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PDBsum entry 1mz6

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Hydrolase, hydrolase inhibitor PDB id
1mz6
Jmol
Contents
Protein chain
620 a.a. *
Ligands
NAG ×5
DAN
Waters ×40
* Residue conservation analysis
HEADER    HYDROLASE, HYDROLASE INHIBITOR          05-OCT-02   1MZ6
TITLE     TRYPANOSOMA RANGELI SIALIDASE IN COMPLEX WITH THE INHIBITOR DANA
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: SIALIDASE;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: MATURE SIALIDASE;
COMPND   5 EC: 3.2.1.18
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: TRYPANOSOMA RANGELI;
SOURCE   3 ORGANISM_TAXID: 5698
KEYWDS    INIBITOR COMPLEX, TRYPANOSOMAL SIALIDASE, SIALYLTRANSFERASE,
KEYWDS   2 HYDROLASE, HYDROLASE INHIBITOR
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.BUSCHIAZZO,G.A.TAVARES,O.CAMPETELLA,S.SPINELLI,M.L.CREMONA,G.PARIS,
AUTHOR   2 M.F.AMAYA,A.C.C.FRASCH,P.M.ALZARI
REVDAT   3   13-JUL-11 1MZ6    1       VERSN
REVDAT   2   24-FEB-09 1MZ6    1       VERSN
REVDAT   1   16-OCT-02 1MZ6    0
JRNL        AUTH   A.BUSCHIAZZO,G.A.TAVARES,O.CAMPETELLA,S.SPINELLI,
JRNL        AUTH 2 M.L.CREMONA,G.PARIS,M.F.AMAYA,A.C.C.FRASCH,P.M.ALZARI
JRNL        TITL   STRUCTURAL BASIS OF SIALYLTRANSFERASE ACTIVITY IN
JRNL        TITL 2 TRYPANOSOMAL SIALIDASES
JRNL        REF    EMBO J.                       V.  19    16 2000
JRNL        REFN                   ISSN 0261-4189
JRNL        PMID   10619840
JRNL        DOI    10.1093/EMBOJ/19.1.16
REMARK   2
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3
REMARK   3   NUMBER OF REFLECTIONS             : 16159
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.209
REMARK   3   R VALUE            (WORKING SET) : 0.205
REMARK   3   FREE R VALUE                     : 0.287
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 869
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.90
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.97
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1031
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2320
REMARK   3   BIN FREE R VALUE SET COUNT          : 59
REMARK   3   BIN FREE R VALUE                    : 0.3670
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4759
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 90
REMARK   3   SOLVENT ATOMS            : 40
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.26
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.46000
REMARK   3    B22 (A**2) : -0.32000
REMARK   3    B33 (A**2) : -0.15000
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  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.900
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.776
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4961 ; 0.017 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6751 ; 2.395 ; 1.954
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   617 ; 4.585 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   828 ;23.086 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   767 ; 0.143 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3739 ; 0.007 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2544 ; 0.283 ; 0.300
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   528 ; 0.173 ; 0.500
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    31 ; 0.288 ; 0.300
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     1 ; 0.075 ; 0.500
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3065 ; 0.594 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4936 ; 1.121 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1896 ; 1.818 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1815 ; 3.041 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.40
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1MZ6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-OCT-02.
REMARK 100 THE RCSB ID CODE IS RCSB017320.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 27-NOV-97
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : LURE
REMARK 200  BEAMLINE                       : D41A
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.375
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17063
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900
REMARK 200  RESOLUTION RANGE LOW       (A) : 15.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9
REMARK 200  DATA REDUNDANCY                : 6.600
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.13800
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.98
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.30600
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: UNLIGANDED T. RANGELI SIALIDASE 1MZ5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 54.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG-8000, AMMONIUM SULFATE,
REMARK 280  MORPHOLINOETHANESULFONATE, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280  TEMPERATURE 293K
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       38.10000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       52.65000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       46.90000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       52.65000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       38.10000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       46.90000
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: MONOMERIC
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 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     THR A   404
REMARK 465     PRO A   405
REMARK 465     PRO A   406
REMARK 465     SER A   407
REMARK 465     LYS A   408
REMARK 465     GLY A   409
REMARK 465     GLY A   410
REMARK 465     ARG A   591
REMARK 465     SER A   592
REMARK 465     LYS A   593
REMARK 465     ASP A   631
REMARK 465     GLY A   632
REMARK 465     GLY A   633
REMARK 465     ALA A   634
REMARK 465     GLY A   635
REMARK 465     THR A   636
REMARK 465     ALA A   637
REMARK 465     ALA A   638
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     SER A  23    OG
REMARK 470     ARG A  28    CG   CD   NE   CZ   NH1  NH2
REMARK 470     VAL A  31    CG1  CG2
REMARK 470     GLN A 123    CG   CD   OE1  NE2
REMARK 470     ARG A 125    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS A 156    CG   CD   CE   NZ
REMARK 470     GLU A 167    CG   CD   OE1  OE2
REMARK 470     ASN A 391    CG   OD1
REMARK 470     GLU A 541    CG   CD   OE1  OE2
REMARK 470     LYS A 545    CG   CD   CE   NZ
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   7   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES
REMARK 500    ARG A   7   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES
REMARK 500    ARG A  36   NE  -  CZ  -  NH2 ANGL. DEV. =   3.2 DEGREES
REMARK 500    ASP A  60   CB  -  CG  -  OD2 ANGL. DEV. =   8.6 DEGREES
REMARK 500    ASP A 129   CB  -  CG  -  OD1 ANGL. DEV. =  -5.4 DEGREES
REMARK 500    ASP A 129   CB  -  CG  -  OD2 ANGL. DEV. =   8.5 DEGREES
REMARK 500    ASP A 213   CB  -  CG  -  OD2 ANGL. DEV. =   6.4 DEGREES
REMARK 500    ARG A 246   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES
REMARK 500    ASP A 285   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES
REMARK 500    ARG A 299   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.3 DEGREES
REMARK 500    ASP A 316   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES
REMARK 500    ASP A 350   CB  -  CG  -  OD2 ANGL. DEV. =   6.3 DEGREES
REMARK 500    ASP A 351   CB  -  CG  -  OD2 ANGL. DEV. =   7.4 DEGREES
REMARK 500    ASP A 390   CB  -  CG  -  OD2 ANGL. DEV. =   6.5 DEGREES
REMARK 500    CYS A 411   CA  -  CB  -  SG  ANGL. DEV. =   7.3 DEGREES
REMARK 500    ASP A 492   CB  -  CG  -  OD2 ANGL. DEV. =   6.3 DEGREES
REMARK 500    LEU A 494   CA  -  CB  -  CG  ANGL. DEV. =  20.5 DEGREES
REMARK 500    LEU A 542   CA  -  CB  -  CG  ANGL. DEV. =  16.7 DEGREES
REMARK 500    LEU A 542   CB  -  CG  -  CD1 ANGL. DEV. = -10.5 DEGREES
REMARK 500    ASP A 554   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 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    LYS A  14       27.18     47.15
REMARK 500    ASN A  15      -49.59   -140.14
REMARK 500    ASN A  24       36.02    -91.14
REMARK 500    ASN A  61       44.64    -91.80
REMARK 500    SER A  62     -166.73   -117.10
REMARK 500    SER A  90     -174.78   -173.50
REMARK 500    LYS A 116       -6.05   -143.28
REMARK 500    ALA A 143     -140.77   -120.07
REMARK 500    ALA A 144      168.72    167.73
REMARK 500    ASN A 145       98.10    -43.04
REMARK 500    LYS A 147      100.36    179.23
REMARK 500    LYS A 174      -68.76   -100.93
REMARK 500    VAL A 180      124.39     91.35
REMARK 500    ALA A 183     -157.86   -105.71
REMARK 500    ASP A 213       48.67   -145.56
REMARK 500    GLU A 238       63.25     23.75
REMARK 500    ALA A 267       50.87    -65.13
REMARK 500    THR A 270      -78.79   -145.24
REMARK 500    SER A 281       10.23     56.73
REMARK 500    ARG A 312     -127.90     56.65
REMARK 500    ARG A 317       75.30     53.28
REMARK 500    GLN A 326      -61.26   -126.54
REMARK 500    SER A 341     -119.67    -95.63
REMARK 500    CYS A 397       97.70    -69.36
REMARK 500    SER A 425     -119.65   -119.98
REMARK 500    CYS A 439      -53.28   -123.83
REMARK 500    ASN A 446       57.61     33.12
REMARK 500    ASN A 457      115.29   -163.43
REMARK 500    VAL A 467      -97.14   -113.95
REMARK 500    ALA A 479      -36.06    -29.67
REMARK 500    TYR A 481      -63.73    -95.63
REMARK 500    ASP A 511       47.70   -143.91
REMARK 500    ARG A 523       33.88     77.43
REMARK 500    LEU A 542      137.18    -22.99
REMARK 500    HIS A 543      -23.73     84.44
REMARK 500    ASP A 554       42.84     30.91
REMARK 500    ASP A 598       74.83   -112.03
REMARK 500    ASN A 605       72.00     49.50
REMARK 500    ASN A 610       36.77    -90.13
REMARK 500    LEU A 613      150.56    -47.42
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    LYS A 116        23.7      L          L   OUTSIDE RANGE
REMARK 500    TRP A 121        24.4      L          L   OUTSIDE RANGE
REMARK 500    VAL A 192        24.2      L          L   OUTSIDE RANGE
REMARK 500    ILE A 628        24.1      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 651
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 652
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 653
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 654
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 655
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAN A 700
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1MZ5   RELATED DB: PDB
REMARK 900 TRYPANOSOMA RANGELI SIALIDASE
REMARK 900 RELATED ID: 1MR5   RELATED DB: PDB
REMARK 900 ORTHORHOMBIC FORM OF TRYPANOSOMA CRUZI TRANS-SIALIDASE
REMARK 900 RELATED ID: 1MS0   RELATED DB: PDB
REMARK 900 MONOCLINIC FORM OF TRYPANOSOMA CRUZI TRANS-SIALIDASE, IN
REMARK 900 COMPLEX WITH 3-DEOXY-2,3-DEHYDRO-N-ACETYLNEURAMINIC ACID
REMARK 900 (DANA)AND LACTOSE
REMARK 900 RELATED ID: 1MS1   RELATED DB: PDB
REMARK 900 MONOCLINIC FORM OF TRYPANOSOMA CRUZI TRANS-SIALIDASE, IN
REMARK 900 COMPLEX WITH 3-DEOXY-2,3-DEHYDRO-N-ACETYLNEURAMINIC ACID
REMARK 900 (DANA)
REMARK 900 RELATED ID: 1MS3   RELATED DB: PDB
REMARK 900 MONOCLINIC FORM OF TRYPANOSOMA CRUZI TRANS-SIALIDASE
REMARK 900 RELATED ID: 1MS4   RELATED DB: PDB
REMARK 900 TRICLINIC FORM OF TRYPANOSOMA CRUZI TRANS-SIALIDASE
REMARK 900 RELATED ID: 1MS5   RELATED DB: PDB
REMARK 900 TRICLINIC FORM OF TRYPANOSOMA CRUZI TRANS-SIALIDASE, SOAKED
REMARK 900 WITH N-ACETYLNEURAMINYL-A-2,3-THIO-GALACTOSIDE (NA-S-GAL)
REMARK 900 RELATED ID: 1MS8   RELATED DB: PDB
REMARK 900 TRICLINIC FORM OF TRYPANOSOMA CRUZI TRANS-SIALIDASE, IN
REMARK 900 COMPLEX WITH 3-DEOXY-2,3-DEHYDRO-N-ACETYLNEURAMINIC ACID
REMARK 900 (DANA)
REMARK 900 RELATED ID: 1MS9   RELATED DB: PDB
REMARK 900 TRICLINIC FORM OF TRYPANOSOMA CRUZI TRANS-SIALIDASE, IN
REMARK 900 COMPLEX WITH LACTOSE
DBREF  1MZ6 A    1   638  UNP    O44049   O44049_TRYRA    23    660
SEQADV 1MZ6 VAL A  177  UNP  O44049    ILE   199 CONFLICT
SEQRES   1 A  638  LEU ALA PRO GLY SER SER ARG VAL GLU LEU PHE LYS ARG
SEQRES   2 A  638  LYS ASN SER THR VAL PRO PHE GLU GLU SER ASN GLY THR
SEQRES   3 A  638  ILE ARG GLU ARG VAL VAL HIS SER PHE ARG ILE PRO THR
SEQRES   4 A  638  ILE VAL ASN VAL ASP GLY VAL MET VAL ALA THR ALA ASP
SEQRES   5 A  638  ALA ARG TYR GLU THR SER PHE ASP ASN SER PHE ILE GLU
SEQRES   6 A  638  THR ALA VAL LYS TYR SER VAL ASP ASP GLY ALA THR TRP
SEQRES   7 A  638  ASN THR GLN ILE ALA ILE LYS ASN SER ARG ALA SER SER
SEQRES   8 A  638  VAL SER ARG VAL MET ASP ALA THR VAL ILE VAL LYS GLY
SEQRES   9 A  638  ASN LYS LEU TYR ILE LEU VAL GLY SER PHE ASN LYS THR
SEQRES  10 A  638  ARG ASN SER TRP THR GLN HIS ARG ASP GLY SER ASP TRP
SEQRES  11 A  638  GLU PRO LEU LEU VAL VAL GLY GLU VAL THR LYS SER ALA
SEQRES  12 A  638  ALA ASN GLY LYS THR THR ALA THR ILE SER TRP GLY LYS
SEQRES  13 A  638  PRO VAL SER LEU LYS PRO LEU PHE PRO ALA GLU PHE ASP
SEQRES  14 A  638  GLY ILE LEU THR LYS GLU PHE VAL GLY GLY VAL GLY ALA
SEQRES  15 A  638  ALA ILE VAL GLY SER ASN GLY ASN LEU VAL TYR PRO VAL
SEQRES  16 A  638  GLN ILE ALA ASP MET GLY GLY ARG VAL PHE THR LYS ILE
SEQRES  17 A  638  MET TYR SER GLU ASP ASP GLY ASN THR TRP LYS PHE ALA
SEQRES  18 A  638  GLU GLY ARG SER LYS PHE GLY CYS SER GLU PRO ALA VAL
SEQRES  19 A  638  LEU GLU TRP GLU GLY LYS LEU ILE ILE ASN ASN ARG VAL
SEQRES  20 A  638  ASP GLY ASN ARG ARG LEU VAL TYR GLU SER SER ASP MET
SEQRES  21 A  638  GLY LYS THR TRP VAL GLU ALA LEU GLY THR LEU SER HIS
SEQRES  22 A  638  VAL TRP THR ASN SER PRO THR SER ASN GLN GLN ASP CYS
SEQRES  23 A  638  GLN SER SER PHE VAL ALA VAL THR ILE GLU GLY LYS ARG
SEQRES  24 A  638  VAL MET LEU PHE THR HIS PRO LEU ASN LEU LYS GLY ARG
SEQRES  25 A  638  TRP MET ARG ASP ARG LEU HIS LEU TRP MET THR ASP ASN
SEQRES  26 A  638  GLN ARG ILE PHE ASP VAL GLY GLN ILE SER ILE GLY ASP
SEQRES  27 A  638  GLU ASN SER GLY TYR SER SER VAL LEU TYR LYS ASP ASP
SEQRES  28 A  638  LYS LEU TYR SER LEU HIS GLU ILE ASN THR ASN ASP VAL
SEQRES  29 A  638  TYR SER LEU VAL PHE VAL ARG PHE ILE GLY GLU LEU GLN
SEQRES  30 A  638  LEU MET LYS SER VAL VAL ARG THR TRP LYS GLU GLU ASP
SEQRES  31 A  638  ASN HIS LEU ALA SER ILE CYS THR PRO VAL VAL PRO ALA
SEQRES  32 A  638  THR PRO PRO SER LYS GLY GLY CYS GLY ALA ALA VAL PRO
SEQRES  33 A  638  THR ALA GLY LEU VAL GLY PHE LEU SER HIS SER ALA ASN
SEQRES  34 A  638  GLY SER VAL TRP GLU ASP VAL TYR ARG CYS VAL ASP ALA
SEQRES  35 A  638  ASN VAL ALA ASN ALA GLU ARG VAL PRO ASN GLY LEU LYS
SEQRES  36 A  638  PHE ASN GLY VAL GLY GLY GLY ALA VAL TRP PRO VAL ALA
SEQRES  37 A  638  ARG GLN GLY GLN THR ARG ARG TYR GLN PHE ALA ASN TYR
SEQRES  38 A  638  ARG PHE THR LEU VAL ALA THR VAL THR ILE ASP GLU LEU
SEQRES  39 A  638  PRO LYS GLY THR SER PRO LEU LEU GLY ALA GLY LEU GLU
SEQRES  40 A  638  GLY PRO GLY ASP ALA LYS LEU LEU GLY LEU SER TYR ASP
SEQRES  41 A  638  LYS ASN ARG GLN TRP ARG PRO LEU TYR GLY ALA ALA PRO
SEQRES  42 A  638  ALA SER PRO THR GLY SER TRP GLU LEU HIS LYS LYS TYR
SEQRES  43 A  638  HIS VAL VAL LEU THR MET ALA ASP ARG GLN GLY SER VAL
SEQRES  44 A  638  TYR VAL ASP GLY GLN PRO LEU ALA GLY SER GLY ASN THR
SEQRES  45 A  638  VAL VAL ARG GLY ALA THR LEU PRO ASP ILE SER HIS PHE
SEQRES  46 A  638  TYR ILE GLY GLY PRO ARG SER LYS GLY ALA PRO THR ASP
SEQRES  47 A  638  SER ARG VAL THR VAL THR ASN ILE VAL LEU TYR ASN ARG
SEQRES  48 A  638  ARG LEU ASN SER SER GLU ILE ARG THR LEU PHE LEU SER
SEQRES  49 A  638  GLN ASP MET ILE GLY THR ASP GLY GLY ALA GLY THR ALA
SEQRES  50 A  638  ALA
MODRES 1MZ6 ASN A   15  ASN  GLYCOSYLATION SITE
MODRES 1MZ6 ASN A   24  ASN  GLYCOSYLATION SITE
MODRES 1MZ6 ASN A  115  ASN  GLYCOSYLATION SITE
MODRES 1MZ6 ASN A  429  ASN  GLYCOSYLATION SITE
MODRES 1MZ6 ASN A  614  ASN  GLYCOSYLATION SITE
HET    NAG  A 651      14
HET    NAG  A 652      14
HET    NAG  A 653      14
HET    NAG  A 654      14
HET    NAG  A 655      14
HET    DAN  A 700      20
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     DAN 2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID
FORMUL   2  NAG    5(C8 H15 N O6)
FORMUL   7  DAN    C11 H17 N O8
FORMUL   8  HOH   *40(H2 O)
HELIX    1   1 SER A  120  HIS A  124  5                                   5
HELIX    2   2 LYS A  161  PHE A  164  5                                   4
HELIX    3   3 PHE A  372  ALA A  394  1                                  23
HELIX    4   4 ALA A  468  GLY A  471  5                                   4
HELIX    5   5 TYR A  476  TYR A  481  5                                   6
HELIX    6   6 ASN A  614  GLN A  625  1                                  12
SHEET    1   A 4 SER A   6  PHE A  11  0
SHEET    2   A 4 VAL A 364  ARG A 371 -1  O  LEU A 367   N  PHE A  11
SHEET    3   A 4 LEU A 353  THR A 361 -1  O  SER A 355   N  VAL A 370
SHEET    4   A 4 VAL A 346  TYR A 348 -1  N  LEU A 347   O  TYR A 354
SHEET    1   B 2 THR A  17  GLU A  21  0
SHEET    2   B 2 ILE A  27  VAL A  31 -1  N  ARG A  28   O  PHE A  20
SHEET    1   C 4 SER A  34  VAL A  43  0
SHEET    2   C 4 VAL A  46  ARG A  54 -1  N  VAL A  46   O  VAL A  43
SHEET    3   C 4 ILE A  64  SER A  71 -1  O  GLU A  65   N  ALA A  53
SHEET    4   C 4 GLN A  81  ILE A  84 -1  N  GLN A  81   O  VAL A  68
SHEET    1   D 7 THR A 151  TRP A 154  0
SHEET    2   D 7 TRP A 130  THR A 140 -1  N  GLU A 138   O  SER A 153
SHEET    3   D 7 VAL A 158  SER A 159 -1  O  VAL A 158   N  LEU A 134
SHEET    4   D 7 TRP A 130  THR A 140 -1  N  LEU A 134   O  VAL A 158
SHEET    5   D 7 LYS A 106  PHE A 114 -1  N  LEU A 107   O  GLY A 137
SHEET    6   D 7 ARG A  94  LYS A 103 -1  N  ARG A  94   O  PHE A 114
SHEET    7   D 7 GLY A 181  ALA A 182  1  N  GLY A 181   O  ALA A  98
SHEET    1   E 7 GLU A 167  PHE A 168  0
SHEET    2   E 7 ILE A 171  GLY A 178 -1  N  ILE A 171   O  PHE A 168
SHEET    3   E 7 LEU A 191  ASP A 199 -1  N  GLN A 196   O  VAL A 177
SHEET    4   E 7 ILE A 184  VAL A 185 -1  O  ILE A 184   N  VAL A 192
SHEET    5   E 7 LEU A 191  ASP A 199 -1  N  VAL A 192   O  ILE A 184
SHEET    6   E 7 VAL A 204  SER A 211 -1  O  PHE A 205   N  ILE A 197
SHEET    7   E 7 LYS A 219  PHE A 220 -1  O  LYS A 219   N  TYR A 210
SHEET    1   F 4 CYS A 229  TRP A 237  0
SHEET    2   F 4 LYS A 240  VAL A 247 -1  N  LYS A 240   O  TRP A 237
SHEET    3   F 4 VAL A 254  SER A 257 -1  O  TYR A 255   N  ILE A 243
SHEET    4   F 4 VAL A 265  GLU A 266 -1  N  VAL A 265   O  GLU A 256
SHEET    1   G 4 SER A 289  ILE A 295  0
SHEET    2   G 4 LYS A 298  PRO A 306 -1  O  LYS A 298   N  ILE A 295
SHEET    3   G 4 LEU A 318  THR A 323 -1  N  HIS A 319   O  HIS A 305
SHEET    4   G 4 ILE A 328  GLN A 333 -1  N  PHE A 329   O  MET A 322
SHEET    1   H17 TRP A 525  TYR A 529  0
SHEET    2   H17 LYS A 513  ASP A 520 -1  O  GLY A 516   N  LEU A 528
SHEET    3   H17 THR A 498  LEU A 506 -1  N  SER A 499   O  TYR A 519
SHEET    4   H17 ILE A 582  GLY A 588 -1  N  SER A 583   O  GLY A 505
SHEET    5   H17 GLY A 462  PRO A 466 -1  O  ALA A 463   N  ILE A 587
SHEET    6   H17 ALA A 442  ALA A 445 -1  N  ASN A 443   O  VAL A 464
SHEET    7   H17 VAL A 432  ASP A 435 -1  O  TRP A 433   N  ALA A 442
SHEET    8   H17 LEU A 420  ALA A 428 -1  N  SER A 425   O  GLU A 434
SHEET    9   H17 VAL A 601  TYR A 609 -1  O  ILE A 606   N  LEU A 424
SHEET   10   H17 GLY A 453  PHE A 456 -1  O  LEU A 454   N  VAL A 603
SHEET   11   H17 ALA A 447  VAL A 450 -1  O  GLU A 448   N  LYS A 455
SHEET   12   H17 GLY A 453  PHE A 456 -1  O  GLY A 453   N  VAL A 450
SHEET   13   H17 VAL A 601  TYR A 609 -1  O  VAL A 601   N  PHE A 456
SHEET   14   H17 PHE A 483  ILE A 491 -1  O  THR A 484   N  TYR A 609
SHEET   15   H17 TYR A 546  ALA A 553 -1  N  TYR A 546   O  VAL A 489
SHEET   16   H17 GLN A 556  VAL A 561 -1  N  GLN A 556   O  ALA A 553
SHEET   17   H17 GLN A 564  PRO A 565 -1  O  GLN A 564   N  VAL A 561
SSBOND   1 CYS A  397    CYS A  411                          1555   1555  1.98
LINK         ND2 ASN A  15                 C1  NAG A 654     1555   1555  1.46
LINK         ND2 ASN A  24                 C1  NAG A 655     1555   1555  1.42
LINK         ND2 ASN A 115                 C1  NAG A 653     1555   1555  1.47
LINK         ND2 ASN A 429                 C1  NAG A 652     1555   1555  1.44
LINK         ND2 ASN A 614                 C1  NAG A 651     1555   1555  1.43
SITE     1 AC1  3 ASN A 614  SER A 616  GLU A 617
SITE     1 AC2  4 ASN A 429  SER A 431  VAL A 432  GLU A 434
SITE     1 AC3  3 ASN A 115  SER A 128  GLU A 131
SITE     1 AC4  2 LYS A  12  ASN A  15
SITE     1 AC5  2 ASN A  24  THR A  26
SITE     1 AC6 11 ARG A  36  ARG A  54  ASP A  60  MET A  96
SITE     2 AC6 11 ASP A  97  TRP A 121  ARG A 246  ARG A 315
SITE     3 AC6 11 TYR A 343  HOH A 725  HOH A 737
CRYST1   76.200   93.800  105.300  90.00  90.00  90.00 P 21 21 21    4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013123  0.000000  0.000000        0.00000
SCALE2      0.000000  0.010661  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009497        0.00000
      
PROCHECK
Go to PROCHECK summary
 References