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PDBsum entry 3u3h

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Isomerase PDB id
3u3h
Jmol
Contents
Protein chain
386 a.a.
Ligands
03W
FMT
MRD
Metals
_MG ×2
Waters ×524
HEADER    ISOMERASE                               05-OCT-11   3U3H
TITLE     X-RAY CRYSTALLOGRAPHIC ANALYSIS OF D-XYLOSE ISOMERASE-CATALYZED
TITLE    2 ISOMERIZATION OF (R)-GLYCERALDEHYDE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: XYLOSE ISOMERASE;
COMPND   3 CHAIN: A;
COMPND   4 EC: 5.3.1.5
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOMYCES RUBIGINOSUS;
SOURCE   3 ORGANISM_TAXID: 1929
KEYWDS    ALDOSE-KETOSE ISOMERASES, GLYCERALDEHYDE, HYDRIDE SHIFT, ENZYME
KEYWDS   2 PROMISCUITY, ISOMERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    K.N.ALLEN,N.R.SILVAGGI,M.M.TOTEVA,J.P.RICHARD
REVDAT   2   07-DEC-11 3U3H    1       JRNL
REVDAT   1   26-OCT-11 3U3H    0
JRNL        AUTH   M.M.TOTEVA,N.R.SILVAGGI,K.N.ALLEN,J.P.RICHARD
JRNL        TITL   BINDING ENERGY AND CATALYSIS BY D-XYLOSE ISOMERASE: KINETIC,
JRNL        TITL 2 PRODUCT, AND X-RAY CRYSTALLOGRAPHIC ANALYSIS OF
JRNL        TITL 3 ENZYME-CATALYZED ISOMERIZATION OF (R)-GLYCERALDEHYDE.
JRNL        REF    BIOCHEMISTRY                  V.  50 10170 2011
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   21995300
JRNL        DOI    10.1021/BI201378C
REMARK   2
REMARK   2 RESOLUTION.    0.97 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: DEV_881)
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK   3               : ZWART
REMARK   3
REMARK   3    REFINEMENT TARGET : ML
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 0.97
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.97
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.8
REMARK   3   NUMBER OF REFLECTIONS             : 262128
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.116
REMARK   3   R VALUE            (WORKING SET) : 0.116
REMARK   3   FREE R VALUE                     : 0.125
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.960
REMARK   3   FREE R VALUE TEST SET COUNT      : 13001
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE
REMARK   3     1 19.9766 -  3.0106    0.99     8986   470  0.1407 0.1480
REMARK   3     2  3.0106 -  2.3908    0.99     8765   462  0.1343 0.1475
REMARK   3     3  2.3908 -  2.0890    0.99     8653   463  0.1167 0.1192
REMARK   3     4  2.0890 -  1.8982    0.99     8651   457  0.1206 0.1226
REMARK   3     5  1.8982 -  1.7622    0.98     8576   414  0.1140 0.1183
REMARK   3     6  1.7622 -  1.6584    0.98     8501   458  0.1050 0.1144
REMARK   3     7  1.6584 -  1.5753    0.98     8485   481  0.1006 0.1063
REMARK   3     8  1.5753 -  1.5068    0.98     8530   428  0.0974 0.1111
REMARK   3     9  1.5068 -  1.4488    0.98     8389   479  0.0963 0.1009
REMARK   3    10  1.4488 -  1.3988    0.98     8503   462  0.0964 0.1017
REMARK   3    11  1.3988 -  1.3551    0.98     8442   425  0.0948 0.0959
REMARK   3    12  1.3551 -  1.3164    0.97     8433   434  0.0914 0.0973
REMARK   3    13  1.3164 -  1.2817    0.97     8382   423  0.0893 0.1058
REMARK   3    14  1.2817 -  1.2504    0.97     8457   422  0.0900 0.1016
REMARK   3    15  1.2504 -  1.2220    0.97     8478   393  0.0863 0.0934
REMARK   3    16  1.2220 -  1.1960    0.97     8358   439  0.0821 0.0919
REMARK   3    17  1.1960 -  1.1721    0.97     8343   450  0.0794 0.0951
REMARK   3    18  1.1721 -  1.1500    0.97     8357   464  0.0750 0.0805
REMARK   3    19  1.1500 -  1.1294    0.97     8258   444  0.0750 0.0937
REMARK   3    20  1.1294 -  1.1103    0.96     8362   449  0.0791 0.0945
REMARK   3    21  1.1103 -  1.0924    0.96     8259   413  0.0829 0.0996
REMARK   3    22  1.0924 -  1.0756    0.96     8276   417  0.0888 0.0990
REMARK   3    23  1.0756 -  1.0598    0.95     8167   436  0.0981 0.1193
REMARK   3    24  1.0598 -  1.0448    0.94     8156   407  0.1129 0.1329
REMARK   3    25  1.0448 -  1.0307    0.94     8062   414  0.1329 0.1464
REMARK   3    26  1.0307 -  1.0173    0.93     8012   429  0.1552 0.1894
REMARK   3    27  1.0173 -  1.0046    0.92     7908   410  0.1803 0.1999
REMARK   3    28  1.0046 -  0.9925    0.91     7830   413  0.2041 0.2234
REMARK   3    29  0.9925 -  0.9810    0.88     7526   387  0.2334 0.2617
REMARK   3    30  0.9810 -  0.9700    0.81     7022   358  0.2592 0.2804
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 0.90
REMARK   3   SHRINKAGE RADIUS   : 0.60
REMARK   3   K_SOL              : 0.45
REMARK   3   B_SOL              : 42.50
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.090
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 8.430
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) : 0.04970
REMARK   3    B22 (A**2) : -0.13280
REMARK   3    B33 (A**2) : 0.08300
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : -0.00000
REMARK   3
REMARK   3  TWINNING INFORMATION.
REMARK   3   FRACTION: NULL
REMARK   3   OPERATOR: NULL
REMARK   3
REMARK   3  DEVIATIONS FROM IDEAL VALUES.
REMARK   3                 RMSD          COUNT
REMARK   3   BOND      :  0.008           3289
REMARK   3   ANGLE     :  1.343           4463
REMARK   3   CHIRALITY :  0.075            456
REMARK   3   PLANARITY :  0.009            605
REMARK   3   DIHEDRAL  : 13.319           1235
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  NCS DETAILS
REMARK   3   NUMBER OF NCS GROUPS : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 3U3H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-OCT-11.
REMARK 100 THE RCSB ID CODE IS RCSB068258.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 18-FEB-05
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : NSLS
REMARK 200  BEAMLINE                       : X12B
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97890
REMARK 200  MONOCHROMATOR                  : SI111
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 272713
REMARK 200  RESOLUTION RANGE HIGH      (A) : 0.970
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.972
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7
REMARK 200  DATA REDUNDANCY                : 8.500
REMARK 200  R MERGE                    (I) : 0.05500
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 39.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.00
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.04
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.30
REMARK 200  R MERGE FOR SHELL          (I) : 0.29100
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 6.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: EPMR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 54.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20MG/ML XI IN WATER WAS MIXED WITH AN
REMARK 280  EQUAL VOLUME OF WELL SOLUTION CONSISTING OF 0.2-0.3M MG FORMATE,
REMARK 280  PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X,Y,-Z
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       46.32550
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       49.07400
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       51.29850
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       46.32550
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       49.07400
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       51.29850
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       46.32550
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       49.07400
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       51.29850
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       46.32550
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       49.07400
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       51.29850
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: 32890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 45160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -147.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       92.65100
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      196.29600
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   3 -1.000000  0.000000  0.000000       92.65100
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000      102.59700
REMARK 350   BIOMT1   4  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000      196.29600
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000      102.59700
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     MET A     1
REMARK 465     GLY A   388
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480   M RES C SSEQI ATOMS
REMARK 480     GLU A   69   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   O    HOH A   423     O    HOH A   439     4576     1.82
REMARK 500   O    HOH A   428     O    HOH A   436     7556     2.14
REMARK 500   O    HOH A   432     O    HOH A   436     7556     2.15
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    THR A  17      -76.26    -85.39
REMARK 500    PHE A  94      -26.39   -140.57
REMARK 500    GLU A 186      102.15     79.30
REMARK 500    ASN A 247     -169.99   -168.16
REMARK 500    LYS A 253     -176.90   -172.04
REMARK 500    TYR A 254      153.88    -45.74
REMARK 500    ALA A 343       62.09   -151.55
REMARK 500    PHE A 357      -70.09   -156.04
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 A 389        DISTANCE =  5.51 ANGSTROMS
REMARK 525    HOH A 434        DISTANCE =  6.07 ANGSTROMS
REMARK 525    HOH A 435        DISTANCE =  5.51 ANGSTROMS
REMARK 525    HOH A1349        DISTANCE =  5.64 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A 500  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 217   OE1
REMARK 620 2 GLU A 181   OE2  92.0
REMARK 620 3 ASP A 245   OD2  97.8  92.1
REMARK 620 4 ASP A 287   OD2  92.5 170.0  96.1
REMARK 620 5 03W A 400   O2  174.9  87.3  87.3  87.4
REMARK 620 6 03W A 400   O1   98.9  87.6 163.3  82.9  76.0
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A 501  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 217   OE2
REMARK 620 2 ASP A 255   OD2 145.3
REMARK 620 3 ASP A 255   OD1 100.9  51.2
REMARK 620 4 ASP A 257   OD1 101.8  86.3  66.8
REMARK 620 5 GLU A 217   OE1  33.4 148.5 130.3 124.5
REMARK 620 6 HOH A1329   O    56.2  96.8  46.1  70.5  88.8
REMARK 620 7 HOH A1000   O   104.8 106.1 153.9 102.9  75.7 155.9
REMARK 620 N                    1     2     3     4     5     6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 03W A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD A 2000
DBREF  3U3H A    1   388  UNP    P24300   XYLA_STRRU       1    388
SEQRES   1 A  388  MET ASN TYR GLN PRO THR PRO GLU ASP ARG PHE THR PHE
SEQRES   2 A  388  GLY LEU TRP THR VAL GLY TRP GLN GLY ARG ASP PRO PHE
SEQRES   3 A  388  GLY ASP ALA THR ARG ARG ALA LEU ASP PRO VAL GLU SER
SEQRES   4 A  388  VAL ARG ARG LEU ALA GLU LEU GLY ALA HIS GLY VAL THR
SEQRES   5 A  388  PHE HIS ASP ASP ASP LEU ILE PRO PHE GLY SER SER ASP
SEQRES   6 A  388  SER GLU ARG GLU GLU HIS VAL LYS ARG PHE ARG GLN ALA
SEQRES   7 A  388  LEU ASP ASP THR GLY MET LYS VAL PRO MET ALA THR THR
SEQRES   8 A  388  ASN LEU PHE THR HIS PRO VAL PHE LYS ASP GLY GLY PHE
SEQRES   9 A  388  THR ALA ASN ASP ARG ASP VAL ARG ARG TYR ALA LEU ARG
SEQRES  10 A  388  LYS THR ILE ARG ASN ILE ASP LEU ALA VAL GLU LEU GLY
SEQRES  11 A  388  ALA GLU THR TYR VAL ALA TRP GLY GLY ARG GLU GLY ALA
SEQRES  12 A  388  GLU SER GLY GLY ALA LYS ASP VAL ARG ASP ALA LEU ASP
SEQRES  13 A  388  ARG MET LYS GLU ALA PHE ASP LEU LEU GLY GLU TYR VAL
SEQRES  14 A  388  THR SER GLN GLY TYR ASP ILE ARG PHE ALA ILE GLU PRO
SEQRES  15 A  388  LYS PRO ASN GLU PRO ARG GLY ASP ILE LEU LEU PRO THR
SEQRES  16 A  388  VAL GLY HIS ALA LEU ALA PHE ILE GLU ARG LEU GLU ARG
SEQRES  17 A  388  PRO GLU LEU TYR GLY VAL ASN PRO GLU VAL GLY HIS GLU
SEQRES  18 A  388  GLN MET ALA GLY LEU ASN PHE PRO HIS GLY ILE ALA GLN
SEQRES  19 A  388  ALA LEU TRP ALA GLY LYS LEU PHE HIS ILE ASP LEU ASN
SEQRES  20 A  388  GLY GLN ASN GLY ILE LYS TYR ASP GLN ASP LEU ARG PHE
SEQRES  21 A  388  GLY ALA GLY ASP LEU ARG ALA ALA PHE TRP LEU VAL ASP
SEQRES  22 A  388  LEU LEU GLU SER ALA GLY TYR SER GLY PRO ARG HIS PHE
SEQRES  23 A  388  ASP PHE LYS PRO PRO ARG THR GLU ASP PHE ASP GLY VAL
SEQRES  24 A  388  TRP ALA SER ALA ALA GLY CYS MET ARG ASN TYR LEU ILE
SEQRES  25 A  388  LEU LYS GLU ARG ALA ALA ALA PHE ARG ALA ASP PRO GLU
SEQRES  26 A  388  VAL GLN GLU ALA LEU ARG ALA SER ARG LEU ASP GLU LEU
SEQRES  27 A  388  ALA ARG PRO THR ALA ALA ASP GLY LEU GLN ALA LEU LEU
SEQRES  28 A  388  ASP ASP ARG SER ALA PHE GLU GLU PHE ASP VAL ASP ALA
SEQRES  29 A  388  ALA ALA ALA ARG GLY MET ALA PHE GLU ARG LEU ASP GLN
SEQRES  30 A  388  LEU ALA MET ASP HIS LEU LEU GLY ALA ARG GLY
HET    03W  A 400       7
HET    FMT  A 401       4
HET     MG  A 500       1
HET     MG  A 501       3
HET    MRD  A2000      22
HETNAM     03W (2R)-PROPANE-1,1,2,3-TETROL
HETNAM     FMT FORMIC ACID
HETNAM      MG MAGNESIUM ION
HETNAM     MRD (4R)-2-METHYLPENTANE-2,4-DIOL
FORMUL   2  03W    C3 H8 O4
FORMUL   3  FMT    C H2 O2
FORMUL   4   MG    2(MG 2+)
FORMUL   6  MRD    C6 H14 O2
FORMUL   7  HOH   *524(H2 O)
HELIX    1   1 THR A    6  ASP A    9  5                                   4
HELIX    2   2 LEU A   15  GLY A   19  1                                   5
HELIX    3   3 ASP A   35  LEU A   46  1                                  12
HELIX    4   4 ASP A   55  ILE A   59  1                                   5
HELIX    5   5 SER A   64  GLY A   83  1                                  20
HELIX    6   6 HIS A   96  LYS A  100  5                                   5
HELIX    7   7 ASP A  108  LEU A  129  1                                  22
HELIX    8   8 SER A  145  LYS A  149  5                                   5
HELIX    9   9 ASP A  150  GLY A  173  1                                  24
HELIX   10  10 THR A  195  GLU A  204  1                                  10
HELIX   11  11 ARG A  208  GLU A  210  5                                   3
HELIX   12  12 GLU A  217  MET A  223  1                                   7
HELIX   13  13 ASN A  227  ALA A  238  1                                  12
HELIX   14  14 ASP A  264  GLY A  279  1                                  16
HELIX   15  15 ASP A  295  ASP A  323  1                                  29
HELIX   16  16 ASP A  323  SER A  333  1                                  11
HELIX   17  17 ARG A  334  ALA A  339  1                                   6
HELIX   18  18 GLY A  346  ASP A  353  1                                   8
HELIX   19  19 ARG A  354  PHE A  357  5                                   4
HELIX   20  20 ASP A  361  ARG A  368  1                                   8
HELIX   21  21 ALA A  371  GLY A  385  1                                  15
SHEET    1   A 8 TYR A 212  VAL A 214  0
SHEET    2   A 8 ARG A 177  ILE A 180  1  N  ILE A 180   O  GLY A 213
SHEET    3   A 8 THR A 133  ALA A 136  1  N  TYR A 134   O  ARG A 177
SHEET    4   A 8 LYS A  85  THR A  90  1  N  ALA A  89   O  VAL A 135
SHEET    5   A 8 GLY A  50  HIS A  54  1  N  VAL A  51   O  LYS A  85
SHEET    6   A 8 PHE A  11  GLY A  14  1  N  PHE A  13   O  THR A  52
SHEET    7   A 8 ARG A 284  PHE A 286  1  O  PHE A 286   N  THR A  12
SHEET    8   A 8 ASP A 245  LEU A 246  1  N  LEU A 246   O  HIS A 285
SHEET    1   B 2 GLY A 142  ALA A 143  0
SHEET    2   B 2 ASP A 190  ILE A 191 -1  O  ASP A 190   N  ALA A 143
LINK         OE1 GLU A 217                MG  A MG A 500     1555   1555  2.03
LINK         OE2 GLU A 217                MG  B MG A 501     1555   1555  2.07
LINK         OE2 GLU A 181                MG  A MG A 500     1555   1555  2.09
LINK         OD2 ASP A 245                MG  A MG A 500     1555   1555  2.09
LINK         OD2AASP A 255                MG  A MG A 501     1555   1555  2.10
LINK         OD2 ASP A 287                MG  A MG A 500     1555   1555  2.11
LINK         O2 A03W A 400                MG  A MG A 500     1555   1555  2.12
LINK         OE2 GLU A 217                MG  C MG A 501     1555   1555  2.15
LINK         OE2 GLU A 217                MG  A MG A 501     1555   1555  2.16
LINK         O1 A03W A 400                MG  A MG A 500     1555   1555  2.16
LINK         OD1AASP A 255                MG  A MG A 501     1555   1555  2.21
LINK         OD1 ASP A 257                MG  B MG A 501     1555   1555  2.28
LINK         OD1 ASP A 257                MG  A MG A 501     1555   1555  2.52
LINK         OE1 GLU A 217                MG  C MG A 501     1555   1555  2.74
LINK        MG  A MG A 501                 O   HOH A1329     1555   1555  2.76
LINK        MG  B MG A 501                 O   HOH A1000     1555   1555  2.03
LINK        MG  C MG A 501                 O   HOH A1000     1555   1555  2.12
LINK        MG  A MG A 501                 O   HOH A1000     1555   1555  2.62
CISPEP   1 GLU A  186    PRO A  187          0        22.05
SITE     1 AC1 13 TRP A  16  HIS A  54  TRP A 137  GLU A 181
SITE     2 AC1 13 GLU A 217  ASP A 245  ASP A 287  HOH A 431
SITE     3 AC1 13  MG A 500   MG A 501  HOH A1076  HOH A1093
SITE     4 AC1 13 HOH A1370
SITE     1 AC2 11 PHE A  26  TRP A 137  GLU A 181  LYS A 183
SITE     2 AC2 11 GLU A 217  HIS A 220  ASP A 255  ASP A 287
SITE     3 AC2 11  MG A 500   MG A 501  HOH A1000
SITE     1 AC3  6 GLU A 181  GLU A 217  ASP A 245  ASP A 287
SITE     2 AC3  6 03W A 400  FMT A 401
SITE     1 AC4  8 GLU A 217  HIS A 220  ASP A 255  ASP A 257
SITE     2 AC4  8 03W A 400  FMT A 401  HOH A1000  HOH A1329
SITE     1 AC5  7 PRO A  25  PHE A  26  HIS A  54  THR A  95
SITE     2 AC5  7 HOH A 486  HOH A1152  HOH A1323
CRYST1   92.651   98.148  102.597  90.00  90.00  90.00 I 2 2 2       8
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.010793  0.000000  0.000000        0.00000
SCALE2      0.000000  0.010189  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009747        0.00000
      
PROCHECK
Go to PROCHECK summary
 References