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PDBsum entry 3eqa

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Hydrolase PDB id
3eqa
Jmol
Contents
Protein chain
458 a.a.
Ligands
NAG-NAG-BMA-MAN
NAG-NAG-BMA-MAN-
MAN-MAN-MAN-MAN
MAN ×7
TRS
GOL
Waters ×390
HEADER    HYDROLASE                               30-SEP-08   3EQA
TITLE     CATALYTIC DOMAIN OF GLUCOAMYLASE FROM ASPERGILLUS NIGER COMPLEXED WITH
TITLE    2 TRIS AND GLYCEROL
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: GLUCOAMYLASE;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: CATALYTIC DOMAIN (RESIDUES 25-494);
COMPND   5 SYNONYM: GLUCAN 1,4-ALPHA-GLUCOSIDASE; 1,4-ALPHA-D-GLUCAN
COMPND   6 GLUCOHYDROLASE;
COMPND   7 EC: 3.2.1.3;
COMPND   8 OTHER_DETAILS: PREPARED BY SUBTILISIN C-TERMINAL CLEAVAGE, COMPLEXED
COMPND   9 WITH TRIS AND GLYCEROL
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ASPERGILLUS NIGER;
SOURCE   3 ORGANISM_TAXID: 5061;
SOURCE   4 OTHER_DETAILS: GENE GLAA
KEYWDS    HYDROLASE, GLYCOPROTEIN, GLYCOSIDASE, POLYSACCHARIDE DEGRADATION
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.LEE,M.PAETZEL
REVDAT   4   13-JUL-11 3EQA    1       VERSN
REVDAT   3   16-FEB-11 3EQA    1       JRNL
REVDAT   2   09-FEB-11 3EQA    1       JRNL
REVDAT   1   13-OCT-09 3EQA    0
JRNL        AUTH   J.LEE,M.PAETZEL
JRNL        TITL   STRUCTURE OF THE CATALYTIC DOMAIN OF GLUCOAMYLASE FROM
JRNL        TITL 2 ASPERGILLUS NIGER.
JRNL        REF    ACTA CRYSTALLOGR.,SECT.F      V.  67   188 2011
JRNL        REFN                   ESSN 1744-3091
JRNL        PMID   21301084
JRNL        DOI    10.1107/S1744309110049390
REMARK   2
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.0
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELYHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.5
REMARK   3   NUMBER OF REFLECTIONS             : 33439
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) : 0.184
REMARK   3   R VALUE            (WORKING SET) : 0.181
REMARK   3   FREE R VALUE                     : 0.229
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.300
REMARK   3   FREE R VALUE TEST SET COUNT      : 1762
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95
REMARK   3   REFLECTION IN BIN     (WORKING SET) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 67.72
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2330
REMARK   3   BIN FREE R VALUE SET COUNT          : 67
REMARK   3   BIN FREE R VALUE                    : 0.2770
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3474
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 235
REMARK   3   SOLVENT ATOMS            : 390
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.86
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.41000
REMARK   3    B22 (A**2) : -1.73000
REMARK   3    B33 (A**2) : 1.32000
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      : NULL
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  NULL ; 0.009 ;  NULL
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  NULL ; 1.150 ;  NULL
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  NULL ; 0.076 ;  NULL
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  NULL ; 0.004 ;  NULL
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ; 0.186 ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ; 0.304 ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
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):  NULL ; 0.119 ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ; 0.131 ;  NULL
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):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL
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 : NULL
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : NULL
REMARK   3   ION PROBE RADIUS   : NULL
REMARK   3   SHRINKAGE RADIUS   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 3EQA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-OCT-08.
REMARK 100 THE RCSB ID CODE IS RCSB049641.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 28-AUG-05
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 8.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ALS
REMARK 200  BEAMLINE                       : 8.2.2
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL, SI(111)
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35298
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.5
REMARK 200  DATA REDUNDANCY                : 4.400
REMARK 200  R MERGE                    (I) : 0.07600
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 21.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97
REMARK 200  COMPLETENESS FOR SHELL     (%) : 71.6
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.29200
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3GLY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 45.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM TRIS-ACETATE (PH 8.5), 22.5 %
REMARK 280  PEG 6000, 0.4 M SODIUM ACETATE, 10 % GLYCEROL, VAPOR DIFFUSION,
REMARK 280  SITTING DROP, 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       28.91300
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       53.39650
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.61100
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       53.39650
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.91300
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       36.61100
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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     ALA A    25
REMARK 465     THR A    26
REMARK 465     LEU A    27
REMARK 465     ASP A    28
REMARK 465     SER A    29
REMARK 465     THR A   488
REMARK 465     SER A   489
REMARK 465     TRP A   490
REMARK 465     PRO A   491
REMARK 465     SER A   492
REMARK 465     ILE A   493
REMARK 465     VAL A   494
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    TYR A 171       58.13    -93.94
REMARK 500    SER A 232     -153.40   -117.99
REMARK 500    ASN A 271      -51.24    -29.94
REMARK 500    ASN A 337      -11.14     85.76
REMARK 500    SER A 423     -169.40    -78.61
REMARK 500    SER A 435     -154.34     61.50
REMARK 500    ALA A 466       41.60   -148.49
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 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 551
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 552
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 553
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 554
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 555
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 556
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 571
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 572
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 801
DBREF  3EQA A   25   494  UNP    P69328   AMYG_ASPNG      25    494
SEQRES   1 A  470  ALA THR LEU ASP SER TRP LEU SER ASN GLU ALA THR VAL
SEQRES   2 A  470  ALA ARG THR ALA ILE LEU ASN ASN ILE GLY ALA ASP GLY
SEQRES   3 A  470  ALA TRP VAL SER GLY ALA ASP SER GLY ILE VAL VAL ALA
SEQRES   4 A  470  SER PRO SER THR ASP ASN PRO ASP TYR PHE TYR THR TRP
SEQRES   5 A  470  THR ARG ASP SER GLY LEU VAL LEU LYS THR LEU VAL ASP
SEQRES   6 A  470  LEU PHE ARG ASN GLY ASP THR SER LEU LEU SER THR ILE
SEQRES   7 A  470  GLU ASN TYR ILE SER ALA GLN ALA ILE VAL GLN GLY ILE
SEQRES   8 A  470  SER ASN PRO SER GLY ASP LEU SER SER GLY ALA GLY LEU
SEQRES   9 A  470  GLY GLU PRO LYS PHE ASN VAL ASP GLU THR ALA TYR THR
SEQRES  10 A  470  GLY SER TRP GLY ARG PRO GLN ARG ASP GLY PRO ALA LEU
SEQRES  11 A  470  ARG ALA THR ALA MET ILE GLY PHE GLY GLN TRP LEU LEU
SEQRES  12 A  470  ASP ASN GLY TYR THR SER THR ALA THR ASP ILE VAL TRP
SEQRES  13 A  470  PRO LEU VAL ARG ASN ASP LEU SER TYR VAL ALA GLN TYR
SEQRES  14 A  470  TRP ASN GLN THR GLY TYR ASP LEU TRP GLU GLU VAL ASN
SEQRES  15 A  470  GLY SER SER PHE PHE THR ILE ALA VAL GLN HIS ARG ALA
SEQRES  16 A  470  LEU VAL GLU GLY SER ALA PHE ALA THR ALA VAL GLY SER
SEQRES  17 A  470  SER CYS SER TRP CYS ASP SER GLN ALA PRO GLU ILE LEU
SEQRES  18 A  470  CYS TYR LEU GLN SER PHE TRP THR GLY SER PHE ILE LEU
SEQRES  19 A  470  ALA ASN PHE ASP SER SER ARG SER GLY LYS ASP ALA ASN
SEQRES  20 A  470  THR LEU LEU GLY SER ILE HIS THR PHE ASP PRO GLU ALA
SEQRES  21 A  470  ALA CYS ASP ASP SER THR PHE GLN PRO CYS SER PRO ARG
SEQRES  22 A  470  ALA LEU ALA ASN HIS LYS GLU VAL VAL ASP SER PHE ARG
SEQRES  23 A  470  SER ILE TYR THR LEU ASN ASP GLY LEU SER ASP SER GLU
SEQRES  24 A  470  ALA VAL ALA VAL GLY ARG TYR PRO GLU ASP THR TYR TYR
SEQRES  25 A  470  ASN GLY ASN PRO TRP PHE LEU CYS THR LEU ALA ALA ALA
SEQRES  26 A  470  GLU GLN LEU TYR ASP ALA LEU TYR GLN TRP ASP LYS GLN
SEQRES  27 A  470  GLY SER LEU GLU VAL THR ASP VAL SER LEU ASP PHE PHE
SEQRES  28 A  470  LYS ALA LEU TYR SER ASP ALA ALA THR GLY THR TYR SER
SEQRES  29 A  470  SER SER SER SER THR TYR SER SER ILE VAL ASP ALA VAL
SEQRES  30 A  470  LYS THR PHE ALA ASP GLY PHE VAL SER ILE VAL GLU THR
SEQRES  31 A  470  HIS ALA ALA SER ASN GLY SER MET SER GLU GLN TYR ASP
SEQRES  32 A  470  LYS SER ASP GLY GLU GLN LEU SER ALA ARG ASP LEU THR
SEQRES  33 A  470  TRP SER TYR ALA ALA LEU LEU THR ALA ASN ASN ARG ARG
SEQRES  34 A  470  ASN SER VAL VAL PRO ALA SER TRP GLY GLU THR SER ALA
SEQRES  35 A  470  SER SER VAL PRO GLY THR CYS ALA ALA THR SER ALA ILE
SEQRES  36 A  470  GLY THR TYR SER SER VAL THR VAL THR SER TRP PRO SER
SEQRES  37 A  470  ILE VAL
MODRES 3EQA ASN A  195  ASN  GLYCOSYLATION SITE
MODRES 3EQA ASN A  419  ASN  GLYCOSYLATION SITE
MODRES 3EQA SER A  467  SER  GLYCOSYLATION SITE
MODRES 3EQA SER A  468  SER  GLYCOSYLATION SITE
MODRES 3EQA THR A  476  THR  GLYCOSYLATION SITE
MODRES 3EQA SER A  477  SER  GLYCOSYLATION SITE
MODRES 3EQA SER A  483  SER  GLYCOSYLATION SITE
MODRES 3EQA SER A  484  SER  GLYCOSYLATION SITE
MODRES 3EQA THR A  486  THR  GLYCOSYLATION SITE
HET    NAG  A 501      14
HET    NAG  A 502      14
HET    BMA  A 503      11
HET    MAN  A 504      11
HET    NAG  A 551      14
HET    NAG  A 552      14
HET    BMA  A 553      11
HET    MAN  A 554      11
HET    MAN  A 555      11
HET    MAN  A 556      11
HET    MAN  A 571      11
HET    MAN  A 572      11
HET    MAN  A 600      11
HET    MAN  A 601      11
HET    MAN  A 602      11
HET    MAN  A 603      11
HET    MAN  A 604      11
HET    MAN  A 605      11
HET    MAN  A 606      11
HET    TRS  A 701       8
HET    GOL  A 801       6
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     BMA BETA-D-MANNOSE
HETNAM     MAN ALPHA-D-MANNOSE
HETNAM     TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETNAM     GOL GLYCEROL
HETSYN     TRS TRIS BUFFER
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   2  NAG    4(C8 H15 N O6)
FORMUL   2  BMA    2(C6 H12 O6)
FORMUL   2  MAN    13(C6 H12 O6)
FORMUL  11  TRS    C4 H12 N O3 1+
FORMUL  12  GOL    C3 H8 O3
FORMUL  13  HOH   *390(H2 O)
HELIX    1   1 TRP A   30  ASN A   45  1                                  16
HELIX    2   2 THR A   77  ASN A   93  1                                  17
HELIX    3   3 ASP A   95  SER A   97  5                                   3
HELIX    4   4 LEU A   98  GLN A  113  1                                  16
HELIX    5   5 GLY A  125  GLU A  130  5                                   6
HELIX    6   6 ARG A  149  ASN A  169  1                                  21
HELIX    7   7 TYR A  171  ILE A  178  1                                   8
HELIX    8   8 ILE A  178  TRP A  194  1                                  17
HELIX    9   9 PHE A  210  VAL A  230  1                                  21
HELIX   10  10 CYS A  234  GLN A  249  1                                  16
HELIX   11  11 SER A  250  TRP A  252  5                                   3
HELIX   12  12 ASP A  269  THR A  279  1                                  11
HELIX   13  13 ASP A  287  PHE A  291  5                                   5
HELIX   14  14 SER A  295  SER A  308  1                                  14
HELIX   15  15 TYR A  313  ASP A  317  5                                   5
HELIX   16  16 THR A  334  GLY A  338  5                                   5
HELIX   17  17 TRP A  341  GLY A  363  1                                  23
HELIX   18  18 SER A  371  TYR A  379  1                                   9
HELIX   19  19 SER A  391  ALA A  416  1                                  26
HELIX   20  20 LEU A  439  ASN A  454  1                                  16
HELIX   21  21 GLY A  462  ALA A  466  5                                   5
SHEET    1   A 3 THR A  75  TRP A  76  0
SHEET    2   A 3 LYS A 132  ASN A 134 -1  O  PHE A 133   N  THR A  75
SHEET    3   A 3 THR A 138  ALA A 139 -1  O  THR A 138   N  ASN A 134
SHEET    1   B 3 GLY A 198  TYR A 199  0
SHEET    2   B 3 ASN A 206  SER A 209 -1  O  GLY A 207   N  GLY A 198
SHEET    3   B 3 ASN A 260  PHE A 261 -1  O  PHE A 261   N  SER A 208
SHEET    1   C 2 SER A 364  VAL A 367  0
SHEET    2   C 2 GLY A 385  SER A 388 -1  O  TYR A 387   N  LEU A 365
SHEET    1   D 2 GLN A 425  TYR A 426  0
SHEET    2   D 2 GLN A 433  LEU A 434 -1  O  LEU A 434   N  GLN A 425
SSBOND   1 CYS A  234    CYS A  237                          1555   1555  2.05
SSBOND   2 CYS A  246    CYS A  473                          1555   1555  2.03
SSBOND   3 CYS A  286    CYS A  294                          1555   1555  2.05
LINK         ND2 ASN A 195                 C1  NAG A 501     1555   1555  1.45
LINK         ND2 ASN A 419                 C1  NAG A 551     1555   1555  1.44
LINK         O4  NAG A 501                 C1  NAG A 502     1555   1555  1.43
LINK         O4  NAG A 502                 C1  BMA A 503     1555   1555  1.44
LINK         O3  BMA A 503                 C1  MAN A 504     1555   1555  1.44
LINK         O4  NAG A 551                 C1  NAG A 552     1555   1555  1.44
LINK         O4  NAG A 552                 C1  BMA A 553     1555   1555  1.44
LINK         O3  BMA A 553                 C1  MAN A 554     1555   1555  1.44
LINK         O6  BMA A 553                 C1  MAN A 571     1555   1555  1.44
LINK         O2  MAN A 554                 C1  MAN A 555     1555   1555  1.45
LINK         O2  MAN A 555                 C1  MAN A 556     1555   1555  1.44
LINK         O3  MAN A 571                 C1  MAN A 572     1555   1555  1.45
LINK         OG  SER A 467                 C1  MAN A 600     1555   1555  1.44
LINK         OG  SER A 468                 C1  MAN A 601     1555   1555  1.45
LINK         OG1 THR A 476                 C1  MAN A 602     1555   1555  1.45
LINK         OG  SER A 477                 C1  MAN A 603     1555   1555  1.44
LINK         OG  SER A 483                 C1  MAN A 604     1555   1555  1.44
LINK         OG  SER A 484                 C1  MAN A 605     1555   1555  1.45
LINK         OG1 THR A 486                 C1  MAN A 606     1555   1555  1.45
CISPEP   1 GLY A   47    ALA A   48          0         3.68
CISPEP   2 ASN A   69    PRO A   70          0         3.21
CISPEP   3 ARG A  146    PRO A  147          0        -4.10
CISPEP   4 PHE A  261    ASP A  262          0        -6.32
SITE     1 AC1  9 ASN A 195  THR A 197  TYR A 247  NAG A 502
SITE     2 AC1  9 HOH A1047  HOH A1085  HOH A1105  HOH A1148
SITE     3 AC1  9 HOH A1185
SITE     1 AC2  5 CYS A 473  NAG A 501  BMA A 503  HOH A1223
SITE     2 AC2  5 HOH A1373
SITE     1 AC3  3 NAG A 502  MAN A 504  HOH A1383
SITE     1 AC4  5 SER A 250  TRP A 252  PHE A 261  BMA A 503
SITE     2 AC4  5 HOH A1351
SITE     1 AC5  7 VAL A  37  TRP A  52  ASN A 419  SER A 421
SITE     2 AC5  7 ASP A 438  NAG A 552  HOH A1290
SITE     1 AC6 10 ARG A 437  NAG A 551  BMA A 553  MAN A 571
SITE     2 AC6 10 MAN A 572  HOH A1107  HOH A1171  HOH A1179
SITE     3 AC6 10 HOH A1290  HOH A1377
SITE     1 AC7  5 NAG A 552  MAN A 554  MAN A 571  HOH A1256
SITE     2 AC7  5 HOH A1331
SITE     1 AC8  3 BMA A 553  MAN A 555  HOH A1340
SITE     1 AC9  8 VAL A  53  SER A  54  PRO A  65  PHE A  73
SITE     2 AC9  8 MAN A 554  MAN A 556  HOH A1161  HOH A1340
SITE     1 BC1  1 MAN A 555
SITE     1 BC2  4 NAG A 552  BMA A 553  MAN A 572  HOH A1240
SITE     1 BC3  8 SER A  66  ASN A  69  SER A 435  ARG A 437
SITE     2 BC3  8 NAG A 552  MAN A 571  HOH A1146  HOH A1229
SITE     1 BC4  9 ASP A 287  GLU A 463  THR A 464  SER A 465
SITE     2 BC4  9 ALA A 466  SER A 467  SER A 468  HOH A1221
SITE     3 BC4  9 HOH A1232
SITE     1 BC5  2 SER A 468  PRO A 470
SITE     1 BC6  4 THR A 476  SER A 477  MAN A 603  HOH A1296
SITE     1 BC7  4 SER A 477  MAN A 602  HOH A1079  HOH A1272
SITE     1 BC8  9 ARG A 184  ASP A 369  SER A 483  SER A 484
SITE     2 BC8  9 MAN A 606  HOH A1238  HOH A1258  HOH A1300
SITE     3 BC8  9 HOH A1338
SITE     1 BC9  6 ALA A 110  ILE A 111  GLY A 114  SER A 484
SITE     2 BC9  6 VAL A 485  HOH A1167
SITE     1 CC1  6 ASP A 369  VAL A 370  SER A 484  THR A 486
SITE     2 CC1  6 MAN A 604  HOH A1300
SITE     1 CC2  6 TRP A  76  ARG A  78  ASP A  79  LEU A 201
SITE     2 CC2  6 GLU A 203  GOL A 801
SITE     1 CC3  8 TYR A  72  SER A  97  TRP A 202  GLU A 203
SITE     2 CC3  8 GLU A 204  ARG A 329  TRS A 701  HOH A1420
CRYST1   57.826   73.222  106.793  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      0.017293  0.000000  0.000000        0.00000
SCALE2      0.000000  0.013657  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009364        0.00000
      
PROCHECK
Go to PROCHECK summary
 References