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PDBsum entry 1acz

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Polysaccharide degradation PDB id
1acz
Jmol
Contents
Protein chain
108 a.a.
Ligands
GLC-GLC-GLC-GLC-
GLC-GLC-GLC
×2
HEADER    POLYSACCHARIDE DEGRADATION              10-FEB-97   1ACZ
TITLE     GLUCOAMYLASE, GRANULAR STARCH-BINDING DOMAIN COMPLEX WITH
TITLE    2 CYCLODEXTRIN, NMR, 5 STRUCTURES
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: GLUCOAMYLASE;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: STARCH-BINDING DOMAIN, RESIDUES 509 - 616;
COMPND   5 SYNONYM: 1,4-ALPHA-D-GLUCAN GLUCOHYDROLASE;
COMPND   6 EC: 3.2.1.3;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ASPERGILLUS NIGER;
SOURCE   3 ORGANISM_TAXID: 5061;
SOURCE   4 STRAIN: AB4.1;
SOURCE   5 EXPRESSION_SYSTEM: ASPERGILLUS NIGER;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 5061;
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PIGF;
SOURCE   8 EXPRESSION_SYSTEM_GENE: GLAA
KEYWDS    HYDROLASE, STARCH BINDING DOMAIN, GLYCOSIDASE,
KEYWDS   2 POLYSACCHARIDE DEGRADATION, GLYCOPROTEIN, ALTERNATIVE
KEYWDS   3 SPLICING, SIGNAL
EXPDTA    SOLUTION NMR
NUMMDL    5
AUTHOR    K.SORIMACHI,M.-F.LE GAL-COEFFET,G.WILLIAMSON,D.B.ARCHER,
AUTHOR   2 M.P.WILLIAMSON
REVDAT   2   24-FEB-09 1ACZ    1       VERSN
REVDAT   1   07-JUL-97 1ACZ    0
JRNL        AUTH   K.SORIMACHI,M.F.LE GAL-COEFFET,G.WILLIAMSON,
JRNL        AUTH 2 D.B.ARCHER,M.P.WILLIAMSON
JRNL        TITL   SOLUTION STRUCTURE OF THE GRANULAR STARCH BINDING
JRNL        TITL 2 DOMAIN OF ASPERGILLUS NIGER GLUCOAMYLASE BOUND TO
JRNL        TITL 3 BETA-CYCLODEXTRIN.
JRNL        REF    STRUCTURE                     V.   5   647 1997
JRNL        REFN                   ISSN 0969-2126
JRNL        PMID   9195884
JRNL        DOI    10.1016/S0969-2126(97)00220-7
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   K.SORIMACHI,A.J.JACKS,M.F.LE GAL-COEFFET,
REMARK   1  AUTH 2 G.WILLIAMSON,D.B.ARCHER,M.P.WILLIAMSON
REMARK   1  TITL   SOLUTION STRUCTURE OF THE GRANULAR STARCH BINDING
REMARK   1  TITL 2 DOMAIN OF GLUCOAMYLASE FROM ASPERGILLUS NIGER BY
REMARK   1  TITL 3 NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY
REMARK   1  REF    J.MOL.BIOL.                   V. 259   970 1996
REMARK   1  REFN                   ISSN 0022-2836
REMARK   1 REFERENCE 2
REMARK   1  AUTH   A.J.JACKS,K.SORIMACHI,M.F.LE GAL-COEFFET,
REMARK   1  AUTH 2 G.WILLIAMSON,D.B.ARCHER,M.P.WILLIAMSON
REMARK   1  TITL   1H AND 15N ASSIGNMENTS AND SECONDARY STRUCTURE OF
REMARK   1  TITL 2 THE STARCH-BINDING DOMAIN OF GLUCOAMYLASE FROM
REMARK   1  TITL 3 ASPERGILLUS NIGER
REMARK   1  REF    EUR.J.BIOCHEM.                V. 233   568 1995
REMARK   1  REFN                   ISSN 0014-2956
REMARK   2
REMARK   2 RESOLUTION. NOT APPLICABLE.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.1
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1ACZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210  EXPERIMENT TYPE                : NMR
REMARK 210  TEMPERATURE           (KELVIN) : 310
REMARK 210  PH                             : 5.7
REMARK 210  IONIC STRENGTH                 : NULL
REMARK 210  PRESSURE                       : NULL
REMARK 210  SAMPLE CONTENTS                : NULL
REMARK 210
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 15N-EDITED TOCSY, NOESY
REMARK 210  SPECTROMETER FIELD STRENGTH    : 500 MHZ
REMARK 210  SPECTROMETER MODEL             : AMX 500
REMARK 210  SPECTROMETER MANUFACTURER      : BRUKER
REMARK 210
REMARK 210  STRUCTURE DETERMINATION.
REMARK 210   SOFTWARE USED                 : X-PLOR
REMARK 210   METHOD USED                   : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 5
REMARK 210 CONFORMERS, SELECTION CRITERIA  : RANDOM FROM 81 GOOD STRUCTURES
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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   O    GLY A   535     O    LEU A   540              2.14
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  5 TYR A 532   CB  -  CG  -  CD2 ANGL. DEV. =  -3.7 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  1 THR A 510       18.35   -143.48
REMARK 500  1 LEU A 521      119.47   -162.13
REMARK 500  1 ALA A 523       12.35   -149.72
REMARK 500  1 THR A 524      161.14     49.69
REMARK 500  1 THR A 525     -155.36   -144.32
REMARK 500  1 THR A 526       59.76   -154.76
REMARK 500  1 TYR A 527       29.56     37.64
REMARK 500  1 GLU A 529     -178.71    167.24
REMARK 500  1 LEU A 540       32.27    -98.39
REMARK 500  1 GLU A 544       91.43    168.55
REMARK 500  1 ASP A 547       35.00   -141.14
REMARK 500  1 TYR A 556     -131.04    -58.93
REMARK 500  1 THR A 557     -153.82    -76.91
REMARK 500  1 SER A 559      -75.99    -88.52
REMARK 500  1 ASP A 560       74.62    169.54
REMARK 500  1 TRP A 563       81.14     42.65
REMARK 500  1 VAL A 565      159.91    174.09
REMARK 500  1 THR A 566       89.75   -159.25
REMARK 500  1 GLU A 573     -158.26   -162.50
REMARK 500  1 ASP A 586       74.67     52.66
REMARK 500  1 SER A 587      110.89   -170.49
REMARK 500  1 TRP A 590       88.91    -41.81
REMARK 500  1 GLU A 591       94.05    -58.33
REMARK 500  1 PRO A 594     -165.94    -74.05
REMARK 500  1 VAL A 611       66.23   -160.11
REMARK 500  1 ASP A 613     -168.46   -163.90
REMARK 500  2 THR A 510      -53.53   -135.47
REMARK 500  2 LEU A 521       92.78   -162.40
REMARK 500  2 ALA A 523       31.80   -163.49
REMARK 500  2 THR A 524      164.01     53.44
REMARK 500  2 GLU A 529      159.24    172.68
REMARK 500  2 ASP A 542       -5.49     63.04
REMARK 500  2 ASP A 547       40.03   -146.67
REMARK 500  2 ALA A 553       82.12   -154.48
REMARK 500  2 TYR A 556      164.55    -45.25
REMARK 500  2 SER A 558     -107.73    -80.40
REMARK 500  2 TRP A 563      123.61     54.93
REMARK 500  2 TYR A 564     -158.83   -145.69
REMARK 500  2 VAL A 565      157.83    169.66
REMARK 500  2 THR A 566       89.15   -158.35
REMARK 500  2 LEU A 569       94.73   -160.93
REMARK 500  2 ALA A 571     -166.06   -162.26
REMARK 500  2 GLU A 573     -156.39   -162.85
REMARK 500  2 GLU A 583       -5.10     58.24
REMARK 500  2 ASP A 585      -73.02   -125.90
REMARK 500  2 ASP A 586      -62.47   -128.17
REMARK 500  2 SER A 587     -133.89   -123.39
REMARK 500  2 GLU A 591     -130.08   -100.27
REMARK 500  2 SER A 592       70.09     84.60
REMARK 500  2 ASN A 595     -174.66    -68.45
REMARK 500  2 THR A 606       34.67   -167.90
REMARK 500  2 VAL A 611       57.16   -160.71
REMARK 500  3 THR A 510      -60.25   -137.54
REMARK 500  3 PRO A 512       35.03    -80.87
REMARK 500  3 ALA A 523     -137.60   -144.41
REMARK 500  3 THR A 524      116.25    164.58
REMARK 500  3 THR A 525     -162.67   -162.06
REMARK 500  3 THR A 526      101.38    -45.61
REMARK 500  3 TYR A 527       89.47    -63.68
REMARK 500  3 GLU A 529     -158.72    -88.43
REMARK 500  3 LEU A 540       63.97   -119.00
REMARK 500  3 ASP A 542      -26.88     79.41
REMARK 500  3 GLU A 544       95.11    176.62
REMARK 500  3 ASP A 547       36.13   -145.06
REMARK 500  3 ASP A 554       82.79    -39.89
REMARK 500  3 TYR A 556     -165.91    -58.25
REMARK 500  3 THR A 557     -112.03    -77.32
REMARK 500  3 SER A 558     -110.46    -54.86
REMARK 500  3 ASP A 560       81.71    176.31
REMARK 500  3 TRP A 563      149.27     43.99
REMARK 500  3 VAL A 565      159.10    169.28
REMARK 500  3 THR A 566       76.06   -160.61
REMARK 500  3 VAL A 567     -160.27   -102.67
REMARK 500  3 LEU A 569       81.59   -160.37
REMARK 500  3 ALA A 571      -67.74   -162.07
REMARK 500  3 ASP A 585      -75.14   -110.71
REMARK 500  3 ASP A 586      -97.34    -61.12
REMARK 500  3 SER A 587     -145.91   -166.20
REMARK 500  3 TRP A 590       91.46    -54.16
REMARK 500  3 ASP A 593      -68.85    -90.52
REMARK 500  3 TYR A 598       91.61    -65.96
REMARK 500  3 PRO A 601     -168.62    -79.47
REMARK 500  3 ALA A 603       98.52     70.21
REMARK 500  3 THR A 606      -80.64   -105.89
REMARK 500  3 VAL A 611       78.53   -160.05
REMARK 500  4 THR A 510       94.51     69.86
REMARK 500  4 THR A 511      175.33     58.21
REMARK 500  4 PRO A 512      -83.29    -78.39
REMARK 500  4 THR A 513       21.68   -153.70
REMARK 500  4 LEU A 521      102.20   -162.00
REMARK 500  4 ALA A 523     -139.96   -158.05
REMARK 500  4 THR A 525     -158.09    -56.17
REMARK 500  4 TYR A 527      -33.09    -35.74
REMARK 500  4 GLU A 529      142.50    173.22
REMARK 500  4 ASP A 542      -31.35     78.75
REMARK 500  4 GLU A 544       91.39   -172.92
REMARK 500  4 THR A 545      -16.46    -48.98
REMARK 500  4 ASP A 547       49.59   -151.14
REMARK 500  4 SER A 552     -101.50   -131.86
REMARK 500  4 ASP A 554       87.85    -36.49
REMARK 500  4 LYS A 555      -85.20     67.59
REMARK 500  4 TYR A 556     -125.59     43.39
REMARK 500  4 THR A 557     -128.95   -147.41
REMARK 500  4 SER A 558      -99.07    -42.67
REMARK 500  4 ASP A 560       95.43     74.41
REMARK 500  4 TRP A 563      101.60     31.18
REMARK 500  4 VAL A 565      153.43    178.17
REMARK 500  4 THR A 566       84.27   -160.10
REMARK 500  4 LEU A 569       79.46   -160.37
REMARK 500  4 ALA A 571      -37.11   -164.45
REMARK 500  4 GLU A 573     -133.82   -161.32
REMARK 500  4 ASP A 586      105.19     80.37
REMARK 500  4 TRP A 590       88.21    -57.97
REMARK 500  4 GLU A 591       95.84    -64.20
REMARK 500  4 PRO A 601     -168.93    -79.36
REMARK 500  4 GLN A 602      179.63    -56.53
REMARK 500  4 CYS A 604       96.12    -65.03
REMARK 500  4 ALA A 609     -144.86   -140.24
REMARK 500  4 VAL A 611       76.31   -161.04
REMARK 500  5 THR A 510       38.54    178.80
REMARK 500  5 THR A 511       61.62     63.55
REMARK 500  5 ALA A 523     -144.75   -169.04
REMARK 500  5 THR A 524      114.62    173.84
REMARK 500  5 THR A 525     -149.88   -131.55
REMARK 500  5 THR A 526       52.29   -114.62
REMARK 500  5 TYR A 527       36.13     37.04
REMARK 500  5 GLU A 529     -157.47    -63.73
REMARK 500  5 SER A 536       47.10    -82.69
REMARK 500  5 ASP A 542      -11.38    -49.07
REMARK 500  5 GLU A 544       94.20    172.45
REMARK 500  5 THR A 545      -16.71    -48.84
REMARK 500  5 ASP A 547       45.00   -141.34
REMARK 500  5 ILE A 549       82.51   -156.59
REMARK 500  5 SER A 552      -96.54   -129.95
REMARK 500  5 LYS A 555       89.34     69.88
REMARK 500  5 THR A 557      -91.86   -164.87
REMARK 500  5 SER A 559      -83.69   -152.31
REMARK 500  5 ASP A 560       14.69   -146.90
REMARK 500  5 TRP A 563      101.03     33.39
REMARK 500  5 VAL A 567     -167.31   -123.63
REMARK 500  5 LEU A 569       88.92   -160.66
REMARK 500  5 ALA A 571     -163.99   -162.63
REMARK 500  5 GLU A 573     -139.04   -163.84
REMARK 500  5 ASP A 586       84.11     57.42
REMARK 500  5 SER A 587      112.66   -171.21
REMARK 500  5 GLU A 589       71.76   -112.43
REMARK 500  5 TRP A 590       89.84    -44.27
REMARK 500  5 GLU A 591       93.67    -56.72
REMARK 500  5 ASP A 593      -65.79    -90.16
REMARK 500  5 ARG A 596     -165.02   -160.14
REMARK 500  5 TYR A 598      100.56    177.92
REMARK 500  5 VAL A 600      125.32     65.70
REMARK 500  5 PRO A 601     -169.06    -79.43
REMARK 500  5 GLN A 602      -83.09    -77.89
REMARK 500  5 ALA A 603      173.02     60.44
REMARK 500  5 ALA A 609     -156.73   -137.81
REMARK 500  5 VAL A 611       71.38   -160.04
REMARK 500  5 ASP A 613     -164.92   -162.77
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  1 ARG A 581         0.18    SIDE_CHAIN
REMARK 500  1 ARG A 596         0.20    SIDE_CHAIN
REMARK 500  1 ARG A 616         0.28    SIDE_CHAIN
REMARK 500  2 ARG A 581         0.16    SIDE_CHAIN
REMARK 500  2 ARG A 596         0.25    SIDE_CHAIN
REMARK 500  2 ARG A 616         0.32    SIDE_CHAIN
REMARK 500  3 ARG A 581         0.12    SIDE_CHAIN
REMARK 500  3 ARG A 596         0.09    SIDE_CHAIN
REMARK 500  3 ARG A 616         0.26    SIDE_CHAIN
REMARK 500  4 ARG A 581         0.14    SIDE_CHAIN
REMARK 500  4 ARG A 596         0.30    SIDE_CHAIN
REMARK 500  4 ARG A 616         0.26    SIDE_CHAIN
REMARK 500  5 ARG A 581         0.32    SIDE_CHAIN
REMARK 500  5 ARG A 596         0.28    SIDE_CHAIN
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 GLC A 1
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 2
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 3
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 4
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 5
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 6
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 7
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 617B
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 618B
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 619B
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 620B
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 621B
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 622B
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 623B
DBREF  1ACZ A  509   616  UNP    P04064   AMYG_ASPNG     533    640
SEQRES   1 A  108  CYS THR THR PRO THR ALA VAL ALA VAL THR PHE ASP LEU
SEQRES   2 A  108  THR ALA THR THR THR TYR GLY GLU ASN ILE TYR LEU VAL
SEQRES   3 A  108  GLY SER ILE SER GLN LEU GLY ASP TRP GLU THR SER ASP
SEQRES   4 A  108  GLY ILE ALA LEU SER ALA ASP LYS TYR THR SER SER ASP
SEQRES   5 A  108  PRO LEU TRP TYR VAL THR VAL THR LEU PRO ALA GLY GLU
SEQRES   6 A  108  SER PHE GLU TYR LYS PHE ILE ARG ILE GLU SER ASP ASP
SEQRES   7 A  108  SER VAL GLU TRP GLU SER ASP PRO ASN ARG GLU TYR THR
SEQRES   8 A  108  VAL PRO GLN ALA CYS GLY THR SER THR ALA THR VAL THR
SEQRES   9 A  108  ASP THR TRP ARG
HET    GLC  A   1      11
HET    GLC  A   2      11
HET    GLC  A   3      11
HET    GLC  A   4      11
HET    GLC  A   5      11
HET    GLC  A   6      11
HET    GLC  A   7      11
HET    GLC  A 617B     11
HET    GLC  A 618B     11
HET    GLC  A 619B     11
HET    GLC  A 620B     11
HET    GLC  A 621B     11
HET    GLC  A 622B     11
HET    GLC  A 623B     11
HETNAM     GLC ALPHA-D-GLUCOSE
FORMUL   2  GLC    14(C6 H12 O6)
HELIX    1   1 THR A  545  ASP A  547  5                                   3
SHEET    1   A 7 SER A 607  TRP A 615  0
SHEET    2   A 7 THR A 513  ALA A 523  1  N  THR A 518   O  ALA A 609
SHEET    3   A 7 PRO A 561  ALA A 571 -1  N  VAL A 567   O  VAL A 517
SHEET    4   A 7 ILE A 549  SER A 552 -1  N  SER A 552   O  TYR A 564
SHEET    5   A 7 ASN A 530  SER A 536 -1  N  LEU A 533   O  ILE A 549
SHEET    6   A 7 GLU A 573  ILE A 582 -1  N  LYS A 578   O  VAL A 534
SHEET    7   A 7 GLU A 589  GLU A 591 -1  N  GLU A 589   O  ARG A 581
SSBOND   1 CYS A  509    CYS A  604                          1555   1555  2.02
LINK         C1  GLC A   1                 O4  GLC A   7     1555   1555  1.40
LINK         O4  GLC A   1                 C1  GLC A   2     1555   1555  1.40
LINK         O4  GLC A   2                 C1  GLC A   3     1555   1555  1.40
LINK         O4  GLC A   3                 C1  GLC A   4     1555   1555  1.40
LINK         O4  GLC A   4                 C1  GLC A   5     1555   1555  1.40
LINK         O4  GLC A   5                 C1  GLC A   6     1555   1555  1.40
LINK         O4  GLC A   6                 C1  GLC A   7     1555   1555  1.40
LINK         C1  GLC A 617B                O4  GLC A 623B    1555   1555  1.40
LINK         O4  GLC A 617B                C1  GLC A 618B    1555   1555  1.40
LINK         O4  GLC A 618B                C1  GLC A 619B    1555   1555  1.40
LINK         O4  GLC A 619B                C1  GLC A 620B    1555   1555  1.40
LINK         O4  GLC A 620B                C1  GLC A 621B    1555   1555  1.40
LINK         O4  GLC A 621B                C1  GLC A 622B    1555   1555  1.40
LINK         O4  GLC A 622B                C1  GLC A 623B    1555   1555  1.40
SITE     1 AC1  4 GLC A   2  GLC A   6  GLC A   7  TRP A 590
SITE     1 AC2  4 GLC A   1  GLC A   3  GLC A   4  TRP A 543
SITE     1 AC3  3 GLC A   2  GLC A   4  TRP A 543
SITE     1 AC4  3 GLC A   2  GLC A   3  GLC A   5
SITE     1 AC5  2 GLC A   4  GLC A   6
SITE     1 AC6  3 GLC A   1  GLC A   5  GLC A   7
SITE     1 AC7  2 GLC A   1  GLC A   6
SITE     1 AC8  6 TYR A 527  LYS A 555  TYR A 556  THR A 557
SITE     2 AC8  6 GLC A 618B GLC A 623B
SITE     1 AC9  7 TYR A 556  THR A 557  PRO A 561  GLC A 617B
SITE     2 AC9  7 GLC A 619B GLC A 621B GLC A 623B
SITE     1 BC1  6 THR A 524  THR A 525  THR A 557  PRO A 561
SITE     2 BC1  6 GLC A 618B GLC A 620B
SITE     1 BC2  5 THR A 524  TYR A 556  PRO A 561  GLC A 619B
SITE     2 BC2  5 GLC A 621B
SITE     1 BC3  4 TYR A 556  GLC A 618B GLC A 620B GLC A 622B
SITE     1 BC4  3 LYS A 555  GLC A 621B GLC A 623B
SITE     1 BC5  3 GLC A 617B GLC A 618B GLC A 622B
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1
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      1.000000  0.000000  0.000000        0.00000
SCALE2      0.000000  1.000000  0.000000        0.00000
SCALE3      0.000000  0.000000  1.000000        0.00000
      
PROCHECK
Go to PROCHECK summary
 References