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PDBsum entry 3q26

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Sugar binding protein, protein fibril PDB id
3q26
Jmol
Contents
Protein chain
395 a.a.
Ligands
MAL
GOL ×6
SO4 ×3
Waters ×388
HEADER    SUGAR BINDING PROTEIN, PROTEIN FIBRIL   19-DEC-10   3Q26
TITLE     CYRSTAL STRUCTURE OF HUMAN ALPHA-SYNUCLEIN (10-42) 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 GENE: SNCA;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 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 3Q26    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.    1.54 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) : 1.54
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 63.62
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 2.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0
REMARK   3   NUMBER OF REFLECTIONS             : 53761
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.142
REMARK   3   R VALUE            (WORKING SET) : 0.140
REMARK   3   FREE R VALUE                     : 0.183
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 2689
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 63.6693 -  4.1089    1.00     2893   153  0.1608 0.1699
REMARK   3     2  4.1089 -  3.2613    1.00     2763   145  0.1383 0.1605
REMARK   3     3  3.2613 -  2.8491    1.00     2735   144  0.1600 0.1984
REMARK   3     4  2.8491 -  2.5886    1.00     2709   143  0.1518 0.1836
REMARK   3     5  2.5886 -  2.4030    1.00     2695   142  0.1411 0.1825
REMARK   3     6  2.4030 -  2.2614    1.00     2708   142  0.1355 0.1863
REMARK   3     7  2.2614 -  2.1481    1.00     2673   141  0.1292 0.1574
REMARK   3     8  2.1481 -  2.0546    1.00     2667   140  0.1243 0.1734
REMARK   3     9  2.0546 -  1.9755    1.00     2686   142  0.1125 0.1706
REMARK   3    10  1.9755 -  1.9073    1.00     2677   141  0.1066 0.1519
REMARK   3    11  1.9073 -  1.8477    1.00     2644   139  0.1096 0.1869
REMARK   3    12  1.8477 -  1.7949    1.00     2661   140  0.1133 0.2073
REMARK   3    13  1.7949 -  1.7476    1.00     2652   139  0.1225 0.1719
REMARK   3    14  1.7476 -  1.7050    1.00     2673   141  0.1171 0.2015
REMARK   3    15  1.7050 -  1.6662    1.00     2648   139  0.1300 0.1925
REMARK   3    16  1.6662 -  1.6307    1.00     2646   140  0.1542 0.2323
REMARK   3    17  1.6307 -  1.5981    1.00     2666   140  0.1691 0.2470
REMARK   3    18  1.5981 -  1.5680    1.00     2618   138  0.1602 0.2499
REMARK   3    19  1.5680 -  1.5400    1.00     2658   140  0.1835 0.2655
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              : 29.04
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.180
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 19.84
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.42
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 2.54500
REMARK   3    B22 (A**2) : -1.23570
REMARK   3    B33 (A**2) : -1.30920
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      :  0.009           3299
REMARK   3   ANGLE     :  1.180           4505
REMARK   3   CHIRALITY :  0.077            500
REMARK   3   PLANARITY :  0.005            579
REMARK   3   DIHEDRAL  : 12.995           1232
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
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 3Q26 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JAN-11.
REMARK 100 THE RCSB ID CODE IS RCSB063099.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 15-OCT-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-C
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97949
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   : 53765
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.540
REMARK 200  RESOLUTION RANGE LOW       (A) : 63.615
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : 0.07700
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 17.7200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.54
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.58
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.56100
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 3.600
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   (%): 39.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M TRI-LITHIUM CITRATE, 2.2 M
REMARK 280  AMMONIUM SULFATE, PH 8.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280  TEMPERATURE 290K
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       24.37000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       63.61500
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       28.74500
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       63.61500
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.37000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       28.74500
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     MET A     1
REMARK 465     LYS A   374
REMARK 465     GLU A   375
REMARK 465     GLY A   376
REMARK 465     VAL A   377
REMARK 465     VAL A   378
REMARK 465     ALA A   379
REMARK 465     ALA A   380
REMARK 465     ALA A   381
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     LYS A   2    CG   CD   CE   NZ
REMARK 470     LYS A  26    CD   CE   NZ
REMARK 470     LYS A  84    CG   CD   CE   NZ
REMARK 470     LYS A 180    CD   CE   NZ
REMARK 470     LYS A 240    CG   CD   CE   NZ
REMARK 470     LYS A 372    CE   NZ
REMARK 470     GLU A 382    CG   CD   OE1  OE2
REMARK 470     LYS A 385    CG   CD   CE   NZ
REMARK 470     GLN A 386    CG   CD   OE1  NE2
REMARK 470     GLU A 390    CG   CD   OE1  OE2
REMARK 470     LYS A 394    CG   CD   CE   NZ
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    ASP A  56     -167.26   -106.30
REMARK 500    ALA A 169      -80.94    -83.39
REMARK 500    ASP A 210     -169.23   -121.74
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 GOL A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 412
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3Q25   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  3Q26 A    2   367  UNP    P0AEX9   MALE_ECOLI      27    392
DBREF  3Q26 A  372   404  UNP    P37840   SYUA_HUMAN      10     42
SEQADV 3Q26 MET A    1  UNP  P0AEX9              INITIATING METHIONINE
SEQADV 3Q26 ASN A  368  UNP  P0AEX9              LINKER
SEQADV 3Q26 SER A  369  UNP  P0AEX9              LINKER
SEQADV 3Q26 SER A  370  UNP  P0AEX9              LINKER
SEQADV 3Q26 SER A  371  UNP  P0AEX9              LINKER
SEQRES   1 A  404  MET LYS ILE GLU GLU GLY LYS LEU VAL ILE TRP ILE ASN
SEQRES   2 A  404  GLY ASP LYS GLY TYR ASN GLY LEU ALA GLU VAL GLY LYS
SEQRES   3 A  404  LYS PHE GLU LYS ASP THR GLY ILE LYS VAL THR VAL GLU
SEQRES   4 A  404  HIS PRO ASP LYS LEU GLU GLU LYS PHE PRO GLN VAL ALA
SEQRES   5 A  404  ALA THR GLY ASP GLY PRO ASP ILE ILE PHE TRP ALA HIS
SEQRES   6 A  404  ASP ARG PHE GLY GLY TYR ALA GLN SER GLY LEU LEU ALA
SEQRES   7 A  404  GLU ILE THR PRO ASP LYS ALA PHE GLN ASP LYS LEU TYR
SEQRES   8 A  404  PRO PHE THR TRP ASP ALA VAL ARG TYR ASN GLY LYS LEU
SEQRES   9 A  404  ILE ALA TYR PRO ILE ALA VAL GLU ALA LEU SER LEU ILE
SEQRES  10 A  404  TYR ASN LYS ASP LEU LEU PRO ASN PRO PRO LYS THR TRP
SEQRES  11 A  404  GLU GLU ILE PRO ALA LEU ASP LYS GLU LEU LYS ALA LYS
SEQRES  12 A  404  GLY LYS SER ALA LEU MET PHE ASN LEU GLN GLU PRO TYR
SEQRES  13 A  404  PHE THR TRP PRO LEU ILE ALA ALA ASP GLY GLY TYR ALA
SEQRES  14 A  404  PHE LYS TYR GLU ASN GLY LYS TYR ASP ILE LYS ASP VAL
SEQRES  15 A  404  GLY VAL ASP ASN ALA GLY ALA LYS ALA GLY LEU THR PHE
SEQRES  16 A  404  LEU VAL ASP LEU ILE LYS ASN LYS HIS MET ASN ALA ASP
SEQRES  17 A  404  THR ASP TYR SER ILE ALA GLU ALA ALA PHE ASN LYS GLY
SEQRES  18 A  404  GLU THR ALA MET THR ILE ASN GLY PRO TRP ALA TRP SER
SEQRES  19 A  404  ASN ILE ASP THR SER LYS VAL ASN TYR GLY VAL THR VAL
SEQRES  20 A  404  LEU PRO THR PHE LYS GLY GLN PRO SER LYS PRO PHE VAL
SEQRES  21 A  404  GLY VAL LEU SER ALA GLY ILE ASN ALA ALA SER PRO ASN
SEQRES  22 A  404  LYS GLU LEU ALA LYS GLU PHE LEU GLU ASN TYR LEU LEU
SEQRES  23 A  404  THR ASP GLU GLY LEU GLU ALA VAL ASN LYS ASP LYS PRO
SEQRES  24 A  404  LEU GLY ALA VAL ALA LEU LYS SER TYR GLU GLU GLU LEU
SEQRES  25 A  404  ALA LYS ASP PRO ARG ILE ALA ALA THR MET GLU ASN ALA
SEQRES  26 A  404  GLN LYS GLY GLU ILE MET PRO ASN ILE PRO GLN MET SER
SEQRES  27 A  404  ALA PHE TRP TYR ALA VAL ARG THR ALA VAL ILE ASN ALA
SEQRES  28 A  404  ALA SER GLY ARG GLN THR VAL ASP GLU ALA LEU LYS ASP
SEQRES  29 A  404  ALA GLN THR ASN SER SER SER LYS ALA LYS GLU GLY VAL
SEQRES  30 A  404  VAL ALA ALA ALA GLU LYS THR LYS GLN GLY VAL ALA GLU
SEQRES  31 A  404  ALA ALA GLY LYS THR LYS GLU GLY VAL LEU TYR VAL GLY
SEQRES  32 A  404  SER
HET    MAL  A5044      46
HET    GOL  A   1       6
HET    GOL  A 405       6
HET    GOL  A 406       6
HET    SO4  A 407       5
HET    SO4  A 408       5
HET    SO4  A 409       5
HET    GOL  A 410       6
HET    GOL  A 411       6
HET    GOL  A 412       6
HETNAM     MAL MALTOSE
HETNAM     GOL GLYCEROL
HETNAM     SO4 SULFATE ION
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   2  MAL    C12 H22 O11
FORMUL   3  GOL    6(C3 H8 O3)
FORMUL   6  SO4    3(O4 S 2-)
FORMUL  12  HOH   *388(H2 O)
HELIX    1   1 GLY A   17  GLY A   33  1                                  17
HELIX    2   2 LYS A   43  ALA A   53  1                                  11
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 THR A  129  GLU A  131  5                                   3
HELIX    7   7 GLU A  132  ALA A  142  1                                  11
HELIX    8   8 GLU A  154  PHE A  157  5                                   4
HELIX    9   9 THR A  158  ASP A  165  1                                   8
HELIX   10  10 ASN A  186  ASN A  202  1                                  17
HELIX   11  11 ASP A  210  LYS A  220  1                                  11
HELIX   12  12 GLY A  229  TRP A  231  5                                   3
HELIX   13  13 ALA A  232  LYS A  240  1                                   9
HELIX   14  14 ASN A  273  TYR A  284  1                                  12
HELIX   15  15 THR A  287  LYS A  298  1                                  12
HELIX   16  16 LEU A  305  ALA A  313  1                                   9
HELIX   17  17 ASP A  315  GLY A  328  1                                  14
HELIX   18  18 GLN A  336  SER A  353  1                                  18
HELIX   19  19 THR A  357  SER A  370  1                                  14
HELIX   20  20 GLU A  382  THR A  395  1                                  14
SHEET    1   A 6 LYS A  35  GLU A  39  0
SHEET    2   A 6 LYS A   7  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  GLU A 112   O  GLY A 261
SHEET    6   A 6 ALA A 302  VAL A 303 -1  O  ALA A 302   N  VAL A 111
SHEET    1   B 5 LYS A  35  GLU A  39  0
SHEET    2   B 5 LYS A   7  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  ASN A 119   O  ALA A 224
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 181   N  LYS A 171
SITE     1 AC1 22 ASN A  13  ASP A  15  LYS A  16  TRP A  63
SITE     2 AC1 22 ALA A  64  ASP A  66  ARG A  67  GLU A 112
SITE     3 AC1 22 GLU A 154  PRO A 155  TYR A 156  TRP A 231
SITE     4 AC1 22 TRP A 341  ARG A 345  HOH A 417  HOH A 432
SITE     5 AC1 22 HOH A 507  HOH A 555  HOH A 587  HOH A 590
SITE     6 AC1 22 HOH A 603  HOH A 686
SITE     1 AC2  3 ASP A  88  LYS A 306  GLU A 310
SITE     1 AC3 10 TYR A 118  ASP A 165  ALA A 187  GLY A 188
SITE     2 AC3 10 ALA A 191  THR A 246  LYS A 252  GLY A 403
SITE     3 AC3 10 SER A 404  HOH A 783
SITE     1 AC4  3 THR A 357  HOH A 445  HOH A 673
SITE     1 AC5  6 PRO A  41  ASP A  42  LYS A  47  HOH A 599
SITE     2 AC5  6 HOH A 689  HOH A 782
SITE     1 AC6  4 LYS A  27  LYS A  30  SER A 212  HOH A 764
SITE     1 AC7  7 ASN A 151  GLN A 153  GLU A 154  ASP A 210
SITE     2 AC7  7 TYR A 211  HOH A 544  HOH A 716
SITE     1 AC8  4 ASP A  83  LYS A  84  HOH A 608  HOH A 703
SITE     1 AC9  4 GLY A  14  HIS A  40  ASP A  42  HOH A 562
SITE     1 BC1  6 GLU A  23  VAL A  24  LYS A  27  TYR A 284
SITE     2 BC1  6 GLU A 289  HOH A 698
CRYST1   48.740   57.490  127.230  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      0.020517  0.000000  0.000000        0.00000
SCALE2      0.000000  0.017394  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007860        0.00000
      
PROCHECK
Go to PROCHECK summary
 References