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PDBsum entry 2dgk

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Top Page protein ligands Protein-protein interface(s) links
Lyase PDB id
2dgk
Jmol
Contents
Protein chains
(+ 0 more) 438 a.a.
Ligands
SO4 ×6
PLP ×6
EDO ×8
Waters ×1695
HEADER    LYASE                                   14-MAR-06   2DGK
TITLE     CRYSTAL STRUCTURE OF AN N-TERMINAL DELETION MUTANT OF ESCHERICHIA COLI
TITLE    2 GADB IN AN AUTOINHIBITED STATE (ALDAMINE)
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: GLUTAMATE DECARBOXYLASE BETA;
COMPND   3 CHAIN: A, B, C, D, E, F;
COMPND   4 FRAGMENT: GADBD1-14;
COMPND   5 SYNONYM: GAD-BETA, GADB;
COMPND   6 EC: 4.1.1.15;
COMPND   7 ENGINEERED: YES;
COMPND   8 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE   3 ORGANISM_TAXID: 562;
SOURCE   4 STRAIN: JM109;
SOURCE   5 GENE: GADB;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PQE60
KEYWDS    GADB, GADBD1-14, AUTOINHIBITION, SUBSTITUTED ALDAMINE, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    M.G.GRUETTER,G.CAPITANI,H.GUT
REVDAT   3   13-JUL-11 2DGK    1       VERSN
REVDAT   2   24-FEB-09 2DGK    1       VERSN
REVDAT   1   20-JUN-06 2DGK    0
JRNL        AUTH   H.GUT,E.PENNACCHIETTI,R.A.JOHN,F.BOSSA,G.CAPITANI,
JRNL        AUTH 2 D.DE BIASE,M.G.GRUETTER
JRNL        TITL   ESCHERICHIA COLI ACID RESISTANCE: PH-SENSING, ACTIVATION BY
JRNL        TITL 2 CHLORIDE AND AUTOINHIBITION IN GADB
JRNL        REF    EMBO J.                       V.  25  2643 2006
JRNL        REFN                   ISSN 0261-4189
JRNL        PMID   16675957
JRNL        DOI    10.1038/SJ.EMBOJ.7601107
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   G.CAPITANI,D.DE BIASE,C.AURIZI,H.GUT,F.BOSSA,M.G.GRUETTER
REMARK   1  TITL   CRYSTAL STRUCTURE AND FUNCTIONAL ANALYSIS OF ESCHERICHIA
REMARK   1  TITL 2 COLI GLUTAMATE DECARBOXYLASE
REMARK   1  REF    EMBO J.                       V.  22  4027 2003
REMARK   1  REFN                   ISSN 0261-4189
REMARK   1  PMID   12912902
REMARK   1  DOI    10.1093/EMBOJ/CDG403
REMARK   2
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.1
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.0
REMARK   3   NUMBER OF REFLECTIONS             : 230716
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.218
REMARK   3   FREE R VALUE                     : 0.246
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 2308
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.97
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.60
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2740
REMARK   3   BIN FREE R VALUE                    : 0.2970
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 225
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 20922
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 152
REMARK   3   SOLVENT ATOMS            : 1695
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 32.00
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.90
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.25
REMARK   3   ESD FROM SIGMAA              (A) : 0.20
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.29
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.25
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.006
REMARK   3   BOND ANGLES            (DEGREES) : 1.23
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : NULL
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2DGK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-MAR-06.
REMARK 100 THE RCSB ID CODE IS RCSB025392.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 30-APR-05
REMARK 200  TEMPERATURE           (KELVIN) : 90.0
REMARK 200  PH                             : 5.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SLS
REMARK 200  BEAMLINE                       : X06SA
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.954
REMARK 200  MONOCHROMATOR                  : LN2 COOLED FIXED-EXIT SI(111)
REMARK 200                                   MONOCHROMATOR
REMARK 200  OPTICS                         : DYNAMICALLY BENDABLE MIRROR
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : XDS
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 230800
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9
REMARK 200  DATA REDUNDANCY                : 7.300
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.06800
REMARK 200   FOR THE DATA SET  : 17.3000
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) : 2.20
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.7
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.00
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.21700
REMARK 200   FOR SHELL         : 8.700
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 1PMO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 49.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22.5% PEG 2000 MME, 0.18M LITIUM
REMARK 280  SULFATE, 0.1M SODIUM ACETATE, PH 5.5, VAPOR DIFFUSION, SITTING
REMARK 280  DROP, TEMPERATURE 293K
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       46.38500
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      100.71000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       79.28000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      100.71000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       46.38500
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       79.28000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
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: 12450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -82.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -78.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30270 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -75.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
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: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3670 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E
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: 6
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, F
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     ASP A    15
REMARK 465     SER A    16
REMARK 465     ARG A    17
REMARK 465     PHE A    18
REMARK 465     GLY A    19
REMARK 465     ALA A    20
REMARK 465     LYS A    21
REMARK 465     SER A    22
REMARK 465     ILE A    23
REMARK 465     SER A    24
REMARK 465     THR A    25
REMARK 465     ILE A    26
REMARK 465     ALA A    27
REMARK 465     GLU A    28
REMARK 465     ASP B    15
REMARK 465     SER B    16
REMARK 465     ARG B    17
REMARK 465     PHE B    18
REMARK 465     GLY B    19
REMARK 465     ALA B    20
REMARK 465     LYS B    21
REMARK 465     SER B    22
REMARK 465     ILE B    23
REMARK 465     SER B    24
REMARK 465     THR B    25
REMARK 465     ILE B    26
REMARK 465     ALA B    27
REMARK 465     GLU B    28
REMARK 465     ASP C    15
REMARK 465     SER C    16
REMARK 465     ARG C    17
REMARK 465     PHE C    18
REMARK 465     GLY C    19
REMARK 465     ALA C    20
REMARK 465     LYS C    21
REMARK 465     SER C    22
REMARK 465     ILE C    23
REMARK 465     SER C    24
REMARK 465     THR C    25
REMARK 465     ILE C    26
REMARK 465     ALA C    27
REMARK 465     GLU C    28
REMARK 465     SER C    29
REMARK 465     ASP D    15
REMARK 465     SER D    16
REMARK 465     ARG D    17
REMARK 465     PHE D    18
REMARK 465     GLY D    19
REMARK 465     ALA D    20
REMARK 465     LYS D    21
REMARK 465     SER D    22
REMARK 465     ILE D    23
REMARK 465     SER D    24
REMARK 465     THR D    25
REMARK 465     ILE D    26
REMARK 465     ALA D    27
REMARK 465     GLU D    28
REMARK 465     ASP E    15
REMARK 465     SER E    16
REMARK 465     ARG E    17
REMARK 465     PHE E    18
REMARK 465     GLY E    19
REMARK 465     ALA E    20
REMARK 465     LYS E    21
REMARK 465     SER E    22
REMARK 465     ILE E    23
REMARK 465     SER E    24
REMARK 465     THR E    25
REMARK 465     ILE E    26
REMARK 465     ALA E    27
REMARK 465     GLU E    28
REMARK 465     ASP F    15
REMARK 465     SER F    16
REMARK 465     ARG F    17
REMARK 465     PHE F    18
REMARK 465     GLY F    19
REMARK 465     ALA F    20
REMARK 465     LYS F    21
REMARK 465     SER F    22
REMARK 465     ILE F    23
REMARK 465     SER F    24
REMARK 465     THR F    25
REMARK 465     ILE F    26
REMARK 465     ALA F    27
REMARK 465     GLU F    28
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    GLN A 186       76.24   -171.48
REMARK 500    LEU A 250      -69.39   -121.84
REMARK 500    ALA A 255       59.40   -153.87
REMARK 500    ASP A 261     -149.31    -95.91
REMARK 500    LYS A 276     -114.48   -104.26
REMARK 500    PHE A 317      -96.72   -124.79
REMARK 500    PRO A 376       69.53    -68.04
REMARK 500    THR A 416        7.95    -62.36
REMARK 500    GLN A 459       25.57   -152.79
REMARK 500    ALA B  56       -0.36     60.98
REMARK 500    LEU B 187       43.29    -92.06
REMARK 500    ALA B 255       57.34   -148.44
REMARK 500    ASP B 261     -146.77    -94.23
REMARK 500    LYS B 276     -114.18   -103.41
REMARK 500    PHE B 317     -100.61   -121.30
REMARK 500    GLN B 459       32.97   -143.04
REMARK 500    TYR C  90       66.52   -119.09
REMARK 500    GLN C 186       76.09   -157.52
REMARK 500    LEU C 187       41.01    -90.93
REMARK 500    ALA C 255       53.85   -149.17
REMARK 500    ASP C 261     -146.62    -94.54
REMARK 500    LYS C 276     -113.24   -103.39
REMARK 500    PHE C 317      -97.46   -122.39
REMARK 500    PRO C 376       68.23    -67.97
REMARK 500    ALA C 415       26.33   -144.32
REMARK 500    GLN C 459       23.60   -147.67
REMARK 500    ARG D 178       79.58   -110.61
REMARK 500    GLN D 186       76.16   -172.99
REMARK 500    LEU D 250      -69.31   -123.27
REMARK 500    ASP D 261     -147.36    -94.31
REMARK 500    LYS D 276     -113.39   -101.47
REMARK 500    PHE D 317      -96.98   -123.27
REMARK 500    GLU D 414       48.00   -102.53
REMARK 500    ALA D 415       34.19   -144.00
REMARK 500    GLN D 459       21.54   -145.66
REMARK 500    ALA E  56        5.04     59.42
REMARK 500    ALA E 148       23.92    -79.98
REMARK 500    THR E 152       45.28   -141.62
REMARK 500    LEU E 187       31.26    -83.78
REMARK 500    LEU E 250      -68.00   -123.89
REMARK 500    ALA E 255       57.90   -148.63
REMARK 500    ASP E 261     -148.39    -94.05
REMARK 500    LYS E 276     -112.83   -100.26
REMARK 500    PHE E 317      -98.91   -122.36
REMARK 500    GLN E 459       10.19   -142.76
REMARK 500    GLN F 186       80.55   -155.75
REMARK 500    LEU F 187       45.18    -89.43
REMARK 500    LEU F 250      -67.31   -123.36
REMARK 500    ALA F 255       58.94   -151.82
REMARK 500    ASP F 261     -148.90    -95.56
REMARK 500
REMARK 500 THIS ENTRY HAS      52 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 A4939        DISTANCE =  5.03 ANGSTROMS
REMARK 525    HOH A5014        DISTANCE =  5.18 ANGSTROMS
REMARK 525    HOH B4846        DISTANCE =  5.12 ANGSTROMS
REMARK 525    HOH B4931        DISTANCE =  5.93 ANGSTROMS
REMARK 525    HOH B4987        DISTANCE =  5.27 ANGSTROMS
REMARK 525    HOH B5024        DISTANCE =  5.15 ANGSTROMS
REMARK 525    HOH B5029        DISTANCE =  5.04 ANGSTROMS
REMARK 525    HOH B5052        DISTANCE =  5.03 ANGSTROMS
REMARK 525    HOH B5071        DISTANCE =  5.26 ANGSTROMS
REMARK 525    HOH C4956        DISTANCE =  5.02 ANGSTROMS
REMARK 525    HOH C5031        DISTANCE =  5.08 ANGSTROMS
REMARK 525    HOH C5039        DISTANCE =  5.09 ANGSTROMS
REMARK 525    HOH C5049        DISTANCE =  6.45 ANGSTROMS
REMARK 525    HOH C5052        DISTANCE =  5.35 ANGSTROMS
REMARK 525    HOH C5095        DISTANCE =  5.10 ANGSTROMS
REMARK 525    HOH D5011        DISTANCE =  5.13 ANGSTROMS
REMARK 525    HOH D5036        DISTANCE =  5.24 ANGSTROMS
REMARK 525    HOH D5039        DISTANCE =  5.47 ANGSTROMS
REMARK 525    HOH D5076        DISTANCE =  5.09 ANGSTROMS
REMARK 525    HOH E4967        DISTANCE =  5.24 ANGSTROMS
REMARK 525    HOH E5000        DISTANCE =  5.32 ANGSTROMS
REMARK 525    HOH F4822        DISTANCE =  5.14 ANGSTROMS
REMARK 525    HOH F4961        DISTANCE =  5.42 ANGSTROMS
REMARK 525    HOH F5024        DISTANCE =  5.20 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 4770
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 4771
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 4772
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 4773
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 4774
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 4775
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 1500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP C 1502
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP D 1503
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP E 1504
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP F 1505
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 2191
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 2192
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2193
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 2194
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 2195
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 2196
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 2197
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 2198
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PMM   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ESCHERICHIA COLI GADB (LOW PH)
REMARK 900 RELATED ID: 1PMO   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ESCHERICHIA COLI GADB (NEUTRAL PH)
REMARK 900 RELATED ID: 2DGL   RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH BROMIDE
REMARK 900 RELATED ID: 2DGM   RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH IODIDE
DBREF  2DGK A   15   466  UNP    P69910   DCEB_ECOLI      15    466
DBREF  2DGK B   15   466  UNP    P69910   DCEB_ECOLI      15    466
DBREF  2DGK C   15   466  UNP    P69910   DCEB_ECOLI      15    466
DBREF  2DGK D   15   466  UNP    P69910   DCEB_ECOLI      15    466
DBREF  2DGK E   15   466  UNP    P69910   DCEB_ECOLI      15    466
DBREF  2DGK F   15   466  UNP    P69910   DCEB_ECOLI      15    466
SEQADV 2DGK     A       UNP  P69910    MET     1 DELETION
SEQADV 2DGK     A       UNP  P69910    ASP     2 DELETION
SEQADV 2DGK     A       UNP  P69910    LYS     3 DELETION
SEQADV 2DGK     A       UNP  P69910    LYS     4 DELETION
SEQADV 2DGK     A       UNP  P69910    GLN     5 DELETION
SEQADV 2DGK     A       UNP  P69910    VAL     6 DELETION
SEQADV 2DGK     A       UNP  P69910    THR     7 DELETION
SEQADV 2DGK     A       UNP  P69910    ASP     8 DELETION
SEQADV 2DGK     A       UNP  P69910    LEU     9 DELETION
SEQADV 2DGK     A       UNP  P69910    ARG    10 DELETION
SEQADV 2DGK     A       UNP  P69910    SER    11 DELETION
SEQADV 2DGK     A       UNP  P69910    GLU    12 DELETION
SEQADV 2DGK     A       UNP  P69910    LEU    13 DELETION
SEQADV 2DGK     A       UNP  P69910    LEU    14 DELETION
SEQADV 2DGK     B       UNP  P69910    MET     1 DELETION
SEQADV 2DGK     B       UNP  P69910    ASP     2 DELETION
SEQADV 2DGK     B       UNP  P69910    LYS     3 DELETION
SEQADV 2DGK     B       UNP  P69910    LYS     4 DELETION
SEQADV 2DGK     B       UNP  P69910    GLN     5 DELETION
SEQADV 2DGK     B       UNP  P69910    VAL     6 DELETION
SEQADV 2DGK     B       UNP  P69910    THR     7 DELETION
SEQADV 2DGK     B       UNP  P69910    ASP     8 DELETION
SEQADV 2DGK     B       UNP  P69910    LEU     9 DELETION
SEQADV 2DGK     B       UNP  P69910    ARG    10 DELETION
SEQADV 2DGK     B       UNP  P69910    SER    11 DELETION
SEQADV 2DGK     B       UNP  P69910    GLU    12 DELETION
SEQADV 2DGK     B       UNP  P69910    LEU    13 DELETION
SEQADV 2DGK     B       UNP  P69910    LEU    14 DELETION
SEQADV 2DGK     C       UNP  P69910    MET     1 DELETION
SEQADV 2DGK     C       UNP  P69910    ASP     2 DELETION
SEQADV 2DGK     C       UNP  P69910    LYS     3 DELETION
SEQADV 2DGK     C       UNP  P69910    LYS     4 DELETION
SEQADV 2DGK     C       UNP  P69910    GLN     5 DELETION
SEQADV 2DGK     C       UNP  P69910    VAL     6 DELETION
SEQADV 2DGK     C       UNP  P69910    THR     7 DELETION
SEQADV 2DGK     C       UNP  P69910    ASP     8 DELETION
SEQADV 2DGK     C       UNP  P69910    LEU     9 DELETION
SEQADV 2DGK     C       UNP  P69910    ARG    10 DELETION
SEQADV 2DGK     C       UNP  P69910    SER    11 DELETION
SEQADV 2DGK     C       UNP  P69910    GLU    12 DELETION
SEQADV 2DGK     C       UNP  P69910    LEU    13 DELETION
SEQADV 2DGK     C       UNP  P69910    LEU    14 DELETION
SEQADV 2DGK     D       UNP  P69910    MET     1 DELETION
SEQADV 2DGK     D       UNP  P69910    ASP     2 DELETION
SEQADV 2DGK     D       UNP  P69910    LYS     3 DELETION
SEQADV 2DGK     D       UNP  P69910    LYS     4 DELETION
SEQADV 2DGK     D       UNP  P69910    GLN     5 DELETION
SEQADV 2DGK     D       UNP  P69910    VAL     6 DELETION
SEQADV 2DGK     D       UNP  P69910    THR     7 DELETION
SEQADV 2DGK     D       UNP  P69910    ASP     8 DELETION
SEQADV 2DGK     D       UNP  P69910    LEU     9 DELETION
SEQADV 2DGK     D       UNP  P69910    ARG    10 DELETION
SEQADV 2DGK     D       UNP  P69910    SER    11 DELETION
SEQADV 2DGK     D       UNP  P69910    GLU    12 DELETION
SEQADV 2DGK     D       UNP  P69910    LEU    13 DELETION
SEQADV 2DGK     D       UNP  P69910    LEU    14 DELETION
SEQADV 2DGK     E       UNP  P69910    MET     1 DELETION
SEQADV 2DGK     E       UNP  P69910    ASP     2 DELETION
SEQADV 2DGK     E       UNP  P69910    LYS     3 DELETION
SEQADV 2DGK     E       UNP  P69910    LYS     4 DELETION
SEQADV 2DGK     E       UNP  P69910    GLN     5 DELETION
SEQADV 2DGK     E       UNP  P69910    VAL     6 DELETION
SEQADV 2DGK     E       UNP  P69910    THR     7 DELETION
SEQADV 2DGK     E       UNP  P69910    ASP     8 DELETION
SEQADV 2DGK     E       UNP  P69910    LEU     9 DELETION
SEQADV 2DGK     E       UNP  P69910    ARG    10 DELETION
SEQADV 2DGK     E       UNP  P69910    SER    11 DELETION
SEQADV 2DGK     E       UNP  P69910    GLU    12 DELETION
SEQADV 2DGK     E       UNP  P69910    LEU    13 DELETION
SEQADV 2DGK     E       UNP  P69910    LEU    14 DELETION
SEQADV 2DGK     F       UNP  P69910    MET     1 DELETION
SEQADV 2DGK     F       UNP  P69910    ASP     2 DELETION
SEQADV 2DGK     F       UNP  P69910    LYS     3 DELETION
SEQADV 2DGK     F       UNP  P69910    LYS     4 DELETION
SEQADV 2DGK     F       UNP  P69910    GLN     5 DELETION
SEQADV 2DGK     F       UNP  P69910    VAL     6 DELETION
SEQADV 2DGK     F       UNP  P69910    THR     7 DELETION
SEQADV 2DGK     F       UNP  P69910    ASP     8 DELETION
SEQADV 2DGK     F       UNP  P69910    LEU     9 DELETION
SEQADV 2DGK     F       UNP  P69910    ARG    10 DELETION
SEQADV 2DGK     F       UNP  P69910    SER    11 DELETION
SEQADV 2DGK     F       UNP  P69910    GLU    12 DELETION
SEQADV 2DGK     F       UNP  P69910    LEU    13 DELETION
SEQADV 2DGK     F       UNP  P69910    LEU    14 DELETION
SEQRES   1 A  452  ASP SER ARG PHE GLY ALA LYS SER ILE SER THR ILE ALA
SEQRES   2 A  452  GLU SER LYS ARG PHE PRO LEU HIS GLU MET ARG ASP ASP
SEQRES   3 A  452  VAL ALA PHE GLN ILE ILE ASN ASP GLU LEU TYR LEU ASP
SEQRES   4 A  452  GLY ASN ALA ARG GLN ASN LEU ALA THR PHE CYS GLN THR
SEQRES   5 A  452  TRP ASP ASP GLU ASN VAL HIS LYS LEU MET ASP LEU SER
SEQRES   6 A  452  ILE ASN LYS ASN TRP ILE ASP LYS GLU GLU TYR PRO GLN
SEQRES   7 A  452  SER ALA ALA ILE ASP LEU ARG CYS VAL ASN MET VAL ALA
SEQRES   8 A  452  ASP LEU TRP HIS ALA PRO ALA PRO LYS ASN GLY GLN ALA
SEQRES   9 A  452  VAL GLY THR ASN THR ILE GLY SER SER GLU ALA CYS MET
SEQRES  10 A  452  LEU GLY GLY MET ALA MET LYS TRP ARG TRP ARG LYS ARG
SEQRES  11 A  452  MET GLU ALA ALA GLY LYS PRO THR ASP LYS PRO ASN LEU
SEQRES  12 A  452  VAL CYS GLY PRO VAL GLN ILE CYS TRP HIS LYS PHE ALA
SEQRES  13 A  452  ARG TYR TRP ASP VAL GLU LEU ARG GLU ILE PRO MET ARG
SEQRES  14 A  452  PRO GLY GLN LEU PHE MET ASP PRO LYS ARG MET ILE GLU
SEQRES  15 A  452  ALA CYS ASP GLU ASN THR ILE GLY VAL VAL PRO THR PHE
SEQRES  16 A  452  GLY VAL THR TYR THR GLY ASN TYR GLU PHE PRO GLN PRO
SEQRES  17 A  452  LEU HIS ASP ALA LEU ASP LYS PHE GLN ALA ASP THR GLY
SEQRES  18 A  452  ILE ASP ILE ASP MET HIS ILE ASP ALA ALA SER GLY GLY
SEQRES  19 A  452  PHE LEU ALA PRO PHE VAL ALA PRO ASP ILE VAL TRP ASP
SEQRES  20 A  452  PHE ARG LEU PRO ARG VAL LYS SER ILE SER ALA SER GLY
SEQRES  21 A  452  HIS LYS PHE GLY LEU ALA PRO LEU GLY CYS GLY TRP VAL
SEQRES  22 A  452  ILE TRP ARG ASP GLU GLU ALA LEU PRO GLN GLU LEU VAL
SEQRES  23 A  452  PHE ASN VAL ASP TYR LEU GLY GLY GLN ILE GLY THR PHE
SEQRES  24 A  452  ALA ILE ASN PHE SER ARG PRO ALA GLY GLN VAL ILE ALA
SEQRES  25 A  452  GLN TYR TYR GLU PHE LEU ARG LEU GLY ARG GLU GLY TYR
SEQRES  26 A  452  THR LYS VAL GLN ASN ALA SER TYR GLN VAL ALA ALA TYR
SEQRES  27 A  452  LEU ALA ASP GLU ILE ALA LYS LEU GLY PRO TYR GLU PHE
SEQRES  28 A  452  ILE CYS THR GLY ARG PRO ASP GLU GLY ILE PRO ALA VAL
SEQRES  29 A  452  CYS PHE LYS LEU LYS ASP GLY GLU ASP PRO GLY TYR THR
SEQRES  30 A  452  LEU TYR ASP LEU SER GLU ARG LEU ARG LEU ARG GLY TRP
SEQRES  31 A  452  GLN VAL PRO ALA PHE THR LEU GLY GLY GLU ALA THR ASP
SEQRES  32 A  452  ILE VAL VAL MET ARG ILE MET CYS ARG ARG GLY PHE GLU
SEQRES  33 A  452  MET ASP PHE ALA GLU LEU LEU LEU GLU ASP TYR LYS ALA
SEQRES  34 A  452  SER LEU LYS TYR LEU SER ASP HIS PRO LYS LEU GLN GLY
SEQRES  35 A  452  ILE ALA GLN GLN ASN SER PHE LYS HIS THR
SEQRES   1 B  452  ASP SER ARG PHE GLY ALA LYS SER ILE SER THR ILE ALA
SEQRES   2 B  452  GLU SER LYS ARG PHE PRO LEU HIS GLU MET ARG ASP ASP
SEQRES   3 B  452  VAL ALA PHE GLN ILE ILE ASN ASP GLU LEU TYR LEU ASP
SEQRES   4 B  452  GLY ASN ALA ARG GLN ASN LEU ALA THR PHE CYS GLN THR
SEQRES   5 B  452  TRP ASP ASP GLU ASN VAL HIS LYS LEU MET ASP LEU SER
SEQRES   6 B  452  ILE ASN LYS ASN TRP ILE ASP LYS GLU GLU TYR PRO GLN
SEQRES   7 B  452  SER ALA ALA ILE ASP LEU ARG CYS VAL ASN MET VAL ALA
SEQRES   8 B  452  ASP LEU TRP HIS ALA PRO ALA PRO LYS ASN GLY GLN ALA
SEQRES   9 B  452  VAL GLY THR ASN THR ILE GLY SER SER GLU ALA CYS MET
SEQRES  10 B  452  LEU GLY GLY MET ALA MET LYS TRP ARG TRP ARG LYS ARG
SEQRES  11 B  452  MET GLU ALA ALA GLY LYS PRO THR ASP LYS PRO ASN LEU
SEQRES  12 B  452  VAL CYS GLY PRO VAL GLN ILE CYS TRP HIS LYS PHE ALA
SEQRES  13 B  452  ARG TYR TRP ASP VAL GLU LEU ARG GLU ILE PRO MET ARG
SEQRES  14 B  452  PRO GLY GLN LEU PHE MET ASP PRO LYS ARG MET ILE GLU
SEQRES  15 B  452  ALA CYS ASP GLU ASN THR ILE GLY VAL VAL PRO THR PHE
SEQRES  16 B  452  GLY VAL THR TYR THR GLY ASN TYR GLU PHE PRO GLN PRO
SEQRES  17 B  452  LEU HIS ASP ALA LEU ASP LYS PHE GLN ALA ASP THR GLY
SEQRES  18 B  452  ILE ASP ILE ASP MET HIS ILE ASP ALA ALA SER GLY GLY
SEQRES  19 B  452  PHE LEU ALA PRO PHE VAL ALA PRO ASP ILE VAL TRP ASP
SEQRES  20 B  452  PHE ARG LEU PRO ARG VAL LYS SER ILE SER ALA SER GLY
SEQRES  21 B  452  HIS LYS PHE GLY LEU ALA PRO LEU GLY CYS GLY TRP VAL
SEQRES  22 B  452  ILE TRP ARG ASP GLU GLU ALA LEU PRO GLN GLU LEU VAL
SEQRES  23 B  452  PHE ASN VAL ASP TYR LEU GLY GLY GLN ILE GLY THR PHE
SEQRES  24 B  452  ALA ILE ASN PHE SER ARG PRO ALA GLY GLN VAL ILE ALA
SEQRES  25 B  452  GLN TYR TYR GLU PHE LEU ARG LEU GLY ARG GLU GLY TYR
SEQRES  26 B  452  THR LYS VAL GLN ASN ALA SER TYR GLN VAL ALA ALA TYR
SEQRES  27 B  452  LEU ALA ASP GLU ILE ALA LYS LEU GLY PRO TYR GLU PHE
SEQRES  28 B  452  ILE CYS THR GLY ARG PRO ASP GLU GLY ILE PRO ALA VAL
SEQRES  29 B  452  CYS PHE LYS LEU LYS ASP GLY GLU ASP PRO GLY TYR THR
SEQRES  30 B  452  LEU TYR ASP LEU SER GLU ARG LEU ARG LEU ARG GLY TRP
SEQRES  31 B  452  GLN VAL PRO ALA PHE THR LEU GLY GLY GLU ALA THR ASP
SEQRES  32 B  452  ILE VAL VAL MET ARG ILE MET CYS ARG ARG GLY PHE GLU
SEQRES  33 B  452  MET ASP PHE ALA GLU LEU LEU LEU GLU ASP TYR LYS ALA
SEQRES  34 B  452  SER LEU LYS TYR LEU SER ASP HIS PRO LYS LEU GLN GLY
SEQRES  35 B  452  ILE ALA GLN GLN ASN SER PHE LYS HIS THR
SEQRES   1 C  452  ASP SER ARG PHE GLY ALA LYS SER ILE SER THR ILE ALA
SEQRES   2 C  452  GLU SER LYS ARG PHE PRO LEU HIS GLU MET ARG ASP ASP
SEQRES   3 C  452  VAL ALA PHE GLN ILE ILE ASN ASP GLU LEU TYR LEU ASP
SEQRES   4 C  452  GLY ASN ALA ARG GLN ASN LEU ALA THR PHE CYS GLN THR
SEQRES   5 C  452  TRP ASP ASP GLU ASN VAL HIS LYS LEU MET ASP LEU SER
SEQRES   6 C  452  ILE ASN LYS ASN TRP ILE ASP LYS GLU GLU TYR PRO GLN
SEQRES   7 C  452  SER ALA ALA ILE ASP LEU ARG CYS VAL ASN MET VAL ALA
SEQRES   8 C  452  ASP LEU TRP HIS ALA PRO ALA PRO LYS ASN GLY GLN ALA
SEQRES   9 C  452  VAL GLY THR ASN THR ILE GLY SER SER GLU ALA CYS MET
SEQRES  10 C  452  LEU GLY GLY MET ALA MET LYS TRP ARG TRP ARG LYS ARG
SEQRES  11 C  452  MET GLU ALA ALA GLY LYS PRO THR ASP LYS PRO ASN LEU
SEQRES  12 C  452  VAL CYS GLY PRO VAL GLN ILE CYS TRP HIS LYS PHE ALA
SEQRES  13 C  452  ARG TYR TRP ASP VAL GLU LEU ARG GLU ILE PRO MET ARG
SEQRES  14 C  452  PRO GLY GLN LEU PHE MET ASP PRO LYS ARG MET ILE GLU
SEQRES  15 C  452  ALA CYS ASP GLU ASN THR ILE GLY VAL VAL PRO THR PHE
SEQRES  16 C  452  GLY VAL THR TYR THR GLY ASN TYR GLU PHE PRO GLN PRO
SEQRES  17 C  452  LEU HIS ASP ALA LEU ASP LYS PHE GLN ALA ASP THR GLY
SEQRES  18 C  452  ILE ASP ILE ASP MET HIS ILE ASP ALA ALA SER GLY GLY
SEQRES  19 C  452  PHE LEU ALA PRO PHE VAL ALA PRO ASP ILE VAL TRP ASP
SEQRES  20 C  452  PHE ARG LEU PRO ARG VAL LYS SER ILE SER ALA SER GLY
SEQRES  21 C  452  HIS LYS PHE GLY LEU ALA PRO LEU GLY CYS GLY TRP VAL
SEQRES  22 C  452  ILE TRP ARG ASP GLU GLU ALA LEU PRO GLN GLU LEU VAL
SEQRES  23 C  452  PHE ASN VAL ASP TYR LEU GLY GLY GLN ILE GLY THR PHE
SEQRES  24 C  452  ALA ILE ASN PHE SER ARG PRO ALA GLY GLN VAL ILE ALA
SEQRES  25 C  452  GLN TYR TYR GLU PHE LEU ARG LEU GLY ARG GLU GLY TYR
SEQRES  26 C  452  THR LYS VAL GLN ASN ALA SER TYR GLN VAL ALA ALA TYR
SEQRES  27 C  452  LEU ALA ASP GLU ILE ALA LYS LEU GLY PRO TYR GLU PHE
SEQRES  28 C  452  ILE CYS THR GLY ARG PRO ASP GLU GLY ILE PRO ALA VAL
SEQRES  29 C  452  CYS PHE LYS LEU LYS ASP GLY GLU ASP PRO GLY TYR THR
SEQRES  30 C  452  LEU TYR ASP LEU SER GLU ARG LEU ARG LEU ARG GLY TRP
SEQRES  31 C  452  GLN VAL PRO ALA PHE THR LEU GLY GLY GLU ALA THR ASP
SEQRES  32 C  452  ILE VAL VAL MET ARG ILE MET CYS ARG ARG GLY PHE GLU
SEQRES  33 C  452  MET ASP PHE ALA GLU LEU LEU LEU GLU ASP TYR LYS ALA
SEQRES  34 C  452  SER LEU LYS TYR LEU SER ASP HIS PRO LYS LEU GLN GLY
SEQRES  35 C  452  ILE ALA GLN GLN ASN SER PHE LYS HIS THR
SEQRES   1 D  452  ASP SER ARG PHE GLY ALA LYS SER ILE SER THR ILE ALA
SEQRES   2 D  452  GLU SER LYS ARG PHE PRO LEU HIS GLU MET ARG ASP ASP
SEQRES   3 D  452  VAL ALA PHE GLN ILE ILE ASN ASP GLU LEU TYR LEU ASP
SEQRES   4 D  452  GLY ASN ALA ARG GLN ASN LEU ALA THR PHE CYS GLN THR
SEQRES   5 D  452  TRP ASP ASP GLU ASN VAL HIS LYS LEU MET ASP LEU SER
SEQRES   6 D  452  ILE ASN LYS ASN TRP ILE ASP LYS GLU GLU TYR PRO GLN
SEQRES   7 D  452  SER ALA ALA ILE ASP LEU ARG CYS VAL ASN MET VAL ALA
SEQRES   8 D  452  ASP LEU TRP HIS ALA PRO ALA PRO LYS ASN GLY GLN ALA
SEQRES   9 D  452  VAL GLY THR ASN THR ILE GLY SER SER GLU ALA CYS MET
SEQRES  10 D  452  LEU GLY GLY MET ALA MET LYS TRP ARG TRP ARG LYS ARG
SEQRES  11 D  452  MET GLU ALA ALA GLY LYS PRO THR ASP LYS PRO ASN LEU
SEQRES  12 D  452  VAL CYS GLY PRO VAL GLN ILE CYS TRP HIS LYS PHE ALA
SEQRES  13 D  452  ARG TYR TRP ASP VAL GLU LEU ARG GLU ILE PRO MET ARG
SEQRES  14 D  452  PRO GLY GLN LEU PHE MET ASP PRO LYS ARG MET ILE GLU
SEQRES  15 D  452  ALA CYS ASP GLU ASN THR ILE GLY VAL VAL PRO THR PHE
SEQRES  16 D  452  GLY VAL THR TYR THR GLY ASN TYR GLU PHE PRO GLN PRO
SEQRES  17 D  452  LEU HIS ASP ALA LEU ASP LYS PHE GLN ALA ASP THR GLY
SEQRES  18 D  452  ILE ASP ILE ASP MET HIS ILE ASP ALA ALA SER GLY GLY
SEQRES  19 D  452  PHE LEU ALA PRO PHE VAL ALA PRO ASP ILE VAL TRP ASP
SEQRES  20 D  452  PHE ARG LEU PRO ARG VAL LYS SER ILE SER ALA SER GLY
SEQRES  21 D  452  HIS LYS PHE GLY LEU ALA PRO LEU GLY CYS GLY TRP VAL
SEQRES  22 D  452  ILE TRP ARG ASP GLU GLU ALA LEU PRO GLN GLU LEU VAL
SEQRES  23 D  452  PHE ASN VAL ASP TYR LEU GLY GLY GLN ILE GLY THR PHE
SEQRES  24 D  452  ALA ILE ASN PHE SER ARG PRO ALA GLY GLN VAL ILE ALA
SEQRES  25 D  452  GLN TYR TYR GLU PHE LEU ARG LEU GLY ARG GLU GLY TYR
SEQRES  26 D  452  THR LYS VAL GLN ASN ALA SER TYR GLN VAL ALA ALA TYR
SEQRES  27 D  452  LEU ALA ASP GLU ILE ALA LYS LEU GLY PRO TYR GLU PHE
SEQRES  28 D  452  ILE CYS THR GLY ARG PRO ASP GLU GLY ILE PRO ALA VAL
SEQRES  29 D  452  CYS PHE LYS LEU LYS ASP GLY GLU ASP PRO GLY TYR THR
SEQRES  30 D  452  LEU TYR ASP LEU SER GLU ARG LEU ARG LEU ARG GLY TRP
SEQRES  31 D  452  GLN VAL PRO ALA PHE THR LEU GLY GLY GLU ALA THR ASP
SEQRES  32 D  452  ILE VAL VAL MET ARG ILE MET CYS ARG ARG GLY PHE GLU
SEQRES  33 D  452  MET ASP PHE ALA GLU LEU LEU LEU GLU ASP TYR LYS ALA
SEQRES  34 D  452  SER LEU LYS TYR LEU SER ASP HIS PRO LYS LEU GLN GLY
SEQRES  35 D  452  ILE ALA GLN GLN ASN SER PHE LYS HIS THR
SEQRES   1 E  452  ASP SER ARG PHE GLY ALA LYS SER ILE SER THR ILE ALA
SEQRES   2 E  452  GLU SER LYS ARG PHE PRO LEU HIS GLU MET ARG ASP ASP
SEQRES   3 E  452  VAL ALA PHE GLN ILE ILE ASN ASP GLU LEU TYR LEU ASP
SEQRES   4 E  452  GLY ASN ALA ARG GLN ASN LEU ALA THR PHE CYS GLN THR
SEQRES   5 E  452  TRP ASP ASP GLU ASN VAL HIS LYS LEU MET ASP LEU SER
SEQRES   6 E  452  ILE ASN LYS ASN TRP ILE ASP LYS GLU GLU TYR PRO GLN
SEQRES   7 E  452  SER ALA ALA ILE ASP LEU ARG CYS VAL ASN MET VAL ALA
SEQRES   8 E  452  ASP LEU TRP HIS ALA PRO ALA PRO LYS ASN GLY GLN ALA
SEQRES   9 E  452  VAL GLY THR ASN THR ILE GLY SER SER GLU ALA CYS MET
SEQRES  10 E  452  LEU GLY GLY MET ALA MET LYS TRP ARG TRP ARG LYS ARG
SEQRES  11 E  452  MET GLU ALA ALA GLY LYS PRO THR ASP LYS PRO ASN LEU
SEQRES  12 E  452  VAL CYS GLY PRO VAL GLN ILE CYS TRP HIS LYS PHE ALA
SEQRES  13 E  452  ARG TYR TRP ASP VAL GLU LEU ARG GLU ILE PRO MET ARG
SEQRES  14 E  452  PRO GLY GLN LEU PHE MET ASP PRO LYS ARG MET ILE GLU
SEQRES  15 E  452  ALA CYS ASP GLU ASN THR ILE GLY VAL VAL PRO THR PHE
SEQRES  16 E  452  GLY VAL THR TYR THR GLY ASN TYR GLU PHE PRO GLN PRO
SEQRES  17 E  452  LEU HIS ASP ALA LEU ASP LYS PHE GLN ALA ASP THR GLY
SEQRES  18 E  452  ILE ASP ILE ASP MET HIS ILE ASP ALA ALA SER GLY GLY
SEQRES  19 E  452  PHE LEU ALA PRO PHE VAL ALA PRO ASP ILE VAL TRP ASP
SEQRES  20 E  452  PHE ARG LEU PRO ARG VAL LYS SER ILE SER ALA SER GLY
SEQRES  21 E  452  HIS LYS PHE GLY LEU ALA PRO LEU GLY CYS GLY TRP VAL
SEQRES  22 E  452  ILE TRP ARG ASP GLU GLU ALA LEU PRO GLN GLU LEU VAL
SEQRES  23 E  452  PHE ASN VAL ASP TYR LEU GLY GLY GLN ILE GLY THR PHE
SEQRES  24 E  452  ALA ILE ASN PHE SER ARG PRO ALA GLY GLN VAL ILE ALA
SEQRES  25 E  452  GLN TYR TYR GLU PHE LEU ARG LEU GLY ARG GLU GLY TYR
SEQRES  26 E  452  THR LYS VAL GLN ASN ALA SER TYR GLN VAL ALA ALA TYR
SEQRES  27 E  452  LEU ALA ASP GLU ILE ALA LYS LEU GLY PRO TYR GLU PHE
SEQRES  28 E  452  ILE CYS THR GLY ARG PRO ASP GLU GLY ILE PRO ALA VAL
SEQRES  29 E  452  CYS PHE LYS LEU LYS ASP GLY GLU ASP PRO GLY TYR THR
SEQRES  30 E  452  LEU TYR ASP LEU SER GLU ARG LEU ARG LEU ARG GLY TRP
SEQRES  31 E  452  GLN VAL PRO ALA PHE THR LEU GLY GLY GLU ALA THR ASP
SEQRES  32 E  452  ILE VAL VAL MET ARG ILE MET CYS ARG ARG GLY PHE GLU
SEQRES  33 E  452  MET ASP PHE ALA GLU LEU LEU LEU GLU ASP TYR LYS ALA
SEQRES  34 E  452  SER LEU LYS TYR LEU SER ASP HIS PRO LYS LEU GLN GLY
SEQRES  35 E  452  ILE ALA GLN GLN ASN SER PHE LYS HIS THR
SEQRES   1 F  452  ASP SER ARG PHE GLY ALA LYS SER ILE SER THR ILE ALA
SEQRES   2 F  452  GLU SER LYS ARG PHE PRO LEU HIS GLU MET ARG ASP ASP
SEQRES   3 F  452  VAL ALA PHE GLN ILE ILE ASN ASP GLU LEU TYR LEU ASP
SEQRES   4 F  452  GLY ASN ALA ARG GLN ASN LEU ALA THR PHE CYS GLN THR
SEQRES   5 F  452  TRP ASP ASP GLU ASN VAL HIS LYS LEU MET ASP LEU SER
SEQRES   6 F  452  ILE ASN LYS ASN TRP ILE ASP LYS GLU GLU TYR PRO GLN
SEQRES   7 F  452  SER ALA ALA ILE ASP LEU ARG CYS VAL ASN MET VAL ALA
SEQRES   8 F  452  ASP LEU TRP HIS ALA PRO ALA PRO LYS ASN GLY GLN ALA
SEQRES   9 F  452  VAL GLY THR ASN THR ILE GLY SER SER GLU ALA CYS MET
SEQRES  10 F  452  LEU GLY GLY MET ALA MET LYS TRP ARG TRP ARG LYS ARG
SEQRES  11 F  452  MET GLU ALA ALA GLY LYS PRO THR ASP LYS PRO ASN LEU
SEQRES  12 F  452  VAL CYS GLY PRO VAL GLN ILE CYS TRP HIS LYS PHE ALA
SEQRES  13 F  452  ARG TYR TRP ASP VAL GLU LEU ARG GLU ILE PRO MET ARG
SEQRES  14 F  452  PRO GLY GLN LEU PHE MET ASP PRO LYS ARG MET ILE GLU
SEQRES  15 F  452  ALA CYS ASP GLU ASN THR ILE GLY VAL VAL PRO THR PHE
SEQRES  16 F  452  GLY VAL THR TYR THR GLY ASN TYR GLU PHE PRO GLN PRO
SEQRES  17 F  452  LEU HIS ASP ALA LEU ASP LYS PHE GLN ALA ASP THR GLY
SEQRES  18 F  452  ILE ASP ILE ASP MET HIS ILE ASP ALA ALA SER GLY GLY
SEQRES  19 F  452  PHE LEU ALA PRO PHE VAL ALA PRO ASP ILE VAL TRP ASP
SEQRES  20 F  452  PHE ARG LEU PRO ARG VAL LYS SER ILE SER ALA SER GLY
SEQRES  21 F  452  HIS LYS PHE GLY LEU ALA PRO LEU GLY CYS GLY TRP VAL
SEQRES  22 F  452  ILE TRP ARG ASP GLU GLU ALA LEU PRO GLN GLU LEU VAL
SEQRES  23 F  452  PHE ASN VAL ASP TYR LEU GLY GLY GLN ILE GLY THR PHE
SEQRES  24 F  452  ALA ILE ASN PHE SER ARG PRO ALA GLY GLN VAL ILE ALA
SEQRES  25 F  452  GLN TYR TYR GLU PHE LEU ARG LEU GLY ARG GLU GLY TYR
SEQRES  26 F  452  THR LYS VAL GLN ASN ALA SER TYR GLN VAL ALA ALA TYR
SEQRES  27 F  452  LEU ALA ASP GLU ILE ALA LYS LEU GLY PRO TYR GLU PHE
SEQRES  28 F  452  ILE CYS THR GLY ARG PRO ASP GLU GLY ILE PRO ALA VAL
SEQRES  29 F  452  CYS PHE LYS LEU LYS ASP GLY GLU ASP PRO GLY TYR THR
SEQRES  30 F  452  LEU TYR ASP LEU SER GLU ARG LEU ARG LEU ARG GLY TRP
SEQRES  31 F  452  GLN VAL PRO ALA PHE THR LEU GLY GLY GLU ALA THR ASP
SEQRES  32 F  452  ILE VAL VAL MET ARG ILE MET CYS ARG ARG GLY PHE GLU
SEQRES  33 F  452  MET ASP PHE ALA GLU LEU LEU LEU GLU ASP TYR LYS ALA
SEQRES  34 F  452  SER LEU LYS TYR LEU SER ASP HIS PRO LYS LEU GLN GLY
SEQRES  35 F  452  ILE ALA GLN GLN ASN SER PHE LYS HIS THR
HET    SO4  A4770       5
HET    SO4  B4771       5
HET    SO4  C4772       5
HET    SO4  D4773       5
HET    SO4  E4774       5
HET    SO4  F4775       5
HET    PLP  A1500      15
HET    PLP  B1501      15
HET    PLP  C1502      15
HET    PLP  D1503      15
HET    PLP  E1504      15
HET    PLP  F1505      15
HET    EDO  B2191       5
HET    EDO  C2192       5
HET    EDO  A2193       4
HET    EDO  B2194       4
HET    EDO  C2195       4
HET    EDO  D2196       4
HET    EDO  E2197       4
HET    EDO  F2198       4
HETNAM     SO4 SULFATE ION
HETNAM     PLP PYRIDOXAL-5'-PHOSPHATE
HETNAM     EDO 1,2-ETHANEDIOL
HETSYN     PLP VITAMIN B6 PHOSPHATE
HETSYN     EDO ETHYLENE GLYCOL
FORMUL   7  SO4    6(O4 S 2-)
FORMUL  13  PLP    6(C8 H10 N O6 P)
FORMUL  19  EDO    8(C2 H6 O2)
FORMUL  27  HOH   *1695(H2 O)
HELIX    1   1 ARG A   38  LEU A   50  1                                  13
HELIX    2   2 TYR A   51  ASP A   53  5                                   3
HELIX    3   3 ASP A   69  SER A   79  1                                  11
HELIX    4   4 TYR A   90  TRP A  108  1                                  19
HELIX    5   5 GLY A  125  ALA A  148  1                                  24
HELIX    6   6 GLN A  163  TRP A  173  1                                  11
HELIX    7   7 ASP A  190  CYS A  198  1                                   9
HELIX    8   8 PHE A  219  GLY A  235  1                                  17
HELIX    9   9 SER A  246  PHE A  249  5                                   4
HELIX   10  10 LEU A  250  ALA A  255  1                                   6
HELIX   11  11 ASP A  291  LEU A  295  5                                   5
HELIX   12  12 PRO A  296  VAL A  300  5                                   5
HELIX   13  13 ALA A  321  LYS A  359  1                                  39
HELIX   14  14 THR A  391  ARG A  402  1                                  12
HELIX   15  15 GLU A  430  HIS A  451  1                                  22
HELIX   16  16 PRO A  452  GLN A  455  5                                   4
HELIX   17  17 ARG B   38  LEU B   50  1                                  13
HELIX   18  18 TYR B   51  ASP B   53  5                                   3
HELIX   19  19 ASP B   69  SER B   79  1                                  11
HELIX   20  20 TYR B   90  TRP B  108  1                                  19
HELIX   21  21 GLY B  125  ALA B  148  1                                  24
HELIX   22  22 GLN B  163  TRP B  173  1                                  11
HELIX   23  23 ASP B  190  CYS B  198  1                                   9
HELIX   24  24 PHE B  219  GLY B  235  1                                  17
HELIX   25  25 SER B  246  PHE B  249  5                                   4
HELIX   26  26 LEU B  250  ALA B  255  1                                   6
HELIX   27  27 ASP B  291  LEU B  295  5                                   5
HELIX   28  28 PRO B  296  VAL B  300  5                                   5
HELIX   29  29 ALA B  321  ALA B  358  1                                  38
HELIX   30  30 LYS B  359  GLY B  361  5                                   3
HELIX   31  31 THR B  391  LEU B  401  1                                  11
HELIX   32  32 GLU B  430  HIS B  451  1                                  22
HELIX   33  33 PRO B  452  GLN B  455  5                                   4
HELIX   34  34 ARG C   38  LEU C   50  1                                  13
HELIX   35  35 TYR C   51  ASP C   53  5                                   3
HELIX   36  36 ASP C   69  SER C   79  1                                  11
HELIX   37  37 TYR C   90  TRP C  108  1                                  19
HELIX   38  38 GLY C  125  ALA C  148  1                                  24
HELIX   39  39 GLN C  163  TRP C  173  1                                  11
HELIX   40  40 ASP C  190  CYS C  198  1                                   9
HELIX   41  41 PHE C  219  GLY C  235  1                                  17
HELIX   42  42 SER C  246  PHE C  249  5                                   4
HELIX   43  43 LEU C  250  ALA C  255  1                                   6
HELIX   44  44 ASP C  291  LEU C  295  5                                   5
HELIX   45  45 PRO C  296  VAL C  300  5                                   5
HELIX   46  46 ALA C  321  LEU C  360  1                                  40
HELIX   47  47 THR C  391  ARG C  402  1                                  12
HELIX   48  48 GLU C  430  HIS C  451  1                                  22
HELIX   49  49 PRO C  452  GLN C  455  5                                   4
HELIX   50  50 ARG D   38  LEU D   50  1                                  13
HELIX   51  51 TYR D   51  ASP D   53  5                                   3
HELIX   52  52 ASP D   69  SER D   79  1                                  11
HELIX   53  53 TYR D   90  TRP D  108  1                                  19
HELIX   54  54 GLY D  125  ALA D  148  1                                  24
HELIX   55  55 GLN D  163  TRP D  173  1                                  11
HELIX   56  56 ASP D  190  CYS D  198  1                                   9
HELIX   57  57 PHE D  219  GLY D  235  1                                  17
HELIX   58  58 SER D  246  PHE D  249  5                                   4
HELIX   59  59 LEU D  250  ALA D  255  1                                   6
HELIX   60  60 ASP D  291  LEU D  295  5                                   5
HELIX   61  61 PRO D  296  VAL D  300  5                                   5
HELIX   62  62 ALA D  321  LYS D  359  1                                  39
HELIX   63  63 THR D  391  LEU D  401  1                                  11
HELIX   64  64 GLU D  430  HIS D  451  1                                  22
HELIX   65  65 PRO D  452  GLN D  455  5                                   4
HELIX   66  66 ARG E   38  TYR E   51  1                                  14
HELIX   67  67 ASP E   69  SER E   79  1                                  11
HELIX   68  68 TYR E   90  TRP E  108  1                                  19
HELIX   69  69 GLY E  125  ALA E  148  1                                  24
HELIX   70  70 GLN E  163  TRP E  173  1                                  11
HELIX   71  71 ASP E  190  CYS E  198  1                                   9
HELIX   72  72 PHE E  219  GLY E  235  1                                  17
HELIX   73  73 SER E  246  PHE E  249  5                                   4
HELIX   74  74 LEU E  250  ALA E  255  1                                   6
HELIX   75  75 ASP E  291  LEU E  295  5                                   5
HELIX   76  76 PRO E  296  VAL E  300  5                                   5
HELIX   77  77 ALA E  321  ALA E  358  1                                  38
HELIX   78  78 LYS E  359  GLY E  361  5                                   3
HELIX   79  79 THR E  391  ARG E  402  1                                  12
HELIX   80  80 GLY E  412  THR E  416  5                                   5
HELIX   81  81 GLU E  430  HIS E  451  1                                  22
HELIX   82  82 PRO E  452  GLN E  455  5                                   4
HELIX   83  83 ARG F   38  LEU F   50  1                                  13
HELIX   84  84 TYR F   51  ASP F   53  5                                   3
HELIX   85  85 ASP F   69  SER F   79  1                                  11
HELIX   86  86 TYR F   90  TRP F  108  1                                  19
HELIX   87  87 GLY F  125  ALA F  148  1                                  24
HELIX   88  88 GLN F  163  TRP F  173  1                                  11
HELIX   89  89 ASP F  190  CYS F  198  1                                   9
HELIX   90  90 PHE F  219  GLY F  235  1                                  17
HELIX   91  91 SER F  246  PHE F  249  5                                   4
HELIX   92  92 LEU F  250  ALA F  255  1                                   6
HELIX   93  93 ASP F  291  LEU F  295  5                                   5
HELIX   94  94 PRO F  296  VAL F  300  5                                   5
HELIX   95  95 ALA F  321  LYS F  359  1                                  39
HELIX   96  96 THR F  391  ARG F  402  1                                  12
HELIX   97  97 GLY F  412  THR F  416  5                                   5
HELIX   98  98 GLU F  430  HIS F  451  1                                  22
HELIX   99  99 PRO F  452  GLN F  455  5                                   4
SHEET    1   A 4 VAL A 119  THR A 123  0
SHEET    2   A 4 GLY A 285  TRP A 289 -1  O  TRP A 289   N  VAL A 119
SHEET    3   A 4 VAL A 267  SER A 273 -1  N  ILE A 270   O  ILE A 288
SHEET    4   A 4 MET A 240  ASP A 243  1  N  ILE A 242   O  SER A 271
SHEET    1   B 3 GLU A 176  GLU A 179  0
SHEET    2   B 3 ASN A 156  CYS A 159  1  N  LEU A 157   O  ARG A 178
SHEET    3   B 3 THR A 202  VAL A 206  1  O  ILE A 203   N  ASN A 156
SHEET    1   C 2 PHE A 301  VAL A 303  0
SHEET    2   C 2 ILE A 310  THR A 312 -1  O  THR A 312   N  PHE A 301
SHEET    1   D 4 TYR A 363  THR A 368  0
SHEET    2   D 4 ALA A 377  LEU A 382 -1  O  CYS A 379   N  ILE A 366
SHEET    3   D 4 VAL A 419  MET A 424 -1  O  ILE A 423   N  VAL A 378
SHEET    4   D 4 ALA A 408  THR A 410 -1  N  PHE A 409   O  VAL A 420
SHEET    1   E 4 VAL B 119  THR B 123  0
SHEET    2   E 4 GLY B 285  TRP B 289 -1  O  TRP B 289   N  VAL B 119
SHEET    3   E 4 VAL B 267  SER B 273 -1  N  ILE B 270   O  ILE B 288
SHEET    4   E 4 MET B 240  ASP B 243  1  N  ILE B 242   O  SER B 269
SHEET    1   F 3 GLU B 176  GLU B 179  0
SHEET    2   F 3 ASN B 156  CYS B 159  1  N  LEU B 157   O  ARG B 178
SHEET    3   F 3 THR B 202  VAL B 206  1  O  ILE B 203   N  ASN B 156
SHEET    1   G 2 PHE B 301  VAL B 303  0
SHEET    2   G 2 ILE B 310  THR B 312 -1  O  THR B 312   N  PHE B 301
SHEET    1   H 4 TYR B 363  THR B 368  0
SHEET    2   H 4 ALA B 377  LEU B 382 -1  O  CYS B 379   N  ILE B 366
SHEET    3   H 4 VAL B 419  MET B 424 -1  O  ILE B 423   N  VAL B 378
SHEET    4   H 4 ALA B 408  THR B 410 -1  N  PHE B 409   O  VAL B 420
SHEET    1   I 4 VAL C 119  THR C 123  0
SHEET    2   I 4 GLY C 285  TRP C 289 -1  O  TRP C 289   N  VAL C 119
SHEET    3   I 4 VAL C 267  SER C 273 -1  N  ALA C 272   O  TRP C 286
SHEET    4   I 4 MET C 240  ASP C 243  1  N  ILE C 242   O  SER C 269
SHEET    1   J 3 GLU C 176  GLU C 179  0
SHEET    2   J 3 ASN C 156  CYS C 159  1  N  LEU C 157   O  ARG C 178
SHEET    3   J 3 THR C 202  VAL C 206  1  O  ILE C 203   N  ASN C 156
SHEET    1   K 2 PHE C 301  VAL C 303  0
SHEET    2   K 2 ILE C 310  THR C 312 -1  O  THR C 312   N  PHE C 301
SHEET    1   L 4 TYR C 363  THR C 368  0
SHEET    2   L 4 ALA C 377  LEU C 382 -1  O  CYS C 379   N  ILE C 366
SHEET    3   L 4 VAL C 419  MET C 424 -1  O  ILE C 423   N  VAL C 378
SHEET    4   L 4 ALA C 408  THR C 410 -1  N  PHE C 409   O  VAL C 420
SHEET    1   M 4 VAL D 119  THR D 123  0
SHEET    2   M 4 GLY D 285  TRP D 289 -1  O  TRP D 289   N  VAL D 119
SHEET    3   M 4 VAL D 267  SER D 273 -1  N  ILE D 270   O  ILE D 288
SHEET    4   M 4 MET D 240  ASP D 243  1  N  MET D 240   O  LYS D 268
SHEET    1   N 3 GLU D 176  GLU D 179  0
SHEET    2   N 3 ASN D 156  CYS D 159  1  N  LEU D 157   O  ARG D 178
SHEET    3   N 3 THR D 202  VAL D 206  1  O  ILE D 203   N  ASN D 156
SHEET    1   O 2 PHE D 301  VAL D 303  0
SHEET    2   O 2 ILE D 310  THR D 312 -1  O  THR D 312   N  PHE D 301
SHEET    1   P 4 TYR D 363  THR D 368  0
SHEET    2   P 4 ALA D 377  LEU D 382 -1  O  CYS D 379   N  ILE D 366
SHEET    3   P 4 VAL D 419  MET D 424 -1  O  ILE D 423   N  VAL D 378
SHEET    4   P 4 ALA D 408  THR D 410 -1  N  PHE D 409   O  VAL D 420
SHEET    1   Q 4 VAL E 119  THR E 123  0
SHEET    2   Q 4 GLY E 285  TRP E 289 -1  O  TRP E 289   N  VAL E 119
SHEET    3   Q 4 VAL E 267  SER E 273 -1  N  ALA E 272   O  TRP E 286
SHEET    4   Q 4 MET E 240  ASP E 243  1  N  ILE E 242   O  SER E 271
SHEET    1   R 3 GLU E 176  GLU E 179  0
SHEET    2   R 3 ASN E 156  CYS E 159  1  N  LEU E 157   O  ARG E 178
SHEET    3   R 3 THR E 202  VAL E 206  1  O  ILE E 203   N  ASN E 156
SHEET    1   S 2 PHE E 301  VAL E 303  0
SHEET    2   S 2 ILE E 310  THR E 312 -1  O  THR E 312   N  PHE E 301
SHEET    1   T 4 TYR E 363  THR E 368  0
SHEET    2   T 4 ALA E 377  LEU E 382 -1  O  CYS E 379   N  ILE E 366
SHEET    3   T 4 VAL E 419  MET E 424 -1  O  ILE E 423   N  VAL E 378
SHEET    4   T 4 ALA E 408  THR E 410 -1  N  PHE E 409   O  VAL E 420
SHEET    1   U 4 VAL F 119  THR F 123  0
SHEET    2   U 4 GLY F 285  TRP F 289 -1  O  TRP F 289   N  VAL F 119
SHEET    3   U 4 VAL F 267  SER F 273 -1  N  ILE F 270   O  ILE F 288
SHEET    4   U 4 MET F 240  ASP F 243  1  N  ILE F 242   O  SER F 271
SHEET    1   V 3 GLU F 176  GLU F 179  0
SHEET    2   V 3 ASN F 156  CYS F 159  1  N  LEU F 157   O  ARG F 178
SHEET    3   V 3 THR F 202  VAL F 206  1  O  VAL F 206   N  VAL F 158
SHEET    1   W 2 PHE F 301  VAL F 303  0
SHEET    2   W 2 ILE F 310  THR F 312 -1  O  THR F 312   N  PHE F 301
SHEET    1   X 4 TYR F 363  THR F 368  0
SHEET    2   X 4 ALA F 377  LEU F 382 -1  O  CYS F 379   N  ILE F 366
SHEET    3   X 4 VAL F 419  MET F 424 -1  O  ILE F 423   N  VAL F 378
SHEET    4   X 4 ALA F 408  THR F 410 -1  N  PHE F 409   O  VAL F 420
LINK         C4A PLP A1500                 NZ  LYS A 276     1555   1555  1.48
LINK         C4A PLP A1500                 NE2 HIS A 465     1555   1555  1.45
LINK         C4A PLP B1501                 NZ  LYS B 276     1555   1555  1.48
LINK         C4A PLP B1501                 NE2 HIS B 465     1555   1555  1.45
LINK         C4A PLP C1502                 NZ  LYS C 276     1555   1555  1.48
LINK         C4A PLP C1502                 NE2 HIS C 465     1555   1555  1.45
LINK         C4A PLP D1503                 NZ  LYS D 276     1555   1555  1.48
LINK         C4A PLP D1503                 NE2 HIS D 465     1555   1555  1.45
LINK         C4A PLP E1504                 NZ  LYS E 276     1555   1555  1.48
LINK         C4A PLP E1504                 NE2 HIS E 465     1555   1555  1.45
LINK         C4A PLP F1505                 NZ  LYS F 276     1555   1555  1.48
LINK         C4A PLP F1505                 NE2 HIS F 465     1555   1555  1.45
SITE     1 AC1  6 PRO A 113  LYS A 114  ASP A 291  GLU A 292
SITE     2 AC1  6 HOH A5007  HOH A5008
SITE     1 AC2  6 LYS B 114  ASP B 291  GLU B 292  HOH B4952
SITE     2 AC2  6 HOH B4994  HOH B5041
SITE     1 AC3  6 LYS C 114  ASP C 291  GLU C 292  HOH C4881
SITE     2 AC3  6 HOH C4889  HOH C4993
SITE     1 AC4  7 PRO D 113  LYS D 114  ASP D 291  GLU D 292
SITE     2 AC4  7 HOH D5003  HOH D5044  HOH D5045
SITE     1 AC5  3 LYS E 114  ASP E 291  GLU E 292
SITE     1 AC6  4 LYS F 114  ASP F 291  GLU F 292  HOH F4963
SITE     1 AC7 17 GLY A 125  SER A 126  SER A 127  GLN A 163
SITE     2 AC7 17 CYS A 165  THR A 208  THR A 212  ASP A 243
SITE     3 AC7 17 ALA A 245  SER A 273  HIS A 275  LYS A 276
SITE     4 AC7 17 HIS A 465  HOH A4774  HOH A4783  PHE B 317
SITE     5 AC7 17 SER B 318
SITE     1 AC8 16 PHE A 317  SER A 318  GLY B 125  SER B 126
SITE     2 AC8 16 SER B 127  GLN B 163  THR B 208  THR B 212
SITE     3 AC8 16 ASP B 243  ALA B 245  SER B 273  HIS B 275
SITE     4 AC8 16 LYS B 276  HIS B 465  HOH B4782  HOH B4888
SITE     1 AC9 16 GLY C 125  SER C 126  SER C 127  GLN C 163
SITE     2 AC9 16 THR C 208  THR C 212  ASP C 243  ALA C 245
SITE     3 AC9 16 SER C 273  HIS C 275  LYS C 276  HIS C 465
SITE     4 AC9 16 HOH C4830  PHE D 317  SER D 318  HOH D4779
SITE     1 BC1 17 PHE C 317  SER C 318  GLY D 125  SER D 126
SITE     2 BC1 17 SER D 127  GLN D 163  CYS D 165  THR D 208
SITE     3 BC1 17 THR D 212  ASP D 243  ALA D 245  SER D 273
SITE     4 BC1 17 HIS D 275  LYS D 276  HIS D 465  HOH D4777
SITE     5 BC1 17 HOH D4825
SITE     1 BC2 17 GLY E 125  SER E 126  SER E 127  GLN E 163
SITE     2 BC2 17 CYS E 165  THR E 208  THR E 212  ASP E 243
SITE     3 BC2 17 ALA E 245  SER E 273  HIS E 275  LYS E 276
SITE     4 BC2 17 HIS E 465  HOH E4794  HOH E4824  PHE F 317
SITE     5 BC2 17 SER F 318
SITE     1 BC3 18 PHE E 317  SER E 318  HOH E4790  GLY F 125
SITE     2 BC3 18 SER F 126  SER F 127  GLN F 163  CYS F 165
SITE     3 BC3 18 THR F 208  GLY F 210  THR F 212  ASP F 243
SITE     4 BC3 18 ALA F 245  SER F 273  HIS F 275  LYS F 276
SITE     5 BC3 18 HIS F 465  HOH F4898
SITE     1 BC4  5 ASN A  81  HOH A4779  ARG B  57  ASP B  68
SITE     2 BC4  5 TYR C  51
SITE     1 BC5  5 TYR B  51  ARG C  57  ASP C  68  HOH C4982
SITE     2 BC5  5 ASN D  81
SITE     1 BC6  5 GLN A  92  ARG A  99  HOH A4970  GLU B  49
SITE     2 BC6  5 ASP C 432
SITE     1 BC7  5 GLU A  49  GLN B  92  ARG B  99  HOH B4808
SITE     2 BC7  5 ASP F 432
SITE     1 BC8  6 GLN C  92  ARG C  99  HOH C4988  GLU D  49
SITE     2 BC8  6 LEU D  52  ASP E 432
SITE     1 BC9  6 ASP B 432  LEU B 436  GLU C  49  GLN D  92
SITE     2 BC9  6 ARG D  99  HOH D4938
SITE     1 CC1  6 ASP A 432  GLN E  92  ARG E  99  HOH E4879
SITE     2 CC1  6 GLU F  49  LEU F  52
SITE     1 CC2  8 ASP D 432  PHE D 433  LEU D 436  GLU E  49
SITE     2 CC2  8 LEU E  52  GLN F  92  ARG F  99  HOH F4942
CRYST1   92.770  158.560  201.420  90.00  90.00  90.00 P 21 21 21   24
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      0.010779  0.000000  0.000000        0.00000
SCALE2      0.000000  0.006307  0.000000        0.00000
SCALE3      0.000000  0.000000  0.004965        0.00000
      
PROCHECK
Go to PROCHECK summary
 References