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PDBsum entry 3q25

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Sugar binding protein, protein fibril PDB id
3q25
Jmol
Contents
Protein chain
388 a.a.
Ligands
MAL
SO4 ×10
GOL ×6
Waters ×279
HEADER    SUGAR BINDING PROTEIN, PROTEIN FIBRIL   19-DEC-10   3Q25
TITLE     CRYSTAL STRUCTURE OF HUMAN ALPHA-SYNUCLEIN (1-19) FUSED TO MALTOSE
TITLE    2 BINDING PROTEIN (MBP)
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: MALTOSE-BINDING PERIPLASMIC PROTEIN/ALPHA-SYNUCLEIN
COMPND   3 CHIMERIC PROTEIN;
COMPND   4 CHAIN: A;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI, HOMO SAPIENS;
SOURCE   3 ORGANISM_TAXID: 562, 9606;
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PMAL-C2X
KEYWDS    FUSION PROTEIN, AMYLOID, SUGAR BINDING PROTEIN, PROTEIN FIBRIL
EXPDTA    X-RAY DIFFRACTION
AUTHOR    M.ZHAO,M.R.SAWAYA,D.CASCIO,D.EISENBERG
REVDAT   1   01-JUN-11 3Q25    0
JRNL        AUTH   M.ZHAO,D.CASCIO,M.R.SAWAYA,D.EISENBERG
JRNL        TITL   STRUCTURES OF SEGMENTS OF ALPHA-SYNUCLEIN FUSED TO
JRNL        TITL 2 MALTOSE-BINDING PROTEIN SUGGEST INTERMEDIATE STATES DURING
JRNL        TITL 3 AMYLOID FORMATION
JRNL        REF    PROTEIN SCI.                  V.  20   996 2011
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   21462277
JRNL        DOI    10.1002/PRO.630
REMARK   2
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.4_486)
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK   3               : ZWART
REMARK   3
REMARK   3    REFINEMENT TARGET : ML
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.80
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 2.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5
REMARK   3   NUMBER OF REFLECTIONS             : 42101
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.171
REMARK   3   R VALUE            (WORKING SET) : 0.170
REMARK   3   FREE R VALUE                     : 0.196
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 2105
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE
REMARK   3     1 37.8028 -  4.6833    0.95     2768   146  0.1815 0.2010
REMARK   3     2  4.6833 -  3.7183    0.99     2726   143  0.1388 0.1432
REMARK   3     3  3.7183 -  3.2486    1.00     2720   143  0.1573 0.1598
REMARK   3     4  3.2486 -  2.9517    1.00     2692   142  0.1749 0.2075
REMARK   3     5  2.9517 -  2.7402    1.00     2687   141  0.1803 0.2135
REMARK   3     6  2.7402 -  2.5787    1.00     2661   140  0.1735 0.2231
REMARK   3     7  2.5787 -  2.4496    1.00     2667   141  0.1797 0.2330
REMARK   3     8  2.4496 -  2.3430    1.00     2639   139  0.1752 0.2192
REMARK   3     9  2.3430 -  2.2528    1.00     2650   139  0.1701 0.2241
REMARK   3    10  2.2528 -  2.1750    1.00     2647   139  0.1728 0.1962
REMARK   3    11  2.1750 -  2.1070    1.00     2627   139  0.1654 0.2231
REMARK   3    12  2.1070 -  2.0468    1.00     2651   139  0.1754 0.2217
REMARK   3    13  2.0468 -  1.9929    1.00     2605   138  0.1895 0.2581
REMARK   3    14  1.9929 -  1.9443    1.00     2627   138  0.2059 0.2326
REMARK   3    15  1.9443 -  1.9001    1.00     2629   138  0.2222 0.2502
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.30
REMARK   3   SHRINKAGE RADIUS   : 1.06
REMARK   3   K_SOL              : 0.38
REMARK   3   B_SOL              : 45.64
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.200
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 34.33
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.92
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 2.90580
REMARK   3    B22 (A**2) : 2.90580
REMARK   3    B33 (A**2) : -5.81170
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  TWINNING INFORMATION.
REMARK   3   FRACTION: NULL
REMARK   3   OPERATOR: NULL
REMARK   3
REMARK   3  DEVIATIONS FROM IDEAL VALUES.
REMARK   3                 RMSD          COUNT
REMARK   3   BOND      :  0.006           3174
REMARK   3   ANGLE     :  0.947           4319
REMARK   3   CHIRALITY :  0.066            470
REMARK   3   PLANARITY :  0.004            547
REMARK   3   DIHEDRAL  : 11.503           1152
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 1
REMARK   3   TLS GROUP : 1
REMARK   3    SELECTION: ALL
REMARK   3    ORIGIN FOR THE GROUP (A):   3.6125  29.4950  10.4683
REMARK   3    T TENSOR
REMARK   3      T11:   0.0521 T22:   0.1267
REMARK   3      T33:   0.0632 T12:   0.0176
REMARK   3      T13:   0.0181 T23:  -0.0490
REMARK   3    L TENSOR
REMARK   3      L11:   0.3495 L22:   0.5623
REMARK   3      L33:   1.5346 L12:  -0.0364
REMARK   3      L13:   0.2585 L23:   0.0716
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0009 S12:   0.0180 S13:   0.0343
REMARK   3      S21:  -0.0154 S22:   0.0031 S23:  -0.0405
REMARK   3      S31:  -0.2371 S32:  -0.0165 S33:  -0.0094
REMARK   3
REMARK   3  NCS DETAILS
REMARK   3   NUMBER OF NCS GROUPS : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 3Q25 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JAN-11.
REMARK 100 THE RCSB ID CODE IS RCSB063098.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 26-APR-10
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 8.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 24-ID-E
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97914
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : XSCALE
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 42116
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900
REMARK 200  RESOLUTION RANGE LOW       (A) : 37.795
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : 0.05100
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 25.2600
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) : 1.95
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.55700
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 4.500
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 1ANF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 59.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.2 M AMMONIUM SULFATE, 20% (W/V)
REMARK 280  GLYCEROL, PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4
REMARK 290       7555   Y,X,-Z
REMARK 290       8555   -Y,-X,-Z+1/2
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        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       86.32000
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       38.73500
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       38.73500
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      129.48000
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       38.73500
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       38.73500
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       43.16000
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       38.73500
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       38.73500
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      129.48000
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       38.73500
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       38.73500
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       43.16000
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       86.32000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -231.0 KCAL/MOL
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   BIOMT1   2  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  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     MET A     1
REMARK 465     LYS A     2
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     ILE A   3    CG1  CG2  CD1
REMARK 470     LYS A  26    CE   NZ
REMARK 470     LYS A 128    CG   CD   CE   NZ
REMARK 470     LYS A 176    CE   NZ
REMARK 470     LYS A 240    CG   CD   CE   NZ
REMARK 470     LYS A 296    CG   CD   CE   NZ
REMARK 470     GLU A 310    CG   CD   OE1  OE2
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    LEU A 123       88.15   -157.03
REMARK 500    ASN A 151      109.54    -59.33
REMARK 500    ALA A 169      -80.16    -80.90
REMARK 500    GLU A 384      -64.60     69.96
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 MAL A 5044
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 391
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 392
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 393
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 394
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 395
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 396
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 397
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 398
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 399
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 404
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3Q26   RELATED DB: PDB
REMARK 900 RELATED ID: 3Q27   RELATED DB: PDB
REMARK 900 RELATED ID: 3Q28   RELATED DB: PDB
REMARK 900 RELATED ID: 3Q29   RELATED DB: PDB
DBREF  3Q25 A    2   367  UNP    P0AEX9   MALE_ECOLI      27    392
DBREF  3Q25 A  372   390  UNP    P37840   SYUA_HUMAN       1     19
SEQADV 3Q25 MET A    1  UNP  P0AEX9              INITIATING METHIONINE
SEQADV 3Q25 ASN A  368  UNP  P0AEX9              LINKER
SEQADV 3Q25 SER A  369  UNP  P0AEX9              LINKER
SEQADV 3Q25 SER A  370  UNP  P0AEX9              LINKER
SEQADV 3Q25 SER A  371  UNP  P0AEX9              LINKER
SEQRES   1 A  390  MET LYS ILE GLU GLU GLY LYS LEU VAL ILE TRP ILE ASN
SEQRES   2 A  390  GLY ASP LYS GLY TYR ASN GLY LEU ALA GLU VAL GLY LYS
SEQRES   3 A  390  LYS PHE GLU LYS ASP THR GLY ILE LYS VAL THR VAL GLU
SEQRES   4 A  390  HIS PRO ASP LYS LEU GLU GLU LYS PHE PRO GLN VAL ALA
SEQRES   5 A  390  ALA THR GLY ASP GLY PRO ASP ILE ILE PHE TRP ALA HIS
SEQRES   6 A  390  ASP ARG PHE GLY GLY TYR ALA GLN SER GLY LEU LEU ALA
SEQRES   7 A  390  GLU ILE THR PRO ASP LYS ALA PHE GLN ASP LYS LEU TYR
SEQRES   8 A  390  PRO PHE THR TRP ASP ALA VAL ARG TYR ASN GLY LYS LEU
SEQRES   9 A  390  ILE ALA TYR PRO ILE ALA VAL GLU ALA LEU SER LEU ILE
SEQRES  10 A  390  TYR ASN LYS ASP LEU LEU PRO ASN PRO PRO LYS THR TRP
SEQRES  11 A  390  GLU GLU ILE PRO ALA LEU ASP LYS GLU LEU LYS ALA LYS
SEQRES  12 A  390  GLY LYS SER ALA LEU MET PHE ASN LEU GLN GLU PRO TYR
SEQRES  13 A  390  PHE THR TRP PRO LEU ILE ALA ALA ASP GLY GLY TYR ALA
SEQRES  14 A  390  PHE LYS TYR GLU ASN GLY LYS TYR ASP ILE LYS ASP VAL
SEQRES  15 A  390  GLY VAL ASP ASN ALA GLY ALA LYS ALA GLY LEU THR PHE
SEQRES  16 A  390  LEU VAL ASP LEU ILE LYS ASN LYS HIS MET ASN ALA ASP
SEQRES  17 A  390  THR ASP TYR SER ILE ALA GLU ALA ALA PHE ASN LYS GLY
SEQRES  18 A  390  GLU THR ALA MET THR ILE ASN GLY PRO TRP ALA TRP SER
SEQRES  19 A  390  ASN ILE ASP THR SER LYS VAL ASN TYR GLY VAL THR VAL
SEQRES  20 A  390  LEU PRO THR PHE LYS GLY GLN PRO SER LYS PRO PHE VAL
SEQRES  21 A  390  GLY VAL LEU SER ALA GLY ILE ASN ALA ALA SER PRO ASN
SEQRES  22 A  390  LYS GLU LEU ALA LYS GLU PHE LEU GLU ASN TYR LEU LEU
SEQRES  23 A  390  THR ASP GLU GLY LEU GLU ALA VAL ASN LYS ASP LYS PRO
SEQRES  24 A  390  LEU GLY ALA VAL ALA LEU LYS SER TYR GLU GLU GLU LEU
SEQRES  25 A  390  ALA LYS ASP PRO ARG ILE ALA ALA THR MET GLU ASN ALA
SEQRES  26 A  390  GLN LYS GLY GLU ILE MET PRO ASN ILE PRO GLN MET SER
SEQRES  27 A  390  ALA PHE TRP TYR ALA VAL ARG THR ALA VAL ILE ASN ALA
SEQRES  28 A  390  ALA SER GLY ARG GLN THR VAL ASP GLU ALA LEU LYS ASP
SEQRES  29 A  390  ALA GLN THR ASN SER SER SER MET ASP VAL PHE MET LYS
SEQRES  30 A  390  GLY LEU SER LYS ALA LYS GLU GLY VAL VAL ALA ALA ALA
HET    MAL  A5044      23
HET    SO4  A   1       5
HET    SO4  A   2       5
HET    SO4  A 391       5
HET    SO4  A 392       5
HET    SO4  A 393       5
HET    SO4  A 394       5
HET    SO4  A 395       5
HET    SO4  A 396       5
HET    SO4  A 397       5
HET    SO4  A 398       5
HET    GOL  A 399       6
HET    GOL  A 400       6
HET    GOL  A 401       6
HET    GOL  A 402       6
HET    GOL  A 403       6
HET    GOL  A 404       6
HETNAM     MAL MALTOSE
HETNAM     SO4 SULFATE ION
HETNAM     GOL GLYCEROL
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   2  MAL    C12 H22 O11
FORMUL   3  SO4    10(O4 S 2-)
FORMUL  13  GOL    6(C3 H8 O3)
FORMUL  19  HOH   *279(H2 O)
HELIX    1   1 GLY A   17  GLY A   33  1                                  17
HELIX    2   2 LYS A   43  ALA A   52  1                                  10
HELIX    3   3 ARG A   67  SER A   74  1                                   8
HELIX    4   4 ASP A   83  ASP A   88  1                                   6
HELIX    5   5 TYR A   91  VAL A   98  1                                   8
HELIX    6   6 GLU A  132  ALA A  142  1                                  11
HELIX    7   7 GLU A  154  ASP A  165  1                                  12
HELIX    8   8 ASN A  186  ASN A  202  1                                  17
HELIX    9   9 ASP A  210  LYS A  220  1                                  11
HELIX   10  10 GLY A  229  TRP A  231  5                                   3
HELIX   11  11 ALA A  232  LYS A  240  1                                   9
HELIX   12  12 ASN A  273  TYR A  284  1                                  12
HELIX   13  13 THR A  287  LYS A  298  1                                  12
HELIX   14  14 LEU A  305  ALA A  313  1                                   9
HELIX   15  15 ASP A  315  GLY A  328  1                                  14
HELIX   16  16 GLN A  336  SER A  353  1                                  18
HELIX   17  17 THR A  357  SER A  369  1                                  13
HELIX   18  18 ASP A  373  LYS A  383  1                                  11
SHEET    1   A 6 VAL A  36  GLU A  39  0
SHEET    2   A 6 LEU A   8  TRP A  11  1  N  ILE A  10   O  GLU A  39
SHEET    3   A 6 ILE A  60  ALA A  64  1  O  PHE A  62   N  TRP A  11
SHEET    4   A 6 PHE A 259  ILE A 267 -1  O  GLY A 266   N  ILE A  61
SHEET    5   A 6 TYR A 107  GLU A 112 -1  N  ILE A 109   O  LEU A 263
SHEET    6   A 6 ALA A 302  VAL A 303 -1  O  ALA A 302   N  VAL A 111
SHEET    1   B 5 VAL A  36  GLU A  39  0
SHEET    2   B 5 LEU A   8  TRP A  11  1  N  ILE A  10   O  GLU A  39
SHEET    3   B 5 ILE A  60  ALA A  64  1  O  PHE A  62   N  TRP A  11
SHEET    4   B 5 PHE A 259  ILE A 267 -1  O  GLY A 266   N  ILE A  61
SHEET    5   B 5 GLU A 329  ILE A 330  1  O  GLU A 329   N  VAL A 260
SHEET    1   C 2 ARG A  99  TYR A 100  0
SHEET    2   C 2 LYS A 103  LEU A 104 -1  O  LYS A 103   N  TYR A 100
SHEET    1   D 4 SER A 146  LEU A 148  0
SHEET    2   D 4 THR A 223  ASN A 228  1  O  ALA A 224   N  SER A 146
SHEET    3   D 4 SER A 115  ASN A 119 -1  N  ILE A 117   O  THR A 226
SHEET    4   D 4 TYR A 243  THR A 246 -1  O  THR A 246   N  LEU A 116
SHEET    1   E 2 TYR A 168  GLU A 173  0
SHEET    2   E 2 LYS A 176  GLY A 183 -1  O  ASP A 178   N  LYS A 171
SHEET    1   F 2 THR A 250  PHE A 251  0
SHEET    2   F 2 GLN A 254  PRO A 255 -1  O  GLN A 254   N  PHE A 251
SITE     1 AC1 17 ASN A  13  ASP A  15  LYS A  16  TRP A  63
SITE     2 AC1 17 ALA A  64  ASP A  66  ARG A  67  GLU A 112
SITE     3 AC1 17 GLU A 154  PRO A 155  TYR A 156  TRP A 341
SITE     4 AC1 17 HOH A 409  HOH A 468  HOH A 493  HOH A 502
SITE     5 AC1 17 HOH A 566
SITE     1 AC2  6 ASN A 151  GLU A 154  ASP A 210  TYR A 211
SITE     2 AC2  6 HOH A 466  HOH A 538
SITE     1 AC3  4 PRO A  41  ASP A  42  LYS A  47  HOH A 471
SITE     1 AC4  4 ASN A 186  ALA A 187  HOH A 474  HOH A 536
SITE     1 AC5  3 ASP A  83  LYS A  84  HOH A 460
SITE     1 AC6  2 THR A  54  GLY A  55
SITE     1 AC7  7 GLY A  14  HIS A  40  ASP A  42  HOH A 426
SITE     2 AC7  7 HOH A 471  HOH A 572  HOH A 673
SITE     1 AC8  2 TYR A  18  ASN A  19
SITE     1 AC9  4 LYS A  27  ASN A 283  TYR A 284  HOH A 604
SITE     1 BC1  4 TYR A 118  THR A 246  HOH A 600  HOH A 643
SITE     1 BC2 10 THR A  54  GLY A  57  PRO A  58  ASP A  59
SITE     2 BC2 10 ASN A 268  ALA A 270  PRO A 272  LYS A 383
SITE     3 BC2 10 HOH A 476  HOH A 649
SITE     1 BC3  8 TYR A 168  ALA A 169  PHE A 170  PHE A 259
SITE     2 BC3  8 PRO A 332  ALA A 389  HOH A 453  HOH A 494
SITE     1 BC4  8 LYS A 171  TYR A 172  GLU A 173  LYS A 176
SITE     2 BC4  8 ASP A 178  HOH A 500  HOH A 583  HOH A 653
SITE     1 BC5  7 ASN A  13  ASP A  42  LYS A  43  HOH A 426
SITE     2 BC5  7 HOH A 502  HOH A 572  HOH A 574
SITE     1 BC6  8 ASN A 295  LYS A 296  PRO A 299  ARG A 317
SITE     2 BC6  8 ARG A 355  HOH A 446  HOH A 448  HOH A 589
SITE     1 BC7  6 ARG A  99  TYR A 100  ASN A 101  GLY A 102
SITE     2 BC7  6 HOH A 488  HOH A 529
SITE     1 BC8  8 ALA A  72  GLY A  75  LEU A  76  LEU A  77
SITE     2 BC8  8 GLU A  79  ILE A 105  ASP A 373  HOH A 549
CRYST1   77.470   77.470  172.640  90.00  90.00  90.00 P 43 21 2     8
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      0.012908  0.000000  0.000000        0.00000
SCALE2      0.000000  0.012908  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005792        0.00000
      
PROCHECK
Go to PROCHECK summary
 References