spacer
spacer

PDBsum entry 1n1t

Go to PDB code: 
Top Page protein ligands links
Hydrolase PDB id
1n1t
Jmol
Contents
Protein chain
628 a.a. *
Ligands
SO4 ×2
DAN
Waters ×661
* Residue conservation analysis
HEADER    HYDROLASE                               20-OCT-02   1N1T
TITLE     TRYPANOSOMA RANGELI SIALIDASE IN COMPLEX WITH DANA AT 1.6 A
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: SIALIDASE;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: RESIDUE 23-660;
COMPND   5 EC: 3.2.1.18;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: TRYPANOSOMA RANGELI;
SOURCE   3 ORGANISM_TAXID: 5698;
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: DH5ALPHA;
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PTRCHIS A
KEYWDS    BETA PROPELLER, LECTIN-LIKE FOLD, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    M.F.AMAYA,A.BUSCHIAZZO,T.NGUYEN,P.M.ALZARI
REVDAT   2   24-FEB-09 1N1T    1       VERSN
REVDAT   1   07-JAN-03 1N1T    0
JRNL        AUTH   M.F.AMAYA,A.BUSCHIAZZO,T.NGUYEN,P.M.ALZARI
JRNL        TITL   THE HIGH RESOLUTION STRUCTURES OF FREE AND
JRNL        TITL 2 INHIBITOR-BOUND TRYPANOSOMA RANGELI SIALIDASE AND
JRNL        TITL 3 ITS COMPARISON WITH T. CRUZI TRANS-SIALIDASE
JRNL        REF    J.MOL.BIOL.                   V. 325   773 2003
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   12507479
JRNL        DOI    10.1016/S0022-2836(02)01306-2
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   A.BUSCHIAZZO,G.A.TAVARES,O.CAMPETELLA,S.SPINELLI,
REMARK   1  AUTH 2 M.L.CREMONA,G.PARIS,M.F.AMAYA,A.C.FRASCH,P.M.ALZARI
REMARK   1  TITL   STRUCTURAL BASIS OF SIALYLTRANSFERASE ACTIVITY IN
REMARK   1  TITL 2 TRYPANOSOMAL SIALIDASES
REMARK   1  REF    EMBO J.                       V.  19    16 2000
REMARK   1  REFN                   ISSN 0261-4189
REMARK   1  DOI    10.1093/EMBOJ/19.1.16
REMARK   2
REMARK   2 RESOLUTION.    1.60 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) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.6
REMARK   3   NUMBER OF REFLECTIONS             : 90373
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) : 0.174
REMARK   3   R VALUE            (WORKING SET) : 0.173
REMARK   3   FREE R VALUE                     : 0.197
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 4771
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) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6560
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1780
REMARK   3   BIN FREE R VALUE SET COUNT          : 371
REMARK   3   BIN FREE R VALUE                    : 0.2040
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4831
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 30
REMARK   3   SOLVENT ATOMS            : 661
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.10
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.48000
REMARK   3    B22 (A**2) : 0.06000
REMARK   3    B33 (A**2) : -0.55000
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      : 0.957
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.947
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4962 ; 0.013 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6748 ; 1.610 ; 1.941
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   626 ; 5.373 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   849 ;15.459 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   757 ; 0.123 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3766 ; 0.007 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2287 ; 0.222 ; 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):   756 ; 0.128 ; 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):    30 ; 0.165 ; 0.300
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    24 ; 0.184 ; 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):  3106 ; 0.906 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5005 ; 1.637 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1856 ; 2.489 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1743 ; 3.909 ; 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 1N1T COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-NOV-02.
REMARK 100 THE RCSB ID CODE IS RCSB017412.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 31-JAN-01
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : ID14-4
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 95328
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.6
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.06600
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.63
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.4
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.19200
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: 1N1S
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 54.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG-8000, SODIUM CACODYLATE,
REMARK 280  AMMONIUM SULFATE, PH 7, VAPOR DIFFUSION, HANGING DROP,
REMARK 280  TEMPERATURE 291K
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       36.97250
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       53.25650
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       48.12900
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       53.25650
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.97250
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       48.12900
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   407
REMARK 465     PRO A   408
REMARK 465     PRO A   409
REMARK 465     SER A   410
REMARK 465     LYS A   411
REMARK 465     GLY A   412
REMARK 465     GLY A   635
REMARK 465     GLY A   636
REMARK 465     ALA A   637
REMARK 465     GLY A   638
REMARK 465     THR A   639
REMARK 465     ALA A   640
REMARK 465     ALA A   641
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  26    OG
REMARK 470     GLN A 126    CG   CD   OE1  NE2
REMARK 470     ARG A 128    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU A 170    CG   CD   OE1  OE2
REMARK 470     ASP A 634    CG   OD1  OD2
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  1077     O    HOH A  1249     4445     2.19
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 254   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.5 DEGREES
REMARK 500    ARG A 254   NE  -  CZ  -  NH2 ANGL. DEV. =   6.2 DEGREES
REMARK 500    ASP A 353   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 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    ASN A  18      -66.27   -163.18
REMARK 500    LYS A 119       -1.21   -144.81
REMARK 500    ASN A 148       70.89     25.87
REMARK 500    ASP A 172       77.50     -1.74
REMARK 500    LYS A 177      -61.65   -123.30
REMARK 500    VAL A 183      131.38     86.36
REMARK 500    ALA A 186     -161.70   -104.01
REMARK 500    GLU A 234       63.11     30.76
REMARK 500    THR A 273      -77.67   -138.95
REMARK 500    ARG A 315     -132.39     48.71
REMARK 500    ARG A 320       66.52     68.89
REMARK 500    GLN A 329      -67.24   -132.19
REMARK 500    SER A 344     -126.14   -111.35
REMARK 500    SER A 428     -128.66   -138.11
REMARK 500    ASN A 432     -158.06   -138.01
REMARK 500    VAL A 470      -94.21   -116.65
REMARK 500    LEU A 504      -50.03   -128.02
REMARK 500    ASN A 613       32.47    -94.11
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 SO4 A 801
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 802
REMARK 800 SITE_IDENTIFIER: AC3
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: 1MZ6   RELATED DB: PDB
REMARK 900 NATURAL (GLYCOSYLATED) SIALIDASE FROM TRYPANOSOMA RANGELI
REMARK 900 RELATED ID: 1MZ5   RELATED DB: PDB
REMARK 900 NATURAL (GLYCOSYLATED) SIALIDASE FROM TRYPANOSOMA RANGELI
REMARK 900 IN COMPLEX WITH THE INHIBITOR DANA
REMARK 900 RELATED ID: 1N1S   RELATED DB: PDB
REMARK 900 TRYPANOSOMA RANGELI SIALIDASE
REMARK 900 RELATED ID: 1N1V   RELATED DB: PDB
REMARK 900 TRYPANOSOMA RANGELI SIALIDASE IN COMPLEX WITH DANA
REMARK 900 RELATED ID: 1N1Y   RELATED DB: PDB
REMARK 900 TRYPANOSOMA RANGELI SIALIDASE IN COMPLEX WITH SIALIC ACID
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE AUTHOR MAINTAINS THAT THE SEQUENCE IN
REMARK 999 THE SEQUENCE DATABASE IS INCORRECT
DBREF  1N1T A    4   641  UNP    O44049   O44049_TRYRA    23    660
SEQADV 1N1T ALA A    1  UNP  O44049              CLONING ARTIFACT
SEQADV 1N1T ALA A    2  UNP  O44049              CLONING ARTIFACT
SEQADV 1N1T SER A    3  UNP  O44049              CLONING ARTIFACT
SEQADV 1N1T ILE A   53  UNP  O44049    THR    72 SEE REMARK 999
SEQADV 1N1T VAL A  180  UNP  O44049    ILE   199 SEE REMARK 999
SEQADV 1N1T ALA A  189  UNP  O44049    GLY   208 SEE REMARK 999
SEQADV 1N1T LEU A  375  UNP  O44049    PHE   394 SEE REMARK 999
SEQADV 1N1T VAL A  609  UNP  O44049    ILE   628 SEE REMARK 999
SEQRES   1 A  641  ALA ALA SER LEU ALA PRO GLY SER SER ARG VAL GLU LEU
SEQRES   2 A  641  PHE LYS ARG LYS ASN SER THR VAL PRO PHE GLU GLU SER
SEQRES   3 A  641  ASN GLY THR ILE ARG GLU ARG VAL VAL HIS SER PHE ARG
SEQRES   4 A  641  ILE PRO THR ILE VAL ASN VAL ASP GLY VAL MET VAL ALA
SEQRES   5 A  641  ILE ALA ASP ALA ARG TYR GLU THR SER PHE ASP ASN SER
SEQRES   6 A  641  PHE ILE GLU THR ALA VAL LYS TYR SER VAL ASP ASP GLY
SEQRES   7 A  641  ALA THR TRP ASN THR GLN ILE ALA ILE LYS ASN SER ARG
SEQRES   8 A  641  ALA SER SER VAL SER ARG VAL MET ASP ALA THR VAL ILE
SEQRES   9 A  641  VAL LYS GLY ASN LYS LEU TYR ILE LEU VAL GLY SER PHE
SEQRES  10 A  641  ASN LYS THR ARG ASN SER TRP THR GLN HIS ARG ASP GLY
SEQRES  11 A  641  SER ASP TRP GLU PRO LEU LEU VAL VAL GLY GLU VAL THR
SEQRES  12 A  641  LYS SER ALA ALA ASN GLY LYS THR THR ALA THR ILE SER
SEQRES  13 A  641  TRP GLY LYS PRO VAL SER LEU LYS PRO LEU PHE PRO ALA
SEQRES  14 A  641  GLU PHE ASP GLY ILE LEU THR LYS GLU PHE VAL GLY GLY
SEQRES  15 A  641  VAL GLY ALA ALA ILE VAL ALA SER ASN GLY ASN LEU VAL
SEQRES  16 A  641  TYR PRO VAL GLN ILE ALA ASP MET GLY GLY ARG VAL PHE
SEQRES  17 A  641  THR LYS ILE MET TYR SER GLU ASP ASP GLY ASN THR TRP
SEQRES  18 A  641  LYS PHE ALA GLU GLY ARG SER LYS PHE GLY CYS SER GLU
SEQRES  19 A  641  PRO ALA VAL LEU GLU TRP GLU GLY LYS LEU ILE ILE ASN
SEQRES  20 A  641  ASN ARG VAL ASP GLY ASN ARG ARG LEU VAL TYR GLU SER
SEQRES  21 A  641  SER ASP MET GLY LYS THR TRP VAL GLU ALA LEU GLY THR
SEQRES  22 A  641  LEU SER HIS VAL TRP THR ASN SER PRO THR SER ASN GLN
SEQRES  23 A  641  GLN ASP CYS GLN SER SER PHE VAL ALA VAL THR ILE GLU
SEQRES  24 A  641  GLY LYS ARG VAL MET LEU PHE THR HIS PRO LEU ASN LEU
SEQRES  25 A  641  LYS GLY ARG TRP MET ARG ASP ARG LEU HIS LEU TRP MET
SEQRES  26 A  641  THR ASP ASN GLN ARG ILE PHE ASP VAL GLY GLN ILE SER
SEQRES  27 A  641  ILE GLY ASP GLU ASN SER GLY TYR SER SER VAL LEU TYR
SEQRES  28 A  641  LYS ASP ASP LYS LEU TYR SER LEU HIS GLU ILE ASN THR
SEQRES  29 A  641  ASN ASP VAL TYR SER LEU VAL PHE VAL ARG LEU ILE GLY
SEQRES  30 A  641  GLU LEU GLN LEU MET LYS SER VAL VAL ARG THR TRP LYS
SEQRES  31 A  641  GLU GLU ASP ASN HIS LEU ALA SER ILE CYS THR PRO VAL
SEQRES  32 A  641  VAL PRO ALA THR PRO PRO SER LYS GLY GLY CYS GLY ALA
SEQRES  33 A  641  ALA VAL PRO THR ALA GLY LEU VAL GLY PHE LEU SER HIS
SEQRES  34 A  641  SER ALA ASN GLY SER VAL TRP GLU ASP VAL TYR ARG CYS
SEQRES  35 A  641  VAL ASP ALA ASN VAL ALA ASN ALA GLU ARG VAL PRO ASN
SEQRES  36 A  641  GLY LEU LYS PHE ASN GLY VAL GLY GLY GLY ALA VAL TRP
SEQRES  37 A  641  PRO VAL ALA ARG GLN GLY GLN THR ARG ARG TYR GLN PHE
SEQRES  38 A  641  ALA ASN TYR ARG PHE THR LEU VAL ALA THR VAL THR ILE
SEQRES  39 A  641  ASP GLU LEU PRO LYS GLY THR SER PRO LEU LEU GLY ALA
SEQRES  40 A  641  GLY LEU GLU GLY PRO GLY ASP ALA LYS LEU LEU GLY LEU
SEQRES  41 A  641  SER TYR ASP LYS ASN ARG GLN TRP ARG PRO LEU TYR GLY
SEQRES  42 A  641  ALA ALA PRO ALA SER PRO THR GLY SER TRP GLU LEU HIS
SEQRES  43 A  641  LYS LYS TYR HIS VAL VAL LEU THR MET ALA ASP ARG GLN
SEQRES  44 A  641  GLY SER VAL TYR VAL ASP GLY GLN PRO LEU ALA GLY SER
SEQRES  45 A  641  GLY ASN THR VAL VAL ARG GLY ALA THR LEU PRO ASP ILE
SEQRES  46 A  641  SER HIS PHE TYR ILE GLY GLY PRO ARG SER LYS GLY ALA
SEQRES  47 A  641  PRO THR ASP SER ARG VAL THR VAL THR ASN VAL VAL LEU
SEQRES  48 A  641  TYR ASN ARG ARG LEU ASN SER SER GLU ILE ARG THR LEU
SEQRES  49 A  641  PHE LEU SER GLN ASP MET ILE GLY THR ASP GLY GLY ALA
SEQRES  50 A  641  GLY THR ALA ALA
HET    SO4  A 801       5
HET    SO4  A 802       5
HET    DAN  A 700      20
HETNAM     SO4 SULFATE ION
HETNAM     DAN 2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID
FORMUL   2  SO4    2(O4 S 2-)
FORMUL   4  DAN    C11 H17 N O8
FORMUL   5  HOH   *661(H2 O)
HELIX    1   1 SER A  123  HIS A  127  5                                   5
HELIX    2   2 LYS A  164  PHE A  167  5                                   4
HELIX    3   3 LEU A  375  SER A  398  1                                  24
HELIX    4   4 ALA A  471  GLY A  474  5                                   4
HELIX    5   5 TYR A  479  ASN A  483  5                                   5
HELIX    6   6 ASN A  617  SER A  627  1                                  11
SHEET    1   A 4 SER A   9  PHE A  14  0
SHEET    2   A 4 VAL A 367  ARG A 374 -1  O  LEU A 370   N  PHE A  14
SHEET    3   A 4 LYS A 355  THR A 364 -1  O  SER A 358   N  VAL A 373
SHEET    4   A 4 SER A 347  LYS A 352 -1  O  SER A 348   N  LEU A 359
SHEET    1   B 2 THR A  20  GLU A  24  0
SHEET    2   B 2 ILE A  30  VAL A  34 -1  N  ARG A  31   O  PHE A  23
SHEET    1   C 4 SER A  37  VAL A  46  0
SHEET    2   C 4 VAL A  49  ARG A  57 -1  O  VAL A  49   N  VAL A  46
SHEET    3   C 4 ILE A  67  SER A  74 -1  O  GLU A  68   N  ALA A  56
SHEET    4   C 4 ASN A  82  ILE A  87 -1  O  ASN A  82   N  TYR A  73
SHEET    1   D 7 LYS A 150  TRP A 157  0
SHEET    2   D 7 TRP A 133  ALA A 147 -1  N  GLU A 141   O  SER A 156
SHEET    3   D 7 VAL A 161  SER A 162 -1  O  VAL A 161   N  LEU A 137
SHEET    4   D 7 TRP A 133  ALA A 147 -1  N  LEU A 137   O  VAL A 161
SHEET    5   D 7 LYS A 109  PHE A 117 -1  O  LEU A 110   N  GLY A 140
SHEET    6   D 7 ARG A  97  LYS A 106 -1  O  ARG A  97   N  PHE A 117
SHEET    7   D 7 GLY A 184  ALA A 185  1  O  GLY A 184   N  VAL A 103
SHEET    1   E 7 GLU A 170  PHE A 171  0
SHEET    2   E 7 ILE A 174  GLY A 181 -1  O  ILE A 174   N  PHE A 171
SHEET    3   E 7 LEU A 194  ASP A 202 -1  N  GLN A 199   O  VAL A 180
SHEET    4   E 7 ILE A 187  VAL A 188 -1  O  ILE A 187   N  VAL A 195
SHEET    5   E 7 LEU A 194  ASP A 202 -1  N  VAL A 195   O  ILE A 187
SHEET    6   E 7 VAL A 207  SER A 214 -1  O  PHE A 208   N  ILE A 200
SHEET    7   E 7 LYS A 222  PHE A 223 -1  N  LYS A 222   O  TYR A 213
SHEET    1   F 4 CYS A 232  TRP A 240  0
SHEET    2   F 4 LYS A 243  VAL A 250 -1  O  LYS A 243   N  TRP A 240
SHEET    3   F 4 VAL A 257  SER A 260 -1  O  TYR A 258   N  ILE A 246
SHEET    4   F 4 VAL A 268  GLU A 269 -1  O  VAL A 268   N  GLU A 259
SHEET    1   G 4 PHE A 293  ILE A 298  0
SHEET    2   G 4 LYS A 301  PRO A 309 -1  O  LYS A 301   N  ILE A 298
SHEET    3   G 4 LEU A 321  THR A 326 -1  N  HIS A 322   O  HIS A 308
SHEET    4   G 4 ILE A 331  GLN A 336 -1  N  PHE A 332   O  MET A 325
SHEET    1   H19 TRP A 528  TYR A 532  0
SHEET    2   H19 LYS A 516  ASP A 523 -1  O  GLY A 519   N  LEU A 531
SHEET    3   H19 THR A 501  LEU A 509 -1  N  SER A 502   O  TYR A 522
SHEET    4   H19 ILE A 585  GLY A 591 -1  N  SER A 586   O  GLY A 508
SHEET    5   H19 GLY A 465  PRO A 469 -1  N  ALA A 466   O  ILE A 590
SHEET    6   H19 ALA A 445  ALA A 448 -1  O  ASN A 446   N  VAL A 467
SHEET    7   H19 VAL A 435  ASP A 438 -1  N  TRP A 436   O  ALA A 445
SHEET    8   H19 LEU A 423  ALA A 431 -1  N  SER A 428   O  GLU A 437
SHEET    9   H19 VAL A 604  TYR A 612 -1  O  VAL A 609   N  LEU A 427
SHEET   10   H19 GLY A 456  PHE A 459 -1  O  LEU A 457   N  VAL A 606
SHEET   11   H19 ALA A 450  VAL A 453 -1  O  GLU A 451   N  LYS A 458
SHEET   12   H19 GLY A 456  PHE A 459 -1  O  GLY A 456   N  VAL A 453
SHEET   13   H19 VAL A 604  TYR A 612 -1  O  VAL A 604   N  PHE A 459
SHEET   14   H19 ARG A 485  ILE A 494 -1  O  THR A 487   N  TYR A 612
SHEET   15   H19 LYS A 548  ALA A 556 -1  O  TYR A 549   N  VAL A 492
SHEET   16   H19 GLN A 559  VAL A 564 -1  N  GLN A 559   O  ALA A 556
SHEET   17   H19 GLN A 567  PRO A 568 -1  O  GLN A 567   N  VAL A 564
SHEET   18   H19 GLN A 559  VAL A 564 -1  N  VAL A 564   O  GLN A 567
SHEET   19   H19 ASN A 574  THR A 575 -1  O  ASN A 574   N  GLY A 560
SSBOND   1 CYS A  400    CYS A  414                          1555   1555  2.06
SITE     1 AC1  5 ARG A 472  ARG A 594  SER A 595  LYS A 596
SITE     2 AC1  5 HOH A1223
SITE     1 AC2  3 ARG A 227  LYS A 229  PHE A 230
SITE     1 AC3 18 ARG A  39  ARG A  57  ASP A  63  MET A  99
SITE     2 AC3 18 ASP A 100  TRP A 124  ARG A 249  GLN A 287
SITE     3 AC3 18 ARG A 318  TYR A 346  HOH A 819  HOH A 836
SITE     4 AC3 18 HOH A 868  HOH A 882  HOH A 916  HOH A1011
SITE     5 AC3 18 HOH A1141  HOH A1228
CRYST1   73.945   96.258  106.513  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      0.013524  0.000000  0.000000        0.00000
SCALE2      0.000000  0.010389  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009389        0.00000
      
PROCHECK
Go to PROCHECK summary
 References