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PDBsum entry 2gve

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Isomerase PDB id
2gve
Jmol
Contents
Protein chain
388 a.a.
Ligands
DOD ×512
Metals
_CO ×2
HEADER    ISOMERASE                               02-MAY-06   2GVE
TITLE     TIME-OF-FLIGHT NEUTRON DIFFRACTION STRUCTURE OF D-XYLOSE ISOMERASE
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    TIM BARREL-BETA-ALPHA-BARRELS, TWO METAL BINDING SITES, PROTONATION
KEYWDS   2 STATES OF RESIDUES, ISOMERASE
EXPDTA    NEUTRON DIFFRACTION
AUTHOR    A.K.KATZ,X.LI,H.L.CARRELL,B.L.HANSON,P.LANGAN,L.COATES,
AUTHOR   2 B.P.SCHOENBORN,J.P.GLUSKER,G.J.BUNICK
REVDAT   4   13-JUL-11 2GVE    1       VERSN
REVDAT   3   24-FEB-09 2GVE    1       VERSN
REVDAT   2   13-JUN-06 2GVE    1       JRNL
REVDAT   1   16-MAY-06 2GVE    0
JRNL        AUTH   A.K.KATZ,X.LI,H.L.CARRELL,B.L.HANSON,P.LANGAN,L.COATES,
JRNL        AUTH 2 B.P.SCHOENBORN,J.P.GLUSKER,G.J.BUNICK
JRNL        TITL   LOCATING ACTIVE-SITE HYDROGEN ATOMS IN D-XYLOSE ISOMERASE:
JRNL        TITL 2 TIME-OF-FLIGHT NEUTRON DIFFRACTION.
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 103  8342 2006
JRNL        REFN                   ISSN 0027-8424
JRNL        PMID   16707576
JRNL        DOI    10.1073/PNAS.0602598103
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   H.L.CARRELL,H.HOIER,J.P.GLUSKER
REMARK   1  TITL   MODES OF BINDING SUBSTRATES AND THEIR ANALOGS TO THE ENZYME
REMARK   1  TITL 2 D-XYLOSE ISOMERASE
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  50   113 1994
REMARK   1  REFN                   ISSN 0907-4449
REMARK   1  PMID   15299449
REMARK   1  DOI    10.1107/S0907444993009345
REMARK   2
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : SHELXL-97
REMARK   3   AUTHORS     : G.M.SHELDRICK
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 3.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL
REMARK   3   CROSS-VALIDATION METHOD           : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION   : 5%, RANDOM
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.271
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.319
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 1184
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 23312
REMARK   3
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : NULL
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : NULL
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : NULL
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : NULL
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS      : 3054
REMARK   3   NUCLEIC ACID ATOMS : 0
REMARK   3   HETEROGEN ATOMS    : 2
REMARK   3   SOLVENT ATOMS      : 512
REMARK   3
REMARK   3  MODEL REFINEMENT.
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : NULL
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : NULL
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : NULL
REMARK   3   NUMBER OF RESTRAINTS                     : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK   3   BOND LENGTHS                         (A) : 0.032
REMARK   3   ANGLE DISTANCES                      (A) : 0.173
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : NULL
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.036
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.055
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.168
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : NULL
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : NULL
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED: NULL
REMARK   3
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER
REMARK   3   SPECIAL CASE: NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2GVE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAY-06.
REMARK 100 THE RCSB ID CODE IS RCSB037594.
REMARK 230
REMARK 230 EXPERIMENTAL DETAILS
REMARK 230  EXPERIMENT TYPE                : NEUTRON DIFFRACTION
REMARK 230  DATE OF DATA COLLECTION        : 15-SEP-03
REMARK 230  TEMPERATURE           (KELVIN) : 293.0
REMARK 230  PH                             : 8.00
REMARK 230  NUMBER OF CRYSTALS USED        : 2
REMARK 230
REMARK 230  NEUTRON SOURCE                 : NULL
REMARK 230  BEAMLINE                       : NULL
REMARK 230  WAVELENGTH OR RANGE        (A) : 0.7-7.0
REMARK 230  MONOCHROMATOR                  : CHOPPER
REMARK 230  OPTICS                         : NULL
REMARK 230
REMARK 230  DETECTOR TYPE                  : AREA DETECTOR
REMARK 230  DETECTOR MANUFACTURER          : TIME-OF-FLIGHT MULTIWIRE HE3
REMARK 230                                   NEUTRON DETECTOR
REMARK 230  INTENSITY-INTEGRATION SOFTWARE : IN-HOUSE SOFTWARE
REMARK 230  DATA SCALING SOFTWARE          : D*TREK MODIFIED FOR NEUTRON TIME
REMARK 230                                   -OF-FLIGHT LAUE
REMARK 230
REMARK 230  NUMBER OF UNIQUE REFLECTIONS   : 34394
REMARK 230  RESOLUTION RANGE HIGH      (A) : 1.800
REMARK 230  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 230  REJECTION CRITERIA  (SIGMA(I)) : 1.500
REMARK 230
REMARK 230 OVERALL.
REMARK 230  COMPLETENESS FOR RANGE     (%) : 78.0
REMARK 230  DATA REDUNDANCY                : NULL
REMARK 230  R MERGE                    (I) : NULL
REMARK 230  R SYM                      (I) : 0.18500
REMARK 230   FOR THE DATA SET  : NULL
REMARK 230
REMARK 230 IN THE HIGHEST RESOLUTION SHELL.
REMARK 230  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 230  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.94
REMARK 230  COMPLETENESS FOR SHELL     (%) : 39.0
REMARK 230  DATA REDUNDANCY IN SHELL       : NULL
REMARK 230  R MERGE FOR SHELL          (I) : NULL
REMARK 230  R SYM FOR SHELL            (I) : 0.26200
REMARK 230   FOR SHELL         : NULL
REMARK 230
REMARK 230 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 230 SOFTWARE USED : SHELXL-97
REMARK 230 STARTING MODEL: 1XIB
REMARK 230
REMARK 230 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 55.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM TRIS-HCL,38%AMSO4,2MM MN2+ AND
REMARK 280  2MM CO2+,XI @ 125MG/ML, PH 8.0, LIQUID DIFFUSION, TEMPERATURE 293K
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       46.94000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       49.84000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       51.45000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       46.94000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       49.84000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       51.45000
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       46.94000
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       49.84000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       51.45000
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       46.94000
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       49.84000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       51.45000
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 300 REMARK: HOMO-TETRAMER CONSISTING OF SUBUNITS RELATED BY
REMARK 300 CRYSTALLOGRAPHIC 222 SYMMETRY
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 32780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 45560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -300.0 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       93.88000
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000       99.68000
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   3 -1.000000  0.000000  0.000000       93.88000
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000      102.90000
REMARK 350   BIOMT1   4  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000       99.68000
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000      102.90000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 O    DOD A3335  LIES ON A SPECIAL POSITION.
REMARK 375 O    DOD A1094  LIES ON A SPECIAL POSITION.
REMARK 375 O    DOD A1279  LIES ON A SPECIAL POSITION.
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   OD2  ASP A   156     D2   DOD A  1250              1.33
REMARK 500   O    LEU A    58     D1   DOD A  1204              1.34
REMARK 500   D1   DOD A  1220     O    DOD A  1285              1.37
REMARK 500   O    PRO A    60     HG   SER A    63              1.38
REMARK 500   O    PRO A    60     DG   SER A    63              1.38
REMARK 500   OE2  GLU A   128     D2   DOD A  3038              1.40
REMARK 500   O    ILE A    59     D1   DOD A  1133              1.41
REMARK 500   O    DOD A  1163     D1   DOD A  1282              1.41
REMARK 500   O    GLY A    62     D1   DOD A  3025              1.43
REMARK 500   OD1  ASP A   264     D2   DOD A  1058              1.43
REMARK 500   OD2  ASP A   110     D2   DOD A  1287              1.43
REMARK 500   D1   DOD A  1285     O    DOD A  1341              1.44
REMARK 500   O    PHE A   242     D2   DOD A  2010              1.44
REMARK 500   O    DOD A  1223     D1   DOD A  1229              1.45
REMARK 500   OD2  ASP A   163     D1   DOD A  1228              1.48
REMARK 500   O    TRP A   270     D1   DOD A  1114              1.49
REMARK 500   OD2  ASP A   264     D1   DOD A  1008              1.50
REMARK 500   D2   DOD A  1228     O    DOD A  1271              1.50
REMARK 500   O    DOD A  1059     D1   DOD A  1105              1.51
REMARK 500   D1   DOD A  1315     O    DOD A  1316              1.51
REMARK 500   O    GLY A    14     HG1  THR A    17              1.52
REMARK 500   O    GLY A    14     DG1  THR A    17              1.52
REMARK 500   O    DOD A  1091     D1   DOD A  1131              1.53
REMARK 500   O    ILE A   252     D1   DOD A  1172              1.54
REMARK 500   D2   DOD A  1078     O    DOD A  1088              1.54
REMARK 500   D1   DOD A  1076     O    DOD A  1193              1.55
REMARK 500   OD2  ASP A   381     D2   DOD A  1127              1.55
REMARK 500   O    DOD A  1009     D1   DOD A  1291              1.55
REMARK 500   O    ARG A   157     D2   DOD A  1048              1.56
REMARK 500   O    LEU A    34     D2   DOD A  1206              1.57
REMARK 500   O    DOD A  1108     D1   DOD A  1206              1.57
REMARK 500   OE1  GLN A   249     D1   DOD A  1021              1.57
REMARK 500   OE2  GLU A   358     D1   DOD A  1360              1.58
REMARK 500   O    DOD A  1348     D1   DOD A  3191              1.58
REMARK 500   D2   DOD A  1221     O    DOD A  3309              1.60
REMARK 500   O    PHE A   162     HH   TYR A   212              1.60
REMARK 500   O    PHE A   162     DH   TYR A   212              1.60
REMARK 500   O    PRO A    60     OG   SER A    63              2.12
REMARK 500   O    ASP A   273     OG   SER A   277              2.17
REMARK 500
REMARK 500 REMARK: NULL
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   OD2  ASP A    28     D2   DOD A  1208     3656     1.25
REMARK 500   OD2  ASP A   336     D1   DOD A  1032     7556     1.38
REMARK 500   D2   DOD A  1063     D1   DOD A  1092     4566     1.43
REMARK 500   O    DOD A  1212     D1   DOD A  1323     2665     1.55
REMARK 500   D2   DOD A  1063     O    DOD A  1092     4566     1.57
REMARK 500   O    PRO A    25     D2   DOD A  1303     3656     1.59
REMARK 500   D2   DOD A  1041     O    DOD A  1056     4566     1.59
REMARK 500   O    PHE A   372     D2   DOD A  1071     3656     1.60
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION
REMARK 500    TYR A   3   C     GLN A   4   N       0.200
REMARK 500    GLU A  70   CB    GLU A  70   CG      0.154
REMARK 500    GLU A  70   CD    GLU A  70   OE1     0.112
REMARK 500    GLU A  70   CD    GLU A  70   OE2     0.191
REMARK 500    GLU A 132   CD    GLU A 132   OE1     0.108
REMARK 500    ARG A 340   CZ    ARG A 340   NH2     0.078
REMARK 500    GLU A 359   CD    GLU A 359   OE1     0.237
REMARK 500    GLU A 359   CD    GLU A 359   OE2     0.121
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    ARG A  23   NE  -  CZ  -  NH1 ANGL. DEV. =   5.3 DEGREES
REMARK 500    ARG A  42   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES
REMARK 500    GLU A  67   CG  -  CD  -  OE2 ANGL. DEV. = -12.5 DEGREES
REMARK 500    ARG A  68   CD  -  NE  -  CZ  ANGL. DEV. = -11.5 DEGREES
REMARK 500    ARG A  68   NH1 -  CZ  -  NH2 ANGL. DEV. = -12.4 DEGREES
REMARK 500    ARG A  68   NE  -  CZ  -  NH2 ANGL. DEV. =   9.7 DEGREES
REMARK 500    ARG A  74   NE  -  CZ  -  NH1 ANGL. DEV. =   6.4 DEGREES
REMARK 500    ARG A  74   NE  -  CZ  -  NH2 ANGL. DEV. =  -9.6 DEGREES
REMARK 500    ARG A  76   NH1 -  CZ  -  NH2 ANGL. DEV. =   7.3 DEGREES
REMARK 500    ARG A  76   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.3 DEGREES
REMARK 500    ARG A 113   NE  -  CZ  -  NH1 ANGL. DEV. =   5.2 DEGREES
REMARK 500    ARG A 113   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.4 DEGREES
REMARK 500    ARG A 117   NE  -  CZ  -  NH1 ANGL. DEV. =   5.1 DEGREES
REMARK 500    ARG A 121   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES
REMARK 500    ARG A 121   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.2 DEGREES
REMARK 500    ARG A 152   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES
REMARK 500    ARG A 152   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES
REMARK 500    ARG A 157   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES
REMARK 500    ARG A 188   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES
REMARK 500    ARG A 188   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES
REMARK 500    ARG A 205   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES
REMARK 500    ARG A 208   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES
REMARK 500    ARG A 208   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.7 DEGREES
REMARK 500    TYR A 212   CB  -  CG  -  CD1 ANGL. DEV. =  -4.3 DEGREES
REMARK 500    ARG A 259   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES
REMARK 500    ARG A 266   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES
REMARK 500    ARG A 266   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.1 DEGREES
REMARK 500    ARG A 284   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES
REMARK 500    ARG A 284   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.7 DEGREES
REMARK 500    ARG A 292   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.1 DEGREES
REMARK 500    ARG A 316   NE  -  CZ  -  NH1 ANGL. DEV. =   5.9 DEGREES
REMARK 500    ARG A 316   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.7 DEGREES
REMARK 500    ARG A 331   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.5 DEGREES
REMARK 500    ARG A 334   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES
REMARK 500    ARG A 340   CD  -  NE  -  CZ  ANGL. DEV. =   9.5 DEGREES
REMARK 500    ARG A 340   NE  -  CZ  -  NH1 ANGL. DEV. =  12.7 DEGREES
REMARK 500    ARG A 340   NE  -  CZ  -  NH2 ANGL. DEV. = -10.8 DEGREES
REMARK 500    ARG A 354   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES
REMARK 500    ARG A 354   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.4 DEGREES
REMARK 500    ARG A 368   NE  -  CZ  -  NH1 ANGL. DEV. =   5.6 DEGREES
REMARK 500    ARG A 368   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.6 DEGREES
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      -80.22    -66.64
REMARK 500    PHE A  94      -30.91   -135.62
REMARK 500    GLU A 186      124.93     77.79
REMARK 500    ASN A 215       76.68   -117.47
REMARK 500    ASN A 247     -165.93   -179.07
REMARK 500    LYS A 253     -169.42    170.81
REMARK 500    PRO A 341      151.68    -49.90
REMARK 500    PHE A 357      -67.84   -150.68
REMARK 500    ALA A 386       71.41   -116.19
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    ARG A  41         0.15    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    DOD A1178        DISTANCE =  5.50 ANGSTROMS
REMARK 525    DOD A1258        DISTANCE =  5.29 ANGSTROMS
REMARK 525    DOD A1282        DISTANCE =  5.16 ANGSTROMS
REMARK 525    DOD A2018        DISTANCE =  5.27 ANGSTROMS
REMARK 525    DOD A2031        DISTANCE =  5.06 ANGSTROMS
REMARK 525    DOD A3030        DISTANCE =  8.66 ANGSTROMS
REMARK 525    DOD A3057        DISTANCE =  8.41 ANGSTROMS
REMARK 525    DOD A3065        DISTANCE =  6.29 ANGSTROMS
REMARK 525    DOD A3099        DISTANCE =  6.74 ANGSTROMS
REMARK 525    DOD A3104        DISTANCE = 10.34 ANGSTROMS
REMARK 525    DOD A3108        DISTANCE =  7.77 ANGSTROMS
REMARK 525    DOD A3109        DISTANCE =  7.92 ANGSTROMS
REMARK 525    DOD A3113        DISTANCE = 10.34 ANGSTROMS
REMARK 525    DOD A3115        DISTANCE = 10.33 ANGSTROMS
REMARK 525    DOD A3117        DISTANCE =  6.22 ANGSTROMS
REMARK 525    DOD A3133        DISTANCE =  5.58 ANGSTROMS
REMARK 525    DOD A3142        DISTANCE =  5.68 ANGSTROMS
REMARK 525    DOD A3147        DISTANCE =  6.41 ANGSTROMS
REMARK 525    DOD A3149        DISTANCE =  7.06 ANGSTROMS
REMARK 525    DOD A3160        DISTANCE =  7.54 ANGSTROMS
REMARK 525    DOD A3166        DISTANCE =  5.91 ANGSTROMS
REMARK 525    DOD A3195        DISTANCE = 18.32 ANGSTROMS
REMARK 525    DOD A3196        DISTANCE = 23.53 ANGSTROMS
REMARK 525    DOD A3199        DISTANCE = 26.04 ANGSTROMS
REMARK 525    DOD A3202        DISTANCE = 33.61 ANGSTROMS
REMARK 525    DOD A3204        DISTANCE = 37.86 ANGSTROMS
REMARK 525    DOD A3209        DISTANCE = 38.82 ANGSTROMS
REMARK 525    DOD A3217        DISTANCE =  7.20 ANGSTROMS
REMARK 525    DOD A3224        DISTANCE =  6.19 ANGSTROMS
REMARK 525    DOD A3227        DISTANCE =  5.72 ANGSTROMS
REMARK 525    DOD A3232        DISTANCE =  5.28 ANGSTROMS
REMARK 525    DOD A3234        DISTANCE =  7.19 ANGSTROMS
REMARK 525    DOD A3235        DISTANCE = 10.68 ANGSTROMS
REMARK 525    DOD A3236        DISTANCE = 11.02 ANGSTROMS
REMARK 525    DOD A3238        DISTANCE = 14.41 ANGSTROMS
REMARK 525    DOD A3241        DISTANCE = 15.43 ANGSTROMS
REMARK 525    DOD A3243        DISTANCE =  7.81 ANGSTROMS
REMARK 525    DOD A3244        DISTANCE =  6.75 ANGSTROMS
REMARK 525    DOD A3245        DISTANCE =  5.80 ANGSTROMS
REMARK 525    DOD A3248        DISTANCE =  6.50 ANGSTROMS
REMARK 525    DOD A3255        DISTANCE = 15.10 ANGSTROMS
REMARK 525    DOD A3257        DISTANCE = 13.90 ANGSTROMS
REMARK 525    DOD A3259        DISTANCE = 16.64 ANGSTROMS
REMARK 525    DOD A3262        DISTANCE = 13.99 ANGSTROMS
REMARK 525    DOD A3263        DISTANCE = 11.21 ANGSTROMS
REMARK 525    DOD A3266        DISTANCE = 12.03 ANGSTROMS
REMARK 525    DOD A3268        DISTANCE = 19.01 ANGSTROMS
REMARK 525    DOD A3271        DISTANCE =  8.73 ANGSTROMS
REMARK 525    DOD A3276        DISTANCE = 17.83 ANGSTROMS
REMARK 525    DOD A3281        DISTANCE =  5.41 ANGSTROMS
REMARK 525    DOD A3285        DISTANCE = 13.41 ANGSTROMS
REMARK 525    DOD A3286        DISTANCE = 16.04 ANGSTROMS
REMARK 525    DOD A3287        DISTANCE = 18.08 ANGSTROMS
REMARK 525    DOD A3288        DISTANCE = 15.36 ANGSTROMS
REMARK 525    DOD A3289        DISTANCE = 12.93 ANGSTROMS
REMARK 525    DOD A3290        DISTANCE =  8.93 ANGSTROMS
REMARK 525    DOD A3291        DISTANCE =  7.23 ANGSTROMS
REMARK 525    DOD A3303        DISTANCE = 11.33 ANGSTROMS
REMARK 525    DOD A3305        DISTANCE = 11.07 ANGSTROMS
REMARK 525    DOD A3306        DISTANCE = 10.30 ANGSTROMS
REMARK 525    DOD A3322        DISTANCE =  5.10 ANGSTROMS
REMARK 525    DOD A3323        DISTANCE =  5.28 ANGSTROMS
REMARK 525    DOD A3325        DISTANCE =  7.16 ANGSTROMS
REMARK 525    DOD A3329        DISTANCE = 12.59 ANGSTROMS
REMARK 525    DOD A3331        DISTANCE = 11.41 ANGSTROMS
REMARK 525    DOD A3335        DISTANCE =  8.04 ANGSTROMS
REMARK 525    DOD A3338        DISTANCE =  5.78 ANGSTROMS
REMARK 525    DOD A3351        DISTANCE =  6.84 ANGSTROMS
REMARK 525    DOD A3360        DISTANCE =  5.57 ANGSTROMS
REMARK 525    DOD A3381        DISTANCE =  8.38 ANGSTROMS
REMARK 525    DOD A3385        DISTANCE =  7.40 ANGSTROMS
REMARK 525    DOD A3391        DISTANCE =  5.74 ANGSTROMS
REMARK 525    DOD A3402        DISTANCE =  5.29 ANGSTROMS
REMARK 525    DOD A3403        DISTANCE = 12.36 ANGSTROMS
REMARK 525    DOD A3413        DISTANCE = 21.52 ANGSTROMS
REMARK 525    DOD A3414        DISTANCE =  5.69 ANGSTROMS
REMARK 525    DOD A3417        DISTANCE = 16.52 ANGSTROMS
REMARK 525    DOD A3418        DISTANCE =  8.11 ANGSTROMS
REMARK 525    DOD A3430        DISTANCE = 16.85 ANGSTROMS
REMARK 525    DOD A3431        DISTANCE = 13.80 ANGSTROMS
REMARK 525    DOD A3435        DISTANCE = 16.88 ANGSTROMS
REMARK 525    DOD A3437        DISTANCE =  8.03 ANGSTROMS
REMARK 525    DOD A3485        DISTANCE = 17.60 ANGSTROMS
REMARK 525    DOD A3486        DISTANCE =  9.83 ANGSTROMS
REMARK 525    DOD A3487        DISTANCE =  7.37 ANGSTROMS
REMARK 525    DOD A3489        DISTANCE =  7.76 ANGSTROMS
REMARK 525    DOD A3490        DISTANCE =  9.32 ANGSTROMS
REMARK 525    DOD A3491        DISTANCE = 13.02 ANGSTROMS
REMARK 525    DOD A3492        DISTANCE =  5.51 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                              CO A 391  CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 181   OE2
REMARK 620 2 GLU A 217   OE1  93.7
REMARK 620 3 ASP A 245   OD2  96.8 116.7
REMARK 620 4 ASP A 287   OD2 161.5  91.5  96.6
REMARK 620 5 DOD A1116   O    72.5 114.5 128.2  89.2
REMARK 620 6 DOD A1218   O   102.1 163.0  67.9  71.5  65.5
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CO A 390  CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 217   OE2
REMARK 620 2 ASP A 255   OD2 151.4
REMARK 620 3 ASP A 257   OD1  91.5 101.6
REMARK 620 4 DOD A1018   O    97.7 106.5  94.1
REMARK 620 N                    1     2     3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO A 390
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO A 391
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1XIB   RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF XYLOSE ISOMERASE USED FOR STARTING
REMARK 900 NEUTRON REFINEMENT
REMARK 900 RELATED ID: 2GLK   RELATED DB: PDB
REMARK 900 0.94 ANGSTROM X-RAY STRUCTURE OF XYLOSE ISOMERASE AT 100K
REMARK 900 RELATED ID: 2GUB   RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF METAL FREE XYLOSE ISOMERASE
DBREF  2GVE A    2   388  UNP    P24300   XYLA_STRRU       1    387
SEQADV 2GVE MET A    1  UNP  P24300              INITIATING METHIONINE
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     CO  A 390       1
HET     CO  A 391       1
HETNAM      CO COBALT (II) ION
FORMUL   2   CO    2(CO 2+)
FORMUL   4  DOD   *512(D2 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  GLY A   47  1                                  13
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  GLY A  130  1                                  23
HELIX    8   8 ASP A  150  GLY A  173  1                                  24
HELIX    9   9 THR A  195  GLU A  204  1                                  10
HELIX   10  10 ARG A  208  GLU A  210  5                                   3
HELIX   11  11 GLU A  217  MET A  223  1                                   7
HELIX   12  12 ASN A  227  ALA A  238  1                                  12
HELIX   13  13 ASP A  264  GLY A  279  1                                  16
HELIX   14  14 ASP A  295  ASP A  323  1                                  29
HELIX   15  15 ASP A  323  SER A  333  1                                  11
HELIX   16  16 ASP A  336  ARG A  340  5                                   5
HELIX   17  17 GLY A  346  ASP A  352  1                                   7
HELIX   18  18 ASP A  353  PHE A  357  5                                   5
HELIX   19  19 ASP A  361  ARG A  368  1                                   8
HELIX   20  20 ALA A  371  LEU A  384  1                                  14
SHEET    1   A 8 TYR A 212  VAL A 214  0
SHEET    2   A 8 ARG A 177  ILE A 180  1  N  PHE A 178   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 MET A  88  THR A  90  1  N  ALA A  89   O  THR A 133
SHEET    5   A 8 GLY A  50  HIS A  54  1  N  PHE A  53   O  THR A  90
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  ARG A 284   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         OE2 GLU A 181                CO    CO A 391     1555   1555  2.00
LINK         OE1 GLU A 217                CO    CO A 391     1555   1555  1.99
LINK         OE2 GLU A 217                CO    CO A 390     1555   1555  2.09
LINK         OD2 ASP A 245                CO    CO A 391     1555   1555  2.48
LINK         OD2 ASP A 255                CO    CO A 390     1555   1555  1.94
LINK         OD1 ASP A 257                CO    CO A 390     1555   1555  2.20
LINK         OD2 ASP A 287                CO    CO A 391     1555   1555  2.05
LINK        CO    CO A 390                 O   DOD A1018     1555   1555  1.97
LINK        CO    CO A 391                 O   DOD A1116     1555   1555  2.47
LINK        CO    CO A 391                 O   DOD A1218     1555   1555  2.22
CISPEP   1 GLU A  186    PRO A  187          0         2.70
SITE     1 AC1  5 GLU A 217  HIS A 220  ASP A 255  ASP A 257
SITE     2 AC1  5 DOD A1018
SITE     1 AC2  6 GLU A 181  GLU A 217  ASP A 245  ASP A 287
SITE     2 AC2  6 DOD A1116  DOD A1218
CRYST1   93.880   99.680  102.900  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      0.010652  0.000000  0.000000        0.00000
SCALE2      0.000000  0.010032  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009718        0.00000
      
PROCHECK
Go to PROCHECK summary
 References