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PDBsum entry 3nb0

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Top Page protein ligands Protein-protein interface(s) links
Transferase PDB id
3nb0
Jmol
Contents
Protein chains
638 a.a.
Ligands
G6P ×6
PEG ×6
Waters ×524
HEADER    TRANSFERASE                             02-JUN-10   3NB0
TITLE     GLUCOSE-6-PHOSPHATE ACTIVATED FORM OF YEAST GLYCOGEN SYNTHASE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: GLYCOGEN [STARCH] SYNTHASE ISOFORM 2;
COMPND   3 CHAIN: A, B, C, D;
COMPND   4 EC: 2.4.1.11;
COMPND   5 ENGINEERED: YES;
COMPND   6 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE   3 ORGANISM_COMMON: BREWER'S YEAST,LAGER BEER YEAST,YEAST;
SOURCE   4 ORGANISM_TAXID: 4932;
SOURCE   5 GENE: GSY2, L8479.8, YLR258W;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21-DE3;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS    GLYCOGEN SYNTHASE, GLUCOSE-6-PHOSPHATE, YEAST, ALLOSTERIC ACTIVATION,
KEYWDS   2 TRANSFERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.BASKARAN,T.D.HURLEY
REVDAT   3   20-OCT-10 3NB0    1       JRNL
REVDAT   2   13-OCT-10 3NB0    1       JRNL
REVDAT   1   06-OCT-10 3NB0    0
JRNL        AUTH   S.BASKARAN,P.J.ROACH,A.A.DEPAOLI-ROACH,T.D.HURLEY
JRNL        TITL   STRUCTURAL BASIS FOR GLUCOSE-6-PHOSPHATE ACTIVATION OF
JRNL        TITL 2 GLYCOGEN SYNTHASE.
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 107 17563 2010
JRNL        REFN                   ISSN 0027-8424
JRNL        PMID   20876143
JRNL        DOI    10.1073/PNAS.1006340107
REMARK   2
REMARK   2 RESOLUTION.    2.41 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)
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) : 2.41
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.23
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.060
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.6
REMARK   3   NUMBER OF REFLECTIONS             : 148274
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.213
REMARK   3   R VALUE            (WORKING SET) : 0.211
REMARK   3   FREE R VALUE                     : 0.242
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.020
REMARK   3   FREE R VALUE TEST SET COUNT      : 7445
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 46.2380 -  7.4660    0.91     4786   273  0.1740 0.1940
REMARK   3     2  7.4660 -  5.9300    0.99     5080   260  0.1910 0.2090
REMARK   3     3  5.9300 -  5.1810    0.99     5040   272  0.1930 0.2200
REMARK   3     4  5.1810 -  4.7080    0.99     5057   217  0.1720 0.2070
REMARK   3     5  4.7080 -  4.3710    0.99     5003   278  0.1730 0.1990
REMARK   3     6  4.3710 -  4.1130    0.99     5066   248  0.1810 0.2170
REMARK   3     7  4.1130 -  3.9080    0.99     4983   257  0.1840 0.2100
REMARK   3     8  3.9080 -  3.7370    0.99     4959   274  0.1940 0.2200
REMARK   3     9  3.7370 -  3.5940    0.99     4997   270  0.1920 0.2210
REMARK   3    10  3.5940 -  3.4700    0.99     4944   275  0.2100 0.2330
REMARK   3    11  3.4700 -  3.3610    0.99     4920   248  0.2170 0.2440
REMARK   3    12  3.3610 -  3.2650    0.98     4965   258  0.2370 0.2760
REMARK   3    13  3.2650 -  3.1790    0.98     4843   246  0.2330 0.2730
REMARK   3    14  3.1790 -  3.1020    0.97     4915   250  0.2490 0.2900
REMARK   3    15  3.1020 -  3.0310    0.97     4826   241  0.2440 0.2590
REMARK   3    16  3.0310 -  2.9670    0.96     4755   252  0.2390 0.2880
REMARK   3    17  2.9670 -  2.9070    0.94     4710   263  0.2420 0.2610
REMARK   3    18  2.9070 -  2.8520    0.94     4685   246  0.2400 0.2850
REMARK   3    19  2.8520 -  2.8020    0.94     4658   267  0.2410 0.2710
REMARK   3    20  2.8020 -  2.7540    0.92     4616   214  0.2390 0.3000
REMARK   3    21  2.7540 -  2.7100    0.92     4570   252  0.2450 0.2870
REMARK   3    22  2.7100 -  2.6680    0.91     4499   236  0.2400 0.3240
REMARK   3    23  2.6680 -  2.6290    0.90     4487   239  0.2470 0.2750
REMARK   3    24  2.6290 -  2.5920    0.89     4400   255  0.2510 0.2900
REMARK   3    25  2.5920 -  2.5570    0.89     4419   247  0.2600 0.3080
REMARK   3    26  2.5570 -  2.5230    0.87     4290   244  0.2630 0.2960
REMARK   3    27  2.5230 -  2.4920    0.86     4252   237  0.2580 0.3010
REMARK   3    28  2.4920 -  2.4620    0.85     4249   220  0.2550 0.3110
REMARK   3    29  2.4620 -  2.4330    0.84     4166   206  0.2640 0.2860
REMARK   3    30  2.4330 -  2.4060    0.74     3689   200  0.2800 0.3330
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.11
REMARK   3   SHRINKAGE RADIUS   : 0.90
REMARK   3   K_SOL              : 0.36
REMARK   3   B_SOL              : 58.36
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 2.370
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.550
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 42.44
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 57.19
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -4.83400
REMARK   3    B22 (A**2) : -9.85500
REMARK   3    B33 (A**2) : 14.68900
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      :  0.004          21375
REMARK   3   ANGLE     :  0.737          28968
REMARK   3   CHIRALITY :  0.054           3123
REMARK   3   PLANARITY :  0.003           3747
REMARK   3   DIHEDRAL  : 17.749           7893
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 3NB0 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JUN-10.
REMARK 100 THE RCSB ID CODE IS RCSB059603.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 14-MAR-10
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.2
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 23-ID-D
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 157186
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.200
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5
REMARK 200  DATA REDUNDANCY                : 4.800
REMARK 200  R MERGE                    (I) : 0.08700
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 15.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.44
REMARK 200  COMPLETENESS FOR SHELL     (%) : 79.1
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.55200
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 3NAZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 60.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS PH 6.2, 25% PEG 300,
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X,Y,-Z
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290       8555   X+1/2,-Y+1/2,-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        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       96.36950
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      103.49100
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      102.89950
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       96.36950
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      103.49100
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      102.89950
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       96.36950
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      103.49100
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      102.89950
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       96.36950
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      103.49100
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      102.89950
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 16430 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 99550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -71.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B, D
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   -19
REMARK 465     GLY A   -18
REMARK 465     SER A   -17
REMARK 465     SER A   -16
REMARK 465     HIS A   -15
REMARK 465     HIS A   -14
REMARK 465     HIS A   -13
REMARK 465     HIS A   -12
REMARK 465     HIS A   -11
REMARK 465     HIS A   -10
REMARK 465     SER A    -9
REMARK 465     SER A    -8
REMARK 465     GLY A    -7
REMARK 465     LEU A    -6
REMARK 465     VAL A    -5
REMARK 465     PRO A    -4
REMARK 465     ARG A    -3
REMARK 465     GLY A    -2
REMARK 465     SER A    -1
REMARK 465     HIS A     0
REMARK 465     MET A     1
REMARK 465     GLY A   640
REMARK 465     GLY A   641
REMARK 465     LYS A   642
REMARK 465     LYS A   643
REMARK 465     LEU A   644
REMARK 465     LYS A   645
REMARK 465     VAL A   646
REMARK 465     ALA A   647
REMARK 465     ARG A   648
REMARK 465     PRO A   649
REMARK 465     LEU A   650
REMARK 465     SER A   651
REMARK 465     VAL A   652
REMARK 465     PRO A   653
REMARK 465     GLY A   654
REMARK 465     SER A   655
REMARK 465     PRO A   656
REMARK 465     ARG A   657
REMARK 465     ASP A   658
REMARK 465     LEU A   659
REMARK 465     ARG A   660
REMARK 465     SER A   661
REMARK 465     ASN A   662
REMARK 465     SER A   663
REMARK 465     THR A   664
REMARK 465     VAL A   665
REMARK 465     TYR A   666
REMARK 465     MET A   667
REMARK 465     THR A   668
REMARK 465     PRO A   669
REMARK 465     GLY A   670
REMARK 465     ASP A   671
REMARK 465     LEU A   672
REMARK 465     GLY A   673
REMARK 465     THR A   674
REMARK 465     LEU A   675
REMARK 465     GLN A   676
REMARK 465     GLU A   677
REMARK 465     VAL A   678
REMARK 465     ASN A   679
REMARK 465     ASN A   680
REMARK 465     ALA A   681
REMARK 465     ASP A   682
REMARK 465     ASP A   683
REMARK 465     TYR A   684
REMARK 465     PHE A   685
REMARK 465     SER A   686
REMARK 465     LEU A   687
REMARK 465     GLY A   688
REMARK 465     VAL A   689
REMARK 465     ASN A   690
REMARK 465     PRO A   691
REMARK 465     ALA A   692
REMARK 465     ALA A   693
REMARK 465     ASP A   694
REMARK 465     ASP A   695
REMARK 465     ASP A   696
REMARK 465     ASP A   697
REMARK 465     ASP A   698
REMARK 465     GLY A   699
REMARK 465     PRO A   700
REMARK 465     TYR A   701
REMARK 465     ALA A   702
REMARK 465     ASP A   703
REMARK 465     ASP A   704
REMARK 465     SER A   705
REMARK 465     MET B   -19
REMARK 465     GLY B   -18
REMARK 465     SER B   -17
REMARK 465     SER B   -16
REMARK 465     HIS B   -15
REMARK 465     HIS B   -14
REMARK 465     HIS B   -13
REMARK 465     HIS B   -12
REMARK 465     HIS B   -11
REMARK 465     HIS B   -10
REMARK 465     SER B    -9
REMARK 465     SER B    -8
REMARK 465     GLY B    -7
REMARK 465     LEU B    -6
REMARK 465     VAL B    -5
REMARK 465     PRO B    -4
REMARK 465     ARG B    -3
REMARK 465     GLY B    -2
REMARK 465     SER B    -1
REMARK 465     HIS B     0
REMARK 465     MET B     1
REMARK 465     ALA B   647
REMARK 465     ARG B   648
REMARK 465     PRO B   649
REMARK 465     LEU B   650
REMARK 465     SER B   651
REMARK 465     VAL B   652
REMARK 465     PRO B   653
REMARK 465     GLY B   654
REMARK 465     SER B   655
REMARK 465     PRO B   656
REMARK 465     ARG B   657
REMARK 465     ASP B   658
REMARK 465     LEU B   659
REMARK 465     ARG B   660
REMARK 465     SER B   661
REMARK 465     ASN B   662
REMARK 465     SER B   663
REMARK 465     THR B   664
REMARK 465     VAL B   665
REMARK 465     TYR B   666
REMARK 465     MET B   667
REMARK 465     THR B   668
REMARK 465     PRO B   669
REMARK 465     GLY B   670
REMARK 465     ASP B   671
REMARK 465     LEU B   672
REMARK 465     GLY B   673
REMARK 465     THR B   674
REMARK 465     LEU B   675
REMARK 465     GLN B   676
REMARK 465     GLU B   677
REMARK 465     VAL B   678
REMARK 465     ASN B   679
REMARK 465     ASN B   680
REMARK 465     ALA B   681
REMARK 465     ASP B   682
REMARK 465     ASP B   683
REMARK 465     TYR B   684
REMARK 465     PHE B   685
REMARK 465     SER B   686
REMARK 465     LEU B   687
REMARK 465     GLY B   688
REMARK 465     VAL B   689
REMARK 465     ASN B   690
REMARK 465     PRO B   691
REMARK 465     ALA B   692
REMARK 465     ALA B   693
REMARK 465     ASP B   694
REMARK 465     ASP B   695
REMARK 465     ASP B   696
REMARK 465     ASP B   697
REMARK 465     ASP B   698
REMARK 465     GLY B   699
REMARK 465     PRO B   700
REMARK 465     TYR B   701
REMARK 465     ALA B   702
REMARK 465     ASP B   703
REMARK 465     ASP B   704
REMARK 465     SER B   705
REMARK 465     MET C   -19
REMARK 465     GLY C   -18
REMARK 465     SER C   -17
REMARK 465     SER C   -16
REMARK 465     HIS C   -15
REMARK 465     HIS C   -14
REMARK 465     HIS C   -13
REMARK 465     HIS C   -12
REMARK 465     HIS C   -11
REMARK 465     HIS C   -10
REMARK 465     SER C    -9
REMARK 465     SER C    -8
REMARK 465     GLY C    -7
REMARK 465     LEU C    -6
REMARK 465     VAL C    -5
REMARK 465     PRO C    -4
REMARK 465     ARG C    -3
REMARK 465     GLY C    -2
REMARK 465     SER C    -1
REMARK 465     HIS C     0
REMARK 465     MET C     1
REMARK 465     ARG C   648
REMARK 465     PRO C   649
REMARK 465     LEU C   650
REMARK 465     SER C   651
REMARK 465     VAL C   652
REMARK 465     PRO C   653
REMARK 465     GLY C   654
REMARK 465     SER C   655
REMARK 465     PRO C   656
REMARK 465     ARG C   657
REMARK 465     ASP C   658
REMARK 465     LEU C   659
REMARK 465     ARG C   660
REMARK 465     SER C   661
REMARK 465     ASN C   662
REMARK 465     SER C   663
REMARK 465     THR C   664
REMARK 465     VAL C   665
REMARK 465     TYR C   666
REMARK 465     MET C   667
REMARK 465     THR C   668
REMARK 465     PRO C   669
REMARK 465     GLY C   670
REMARK 465     ASP C   671
REMARK 465     LEU C   672
REMARK 465     GLY C   673
REMARK 465     THR C   674
REMARK 465     LEU C   675
REMARK 465     GLN C   676
REMARK 465     GLU C   677
REMARK 465     VAL C   678
REMARK 465     ASN C   679
REMARK 465     ASN C   680
REMARK 465     ALA C   681
REMARK 465     ASP C   682
REMARK 465     ASP C   683
REMARK 465     TYR C   684
REMARK 465     PHE C   685
REMARK 465     SER C   686
REMARK 465     LEU C   687
REMARK 465     GLY C   688
REMARK 465     VAL C   689
REMARK 465     ASN C   690
REMARK 465     PRO C   691
REMARK 465     ALA C   692
REMARK 465     ALA C   693
REMARK 465     ASP C   694
REMARK 465     ASP C   695
REMARK 465     ASP C   696
REMARK 465     ASP C   697
REMARK 465     ASP C   698
REMARK 465     GLY C   699
REMARK 465     PRO C   700
REMARK 465     TYR C   701
REMARK 465     ALA C   702
REMARK 465     ASP C   703
REMARK 465     ASP C   704
REMARK 465     SER C   705
REMARK 465     MET D   -19
REMARK 465     GLY D   -18
REMARK 465     SER D   -17
REMARK 465     SER D   -16
REMARK 465     HIS D   -15
REMARK 465     HIS D   -14
REMARK 465     HIS D   -13
REMARK 465     HIS D   -12
REMARK 465     HIS D   -11
REMARK 465     HIS D   -10
REMARK 465     SER D    -9
REMARK 465     SER D    -8
REMARK 465     GLY D    -7
REMARK 465     LEU D    -6
REMARK 465     VAL D    -5
REMARK 465     PRO D    -4
REMARK 465     ARG D    -3
REMARK 465     GLY D    -2
REMARK 465     SER D    -1
REMARK 465     HIS D     0
REMARK 465     MET D     1
REMARK 465     SER D   206
REMARK 465     PHE D   207
REMARK 465     GLY D   640
REMARK 465     GLY D   641
REMARK 465     LYS D   642
REMARK 465     LYS D   643
REMARK 465     LEU D   644
REMARK 465     LYS D   645
REMARK 465     VAL D   646
REMARK 465     ALA D   647
REMARK 465     ARG D   648
REMARK 465     PRO D   649
REMARK 465     LEU D   650
REMARK 465     SER D   651
REMARK 465     VAL D   652
REMARK 465     PRO D   653
REMARK 465     GLY D   654
REMARK 465     SER D   655
REMARK 465     PRO D   656
REMARK 465     ARG D   657
REMARK 465     ASP D   658
REMARK 465     LEU D   659
REMARK 465     ARG D   660
REMARK 465     SER D   661
REMARK 465     ASN D   662
REMARK 465     SER D   663
REMARK 465     THR D   664
REMARK 465     VAL D   665
REMARK 465     TYR D   666
REMARK 465     MET D   667
REMARK 465     THR D   668
REMARK 465     PRO D   669
REMARK 465     GLY D   670
REMARK 465     ASP D   671
REMARK 465     LEU D   672
REMARK 465     GLY D   673
REMARK 465     THR D   674
REMARK 465     LEU D   675
REMARK 465     GLN D   676
REMARK 465     GLU D   677
REMARK 465     VAL D   678
REMARK 465     ASN D   679
REMARK 465     ASN D   680
REMARK 465     ALA D   681
REMARK 465     ASP D   682
REMARK 465     ASP D   683
REMARK 465     TYR D   684
REMARK 465     PHE D   685
REMARK 465     SER D   686
REMARK 465     LEU D   687
REMARK 465     GLY D   688
REMARK 465     VAL D   689
REMARK 465     ASN D   690
REMARK 465     PRO D   691
REMARK 465     ALA D   692
REMARK 465     ALA D   693
REMARK 465     ASP D   694
REMARK 465     ASP D   695
REMARK 465     ASP D   696
REMARK 465     ASP D   697
REMARK 465     ASP D   698
REMARK 465     GLY D   699
REMARK 465     PRO D   700
REMARK 465     TYR D   701
REMARK 465     ALA D   702
REMARK 465     ASP D   703
REMARK 465     ASP D   704
REMARK 465     SER D   705
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     SER B 535    OG
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    ASN A  19      101.38   -165.60
REMARK 500    LYS A  40     -129.03     55.26
REMARK 500    THR A  53      -15.78   -142.46
REMARK 500    ARG A  86       -5.38   -141.60
REMARK 500    LEU A  96       71.95    -68.98
REMARK 500    ALA A 100       71.55     27.34
REMARK 500    SER A 110       -1.90    -56.83
REMARK 500    VAL A 111       10.73   -145.15
REMARK 500    TYR A 114        2.89    -60.51
REMARK 500    SER A 115      -71.48    -42.42
REMARK 500    SER A 130       89.21   -167.14
REMARK 500    GLN A 160      -62.88   -100.80
REMARK 500    GLU A 169      151.69     80.20
REMARK 500    ALA A 194     -165.22    179.01
REMARK 500    LYS A 260       33.83     71.62
REMARK 500    LEU A 267       77.12   -119.98
REMARK 500    TYR A 321       81.09    -68.17
REMARK 500    SER A 363     -176.00     76.25
REMARK 500    PRO A 478       49.57    -74.57
REMARK 500    GLU A 509       85.46   -172.06
REMARK 500    LEU A 625       17.87    -63.38
REMARK 500    VAL A 626      -82.52   -131.58
REMARK 500    GLU A 628     -174.84   -173.14
REMARK 500    VAL B  17      -76.38    -44.75
REMARK 500    LYS B  40     -124.01     56.04
REMARK 500    THR B  53      -11.53   -146.24
REMARK 500    SER B 130       66.33   -160.05
REMARK 500    GLU B 169      151.45     76.96
REMARK 500    ALA B 194     -175.55    177.20
REMARK 500    HIS B 220      -71.23    -49.19
REMARK 500    TYR B 321       89.16    -65.81
REMARK 500    SER B 363     -175.40     73.49
REMARK 500    PRO B 401       40.83   -103.73
REMARK 500    ASP B 449       68.24     60.58
REMARK 500    PRO B 478       41.55    -69.39
REMARK 500    LYS B 642       53.22   -162.59
REMARK 500    LYS B 643       93.37    -55.78
REMARK 500    VAL C  17      -75.68    -55.38
REMARK 500    ALA C  18       40.35    -98.49
REMARK 500    ASN C  19      123.38   -177.14
REMARK 500    LYS C  40     -127.01     57.42
REMARK 500    ALA C  52      -71.80    -85.59
REMARK 500    PRO C 131      170.20    -58.20
REMARK 500    GLU C 169      154.29     68.17
REMARK 500    ALA C 194     -172.41   -173.95
REMARK 500    CYS C 212       39.68   -152.66
REMARK 500    CYS C 304       29.43   -143.78
REMARK 500    SER C 363     -177.76     86.63
REMARK 500    PRO C 435      155.72    -47.15
REMARK 500    PRO C 478       48.61    -78.45
REMARK 500
REMARK 500 THIS ENTRY HAS      74 RAMACHANDRAN OUTLIERS.
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 A 835        DISTANCE =  5.16 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE G6P A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE G6P A 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE G6P B 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE G6P B 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE G6P C 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG C 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE G6P D 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG D 1002
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1RZU   RELATED DB: PDB
REMARK 900 RELATED ID: 2BIS   RELATED DB: PDB
REMARK 900 RELATED ID: 2QZS   RELATED DB: PDB
REMARK 900 RELATED ID: 3NAZ   RELATED DB: PDB
REMARK 900 RELATED ID: 3NCH   RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CRYSTALLIZED SEQUENCE HAS BEEN REFERENCED TO UNP ENTRY P27472.
REMARK 999 HOWEVER, RESIDUE A535S IS ANNOTATED IN REMARK 999 GENBANK ENTRY
REMARK 999 ACCESSION CODE AAA88716
DBREF  3NB0 A    1   705  UNP    P27472   GYS2_YEAST       1    705
DBREF  3NB0 B    1   705  UNP    P27472   GYS2_YEAST       1    705
DBREF  3NB0 C    1   705  UNP    P27472   GYS2_YEAST       1    705
DBREF  3NB0 D    1   705  UNP    P27472   GYS2_YEAST       1    705
SEQADV 3NB0 MET A  -19  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 GLY A  -18  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 SER A  -17  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 SER A  -16  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 HIS A  -15  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 HIS A  -14  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 HIS A  -13  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 HIS A  -12  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 HIS A  -11  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 HIS A  -10  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 SER A   -9  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 SER A   -8  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 GLY A   -7  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 LEU A   -6  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 VAL A   -5  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 PRO A   -4  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 ARG A   -3  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 GLY A   -2  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 SER A   -1  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 HIS A    0  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 SER A  535  UNP  P27472    ALA   535 SEE REMARK 999
SEQADV 3NB0 ALA A  589  UNP  P27472    ARG   589 ENGINEERED MUTATION
SEQADV 3NB0 ALA A  592  UNP  P27472    ARG   592 ENGINEERED MUTATION
SEQADV 3NB0 MET B  -19  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 GLY B  -18  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 SER B  -17  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 SER B  -16  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 HIS B  -15  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 HIS B  -14  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 HIS B  -13  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 HIS B  -12  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 HIS B  -11  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 HIS B  -10  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 SER B   -9  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 SER B   -8  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 GLY B   -7  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 LEU B   -6  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 VAL B   -5  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 PRO B   -4  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 ARG B   -3  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 GLY B   -2  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 SER B   -1  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 HIS B    0  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 SER B  535  UNP  P27472    ALA   535 SEE REMARK 999
SEQADV 3NB0 ALA B  589  UNP  P27472    ARG   589 ENGINEERED MUTATION
SEQADV 3NB0 ALA B  592  UNP  P27472    ARG   592 ENGINEERED MUTATION
SEQADV 3NB0 MET C  -19  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 GLY C  -18  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 SER C  -17  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 SER C  -16  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 HIS C  -15  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 HIS C  -14  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 HIS C  -13  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 HIS C  -12  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 HIS C  -11  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 HIS C  -10  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 SER C   -9  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 SER C   -8  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 GLY C   -7  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 LEU C   -6  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 VAL C   -5  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 PRO C   -4  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 ARG C   -3  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 GLY C   -2  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 SER C   -1  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 HIS C    0  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 SER C  535  UNP  P27472    ALA   535 SEE REMARK 999
SEQADV 3NB0 ALA C  589  UNP  P27472    ARG   589 ENGINEERED MUTATION
SEQADV 3NB0 ALA C  592  UNP  P27472    ARG   592 ENGINEERED MUTATION
SEQADV 3NB0 MET D  -19  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 GLY D  -18  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 SER D  -17  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 SER D  -16  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 HIS D  -15  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 HIS D  -14  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 HIS D  -13  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 HIS D  -12  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 HIS D  -11  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 HIS D  -10  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 SER D   -9  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 SER D   -8  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 GLY D   -7  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 LEU D   -6  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 VAL D   -5  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 PRO D   -4  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 ARG D   -3  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 GLY D   -2  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 SER D   -1  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 HIS D    0  UNP  P27472              EXPRESSION TAG
SEQADV 3NB0 SER D  535  UNP  P27472    ALA   535 SEE REMARK 999
SEQADV 3NB0 ALA D  589  UNP  P27472    ARG   589 ENGINEERED MUTATION
SEQADV 3NB0 ALA D  592  UNP  P27472    ARG   592 ENGINEERED MUTATION
SEQRES   1 A  725  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES   2 A  725  LEU VAL PRO ARG GLY SER HIS MET SER ARG ASP LEU GLN
SEQRES   3 A  725  ASN HIS LEU LEU PHE GLU THR ALA THR GLU VAL ALA ASN
SEQRES   4 A  725  ARG VAL GLY GLY ILE TYR SER VAL LEU LYS SER LYS ALA
SEQRES   5 A  725  PRO ILE THR VAL ALA GLN TYR LYS ASP HIS TYR HIS LEU
SEQRES   6 A  725  ILE GLY PRO LEU ASN LYS ALA THR TYR GLN ASN GLU VAL
SEQRES   7 A  725  ASP ILE LEU ASP TRP LYS LYS PRO GLU ALA PHE SER ASP
SEQRES   8 A  725  GLU MET ARG PRO VAL GLN HIS ALA LEU GLN THR MET GLU
SEQRES   9 A  725  SER ARG GLY VAL HIS PHE VAL TYR GLY ARG TRP LEU ILE
SEQRES  10 A  725  GLU GLY ALA PRO LYS VAL ILE LEU PHE ASP LEU ASP SER
SEQRES  11 A  725  VAL ARG GLY TYR SER ASN GLU TRP LYS GLY ASP LEU TRP
SEQRES  12 A  725  SER LEU VAL GLY ILE PRO SER PRO GLU ASN ASP PHE GLU
SEQRES  13 A  725  THR ASN ASP ALA ILE LEU LEU GLY TYR THR VAL ALA TRP
SEQRES  14 A  725  PHE LEU GLY GLU VAL ALA HIS LEU ASP SER GLN HIS ALA
SEQRES  15 A  725  ILE VAL ALA HIS PHE HIS GLU TRP LEU ALA GLY VAL ALA
SEQRES  16 A  725  LEU PRO LEU CYS ARG LYS ARG ARG ILE ASP VAL VAL THR
SEQRES  17 A  725  ILE PHE THR THR HIS ALA THR LEU LEU GLY ARG TYR LEU
SEQRES  18 A  725  CYS ALA SER GLY SER PHE ASP PHE TYR ASN CYS LEU GLU
SEQRES  19 A  725  SER VAL ASP VAL ASP HIS GLU ALA GLY ARG PHE GLY ILE
SEQRES  20 A  725  TYR HIS ARG TYR CYS ILE GLU ARG ALA ALA ALA HIS SER
SEQRES  21 A  725  ALA ASP VAL PHE THR THR VAL SER GLN ILE THR ALA PHE
SEQRES  22 A  725  GLU ALA GLU HIS LEU LEU LYS ARG LYS PRO ASP GLY ILE
SEQRES  23 A  725  LEU PRO ASN GLY LEU ASN VAL ILE LYS PHE GLN ALA PHE
SEQRES  24 A  725  HIS GLU PHE GLN ASN LEU HIS ALA LEU LYS LYS GLU LYS
SEQRES  25 A  725  ILE ASN ASP PHE VAL ARG GLY HIS PHE HIS GLY CYS PHE
SEQRES  26 A  725  ASP PHE ASP LEU ASP ASN THR LEU TYR PHE PHE ILE ALA
SEQRES  27 A  725  GLY ARG TYR GLU TYR LYS ASN LYS GLY ALA ASP MET PHE
SEQRES  28 A  725  ILE GLU ALA LEU ALA ARG LEU ASN TYR ARG LEU LYS VAL
SEQRES  29 A  725  SER GLY SER LYS LYS THR VAL VAL ALA PHE ILE VAL MET
SEQRES  30 A  725  PRO ALA LYS ASN ASN SER PHE THR VAL GLU ALA LEU LYS
SEQRES  31 A  725  GLY GLN ALA GLU VAL ARG ALA LEU GLU ASN THR VAL HIS
SEQRES  32 A  725  GLU VAL THR THR SER ILE GLY LYS ARG ILE PHE ASP HIS
SEQRES  33 A  725  ALA ILE ARG TYR PRO HIS ASN GLY LEU THR THR GLU LEU
SEQRES  34 A  725  PRO THR ASP LEU GLY GLU LEU LEU LYS SER SER ASP LYS
SEQRES  35 A  725  VAL MET LEU LYS ARG ARG ILE LEU ALA LEU ARG ARG PRO
SEQRES  36 A  725  GLU GLY GLN LEU PRO PRO ILE VAL THR HIS ASN MET VAL
SEQRES  37 A  725  ASP ASP ALA ASN ASP LEU ILE LEU ASN LYS ILE ARG GLN
SEQRES  38 A  725  VAL GLN LEU PHE ASN SER PRO SER ASP ARG VAL LYS MET
SEQRES  39 A  725  ILE PHE HIS PRO GLU PHE LEU ASN ALA ASN ASN PRO ILE
SEQRES  40 A  725  LEU GLY LEU ASP TYR ASP GLU PHE VAL ARG GLY CYS HIS
SEQRES  41 A  725  LEU GLY VAL PHE PRO SER TYR TYR GLU PRO TRP GLY TYR
SEQRES  42 A  725  THR PRO ALA GLU CYS THR VAL MET GLY VAL PRO SER ILE
SEQRES  43 A  725  THR THR ASN VAL SER GLY PHE GLY SER TYR MET GLU ASP
SEQRES  44 A  725  LEU ILE GLU THR ASN GLN ALA LYS ASP TYR GLY ILE TYR
SEQRES  45 A  725  ILE VAL ASP ARG ARG PHE LYS ALA PRO ASP GLU SER VAL
SEQRES  46 A  725  GLU GLN LEU VAL ASP TYR MET GLU GLU PHE VAL LYS LYS
SEQRES  47 A  725  THR ARG ARG GLN ARG ILE ASN GLN ARG ASN ALA THR GLU
SEQRES  48 A  725  ALA LEU SER ASP LEU LEU ASP TRP LYS ARG MET GLY LEU
SEQRES  49 A  725  GLU TYR VAL LYS ALA ARG GLN LEU ALA LEU ARG ARG GLY
SEQRES  50 A  725  TYR PRO ASP GLN PHE ARG GLU LEU VAL GLY GLU GLU LEU
SEQRES  51 A  725  ASN ASP SER ASN MET ASP ALA LEU ALA GLY GLY LYS LYS
SEQRES  52 A  725  LEU LYS VAL ALA ARG PRO LEU SER VAL PRO GLY SER PRO
SEQRES  53 A  725  ARG ASP LEU ARG SER ASN SER THR VAL TYR MET THR PRO
SEQRES  54 A  725  GLY ASP LEU GLY THR LEU GLN GLU VAL ASN ASN ALA ASP
SEQRES  55 A  725  ASP TYR PHE SER LEU GLY VAL ASN PRO ALA ALA ASP ASP
SEQRES  56 A  725  ASP ASP ASP GLY PRO TYR ALA ASP ASP SER
SEQRES   1 B  725  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES   2 B  725  LEU VAL PRO ARG GLY SER HIS MET SER ARG ASP LEU GLN
SEQRES   3 B  725  ASN HIS LEU LEU PHE GLU THR ALA THR GLU VAL ALA ASN
SEQRES   4 B  725  ARG VAL GLY GLY ILE TYR SER VAL LEU LYS SER LYS ALA
SEQRES   5 B  725  PRO ILE THR VAL ALA GLN TYR LYS ASP HIS TYR HIS LEU
SEQRES   6 B  725  ILE GLY PRO LEU ASN LYS ALA THR TYR GLN ASN GLU VAL
SEQRES   7 B  725  ASP ILE LEU ASP TRP LYS LYS PRO GLU ALA PHE SER ASP
SEQRES   8 B  725  GLU MET ARG PRO VAL GLN HIS ALA LEU GLN THR MET GLU
SEQRES   9 B  725  SER ARG GLY VAL HIS PHE VAL TYR GLY ARG TRP LEU ILE
SEQRES  10 B  725  GLU GLY ALA PRO LYS VAL ILE LEU PHE ASP LEU ASP SER
SEQRES  11 B  725  VAL ARG GLY TYR SER ASN GLU TRP LYS GLY ASP LEU TRP
SEQRES  12 B  725  SER LEU VAL GLY ILE PRO SER PRO GLU ASN ASP PHE GLU
SEQRES  13 B  725  THR ASN ASP ALA ILE LEU LEU GLY TYR THR VAL ALA TRP
SEQRES  14 B  725  PHE LEU GLY GLU VAL ALA HIS LEU ASP SER GLN HIS ALA
SEQRES  15 B  725  ILE VAL ALA HIS PHE HIS GLU TRP LEU ALA GLY VAL ALA
SEQRES  16 B  725  LEU PRO LEU CYS ARG LYS ARG ARG ILE ASP VAL VAL THR
SEQRES  17 B  725  ILE PHE THR THR HIS ALA THR LEU LEU GLY ARG TYR LEU
SEQRES  18 B  725  CYS ALA SER GLY SER PHE ASP PHE TYR ASN CYS LEU GLU
SEQRES  19 B  725  SER VAL ASP VAL ASP HIS GLU ALA GLY ARG PHE GLY ILE
SEQRES  20 B  725  TYR HIS ARG TYR CYS ILE GLU ARG ALA ALA ALA HIS SER
SEQRES  21 B  725  ALA ASP VAL PHE THR THR VAL SER GLN ILE THR ALA PHE
SEQRES  22 B  725  GLU ALA GLU HIS LEU LEU LYS ARG LYS PRO ASP GLY ILE
SEQRES  23 B  725  LEU PRO ASN GLY LEU ASN VAL ILE LYS PHE GLN ALA PHE
SEQRES  24 B  725  HIS GLU PHE GLN ASN LEU HIS ALA LEU LYS LYS GLU LYS
SEQRES  25 B  725  ILE ASN ASP PHE VAL ARG GLY HIS PHE HIS GLY CYS PHE
SEQRES  26 B  725  ASP PHE ASP LEU ASP ASN THR LEU TYR PHE PHE ILE ALA
SEQRES  27 B  725  GLY ARG TYR GLU TYR LYS ASN LYS GLY ALA ASP MET PHE
SEQRES  28 B  725  ILE GLU ALA LEU ALA ARG LEU ASN TYR ARG LEU LYS VAL
SEQRES  29 B  725  SER GLY SER LYS LYS THR VAL VAL ALA PHE ILE VAL MET
SEQRES  30 B  725  PRO ALA LYS ASN ASN SER PHE THR VAL GLU ALA LEU LYS
SEQRES  31 B  725  GLY GLN ALA GLU VAL ARG ALA LEU GLU ASN THR VAL HIS
SEQRES  32 B  725  GLU VAL THR THR SER ILE GLY LYS ARG ILE PHE ASP HIS
SEQRES  33 B  725  ALA ILE ARG TYR PRO HIS ASN GLY LEU THR THR GLU LEU
SEQRES  34 B  725  PRO THR ASP LEU GLY GLU LEU LEU LYS SER SER ASP LYS
SEQRES  35 B  725  VAL MET LEU LYS ARG ARG ILE LEU ALA LEU ARG ARG PRO
SEQRES  36 B  725  GLU GLY GLN LEU PRO PRO ILE VAL THR HIS ASN MET VAL
SEQRES  37 B  725  ASP ASP ALA ASN ASP LEU ILE LEU ASN LYS ILE ARG GLN
SEQRES  38 B  725  VAL GLN LEU PHE ASN SER PRO SER ASP ARG VAL LYS MET
SEQRES  39 B  725  ILE PHE HIS PRO GLU PHE LEU ASN ALA ASN ASN PRO ILE
SEQRES  40 B  725  LEU GLY LEU ASP TYR ASP GLU PHE VAL ARG GLY CYS HIS
SEQRES  41 B  725  LEU GLY VAL PHE PRO SER TYR TYR GLU PRO TRP GLY TYR
SEQRES  42 B  725  THR PRO ALA GLU CYS THR VAL MET GLY VAL PRO SER ILE
SEQRES  43 B  725  THR THR ASN VAL SER GLY PHE GLY SER TYR MET GLU ASP
SEQRES  44 B  725  LEU ILE GLU THR ASN GLN ALA LYS ASP TYR GLY ILE TYR
SEQRES  45 B  725  ILE VAL ASP ARG ARG PHE LYS ALA PRO ASP GLU SER VAL
SEQRES  46 B  725  GLU GLN LEU VAL ASP TYR MET GLU GLU PHE VAL LYS LYS
SEQRES  47 B  725  THR ARG ARG GLN ARG ILE ASN GLN ARG ASN ALA THR GLU
SEQRES  48 B  725  ALA LEU SER ASP LEU LEU ASP TRP LYS ARG MET GLY LEU
SEQRES  49 B  725  GLU TYR VAL LYS ALA ARG GLN LEU ALA LEU ARG ARG GLY
SEQRES  50 B  725  TYR PRO ASP GLN PHE ARG GLU LEU VAL GLY GLU GLU LEU
SEQRES  51 B  725  ASN ASP SER ASN MET ASP ALA LEU ALA GLY GLY LYS LYS
SEQRES  52 B  725  LEU LYS VAL ALA ARG PRO LEU SER VAL PRO GLY SER PRO
SEQRES  53 B  725  ARG ASP LEU ARG SER ASN SER THR VAL TYR MET THR PRO
SEQRES  54 B  725  GLY ASP LEU GLY THR LEU GLN GLU VAL ASN ASN ALA ASP
SEQRES  55 B  725  ASP TYR PHE SER LEU GLY VAL ASN PRO ALA ALA ASP ASP
SEQRES  56 B  725  ASP ASP ASP GLY PRO TYR ALA ASP ASP SER
SEQRES   1 C  725  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES   2 C  725  LEU VAL PRO ARG GLY SER HIS MET SER ARG ASP LEU GLN
SEQRES   3 C  725  ASN HIS LEU LEU PHE GLU THR ALA THR GLU VAL ALA ASN
SEQRES   4 C  725  ARG VAL GLY GLY ILE TYR SER VAL LEU LYS SER LYS ALA
SEQRES   5 C  725  PRO ILE THR VAL ALA GLN TYR LYS ASP HIS TYR HIS LEU
SEQRES   6 C  725  ILE GLY PRO LEU ASN LYS ALA THR TYR GLN ASN GLU VAL
SEQRES   7 C  725  ASP ILE LEU ASP TRP LYS LYS PRO GLU ALA PHE SER ASP
SEQRES   8 C  725  GLU MET ARG PRO VAL GLN HIS ALA LEU GLN THR MET GLU
SEQRES   9 C  725  SER ARG GLY VAL HIS PHE VAL TYR GLY ARG TRP LEU ILE
SEQRES  10 C  725  GLU GLY ALA PRO LYS VAL ILE LEU PHE ASP LEU ASP SER
SEQRES  11 C  725  VAL ARG GLY TYR SER ASN GLU TRP LYS GLY ASP LEU TRP
SEQRES  12 C  725  SER LEU VAL GLY ILE PRO SER PRO GLU ASN ASP PHE GLU
SEQRES  13 C  725  THR ASN ASP ALA ILE LEU LEU GLY TYR THR VAL ALA TRP
SEQRES  14 C  725  PHE LEU GLY GLU VAL ALA HIS LEU ASP SER GLN HIS ALA
SEQRES  15 C  725  ILE VAL ALA HIS PHE HIS GLU TRP LEU ALA GLY VAL ALA
SEQRES  16 C  725  LEU PRO LEU CYS ARG LYS ARG ARG ILE ASP VAL VAL THR
SEQRES  17 C  725  ILE PHE THR THR HIS ALA THR LEU LEU GLY ARG TYR LEU
SEQRES  18 C  725  CYS ALA SER GLY SER PHE ASP PHE TYR ASN CYS LEU GLU
SEQRES  19 C  725  SER VAL ASP VAL ASP HIS GLU ALA GLY ARG PHE GLY ILE
SEQRES  20 C  725  TYR HIS ARG TYR CYS ILE GLU ARG ALA ALA ALA HIS SER
SEQRES  21 C  725  ALA ASP VAL PHE THR THR VAL SER GLN ILE THR ALA PHE
SEQRES  22 C  725  GLU ALA GLU HIS LEU LEU LYS ARG LYS PRO ASP GLY ILE
SEQRES  23 C  725  LEU PRO ASN GLY LEU ASN VAL ILE LYS PHE GLN ALA PHE
SEQRES  24 C  725  HIS GLU PHE GLN ASN LEU HIS ALA LEU LYS LYS GLU LYS
SEQRES  25 C  725  ILE ASN ASP PHE VAL ARG GLY HIS PHE HIS GLY CYS PHE
SEQRES  26 C  725  ASP PHE ASP LEU ASP ASN THR LEU TYR PHE PHE ILE ALA
SEQRES  27 C  725  GLY ARG TYR GLU TYR LYS ASN LYS GLY ALA ASP MET PHE
SEQRES  28 C  725  ILE GLU ALA LEU ALA ARG LEU ASN TYR ARG LEU LYS VAL
SEQRES  29 C  725  SER GLY SER LYS LYS THR VAL VAL ALA PHE ILE VAL MET
SEQRES  30 C  725  PRO ALA LYS ASN ASN SER PHE THR VAL GLU ALA LEU LYS
SEQRES  31 C  725  GLY GLN ALA GLU VAL ARG ALA LEU GLU ASN THR VAL HIS
SEQRES  32 C  725  GLU VAL THR THR SER ILE GLY LYS ARG ILE PHE ASP HIS
SEQRES  33 C  725  ALA ILE ARG TYR PRO HIS ASN GLY LEU THR THR GLU LEU
SEQRES  34 C  725  PRO THR ASP LEU GLY GLU LEU LEU LYS SER SER ASP LYS
SEQRES  35 C  725  VAL MET LEU LYS ARG ARG ILE LEU ALA LEU ARG ARG PRO
SEQRES  36 C  725  GLU GLY GLN LEU PRO PRO ILE VAL THR HIS ASN MET VAL
SEQRES  37 C  725  ASP ASP ALA ASN ASP LEU ILE LEU ASN LYS ILE ARG GLN
SEQRES  38 C  725  VAL GLN LEU PHE ASN SER PRO SER ASP ARG VAL LYS MET
SEQRES  39 C  725  ILE PHE HIS PRO GLU PHE LEU ASN ALA ASN ASN PRO ILE
SEQRES  40 C  725  LEU GLY LEU ASP TYR ASP GLU PHE VAL ARG GLY CYS HIS
SEQRES  41 C  725  LEU GLY VAL PHE PRO SER TYR TYR GLU PRO TRP GLY TYR
SEQRES  42 C  725  THR PRO ALA GLU CYS THR VAL MET GLY VAL PRO SER ILE
SEQRES  43 C  725  THR THR ASN VAL SER GLY PHE GLY SER TYR MET GLU ASP
SEQRES  44 C  725  LEU ILE GLU THR ASN GLN ALA LYS ASP TYR GLY ILE TYR
SEQRES  45 C  725  ILE VAL ASP ARG ARG PHE LYS ALA PRO ASP GLU SER VAL
SEQRES  46 C  725  GLU GLN LEU VAL ASP TYR MET GLU GLU PHE VAL LYS LYS
SEQRES  47 C  725  THR ARG ARG GLN ARG ILE ASN GLN ARG ASN ALA THR GLU
SEQRES  48 C  725  ALA LEU SER ASP LEU LEU ASP TRP LYS ARG MET GLY LEU
SEQRES  49 C  725  GLU TYR VAL LYS ALA ARG GLN LEU ALA LEU ARG ARG GLY
SEQRES  50 C  725  TYR PRO ASP GLN PHE ARG GLU LEU VAL GLY GLU GLU LEU
SEQRES  51 C  725  ASN ASP SER ASN MET ASP ALA LEU ALA GLY GLY LYS LYS
SEQRES  52 C  725  LEU LYS VAL ALA ARG PRO LEU SER VAL PRO GLY SER PRO
SEQRES  53 C  725  ARG ASP LEU ARG SER ASN SER THR VAL TYR MET THR PRO
SEQRES  54 C  725  GLY ASP LEU GLY THR LEU GLN GLU VAL ASN ASN ALA ASP
SEQRES  55 C  725  ASP TYR PHE SER LEU GLY VAL ASN PRO ALA ALA ASP ASP
SEQRES  56 C  725  ASP ASP ASP GLY PRO TYR ALA ASP ASP SER
SEQRES   1 D  725  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES   2 D  725  LEU VAL PRO ARG GLY SER HIS MET SER ARG ASP LEU GLN
SEQRES   3 D  725  ASN HIS LEU LEU PHE GLU THR ALA THR GLU VAL ALA ASN
SEQRES   4 D  725  ARG VAL GLY GLY ILE TYR SER VAL LEU LYS SER LYS ALA
SEQRES   5 D  725  PRO ILE THR VAL ALA GLN TYR LYS ASP HIS TYR HIS LEU
SEQRES   6 D  725  ILE GLY PRO LEU ASN LYS ALA THR TYR GLN ASN GLU VAL
SEQRES   7 D  725  ASP ILE LEU ASP TRP LYS LYS PRO GLU ALA PHE SER ASP
SEQRES   8 D  725  GLU MET ARG PRO VAL GLN HIS ALA LEU GLN THR MET GLU
SEQRES   9 D  725  SER ARG GLY VAL HIS PHE VAL TYR GLY ARG TRP LEU ILE
SEQRES  10 D  725  GLU GLY ALA PRO LYS VAL ILE LEU PHE ASP LEU ASP SER
SEQRES  11 D  725  VAL ARG GLY TYR SER ASN GLU TRP LYS GLY ASP LEU TRP
SEQRES  12 D  725  SER LEU VAL GLY ILE PRO SER PRO GLU ASN ASP PHE GLU
SEQRES  13 D  725  THR ASN ASP ALA ILE LEU LEU GLY TYR THR VAL ALA TRP
SEQRES  14 D  725  PHE LEU GLY GLU VAL ALA HIS LEU ASP SER GLN HIS ALA
SEQRES  15 D  725  ILE VAL ALA HIS PHE HIS GLU TRP LEU ALA GLY VAL ALA
SEQRES  16 D  725  LEU PRO LEU CYS ARG LYS ARG ARG ILE ASP VAL VAL THR
SEQRES  17 D  725  ILE PHE THR THR HIS ALA THR LEU LEU GLY ARG TYR LEU
SEQRES  18 D  725  CYS ALA SER GLY SER PHE ASP PHE TYR ASN CYS LEU GLU
SEQRES  19 D  725  SER VAL ASP VAL ASP HIS GLU ALA GLY ARG PHE GLY ILE
SEQRES  20 D  725  TYR HIS ARG TYR CYS ILE GLU ARG ALA ALA ALA HIS SER
SEQRES  21 D  725  ALA ASP VAL PHE THR THR VAL SER GLN ILE THR ALA PHE
SEQRES  22 D  725  GLU ALA GLU HIS LEU LEU LYS ARG LYS PRO ASP GLY ILE
SEQRES  23 D  725  LEU PRO ASN GLY LEU ASN VAL ILE LYS PHE GLN ALA PHE
SEQRES  24 D  725  HIS GLU PHE GLN ASN LEU HIS ALA LEU LYS LYS GLU LYS
SEQRES  25 D  725  ILE ASN ASP PHE VAL ARG GLY HIS PHE HIS GLY CYS PHE
SEQRES  26 D  725  ASP PHE ASP LEU ASP ASN THR LEU TYR PHE PHE ILE ALA
SEQRES  27 D  725  GLY ARG TYR GLU TYR LYS ASN LYS GLY ALA ASP MET PHE
SEQRES  28 D  725  ILE GLU ALA LEU ALA ARG LEU ASN TYR ARG LEU LYS VAL
SEQRES  29 D  725  SER GLY SER LYS LYS THR VAL VAL ALA PHE ILE VAL MET
SEQRES  30 D  725  PRO ALA LYS ASN ASN SER PHE THR VAL GLU ALA LEU LYS
SEQRES  31 D  725  GLY GLN ALA GLU VAL ARG ALA LEU GLU ASN THR VAL HIS
SEQRES  32 D  725  GLU VAL THR THR SER ILE GLY LYS ARG ILE PHE ASP HIS
SEQRES  33 D  725  ALA ILE ARG TYR PRO HIS ASN GLY LEU THR THR GLU LEU
SEQRES  34 D  725  PRO THR ASP LEU GLY GLU LEU LEU LYS SER SER ASP LYS
SEQRES  35 D  725  VAL MET LEU LYS ARG ARG ILE LEU ALA LEU ARG ARG PRO
SEQRES  36 D  725  GLU GLY GLN LEU PRO PRO ILE VAL THR HIS ASN MET VAL
SEQRES  37 D  725  ASP ASP ALA ASN ASP LEU ILE LEU ASN LYS ILE ARG GLN
SEQRES  38 D  725  VAL GLN LEU PHE ASN SER PRO SER ASP ARG VAL LYS MET
SEQRES  39 D  725  ILE PHE HIS PRO GLU PHE LEU ASN ALA ASN ASN PRO ILE
SEQRES  40 D  725  LEU GLY LEU ASP TYR ASP GLU PHE VAL ARG GLY CYS HIS
SEQRES  41 D  725  LEU GLY VAL PHE PRO SER TYR TYR GLU PRO TRP GLY TYR
SEQRES  42 D  725  THR PRO ALA GLU CYS THR VAL MET GLY VAL PRO SER ILE
SEQRES  43 D  725  THR THR ASN VAL SER GLY PHE GLY SER TYR MET GLU ASP
SEQRES  44 D  725  LEU ILE GLU THR ASN GLN ALA LYS ASP TYR GLY ILE TYR
SEQRES  45 D  725  ILE VAL ASP ARG ARG PHE LYS ALA PRO ASP GLU SER VAL
SEQRES  46 D  725  GLU GLN LEU VAL ASP TYR MET GLU GLU PHE VAL LYS LYS
SEQRES  47 D  725  THR ARG ARG GLN ARG ILE ASN GLN ARG ASN ALA THR GLU
SEQRES  48 D  725  ALA LEU SER ASP LEU LEU ASP TRP LYS ARG MET GLY LEU
SEQRES  49 D  725  GLU TYR VAL LYS ALA ARG GLN LEU ALA LEU ARG ARG GLY
SEQRES  50 D  725  TYR PRO ASP GLN PHE ARG GLU LEU VAL GLY GLU GLU LEU
SEQRES  51 D  725  ASN ASP SER ASN MET ASP ALA LEU ALA GLY GLY LYS LYS
SEQRES  52 D  725  LEU LYS VAL ALA ARG PRO LEU SER VAL PRO GLY SER PRO
SEQRES  53 D  725  ARG ASP LEU ARG SER ASN SER THR VAL TYR MET THR PRO
SEQRES  54 D  725  GLY ASP LEU GLY THR LEU GLN GLU VAL ASN ASN ALA ASP
SEQRES  55 D  725  ASP TYR PHE SER LEU GLY VAL ASN PRO ALA ALA ASP ASP
SEQRES  56 D  725  ASP ASP ASP GLY PRO TYR ALA ASP ASP SER
HET    G6P  A 901      16
HET    G6P  A 902      16
HET    PEG  A1001       7
HET    PEG  B1002       7
HET    G6P  B 901      16
HET    G6P  B 902      16
HET    PEG  B1001       7
HET    PEG  B 706       7
HET    G6P  C 901      16
HET    PEG  C1001       7
HET    G6P  D 901      16
HET    PEG  D1002       7
HETNAM     G6P ALPHA-D-GLUCOSE-6-PHOSPHATE
HETNAM     PEG DI(HYDROXYETHYL)ETHER
FORMUL   5  G6P    6(C6 H13 O9 P)
FORMUL   7  PEG    6(C4 H10 O3)
FORMUL  17  HOH   *524(H2 O)
HELIX    1   1 GLY A   22  LYS A   40  1                                  19
HELIX    2   2 THR A   53  GLU A   57  1                                   5
HELIX    3   3 LYS A   65  PHE A   69  5                                   5
HELIX    4   4 MET A   73  SER A   85  1                                  13
HELIX    5   5 LEU A  108  GLY A  113  5                                   6
HELIX    6   6 TYR A  114  GLY A  127  1                                  14
HELIX    7   7 ASP A  134  ASP A  158  1                                  25
HELIX    8   8 TRP A  170  GLY A  173  5                                   4
HELIX    9   9 VAL A  174  ARG A  182  1                                   9
HELIX   10  10 THR A  195  CYS A  202  1                                   8
HELIX   11  11 ASP A  208  LEU A  213  1                                   6
HELIX   12  12 GLU A  214  VAL A  216  5                                   3
HELIX   13  13 ASP A  217  PHE A  225  1                                   9
HELIX   14  14 ILE A  227  ALA A  241  1                                  15
HELIX   15  15 SER A  248  LEU A  259  1                                  12
HELIX   16  16 HIS A  280  PHE A  301  1                                  22
HELIX   17  17 ASP A  308  ASP A  310  5                                   3
HELIX   18  18 GLY A  327  SER A  345  1                                  19
HELIX   19  19 THR A  365  TYR A  400  1                                  36
HELIX   20  20 ASP A  412  LEU A  417  1                                   6
HELIX   21  21 LYS A  418  ARG A  433  1                                  16
HELIX   22  22 ASP A  449  ASN A  452  5                                   4
HELIX   23  23 ASP A  453  GLN A  463  1                                  11
HELIX   24  24 ASP A  491  CYS A  499  1                                   9
HELIX   25  25 GLY A  512  MET A  521  1                                  10
HELIX   26  26 SER A  531  ASP A  539  1                                   9
HELIX   27  27 GLU A  542  TYR A  549  1                                   8
HELIX   28  28 ALA A  560  LYS A  577  1                                  18
HELIX   29  29 THR A  579  LEU A  593  1                                  15
HELIX   30  30 SER A  594  LEU A  597  5                                   4
HELIX   31  31 ASP A  598  TYR A  618  1                                  21
HELIX   32  32 TYR A  618  LEU A  625  1                                   8
HELIX   33  33 ASN A  634  ALA A  639  1                                   6
HELIX   34  34 GLY B   23  LYS B   40  1                                  18
HELIX   35  35 THR B   53  GLU B   57  1                                   5
HELIX   36  36 LYS B   65  PHE B   69  5                                   5
HELIX   37  37 SER B   70  GLU B   72  5                                   3
HELIX   38  38 MET B   73  SER B   85  1                                  13
HELIX   39  39 LEU B  108  GLY B  113  5                                   6
HELIX   40  40 TYR B  114  VAL B  126  1                                  13
HELIX   41  41 ASP B  134  ASP B  158  1                                  25
HELIX   42  42 TRP B  170  GLY B  173  5                                   4
HELIX   43  43 VAL B  174  ARG B  182  1                                   9
HELIX   44  44 THR B  195  SER B  204  1                                  10
HELIX   45  45 ASP B  217  PHE B  225  1                                   9
HELIX   46  46 ILE B  227  ALA B  241  1                                  15
HELIX   47  47 SER B  248  LEU B  259  1                                  12
HELIX   48  48 HIS B  280  PHE B  301  1                                  22
HELIX   49  49 ASP B  308  ASP B  310  5                                   3
HELIX   50  50 GLY B  327  GLY B  346  1                                  20
HELIX   51  51 THR B  365  TYR B  400  1                                  36
HELIX   52  52 ASP B  412  LEU B  417  1                                   6
HELIX   53  53 LYS B  418  ALA B  431  1                                  14
HELIX   54  54 ASP B  453  GLN B  463  1                                  11
HELIX   55  55 ASP B  491  CYS B  499  1                                   9
HELIX   56  56 GLY B  512  MET B  521  1                                  10
HELIX   57  57 SER B  531  ASP B  539  1                                   9
HELIX   58  58 GLU B  542  LYS B  547  1                                   6
HELIX   59  59 ALA B  560  LYS B  578  1                                  19
HELIX   60  60 THR B  579  LEU B  593  1                                  15
HELIX   61  61 SER B  594  LEU B  597  5                                   4
HELIX   62  62 ASP B  598  TYR B  618  1                                  21
HELIX   63  63 TYR B  618  GLY B  627  1                                  10
HELIX   64  64 ASN B  634  GLY B  640  1                                   7
HELIX   65  65 GLY C   22  LYS C   40  1                                  19
HELIX   66  66 THR C   53  GLU C   57  1                                   5
HELIX   67  67 LYS C   65  PHE C   69  5                                   5
HELIX   68  68 SER C   70  GLU C   72  5                                   3
HELIX   69  69 MET C   73  ARG C   86  1                                  14
HELIX   70  70 LEU C  108  GLY C  113  5                                   6
HELIX   71  71 TYR C  114  GLY C  127  1                                  14
HELIX   72  72 ASP C  134  ASP C  158  1                                  25
HELIX   73  73 TRP C  170  GLY C  173  5                                   4
HELIX   74  74 VAL C  174  ARG C  183  1                                  10
HELIX   75  75 THR C  195  SER C  204  1                                  10
HELIX   76  76 ASP C  217  PHE C  225  1                                   9
HELIX   77  77 ILE C  227  ALA C  241  1                                  15
HELIX   78  78 SER C  248  LEU C  259  1                                  12
HELIX   79  79 HIS C  280  PHE C  301  1                                  22
HELIX   80  80 ASP C  308  ASP C  310  5                                   3
HELIX   81  81 GLY C  327  GLY C  346  1                                  20
HELIX   82  82 THR C  365  TYR C  400  1                                  36
HELIX   83  83 ASP C  412  LEU C  416  5                                   5
HELIX   84  84 LYS C  418  ARG C  433  1                                  16
HELIX   85  85 ASP C  453  GLN C  463  1                                  11
HELIX   86  86 ASP C  491  CYS C  499  1                                   9
HELIX   87  87 GLY C  512  MET C  521  1                                  10
HELIX   88  88 SER C  531  ILE C  541  1                                  11
HELIX   89  89 GLU C  542  TYR C  549  5                                   8
HELIX   90  90 ALA C  560  LYS C  577  1                                  18
HELIX   91  91 THR C  579  SER C  594  1                                  16
HELIX   92  92 ASP C  595  LEU C  597  5                                   3
HELIX   93  93 ASP C  598  TYR C  618  1                                  21
HELIX   94  94 TYR C  618  GLY C  627  1                                  10
HELIX   95  95 ASN C  634  GLY C  640  1                                   7
HELIX   96  96 GLY D   22  LYS D   40  1                                  19
HELIX   97  97 THR D   53  GLU D   57  1                                   5
HELIX   98  98 LYS D   65  PHE D   69  5                                   5
HELIX   99  99 MET D   73  ARG D   86  1                                  14
HELIX  100 100 LEU D  108  GLY D  113  5                                   6
HELIX  101 101 TYR D  114  VAL D  126  1                                  13
HELIX  102 102 ASP D  134  ASP D  158  1                                  25
HELIX  103 103 TRP D  170  GLY D  173  5                                   4
HELIX  104 104 VAL D  174  ARG D  183  1                                  10
HELIX  105 105 THR D  195  ALA D  203  1                                   9
HELIX  106 106 ASP D  217  GLY D  226  1                                  10
HELIX  107 107 ILE D  227  ALA D  241  1                                  15
HELIX  108 108 SER D  248  LEU D  259  1                                  12
HELIX  109 109 HIS D  280  PHE D  301  1                                  22
HELIX  110 110 ASP D  308  ASP D  310  5                                   3
HELIX  111 111 GLY D  327  SER D  345  1                                  19
HELIX  112 112 THR D  365  TYR D  400  1                                  36
HELIX  113 113 ASP D  412  LEU D  417  1                                   6
HELIX  114 114 LYS D  418  ARG D  433  1                                  16
HELIX  115 115 ASP D  449  ASN D  452  5                                   4
HELIX  116 116 ASP D  453  GLN D  463  1                                  11
HELIX  117 117 ASP D  491  CYS D  499  1                                   9
HELIX  118 118 GLY D  512  MET D  521  1                                  10
HELIX  119 119 SER D  531  GLU D  538  1                                   8
HELIX  120 120 GLU D  542  TYR D  549  1                                   8
HELIX  121 121 ALA D  560  LYS D  577  1                                  18
HELIX  122 122 THR D  579  SER D  594  1                                  16
HELIX  123 123 ASP D  595  LEU D  597  5                                   3
HELIX  124 124 ASP D  598  TYR D  618  1                                  21
HELIX  125 125 TYR D  618  GLY D  627  1                                  10
SHEET    1   A 9 VAL A  58  ILE A  60  0
SHEET    2   A 9 PHE A  90  TRP A  95 -1  O  ARG A  94   N  ASP A  59
SHEET    3   A 9 LYS A 102  PHE A 106 -1  O  VAL A 103   N  GLY A  93
SHEET    4   A 9 TYR A  43  PRO A  48  1  N  LEU A  45   O  ILE A 104
SHEET    5   A 9 ASP A   4  ALA A  14  1  N  GLU A  12   O  HIS A  44
SHEET    6   A 9 HIS A 161  HIS A 168  1  O  HIS A 166   N  THR A  13
SHEET    7   A 9 VAL A 187  THR A 192  1  O  ILE A 189   N  PHE A 167
SHEET    8   A 9 VAL A 243  THR A 246  1  O  THR A 245   N  PHE A 190
SHEET    9   A 9 GLY A 265  ILE A 266  1  O  GLY A 265   N  THR A 246
SHEET    1   B 6 VAL A 472  PHE A 476  0
SHEET    2   B 6 THR A 350  VAL A 356  1  N  VAL A 351   O  LYS A 473
SHEET    3   B 6 THR A 312  ALA A 318  1  N  PHE A 315   O  PHE A 354
SHEET    4   B 6 LEU A 501  VAL A 503  1  O  VAL A 503   N  PHE A 316
SHEET    5   B 6 SER A 525  THR A 528  1  O  ILE A 526   N  GLY A 502
SHEET    6   B 6 ILE A 551  VAL A 554  1  O  TYR A 552   N  THR A 527
SHEET    1   C 2 ASN A 361  PHE A 364  0
SHEET    2   C 2 HIS A 445  MET A 447 -1  O  ASN A 446   N  ASN A 362
SHEET    1   D 9 VAL B  58  ILE B  60  0
SHEET    2   D 9 PHE B  90  TRP B  95 -1  O  ARG B  94   N  ASP B  59
SHEET    3   D 9 LYS B 102  PHE B 106 -1  O  LEU B 105   N  VAL B  91
SHEET    4   D 9 TYR B  43  PRO B  48  1  N  LEU B  45   O  ILE B 104
SHEET    5   D 9 ASP B   4  THR B  13  1  N  GLU B  12   O  ILE B  46
SHEET    6   D 9 HIS B 161  HIS B 168  1  O  HIS B 166   N  THR B  13
SHEET    7   D 9 VAL B 187  THR B 191  1  O  THR B 191   N  PHE B 167
SHEET    8   D 9 VAL B 243  THR B 246  1  O  THR B 245   N  PHE B 190
SHEET    9   D 9 GLY B 265  ILE B 266  1  O  GLY B 265   N  THR B 246
SHEET    1   E 6 VAL B 472  PHE B 476  0
SHEET    2   E 6 THR B 350  VAL B 356  1  N  VAL B 351   O  LYS B 473
SHEET    3   E 6 THR B 312  ALA B 318  1  N  PHE B 315   O  PHE B 354
SHEET    4   E 6 LEU B 501  VAL B 503  1  O  VAL B 503   N  PHE B 316
SHEET    5   E 6 SER B 525  THR B 528  1  O  ILE B 526   N  GLY B 502
SHEET    6   E 6 ILE B 551  VAL B 554  1  O  TYR B 552   N  THR B 527
SHEET    1   F 2 ASN B 361  PHE B 364  0
SHEET    2   F 2 HIS B 445  MET B 447 -1  O  ASN B 446   N  ASN B 362
SHEET    1   G 9 VAL C  58  ILE C  60  0
SHEET    2   G 9 PHE C  90  TRP C  95 -1  O  ARG C  94   N  ASP C  59
SHEET    3   G 9 LYS C 102  PHE C 106 -1  O  VAL C 103   N  GLY C  93
SHEET    4   G 9 TYR C  43  PRO C  48  1  N  LEU C  45   O  ILE C 104
SHEET    5   G 9 ASP C   4  THR C  13  1  N  GLU C  12   O  ILE C  46
SHEET    6   G 9 HIS C 161  HIS C 168  1  O  HIS C 166   N  PHE C  11
SHEET    7   G 9 VAL C 187  THR C 192  1  O  ILE C 189   N  PHE C 167
SHEET    8   G 9 VAL C 243  THR C 246  1  O  THR C 245   N  PHE C 190
SHEET    9   G 9 GLY C 265  ILE C 266  1  O  GLY C 265   N  THR C 246
SHEET    1   H 6 VAL C 472  PHE C 476  0
SHEET    2   H 6 THR C 350  VAL C 356  1  N  VAL C 351   O  LYS C 473
SHEET    3   H 6 THR C 312  ALA C 318  1  N  LEU C 313   O  VAL C 352
SHEET    4   H 6 LEU C 501  VAL C 503  1  O  VAL C 503   N  PHE C 316
SHEET    5   H 6 SER C 525  THR C 528  1  O  ILE C 526   N  GLY C 502
SHEET    6   H 6 ILE C 551  VAL C 554  1  O  TYR C 552   N  THR C 527
SHEET    1   I 2 ASN C 361  PHE C 364  0
SHEET    2   I 2 HIS C 445  MET C 447 -1  O  ASN C 446   N  ASN C 362
SHEET    1   J 9 VAL D  58  ILE D  60  0
SHEET    2   J 9 PHE D  90  TRP D  95 -1  O  ARG D  94   N  ASP D  59
SHEET    3   J 9 LYS D 102  PHE D 106 -1  O  LEU D 105   N  VAL D  91
SHEET    4   J 9 TYR D  43  PRO D  48  1  N  LEU D  45   O  ILE D 104
SHEET    5   J 9 ASP D   4  THR D  13  1  N  GLU D  12   O  ILE D  46
SHEET    6   J 9 HIS D 161  HIS D 168  1  O  HIS D 166   N  PHE D  11
SHEET    7   J 9 VAL D 187  THR D 192  1  O  VAL D 187   N  ALA D 165
SHEET    8   J 9 VAL D 243  THR D 246  1  O  THR D 245   N  PHE D 190
SHEET    9   J 9 GLY D 265  ILE D 266  1  O  GLY D 265   N  THR D 246
SHEET    1   K 6 VAL D 472  PHE D 476  0
SHEET    2   K 6 THR D 350  VAL D 356  1  N  VAL D 351   O  LYS D 473
SHEET    3   K 6 THR D 312  ALA D 318  1  N  LEU D 313   O  THR D 350
SHEET    4   K 6 LEU D 501  VAL D 503  1  O  VAL D 503   N  PHE D 316
SHEET    5   K 6 SER D 525  THR D 528  1  O  ILE D 526   N  GLY D 502
SHEET    6   K 6 ILE D 551  VAL D 554  1  O  VAL D 554   N  THR D 527
SHEET    1   L 2 ASN D 361  PHE D 364  0
SHEET    2   L 2 HIS D 445  MET D 447 -1  O  ASN D 446   N  ASN D 362
CISPEP   1 TYR A  400    PRO A  401          0         2.44
CISPEP   2 TYR B  400    PRO B  401          0        -0.05
CISPEP   3 TYR C  400    PRO C  401          0         2.53
CISPEP   4 TYR D  400    PRO D  401          0         3.61
SITE     1 AC1 14 GLN A 283  ASN A 284  HIS A 286  LYS A 290
SITE     2 AC1 14 HIS A 500  ARG A 580  ARG A 583  ARG A 587
SITE     3 AC1 14 HOH A 796  HOH A 803  HOH A 861  HOH A 865
SITE     4 AC1 14 HIS B 280  HOH B 808
SITE     1 AC2  7 ARG A 199  ARG A 320  LYS A 326  TYR A 513
SITE     2 AC2  7 THR A 514  HOH A 814  HOH A 850
SITE     1 AC3  3 LYS A 391  PHE A 394  HIS C 383
SITE     1 AC4  4 ILE A 274  LYS A 275  GLN A 277  ARG B 581
SITE     1 AC5 10 HIS A 280  HOH A 839  GLN B 283  ASN B 284
SITE     2 AC5 10 HIS B 286  LYS B 290  HIS B 500  ARG B 580
SITE     3 AC5 10 ARG B 583  ARG B 587
SITE     1 AC6 10 GLY B  23  GLU B 169  HIS B 193  ARG B 199
SITE     2 AC6 10 ARG B 320  LYS B 326  TYR B 513  HOH B 774
SITE     3 AC6 10 HOH B 790  HOH B 823
SITE     1 AC7  4 LYS B 391  PHE B 394  GLU D 291  HIS D 383
SITE     1 AC8  5 GLU B 291  ARG B 298  HIS B 383  PHE D 394
SITE     2 AC8  5 HOH D 789
SITE     1 AC9 11 GLN C 283  ASN C 284  HIS C 286  ALA C 287
SITE     2 AC9 11 LYS C 290  HIS C 500  ARG C 580  ARG C 583
SITE     3 AC9 11 ARG C 587  HIS D 280  HOH D 747
SITE     1 BC1  4 GLU A 291  ARG A 298  LYS C 391  PHE C 394
SITE     1 BC2  9 HIS C 280  GLN D 283  ASN D 284  HIS D 286
SITE     2 BC2  9 LYS D 290  HIS D 500  ARG D 580  ARG D 583
SITE     3 BC2  9 ARG D 587
SITE     1 BC3  2 TYR D 340  HOH D 765
CRYST1  192.739  206.982  205.799  90.00  90.00  90.00 I 2 2 2      32
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      0.005188  0.000000  0.000000        0.00000
SCALE2      0.000000  0.004831  0.000000        0.00000
SCALE3      0.000000  0.000000  0.004859        0.00000
      
PROCHECK
Go to PROCHECK summary
 References