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PDBsum entry 2gvy

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Top Page protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
2gvy
Jmol
Contents
Protein chains
476 a.a.
Ligands
NAG
BGC-GLC ×3
GLC-GLC ×3
NDG
Metals
_CA ×2
Waters ×751
HEADER    HYDROLASE                               03-MAY-06   2GVY
TITLE     MONOCLINIC CRYSTAL FORM OF ASPERGILLUS NIGER ALPHA-AMYLASE IN COMPLEX
TITLE    2 WITH MALTOSE AT 1.8 A RESOLUTION
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ALPHA-AMYLASE A;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: TAKA-AMYLASE A, TAA, 1,4- ALPHA-D-GLUCAN GLUCANOHYDROLASE;
COMPND   5 EC: 3.2.1.1;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ASPERGILLUS ORYZAE;
SOURCE   3 ORGANISM_TAXID: 5062;
SOURCE   4 GENE: AMY1;
SOURCE   5 EXPRESSION_SYSTEM: ASPERGILLUS ORYZAE;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 5062
KEYWDS    (BETA-ALPHA)8 BARREL, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.VUJICIC-ZAGAR,B.W.DIJKSTRA
REVDAT   4   13-JUL-11 2GVY    1       VERSN
REVDAT   3   08-SEP-09 2GVY    1       HETATM HETNAM
REVDAT   2   24-FEB-09 2GVY    1       VERSN
REVDAT   1   15-AUG-06 2GVY    0
JRNL        AUTH   A.VUJICIC-ZAGAR,B.W.DIJKSTRA
JRNL        TITL   MONOCLINIC CRYSTAL FORM OF ASPERGILLUS NIGER ALPHA-AMYLASE
JRNL        TITL 2 IN COMPLEX WITH MALTOSE AT 1.8 ANGSTROMS RESOLUTION.
JRNL        REF    ACTA CRYSTALLOGR.,SECT.F      V.  62   716 2006
JRNL        REFN                   ESSN 1744-3091
JRNL        PMID   16880540
JRNL        DOI    10.1107/S1744309106024729
REMARK   2
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
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) : 1.80
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.5
REMARK   3   NUMBER OF REFLECTIONS             : 84733
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) : 0.165
REMARK   3   R VALUE            (WORKING SET) : 0.162
REMARK   3   FREE R VALUE                     : 0.210
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 4244
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) : 1.80
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5757
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.40
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2120
REMARK   3   BIN FREE R VALUE SET COUNT          : 315
REMARK   3   BIN FREE R VALUE                    : 0.2900
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 7372
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 168
REMARK   3   SOLVENT ATOMS            : 751
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.80
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.06000
REMARK   3    B22 (A**2) : 2.21000
REMARK   3    B33 (A**2) : -2.30000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : -0.32000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.126
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.125
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.087
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.792
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.962
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.938
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7745 ; 0.018 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 10596 ; 1.674 ; 1.965
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   950 ; 6.301 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   348 ;36.408 ;25.115
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1134 ;14.648 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ; 9.206 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1196 ; 0.119 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5892 ; 0.008 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  4041 ; 0.217 ; 0.300
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  5453 ; 0.323 ; 0.500
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  1284 ; 0.184 ; 0.500
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     7 ; 0.039 ; 0.500
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    31 ; 0.187 ; 0.300
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    51 ; 0.199 ; 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):  4795 ; 1.387 ; 2.000
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7606 ; 1.981 ; 3.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3411 ; 1.650 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2990 ; 2.250 ; 3.000
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   : 1.20
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 2GVY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-MAY-06.
REMARK 100 THE RCSB ID CODE IS RCSB037614.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 15-DEC-05
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               : ESRF
REMARK 200  BEAMLINE                       : ID29
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97910
REMARK 200  MONOCHROMATOR                  : SI(111)
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : PRODC
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 84823
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800
REMARK 200  RESOLUTION RANGE LOW       (A) : 72.987
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.6
REMARK 200  DATA REDUNDANCY                : 7.000
REMARK 200  R MERGE                    (I) : 0.10400
REMARK 200  R SYM                      (I) : 0.10400
REMARK 200   FOR THE DATA SET  : 5.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.90
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.80
REMARK 200  R MERGE FOR SHELL          (I) : 0.57800
REMARK 200  R SYM FOR SHELL            (I) : 0.57800
REMARK 200   FOR SHELL         : 1.300
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 46.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 6000, 0.1M AMMONIUM SULPHATE,
REMARK 280  0.1M MES, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 296K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,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        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       50.57450
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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     SER A   477
REMARK 465     SER A   478
REMARK 465     SER B   477
REMARK 465     SER B   478
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   CD   LYS A   221     O    HOH A  1159              1.81
REMARK 500   O4   GLC A   999     O    HOH A  1313              1.94
REMARK 500   O    HOH B  1163     O    HOH B  1357              2.18
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    ALA A  78       45.11    -80.14
REMARK 500    SER A 141       32.19    -96.07
REMARK 500    ALA A 329      122.10    -37.07
REMARK 500    ASP A 340      124.46    -31.13
REMARK 500    ALA A 430      130.64    -36.97
REMARK 500    ALA B  78       43.39    -80.63
REMARK 500    GLN B  85      -31.68   -131.32
REMARK 500    ALA B 329      122.00    -33.86
REMARK 500    ASP B 340      119.55    -34.41
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A1134        DISTANCE =  5.08 ANGSTROMS
REMARK 525    HOH B1060        DISTANCE =  5.07 ANGSTROMS
REMARK 525    HOH B1298        DISTANCE =  5.23 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A 801  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 162   O
REMARK 620 2 ASP A 175   OD2  79.3
REMARK 620 3 HOH A1013   O    75.0  89.6
REMARK 620 4 HOH A1083   O    67.5  98.6 139.1
REMARK 620 5 ASN A 121   OD1 156.0 119.9  90.0 118.7
REMARK 620 6 ASP A 175   OD1 115.3  50.6  67.8 144.0  74.3
REMARK 620 7 HIS A 210   O    82.5 160.6  79.2  80.4  76.3 135.1
REMARK 620 8 HOH A1211   O   132.4  75.6 143.3  77.1  69.9  77.1 122.4
REMARK 620 N                    1     2     3     4     5     6     7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA B 802  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 210   O
REMARK 620 2 GLU B 162   O    81.9
REMARK 620 3 HOH B1023   O    82.3  72.6
REMARK 620 4 ASN B 121   OD1  75.9 156.1 112.6
REMARK 620 5 ASP B 175   OD1 137.5 117.0 138.2  75.6
REMARK 620 6 ASP B 175   OD2 159.3  77.7  95.1 123.3  52.8
REMARK 620 7 HOH B1252   O   121.6 131.9  70.5  69.2  75.5  76.0
REMARK 620 8 HOH B1006   O    77.9  75.7 144.6  90.8  71.6  93.3 144.8
REMARK 620 N                    1     2     3     4     5     6     7
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 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 999
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 1011
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 1012
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC B 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC B 999
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC B 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC B 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 802
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2TAA   RELATED DB: PDB
REMARK 900 THE SAME PROTEIN, DIFFERENT CRYSTAL FORM.
REMARK 900 RELATED ID: 6TAA   RELATED DB: PDB
REMARK 900 THE SAME PROTEIN, DIFFERENT CRYSTAL FORM.
REMARK 900 RELATED ID: 7TAA   RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH THE INHIBITOR ACARBOSE,
REMARK 900 DIFFERENT CRYSTAL FORM.
REMARK 900 RELATED ID: 2GUY   RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH MALTOSE, DIFFERENT CRYSTAL
REMARK 900 FORM.
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 CURRENTLY THERE IS NO AMINOACID SEQUENCE DATABASE REFERENCE
REMARK 999 AVAILABLE FOR THE PROTEIN
DBREF  2GVY A    1   478  UNP    P0C1B3   AMYA1_ASPOR     22    499
DBREF  2GVY B    1   478  UNP    P0C1B3   AMYA1_ASPOR     22    499
SEQRES   1 A  478  ALA THR PRO ALA ASP TRP ARG SER GLN SER ILE TYR PHE
SEQRES   2 A  478  LEU LEU THR ASP ARG PHE ALA ARG THR ASP GLY SER THR
SEQRES   3 A  478  THR ALA THR CYS ASN THR ALA ASP GLN LYS TYR CYS GLY
SEQRES   4 A  478  GLY THR TRP GLN GLY ILE ILE ASP LYS LEU ASP TYR ILE
SEQRES   5 A  478  GLN GLY MET GLY PHE THR ALA ILE TRP ILE THR PRO VAL
SEQRES   6 A  478  THR ALA GLN LEU PRO GLN THR THR ALA TYR GLY ASP ALA
SEQRES   7 A  478  TYR HIS GLY TYR TRP GLN GLN ASP ILE TYR SER LEU ASN
SEQRES   8 A  478  GLU ASN TYR GLY THR ALA ASP ASP LEU LYS ALA LEU SER
SEQRES   9 A  478  SER ALA LEU HIS GLU ARG GLY MET TYR LEU MET VAL ASP
SEQRES  10 A  478  VAL VAL ALA ASN HIS MET GLY TYR ASP GLY ALA GLY SER
SEQRES  11 A  478  SER VAL ASP TYR SER VAL PHE LYS PRO PHE SER SER GLN
SEQRES  12 A  478  ASP TYR PHE HIS PRO PHE CYS PHE ILE GLN ASN TYR GLU
SEQRES  13 A  478  ASP GLN THR GLN VAL GLU ASP CYS TRP LEU GLY ASP ASN
SEQRES  14 A  478  THR VAL SER LEU PRO ASP LEU ASP THR THR LYS ASP VAL
SEQRES  15 A  478  VAL LYS ASN GLU TRP TYR ASP TRP VAL GLY SER LEU VAL
SEQRES  16 A  478  SER ASN TYR SER ILE ASP GLY LEU ARG ILE ASP THR VAL
SEQRES  17 A  478  LYS HIS VAL GLN LYS ASP PHE TRP PRO GLY TYR ASN LYS
SEQRES  18 A  478  ALA ALA GLY VAL TYR CYS ILE GLY GLU VAL LEU ASP GLY
SEQRES  19 A  478  ASP PRO ALA TYR THR CYS PRO TYR GLN ASN VAL MET ASP
SEQRES  20 A  478  GLY VAL LEU ASN TYR PRO ILE TYR TYR PRO LEU LEU ASN
SEQRES  21 A  478  ALA PHE LYS SER THR SER GLY SER MET ASP ASP LEU TYR
SEQRES  22 A  478  ASN MET ILE ASN THR VAL LYS SER ASP CYS PRO ASP SER
SEQRES  23 A  478  THR LEU LEU GLY THR PHE VAL GLU ASN HIS ASP ASN PRO
SEQRES  24 A  478  ARG PHE ALA SER TYR THR ASN ASP ILE ALA LEU ALA LYS
SEQRES  25 A  478  ASN VAL ALA ALA PHE ILE ILE LEU ASN ASP GLY ILE PRO
SEQRES  26 A  478  ILE ILE TYR ALA GLY GLN GLU GLN HIS TYR ALA GLY GLY
SEQRES  27 A  478  ASN ASP PRO ALA ASN ARG GLU ALA THR TRP LEU SER GLY
SEQRES  28 A  478  TYR PRO THR ASP SER GLU LEU TYR LYS LEU ILE ALA SER
SEQRES  29 A  478  ALA ASN ALA ILE ARG ASN TYR ALA ILE SER LYS ASP THR
SEQRES  30 A  478  GLY PHE VAL THR TYR LYS ASN TRP PRO ILE TYR LYS ASP
SEQRES  31 A  478  ASP THR THR ILE ALA MET ARG LYS GLY THR ASP GLY SER
SEQRES  32 A  478  GLN ILE VAL THR ILE LEU SER ASN LYS GLY ALA SER GLY
SEQRES  33 A  478  ASP SER TYR THR LEU SER LEU SER GLY ALA GLY TYR THR
SEQRES  34 A  478  ALA GLY GLN GLN LEU THR GLU VAL ILE GLY CYS THR THR
SEQRES  35 A  478  VAL THR VAL GLY SER ASP GLY ASN VAL PRO VAL PRO MET
SEQRES  36 A  478  ALA GLY GLY LEU PRO ARG VAL LEU TYR PRO THR GLU LYS
SEQRES  37 A  478  LEU ALA GLY SER LYS ILE CYS SER SER SER
SEQRES   1 B  478  ALA THR PRO ALA ASP TRP ARG SER GLN SER ILE TYR PHE
SEQRES   2 B  478  LEU LEU THR ASP ARG PHE ALA ARG THR ASP GLY SER THR
SEQRES   3 B  478  THR ALA THR CYS ASN THR ALA ASP GLN LYS TYR CYS GLY
SEQRES   4 B  478  GLY THR TRP GLN GLY ILE ILE ASP LYS LEU ASP TYR ILE
SEQRES   5 B  478  GLN GLY MET GLY PHE THR ALA ILE TRP ILE THR PRO VAL
SEQRES   6 B  478  THR ALA GLN LEU PRO GLN THR THR ALA TYR GLY ASP ALA
SEQRES   7 B  478  TYR HIS GLY TYR TRP GLN GLN ASP ILE TYR SER LEU ASN
SEQRES   8 B  478  GLU ASN TYR GLY THR ALA ASP ASP LEU LYS ALA LEU SER
SEQRES   9 B  478  SER ALA LEU HIS GLU ARG GLY MET TYR LEU MET VAL ASP
SEQRES  10 B  478  VAL VAL ALA ASN HIS MET GLY TYR ASP GLY ALA GLY SER
SEQRES  11 B  478  SER VAL ASP TYR SER VAL PHE LYS PRO PHE SER SER GLN
SEQRES  12 B  478  ASP TYR PHE HIS PRO PHE CYS PHE ILE GLN ASN TYR GLU
SEQRES  13 B  478  ASP GLN THR GLN VAL GLU ASP CYS TRP LEU GLY ASP ASN
SEQRES  14 B  478  THR VAL SER LEU PRO ASP LEU ASP THR THR LYS ASP VAL
SEQRES  15 B  478  VAL LYS ASN GLU TRP TYR ASP TRP VAL GLY SER LEU VAL
SEQRES  16 B  478  SER ASN TYR SER ILE ASP GLY LEU ARG ILE ASP THR VAL
SEQRES  17 B  478  LYS HIS VAL GLN LYS ASP PHE TRP PRO GLY TYR ASN LYS
SEQRES  18 B  478  ALA ALA GLY VAL TYR CYS ILE GLY GLU VAL LEU ASP GLY
SEQRES  19 B  478  ASP PRO ALA TYR THR CYS PRO TYR GLN ASN VAL MET ASP
SEQRES  20 B  478  GLY VAL LEU ASN TYR PRO ILE TYR TYR PRO LEU LEU ASN
SEQRES  21 B  478  ALA PHE LYS SER THR SER GLY SER MET ASP ASP LEU TYR
SEQRES  22 B  478  ASN MET ILE ASN THR VAL LYS SER ASP CYS PRO ASP SER
SEQRES  23 B  478  THR LEU LEU GLY THR PHE VAL GLU ASN HIS ASP ASN PRO
SEQRES  24 B  478  ARG PHE ALA SER TYR THR ASN ASP ILE ALA LEU ALA LYS
SEQRES  25 B  478  ASN VAL ALA ALA PHE ILE ILE LEU ASN ASP GLY ILE PRO
SEQRES  26 B  478  ILE ILE TYR ALA GLY GLN GLU GLN HIS TYR ALA GLY GLY
SEQRES  27 B  478  ASN ASP PRO ALA ASN ARG GLU ALA THR TRP LEU SER GLY
SEQRES  28 B  478  TYR PRO THR ASP SER GLU LEU TYR LYS LEU ILE ALA SER
SEQRES  29 B  478  ALA ASN ALA ILE ARG ASN TYR ALA ILE SER LYS ASP THR
SEQRES  30 B  478  GLY PHE VAL THR TYR LYS ASN TRP PRO ILE TYR LYS ASP
SEQRES  31 B  478  ASP THR THR ILE ALA MET ARG LYS GLY THR ASP GLY SER
SEQRES  32 B  478  GLN ILE VAL THR ILE LEU SER ASN LYS GLY ALA SER GLY
SEQRES  33 B  478  ASP SER TYR THR LEU SER LEU SER GLY ALA GLY TYR THR
SEQRES  34 B  478  ALA GLY GLN GLN LEU THR GLU VAL ILE GLY CYS THR THR
SEQRES  35 B  478  VAL THR VAL GLY SER ASP GLY ASN VAL PRO VAL PRO MET
SEQRES  36 B  478  ALA GLY GLY LEU PRO ARG VAL LEU TYR PRO THR GLU LYS
SEQRES  37 B  478  LEU ALA GLY SER LYS ILE CYS SER SER SER
MODRES 2GVY ASN A  197  ASN  GLYCOSYLATION SITE
MODRES 2GVY ASN B  197  ASN  GLYCOSYLATION SITE
HET    NAG  A 500      14
HET    BGC  A1002      12
HET    GLC  A1001      11
HET    GLC  A1000      12
HET    GLC  A 999      11
HET    BGC  A1003      12
HET    GLC  A1004      11
HET    GLC  A1011      12
HET    GLC  A1012      11
HET     CA  A 801       1
HET    NDG  B 500      14
HET    GLC  B1000      12
HET    GLC  B 999      11
HET    BGC  B1002      12
HET    GLC  B1001      11
HET     CA  B 802       1
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     BGC BETA-D-GLUCOSE
HETNAM     GLC ALPHA-D-GLUCOSE
HETNAM      CA CALCIUM ION
HETNAM     NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE
FORMUL   3  NAG    C8 H15 N O6
FORMUL   4  BGC    3(C6 H12 O6)
FORMUL   4  GLC    9(C6 H12 O6)
FORMUL   8   CA    2(CA 2+)
FORMUL   9  NDG    C8 H15 N O6
FORMUL  13  HOH   *751(H2 O)
HELIX    1   1 THR A    2  SER A    8  1                                   7
HELIX    2   2 LEU A   15  ALA A   20  1                                   6
HELIX    3   3 ASN A   31  GLN A   35  5                                   5
HELIX    4   4 THR A   41  LYS A   48  1                                   8
HELIX    5   5 LYS A   48  MET A   55  1                                   8
HELIX    6   6 THR A   96  ARG A  110  1                                  15
HELIX    7   7 ALA A  128  VAL A  132  5                                   5
HELIX    8   8 ASP A  133  PHE A  137  5                                   5
HELIX    9   9 SER A  142  PHE A  146  5                                   5
HELIX   10  10 ASP A  157  CYS A  164  1                                   8
HELIX   11  11 LYS A  180  SER A  199  1                                  20
HELIX   12  12 THR A  207  VAL A  211  5                                   5
HELIX   13  13 GLN A  212  ASP A  214  5                                   3
HELIX   14  14 PHE A  215  GLY A  224  1                                  10
HELIX   15  15 ASP A  235  CYS A  240  1                                   6
HELIX   16  16 PRO A  241  VAL A  245  5                                   5
HELIX   17  17 ASN A  251  LYS A  263  1                                  13
HELIX   18  18 SER A  268  CYS A  283  1                                  16
HELIX   19  19 ASP A  285  LEU A  288  5                                   4
HELIX   20  20 ARG A  300  THR A  305  1                                   6
HELIX   21  21 ASP A  307  ASN A  321  1                                  15
HELIX   22  22 GLY A  330  HIS A  334  5                                   5
HELIX   23  23 ALA A  346  GLY A  351  5                                   6
HELIX   24  24 SER A  356  ASP A  376  1                                  21
HELIX   25  25 GLU A  467  ALA A  470  5                                   4
HELIX   26  26 THR B    2  ARG B    7  1                                   6
HELIX   27  27 LEU B   15  ALA B   20  1                                   6
HELIX   28  28 ASN B   31  GLN B   35  5                                   5
HELIX   29  29 THR B   41  LYS B   48  1                                   8
HELIX   30  30 LYS B   48  GLY B   54  1                                   7
HELIX   31  31 GLU B   92  GLY B   95  5                                   4
HELIX   32  32 THR B   96  ARG B  110  1                                  15
HELIX   33  33 ALA B  128  VAL B  132  5                                   5
HELIX   34  34 ASP B  133  PHE B  137  5                                   5
HELIX   35  35 SER B  142  PHE B  146  5                                   5
HELIX   36  36 ASP B  157  CYS B  164  1                                   8
HELIX   37  37 LYS B  180  SER B  199  1                                  20
HELIX   38  38 THR B  207  VAL B  211  5                                   5
HELIX   39  39 GLN B  212  ASP B  214  5                                   3
HELIX   40  40 PHE B  215  GLY B  224  1                                  10
HELIX   41  41 ASP B  235  CYS B  240  1                                   6
HELIX   42  42 PRO B  241  VAL B  245  5                                   5
HELIX   43  43 ASN B  251  LYS B  263  1                                  13
HELIX   44  44 SER B  268  CYS B  283  1                                  16
HELIX   45  45 ASP B  285  LEU B  288  5                                   4
HELIX   46  46 ARG B  300  THR B  305  1                                   6
HELIX   47  47 ASP B  307  ASN B  321  1                                  15
HELIX   48  48 GLY B  330  HIS B  334  5                                   5
HELIX   49  49 ALA B  346  GLY B  351  5                                   6
HELIX   50  50 SER B  356  ASP B  376  1                                  21
HELIX   51  51 GLU B  467  ALA B  470  5                                   4
SHEET    1   A 8 GLY A 248  VAL A 249  0
SHEET    2   A 8 TYR A 226  GLY A 229  1  N  GLY A 229   O  GLY A 248
SHEET    3   A 8 GLY A 202  ILE A 205  1  N  LEU A 203   O  ILE A 228
SHEET    4   A 8 TYR A 113  VAL A 118  1  N  VAL A 118   O  ARG A 204
SHEET    5   A 8 ALA A  59  ILE A  62  1  N  ILE A  60   O  MET A 115
SHEET    6   A 8 ILE A  11  LEU A  14  1  N  LEU A  14   O  TRP A  61
SHEET    7   A 8 ILE A 324  TYR A 328  1  O  ILE A 327   N  PHE A  13
SHEET    8   A 8 GLY A 290  THR A 291  1  N  THR A 291   O  ILE A 326
SHEET    1   B 2 THR A  66  GLN A  68  0
SHEET    2   B 2 GLN A  84  LEU A  90 -1  O  GLN A  85   N  ALA A  67
SHEET    1   C 3 TYR A 125  ASP A 126  0
SHEET    2   C 3 VAL A 171  LEU A 173 -1  O  SER A 172   N  TYR A 125
SHEET    3   C 3 LEU A 166  GLY A 167 -1  N  LEU A 166   O  LEU A 173
SHEET    1   D 6 TRP A 385  ASP A 390  0
SHEET    2   D 6 THR A 393  LYS A 398 -1  O  ALA A 395   N  TYR A 388
SHEET    3   D 6 ILE A 405  SER A 410 -1  O  LEU A 409   N  ILE A 394
SHEET    4   D 6 ARG A 461  PRO A 465 -1  O  LEU A 463   N  VAL A 406
SHEET    5   D 6 GLN A 433  GLU A 436 -1  N  THR A 435   O  TYR A 464
SHEET    6   D 6 THR A 441  THR A 444 -1  O  VAL A 443   N  LEU A 434
SHEET    1   E 2 TYR A 419  LEU A 423  0
SHEET    2   E 2 VAL A 451  MET A 455 -1  O  VAL A 453   N  LEU A 421
SHEET    1   F 8 GLY B 248  VAL B 249  0
SHEET    2   F 8 TYR B 226  GLY B 229  1  N  GLY B 229   O  GLY B 248
SHEET    3   F 8 GLY B 202  ILE B 205  1  N  LEU B 203   O  ILE B 228
SHEET    4   F 8 TYR B 113  VAL B 118  1  N  VAL B 118   O  ARG B 204
SHEET    5   F 8 ALA B  59  ILE B  62  1  N  ILE B  60   O  MET B 115
SHEET    6   F 8 ILE B  11  LEU B  14  1  N  LEU B  14   O  TRP B  61
SHEET    7   F 8 ILE B 324  TYR B 328  1  O  PRO B 325   N  ILE B  11
SHEET    8   F 8 GLY B 290  THR B 291  1  N  THR B 291   O  ILE B 326
SHEET    1   G 2 THR B  66  GLN B  68  0
SHEET    2   G 2 GLN B  84  LEU B  90 -1  O  GLN B  85   N  ALA B  67
SHEET    1   H 3 TYR B 125  ASP B 126  0
SHEET    2   H 3 VAL B 171  LEU B 173 -1  O  SER B 172   N  TYR B 125
SHEET    3   H 3 LEU B 166  GLY B 167 -1  N  LEU B 166   O  LEU B 173
SHEET    1   I 6 TRP B 385  ASP B 390  0
SHEET    2   I 6 THR B 393  LYS B 398 -1  O  ARG B 397   N  TRP B 385
SHEET    3   I 6 ILE B 405  SER B 410 -1  O  LEU B 409   N  ILE B 394
SHEET    4   I 6 ARG B 461  PRO B 465 -1  O  ARG B 461   N  ILE B 408
SHEET    5   I 6 GLN B 433  GLU B 436 -1  N  THR B 435   O  TYR B 464
SHEET    6   I 6 THR B 441  THR B 444 -1  O  VAL B 443   N  LEU B 434
SHEET    1   J 2 TYR B 419  LEU B 423  0
SHEET    2   J 2 VAL B 451  MET B 455 -1  O  MET B 455   N  TYR B 419
SSBOND   1 CYS A   30    CYS A   38                          1555   1555  2.07
SSBOND   2 CYS A  150    CYS A  164                          1555   1555  2.52
SSBOND   3 CYS A  240    CYS A  283                          1555   1555  2.01
SSBOND   4 CYS A  440    CYS A  475                          1555   1555  2.07
SSBOND   5 CYS B   30    CYS B   38                          1555   1555  2.08
SSBOND   6 CYS B  150    CYS B  164                          1555   1555  2.09
SSBOND   7 CYS B  240    CYS B  283                          1555   1555  2.00
SSBOND   8 CYS B  440    CYS B  475                          1555   1555  2.08
LINK         ND2 ASN A 197                 C1  NAG A 500     1555   1555  1.44
LINK         ND2 ASN B 197                 C1  NDG B 500     1555   1555  1.46
LINK         O4  GLC A1000                 C1  GLC A 999     1555   1555  1.42
LINK         O4  GLC A1011                 C1  GLC A1012     1555   1555  1.43
LINK         O4  GLC B1000                 C1  GLC B 999     1555   1555  1.44
LINK        CA    CA A 801                 O   GLU A 162     1555   1555  2.48
LINK        CA    CA A 801                 OD2 ASP A 175     1555   1555  2.47
LINK        CA    CA A 801                 O   HOH A1013     1555   1555  2.65
LINK        CA    CA A 801                 O   HOH A1083     1555   1555  2.41
LINK        CA    CA A 801                 OD1 ASN A 121     1555   1555  2.41
LINK        CA    CA A 801                 OD1 ASP A 175     1555   1555  2.72
LINK        CA    CA A 801                 O   HIS A 210     1555   1555  2.38
LINK        CA    CA A 801                 O   HOH A1211     1555   1555  2.35
LINK        CA    CA B 802                 O   HIS B 210     1555   1555  2.39
LINK        CA    CA B 802                 O   GLU B 162     1555   1555  2.39
LINK        CA    CA B 802                 O   HOH B1023     1555   1555  2.59
LINK        CA    CA B 802                 OD1 ASN B 121     1555   1555  2.39
LINK        CA    CA B 802                 OD1 ASP B 175     1555   1555  2.58
LINK        CA    CA B 802                 OD2 ASP B 175     1555   1555  2.49
LINK        CA    CA B 802                 O   HOH B1252     1555   1555  2.53
LINK        CA    CA B 802                 O   HOH B1006     1555   1555  2.51
LINK         O4  BGC A1002                 C1  GLC A1001     1555   1555  1.42
LINK         O4  BGC A1003                 C1  GLC A1004     1555   1555  1.45
LINK         O4  BGC B1002                 C1  GLC B1001     1555   1555  1.44
CISPEP   1 LYS A  138    PRO A  139          0         3.16
CISPEP   2 ASP A  340    PRO A  341          0         8.05
CISPEP   3 LYS B  138    PRO B  139          0         4.74
CISPEP   4 ASP B  340    PRO B  341          0        14.28
SITE     1 AC1  6 TYR A  88  TRP A 190  SER A 193  LEU A 194
SITE     2 AC1  6 ASN A 197  HOH A1180
SITE     1 AC2  4 TYR A 155  LYS A 209  GLC A1001  HOH A1309
SITE     1 AC3 11 TYR A 155  LEU A 166  HIS A 210  GLC A1000
SITE     2 AC3 11 BGC A1002  HOH A1066  HOH A1069  HOH A1168
SITE     3 AC3 11 HOH A1312  HOH A1327  HOH A1372
SITE     1 AC4 13 TYR A  82  HIS A 122  ARG A 204  ASP A 206
SITE     2 AC4 13 THR A 207  GLU A 230  HIS A 296  ASP A 297
SITE     3 AC4 13 ARG A 344  GLC A 999  GLC A1001  HOH A1069
SITE     4 AC4 13 HOH A1372
SITE     1 AC5 13 HIS A  80  TYR A  82  TRP A  83  LEU A 173
SITE     2 AC5 13 ASP A 340  ARG A 344  GLC A1000  HOH A1030
SITE     3 AC5 13 HOH A1069  HOH A1310  HOH A1311  HOH A1312
SITE     4 AC5 13 HOH A1313
SITE     1 AC6  7 GLY A 234  ASP A 235  PRO A 236  GLC A1004
SITE     2 AC6  7 HOH A1141  HOH A1194  HOH A1376
SITE     1 AC7  6 ASP A 233  GLY A 234  ASP A 235  TYR A 256
SITE     2 AC7  6 BGC A1003  HOH A1374
SITE     1 AC8  3 LYS A 280  GLC A1012  HOH A1333
SITE     1 AC9  5 TYR A 382  LYS A 383  GLC A1011  HOH A1146
SITE     2 AC9  5 HOH A1344
SITE     1 BC1  7 ASN A 121  GLU A 162  ASP A 175  HIS A 210
SITE     2 BC1  7 HOH A1013  HOH A1083  HOH A1211
SITE     1 BC2  6 TYR B  88  TRP B 190  SER B 193  ASN B 197
SITE     2 BC2  6 HOH B1159  HOH B1342
SITE     1 BC3 11 TYR B  82  HIS B 122  ARG B 204  ASP B 206
SITE     2 BC3 11 THR B 207  GLU B 230  HIS B 296  ASP B 297
SITE     3 BC3 11 ARG B 344  GLC B 999  GLC B1001
SITE     1 BC4  8 TYR B  82  TRP B  83  ASP B 340  ARG B 344
SITE     2 BC4  8 GLC B1000  HOH B1163  HOH B1178  HOH B1357
SITE     1 BC5  4 TYR B 155  LYS B 209  GLC B1001  HOH B1358
SITE     1 BC6  6 TYR B 155  LEU B 166  HIS B 210  GLC B1000
SITE     2 BC6  6 BGC B1002  HOH B1040
SITE     1 BC7  7 ASN B 121  GLU B 162  ASP B 175  HIS B 210
SITE     2 BC7  7 HOH B1006  HOH B1023  HOH B1252
CRYST1   65.451  101.149   75.185  90.00 103.89  90.00 P 1 21 1      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      0.015279  0.000000  0.003778        0.00000
SCALE2      0.000000  0.009886  0.000000        0.00000
SCALE3      0.000000  0.000000  0.013701        0.00000
      
PROCHECK
Go to PROCHECK summary
 References