS D  98  1  N  PHE D  94   O  VAL D  44
SHEET    4   D 8 LYS D 133  THR D 138  1  N  LYS D 133   O  PHE D  95
SHEET    5   D 8 ASN D 181  PHE D 184  1  N  ASN D 181   O  ASN D 137
SHEET    6   D 8 GLN D 225  ILE D 228  1  N  GLN D 225   O  TYR D 182
SHEET    7   D 8 PHE D 260  GLU D 265  1  N  LYS D 261   O  PHE D 226
SHEET    8   D 8 LEU D 289  ASP D 293  1  N  GLY D 290   O  PHE D 262
SSBOND   1 CYS A  437    CYS D  437                          1555   1555  2.60
SSBOND   2 CYS B  437    CYS C  437                          1555   1555  2.59
LINK        MN    MN A 491                 OE2 GLU A 229     1555   1555  2.14
LINK        MN    MN A 491                 OE1 GLU A 265     1555   1555  2.26
LINK        MN    MN A 491                 OD2 ASP A 336     1555   1555  2.16
LINK        MN    MN A 492                 OE2 GLU A 265     1555   1555  2.15
LINK        MN    MN A 492                 OD2 ASP A 304     1555   1555  2.30
LINK        MN    MN B 491                 OE2 GLU B 229     1555   1555  2.14
LINK        MN    MN B 491                 OE1 GLU B 265     1555   1555  2.26
LINK        MN    MN B 491                 OD2 ASP B 336     1555   1555  2.16
LINK        MN    MN B 492                 OE2 GLU B 265     1555   1555  2.15
LINK        MN    MN B 492                 OD2 ASP B 304     1555   1555  2.30
LINK        MN    MN C 491                 OE2 GLU C 229     1555   1555  2.14
LINK        MN    MN C 491                 OE1 GLU C 265     1555   1555  2.26
LINK        MN    MN C 491                 OD2 ASP C 336     1555   1555  2.16
LINK        MN    MN C 492                 OE2 GLU C 265     1555   1555  2.15
LINK        MN    MN C 492                 OD2 ASP C 304     1555   1555  2.30
LINK        MN    MN D 491                 OE2 GLU D 229     1555   1555  2.14
LINK        MN    MN D 491                 OE1 GLU D 265     1555   1555  2.26
LINK        MN    MN D 491                 OD2 ASP D 336     1555   1555  2.16
LINK        MN    MN D 492                 OE2 GLU D 265     1555   1555  2.15
LINK        MN    MN D 492                 OD2 ASP D 304     1555   1555  2.30
LINK        MN    MN A 491                 OD2 ASP A 293     1555   1555  2.41
LINK        MN    MN A 491                 O   HOH A 538     1555   1555  2.66
LINK        MN    MN A 492                 O   HOH A 544     1555   1555  2.74
LINK        MN    MN A 492                 OD1 ASP A 306     1555   1555  2.58
LINK        MN    MN A 492                 O   HOH A 493     1555   1555  2.66
LINK        MN    MN B 491                 OD2 ASP B 293     1555   1555  2.41
LINK        MN    MN B 491                 O   HOH B 542     1555   1555  2.66
LINK        MN    MN B 492                 OD1 ASP B 306     1555   1555  2.58
LINK        MN    MN B 492                 O   HOH B 496     1555   1555  2.66
LINK        MN    MN B 492                 O   HOH B 548     1555   1555  2.74
LINK        MN    MN C 491                 OD2 ASP C 293     1555   1555  2.41
LINK        MN    MN C 491                 O   HOH C 541     1555   1555  2.66
LINK        MN    MN C 492                 O   HOH C 497     1555   1555  2.66
LINK        MN    MN C 492                 O   HOH C 547     1555   1555  2.74
LINK        MN    MN C 492                 OD1 ASP C 306     1555   1555  2.58
LINK        MN    MN D 491                 O   HOH D 544     1555   1555  2.66
LINK        MN    MN D 491                 OD2 ASP D 293     1555   1555  2.41
LINK        MN    MN D 492                 O   HOH D 499     1555   1555  2.66
LINK        MN    MN D 492                 O   HOH D 550     1555   1555  2.74
LINK        MN    MN D 492                 OD1 ASP D 306     1555   1555  2.58
CISPEP   1 GLU A  234    PRO A  235          0         0.64
CISPEP   2 GLU B  234    PRO B  235          0         0.60
CISPEP   3 GLU C  234    PRO C  235          0         0.66
CISPEP   4 GLU D  234    PRO D  235          0         0.66
SITE     1 MN1  5 GLU A 229  GLU A 265  ASP A 293  ASP A 336
SITE     2 MN1  5 HOH A 538
SITE     1 MN2  5 GLU A 265  ASP A 304  ASP A 306  HOH A 493
SITE     2 MN2  5 HOH A 545
SITE     1 MN3  5 GLU B 229  GLU B 265  ASP B 293  ASP B 336
SITE     2 MN3  5 HOH B 542
SITE     1 MN4  5 GLU B 265  ASP B 304  ASP B 306  HOH B 496
SITE     2 MN4  5 HOH B 549
SITE     1 MN5  5 GLU C 229  GLU C 265  ASP C 293  ASP C 336
SITE     2 MN5  5 HOH C 541
SITE     1 MN6  5 GLU C 265  ASP C 304  ASP C 306  HOH C 497
SITE     2 MN6  5 HOH C 548
SITE     1 MN7  5 GLU D 229  GLU D 265  ASP D 293  ASP D 336
SITE     2 MN7  5 HOH D 544
SITE     1 MN8  5 GLU D 265  ASP D 304  ASP D 306  HOH D 499
SITE     2 MN8  5 HOH D 551
SITE     1 AC1  5 GLU A 229  GLU A 265  ASP A 293  ASP A 336
SITE     2 AC1  5 HOH A 538
SITE     1 AC2  6 GLU A 265  HIS A 268  ASP A 304  ASP A 306
SITE     2 AC2  6 HOH A 493  HOH A 544
SITE     1 AC3  5 GLU B 229  GLU B 265  ASP B 293  ASP B 336
SITE     2 AC3  5 HOH B 542
SITE     1 AC4  6 GLU B 265  HIS B 268  ASP B 304  ASP B 306
SITE     2 AC4  6 HOH B 496  HOH B 548
SITE     1 AC5  5 GLU C 229  GLU C 265  ASP C 293  ASP C 336
SITE     2 AC5  5 HOH C 541
SITE     1 AC6  6 GLU C 265  HIS C 268  ASP C 304  ASP C 306
SITE     2 AC6  6 HOH C 497  HOH C 547
SITE     1 AC7  5 GLU D 229  GLU D 265  ASP D 293  ASP D 336
SITE     2 AC7  5 HOH D 544
SITE     1 AC8  6 GLU D 265  HIS D 268  ASP D 304  ASP D 306
SITE     2 AC8  6 HOH D 499  HOH D 550
CRYST1   86.290  141.850  160.660  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      0.011589  0.000000  0.000000        0.00000
SCALE2      0.000000  0.007050  0.000000        0.00000
SCALE3      0.000000  0.000000  0.006224        0.00000
MTRIX1   1 -0.987670  0.156580 -0.000240       28.20802    1
MTRIX2   1  0.156550  0.987520  0.017440       -2.89316    1
MTRIX3   1  0.002960  0.017180 -0.999850       78.81460    1
MTRIX1   2 -0.742400 -0.012770 -0.669830       55.16944    1
MTRIX2   2 -0.014910 -0.999260  0.035580       50.51254    1
MTRIX3   2 -0.669790  0.036400  0.741660       20.18826    1
MTRIX1   3  0.728360 -0.144810  0.669720      -18.32721    1
MTRIX2   3 -0.144720 -0.987870 -0.056200       56.00223    1
MTRIX3   3  0.669740 -0.055990 -0.740480       59.59824    1
      
PROCHECK
Go to PROCHECK summary
 References