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PDBsum entry 2dgl

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Top Page protein ligands metals Protein-protein interface(s) links
Lyase PDB id
2dgl
Jmol
Contents
Protein chains
(+ 0 more) 450 a.a.
Ligands
PLP ×6
ACY ×6
Metals
_BR ×24
Waters ×134
HEADER    LYASE                                   14-MAR-06   2DGL
TITLE     CRYSTAL STRUCTURE OF ESCHERICHIA COLI GADB IN COMPLEX WITH BROMIDE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: GLUTAMATE DECARBOXYLASE BETA;
COMPND   3 CHAIN: A, B, C, D, E, F;
COMPND   4 SYNONYM: GAD-BETA, GADB;
COMPND   5 EC: 4.1.1.15;
COMPND   6 ENGINEERED: 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 COMPLEXED WITH BROMIDE, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    M.G.GRUETTER,G.CAPITANI,H.GUT
REVDAT   3   13-JUL-11 2DGL    1       VERSN
REVDAT   2   24-FEB-09 2DGL    1       VERSN
REVDAT   1   20-JUN-06 2DGL    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.    3.15 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) : 3.15
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00
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)   (%) : 99.6
REMARK   3   NUMBER OF REFLECTIONS             : 104053
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                     : 0.248
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 2067
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) : 3.15
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.26
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.10
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3110
REMARK   3   BIN FREE R VALUE                    : 0.3420
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 206
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            : 21497
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 138
REMARK   3   SOLVENT ATOMS            : 134
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 39.40
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.70
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) : 0.36
REMARK   3   ESD FROM SIGMAA              (A) : 0.43
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) : 0.42
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.45
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.008
REMARK   3   BOND ANGLES            (DEGREES) : 1.27
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 2DGL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-MAR-06.
REMARK 100 THE RCSB ID CODE IS RCSB025393.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 09-AUG-04
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) : 0.9000
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 : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 104068
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.150
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8
REMARK 200  DATA REDUNDANCY                : 3.600
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.12900
REMARK 200   FOR THE DATA SET  : 9.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.15
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.26
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.47500
REMARK 200   FOR SHELL         : 2.700
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 1PMM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 73.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 2000 MME, 0.18M POTASSIUM
REMARK 280  BROMIDE, 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 63 2 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z
REMARK 290       3555   -X+Y,-X,Z
REMARK 290       4555   -X,-Y,Z+1/2
REMARK 290       5555   Y,-X+Y,Z+1/2
REMARK 290       6555   X-Y,X,Z+1/2
REMARK 290       7555   Y,X,-Z
REMARK 290       8555   X-Y,-Y,-Z
REMARK 290       9555   -X,-X+Y,-Z
REMARK 290      10555   -Y,-X,-Z+1/2
REMARK 290      11555   -X+Y,Y,-Z+1/2
REMARK 290      12555   X,X-Y,-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 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  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      116.86550
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      116.86550
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      116.86550
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      116.86550
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      116.86550
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      116.86550
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 53280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 84800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -209.0 KCAL/MOL
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     MET A     1
REMARK 465     ASP A     2
REMARK 465     LYS A   453
REMARK 465     LEU A   454
REMARK 465     GLN A   455
REMARK 465     GLY A   456
REMARK 465     ILE A   457
REMARK 465     ALA A   458
REMARK 465     GLN A   459
REMARK 465     GLN A   460
REMARK 465     ASN A   461
REMARK 465     SER A   462
REMARK 465     PHE A   463
REMARK 465     LYS A   464
REMARK 465     HIS A   465
REMARK 465     THR A   466
REMARK 465     MET B     1
REMARK 465     ASP B     2
REMARK 465     LYS B   453
REMARK 465     LEU B   454
REMARK 465     GLN B   455
REMARK 465     GLY B   456
REMARK 465     ILE B   457
REMARK 465     ALA B   458
REMARK 465     GLN B   459
REMARK 465     GLN B   460
REMARK 465     ASN B   461
REMARK 465     SER B   462
REMARK 465     PHE B   463
REMARK 465     LYS B   464
REMARK 465     HIS B   465
REMARK 465     THR B   466
REMARK 465     MET C     1
REMARK 465     ASP C     2
REMARK 465     LEU C   454
REMARK 465     GLN C   455
REMARK 465     GLY C   456
REMARK 465     ILE C   457
REMARK 465     ALA C   458
REMARK 465     GLN C   459
REMARK 465     GLN C   460
REMARK 465     ASN C   461
REMARK 465     SER C   462
REMARK 465     PHE C   463
REMARK 465     LYS C   464
REMARK 465     HIS C   465
REMARK 465     THR C   466
REMARK 465     MET D     1
REMARK 465     ASP D     2
REMARK 465     LYS D   453
REMARK 465     LEU D   454
REMARK 465     GLN D   455
REMARK 465     GLY D   456
REMARK 465     ILE D   457
REMARK 465     ALA D   458
REMARK 465     GLN D   459
REMARK 465     GLN D   460
REMARK 465     ASN D   461
REMARK 465     SER D   462
REMARK 465     PHE D   463
REMARK 465     LYS D   464
REMARK 465     HIS D   465
REMARK 465     THR D   466
REMARK 465     MET E     1
REMARK 465     ASP E     2
REMARK 465     GLN E   455
REMARK 465     GLY E   456
REMARK 465     ILE E   457
REMARK 465     ALA E   458
REMARK 465     GLN E   459
REMARK 465     GLN E   460
REMARK 465     ASN E   461
REMARK 465     SER E   462
REMARK 465     PHE E   463
REMARK 465     LYS E   464
REMARK 465     HIS E   465
REMARK 465     THR E   466
REMARK 465     MET F     1
REMARK 465     ASP F     2
REMARK 465     LEU F   454
REMARK 465     GLN F   455
REMARK 465     GLY F   456
REMARK 465     ILE F   457
REMARK 465     ALA F   458
REMARK 465     GLN F   459
REMARK 465     GLN F   460
REMARK 465     ASN F   461
REMARK 465     SER F   462
REMARK 465     PHE F   463
REMARK 465     LYS F   464
REMARK 465     HIS F   465
REMARK 465     THR F   466
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    ASP A  15      147.69    -39.20
REMARK 500    SER A  16     -155.29    -71.91
REMARK 500    ALA A 112      113.76    -39.32
REMARK 500    GLN A 117      106.79   -164.05
REMARK 500    ALA A 118      154.98    -48.85
REMARK 500    LEU A 187       55.91    -92.57
REMARK 500    SER A 246      -68.75    -93.17
REMARK 500    ALA A 255       58.00   -153.30
REMARK 500    TRP A 260      -18.31   -141.52
REMARK 500    ASP A 261     -147.38    -88.63
REMARK 500    LYS A 276      -96.37   -107.79
REMARK 500    PHE A 313       90.51   -162.71
REMARK 500    PHE A 317     -102.80   -122.38
REMARK 500    PRO A 376       73.89    -69.52
REMARK 500    LYS B 114     -108.82    -68.19
REMARK 500    ASN B 115       56.10    -64.88
REMARK 500    GLN B 186       84.23   -150.11
REMARK 500    LEU B 187       56.60    -93.57
REMARK 500    SER B 246      -66.98    -93.99
REMARK 500    LEU B 250      -69.10   -121.81
REMARK 500    ALA B 255       60.38   -154.64
REMARK 500    TRP B 260      -17.10   -141.62
REMARK 500    ASP B 261     -147.35    -88.55
REMARK 500    LYS B 276      -96.49   -107.95
REMARK 500    TYR B 305      105.76   -164.47
REMARK 500    LEU B 306       65.06     62.00
REMARK 500    PHE B 317     -102.20   -146.47
REMARK 500    ILE C 164      -35.67    -38.44
REMARK 500    LEU C 187       55.47    -92.49
REMARK 500    SER C 246      -68.09    -93.56
REMARK 500    LEU C 250      -67.84   -121.44
REMARK 500    ALA C 255       61.21   -153.66
REMARK 500    TRP C 260      -17.25   -142.18
REMARK 500    ASP C 261     -147.53    -88.35
REMARK 500    LYS C 276      -95.22   -107.76
REMARK 500    LEU C 306       71.39     52.88
REMARK 500    PHE C 317      -97.46   -104.82
REMARK 500    ARG C 319      155.50    179.18
REMARK 500    ASP C 384      119.66    -38.02
REMARK 500    LEU D 187       56.93    -93.80
REMARK 500    GLU D 196       -9.21    -59.89
REMARK 500    SER D 246      -68.10    -93.58
REMARK 500    LEU D 250      -68.50   -121.42
REMARK 500    ALA D 255       59.06   -153.88
REMARK 500    TRP D 260      -16.97   -141.42
REMARK 500    ASP D 261     -147.15    -90.06
REMARK 500    LYS D 276      -95.93   -108.52
REMARK 500    PHE D 317     -110.53   -142.31
REMARK 500    ARG D 319      159.19    179.33
REMARK 500    PRO D 362       82.13    -69.28
REMARK 500
REMARK 500 THIS ENTRY HAS      74 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 467
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR F 467
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 468
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 467
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR C 467
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 468
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 469
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 470
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR C 468
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR D 467
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR E 467
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR D 468
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR E 468
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR C 469
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR E 469
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR F 468
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 469
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR F 469
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 470
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 471
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR C 470
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR D 469
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR E 470
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP E 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP F 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY E 518
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY F 528
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY C 538
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY C 548
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY B 558
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 568
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: 2DGK   RELATED DB: PDB
REMARK 900 N-TERMINAL DELETION MUTANT OF THE SAME PROTEIN IN AN
REMARK 900 AUTOINHIBITED STATE (ALDAMINE)
REMARK 900 RELATED ID: 2DGM   RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH IODIDE
DBREF  2DGL A    1   466  UNP    P69910   DCEB_ECOLI       1    466
DBREF  2DGL B    1   466  UNP    P69910   DCEB_ECOLI       1    466
DBREF  2DGL C    1   466  UNP    P69910   DCEB_ECOLI       1    466
DBREF  2DGL D    1   466  UNP    P69910   DCEB_ECOLI       1    466
DBREF  2DGL E    1   466  UNP    P69910   DCEB_ECOLI       1    466
DBREF  2DGL F    1   466  UNP    P69910   DCEB_ECOLI       1    466
SEQRES   1 A  466  MET ASP LYS LYS GLN VAL THR ASP LEU ARG SER GLU LEU
SEQRES   2 A  466  LEU ASP SER ARG PHE GLY ALA LYS SER ILE SER THR ILE
SEQRES   3 A  466  ALA GLU SER LYS ARG PHE PRO LEU HIS GLU MET ARG ASP
SEQRES   4 A  466  ASP VAL ALA PHE GLN ILE ILE ASN ASP GLU LEU TYR LEU
SEQRES   5 A  466  ASP GLY ASN ALA ARG GLN ASN LEU ALA THR PHE CYS GLN
SEQRES   6 A  466  THR TRP ASP ASP GLU ASN VAL HIS LYS LEU MET ASP LEU
SEQRES   7 A  466  SER ILE ASN LYS ASN TRP ILE ASP LYS GLU GLU TYR PRO
SEQRES   8 A  466  GLN SER ALA ALA ILE ASP LEU ARG CYS VAL ASN MET VAL
SEQRES   9 A  466  ALA ASP LEU TRP HIS ALA PRO ALA PRO LYS ASN GLY GLN
SEQRES  10 A  466  ALA VAL GLY THR ASN THR ILE GLY SER SER GLU ALA CYS
SEQRES  11 A  466  MET LEU GLY GLY MET ALA MET LYS TRP ARG TRP ARG LYS
SEQRES  12 A  466  ARG MET GLU ALA ALA GLY LYS PRO THR ASP LYS PRO ASN
SEQRES  13 A  466  LEU VAL CYS GLY PRO VAL GLN ILE CYS TRP HIS LYS PHE
SEQRES  14 A  466  ALA ARG TYR TRP ASP VAL GLU LEU ARG GLU ILE PRO MET
SEQRES  15 A  466  ARG PRO GLY GLN LEU PHE MET ASP PRO LYS ARG MET ILE
SEQRES  16 A  466  GLU ALA CYS ASP GLU ASN THR ILE GLY VAL VAL PRO THR
SEQRES  17 A  466  PHE GLY VAL THR TYR THR GLY ASN TYR GLU PHE PRO GLN
SEQRES  18 A  466  PRO LEU HIS ASP ALA LEU ASP LYS PHE GLN ALA ASP THR
SEQRES  19 A  466  GLY ILE ASP ILE ASP MET HIS ILE ASP ALA ALA SER GLY
SEQRES  20 A  466  GLY PHE LEU ALA PRO PHE VAL ALA PRO ASP ILE VAL TRP
SEQRES  21 A  466  ASP PHE ARG LEU PRO ARG VAL LYS SER ILE SER ALA SER
SEQRES  22 A  466  GLY HIS LYS PHE GLY LEU ALA PRO LEU GLY CYS GLY TRP
SEQRES  23 A  466  VAL ILE TRP ARG ASP GLU GLU ALA LEU PRO GLN GLU LEU
SEQRES  24 A  466  VAL PHE ASN VAL ASP TYR LEU GLY GLY GLN ILE GLY THR
SEQRES  25 A  466  PHE ALA ILE ASN PHE SER ARG PRO ALA GLY GLN VAL ILE
SEQRES  26 A  466  ALA GLN TYR TYR GLU PHE LEU ARG LEU GLY ARG GLU GLY
SEQRES  27 A  466  TYR THR LYS VAL GLN ASN ALA SER TYR GLN VAL ALA ALA
SEQRES  28 A  466  TYR LEU ALA ASP GLU ILE ALA LYS LEU GLY PRO TYR GLU
SEQRES  29 A  466  PHE ILE CYS THR GLY ARG PRO ASP GLU GLY ILE PRO ALA
SEQRES  30 A  466  VAL CYS PHE LYS LEU LYS ASP GLY GLU ASP PRO GLY TYR
SEQRES  31 A  466  THR LEU TYR ASP LEU SER GLU ARG LEU ARG LEU ARG GLY
SEQRES  32 A  466  TRP GLN VAL PRO ALA PHE THR LEU GLY GLY GLU ALA THR
SEQRES  33 A  466  ASP ILE VAL VAL MET ARG ILE MET CYS ARG ARG GLY PHE
SEQRES  34 A  466  GLU MET ASP PHE ALA GLU LEU LEU LEU GLU ASP TYR LYS
SEQRES  35 A  466  ALA SER LEU LYS TYR LEU SER ASP HIS PRO LYS LEU GLN
SEQRES  36 A  466  GLY ILE ALA GLN GLN ASN SER PHE LYS HIS THR
SEQRES   1 B  466  MET ASP LYS LYS GLN VAL THR ASP LEU ARG SER GLU LEU
SEQRES   2 B  466  LEU ASP SER ARG PHE GLY ALA LYS SER ILE SER THR ILE
SEQRES   3 B  466  ALA GLU SER LYS ARG PHE PRO LEU HIS GLU MET ARG ASP
SEQRES   4 B  466  ASP VAL ALA PHE GLN ILE ILE ASN ASP GLU LEU TYR LEU
SEQRES   5 B  466  ASP GLY ASN ALA ARG GLN ASN LEU ALA THR PHE CYS GLN
SEQRES   6 B  466  THR TRP ASP ASP GLU ASN VAL HIS LYS LEU MET ASP LEU
SEQRES   7 B  466  SER ILE ASN LYS ASN TRP ILE ASP LYS GLU GLU TYR PRO
SEQRES   8 B  466  GLN SER ALA ALA ILE ASP LEU ARG CYS VAL ASN MET VAL
SEQRES   9 B  466  ALA ASP LEU TRP HIS ALA PRO ALA PRO LYS ASN GLY GLN
SEQRES  10 B  466  ALA VAL GLY THR ASN THR ILE GLY SER SER GLU ALA CYS
SEQRES  11 B  466  MET LEU GLY GLY MET ALA MET LYS TRP ARG TRP ARG LYS
SEQRES  12 B  466  ARG MET GLU ALA ALA GLY LYS PRO THR ASP LYS PRO ASN
SEQRES  13 B  466  LEU VAL CYS GLY PRO VAL GLN ILE CYS TRP HIS LYS PHE
SEQRES  14 B  466  ALA ARG TYR TRP ASP VAL GLU LEU ARG GLU ILE PRO MET
SEQRES  15 B  466  ARG PRO GLY GLN LEU PHE MET ASP PRO LYS ARG MET ILE
SEQRES  16 B  466  GLU ALA CYS ASP GLU ASN THR ILE GLY VAL VAL PRO THR
SEQRES  17 B  466  PHE GLY VAL THR TYR THR GLY ASN TYR GLU PHE PRO GLN
SEQRES  18 B  466  PRO LEU HIS ASP ALA LEU ASP LYS PHE GLN ALA ASP THR
SEQRES  19 B  466  GLY ILE ASP ILE ASP MET HIS ILE ASP ALA ALA SER GLY
SEQRES  20 B  466  GLY PHE LEU ALA PRO PHE VAL ALA PRO ASP ILE VAL TRP
SEQRES  21 B  466  ASP PHE ARG LEU PRO ARG VAL LYS SER ILE SER ALA SER
SEQRES  22 B  466  GLY HIS LYS PHE GLY LEU ALA PRO LEU GLY CYS GLY TRP
SEQRES  23 B  466  VAL ILE TRP ARG ASP GLU GLU ALA LEU PRO GLN GLU LEU
SEQRES  24 B  466  VAL PHE ASN VAL ASP TYR LEU GLY GLY GLN ILE GLY THR
SEQRES  25 B  466  PHE ALA ILE ASN PHE SER ARG PRO ALA GLY GLN VAL ILE
SEQRES  26 B  466  ALA GLN TYR TYR GLU PHE LEU ARG LEU GLY ARG GLU GLY
SEQRES  27 B  466  TYR THR LYS VAL GLN ASN ALA SER TYR GLN VAL ALA ALA
SEQRES  28 B  466  TYR LEU ALA ASP GLU ILE ALA LYS LEU GLY PRO TYR GLU
SEQRES  29 B  466  PHE ILE CYS THR GLY ARG PRO ASP GLU GLY ILE PRO ALA
SEQRES  30 B  466  VAL CYS PHE LYS LEU LYS ASP GLY GLU ASP PRO GLY TYR
SEQRES  31 B  466  THR LEU TYR ASP LEU SER GLU ARG LEU ARG LEU ARG GLY
SEQRES  32 B  466  TRP GLN VAL PRO ALA PHE THR LEU GLY GLY GLU ALA THR
SEQRES  33 B  466  ASP ILE VAL VAL MET ARG ILE MET CYS ARG ARG GLY PHE
SEQRES  34 B  466  GLU MET ASP PHE ALA GLU LEU LEU LEU GLU ASP TYR LYS
SEQRES  35 B  466  ALA SER LEU LYS TYR LEU SER ASP HIS PRO LYS LEU GLN
SEQRES  36 B  466  GLY ILE ALA GLN GLN ASN SER PHE LYS HIS THR
SEQRES   1 C  466  MET ASP LYS LYS GLN VAL THR ASP LEU ARG SER GLU LEU
SEQRES   2 C  466  LEU ASP SER ARG PHE GLY ALA LYS SER ILE SER THR ILE
SEQRES   3 C  466  ALA GLU SER LYS ARG PHE PRO LEU HIS GLU MET ARG ASP
SEQRES   4 C  466  ASP VAL ALA PHE GLN ILE ILE ASN ASP GLU LEU TYR LEU
SEQRES   5 C  466  ASP GLY ASN ALA ARG GLN ASN LEU ALA THR PHE CYS GLN
SEQRES   6 C  466  THR TRP ASP ASP GLU ASN VAL HIS LYS LEU MET ASP LEU
SEQRES   7 C  466  SER ILE ASN LYS ASN TRP ILE ASP LYS GLU GLU TYR PRO
SEQRES   8 C  466  GLN SER ALA ALA ILE ASP LEU ARG CYS VAL ASN MET VAL
SEQRES   9 C  466  ALA ASP LEU TRP HIS ALA PRO ALA PRO LYS ASN GLY GLN
SEQRES  10 C  466  ALA VAL GLY THR ASN THR ILE GLY SER SER GLU ALA CYS
SEQRES  11 C  466  MET LEU GLY GLY MET ALA MET LYS TRP ARG TRP ARG LYS
SEQRES  12 C  466  ARG MET GLU ALA ALA GLY LYS PRO THR ASP LYS PRO ASN
SEQRES  13 C  466  LEU VAL CYS GLY PRO VAL GLN ILE CYS TRP HIS LYS PHE
SEQRES  14 C  466  ALA ARG TYR TRP ASP VAL GLU LEU ARG GLU ILE PRO MET
SEQRES  15 C  466  ARG PRO GLY GLN LEU PHE MET ASP PRO LYS ARG MET ILE
SEQRES  16 C  466  GLU ALA CYS ASP GLU ASN THR ILE GLY VAL VAL PRO THR
SEQRES  17 C  466  PHE GLY VAL THR TYR THR GLY ASN TYR GLU PHE PRO GLN
SEQRES  18 C  466  PRO LEU HIS ASP ALA LEU ASP LYS PHE GLN ALA ASP THR
SEQRES  19 C  466  GLY ILE ASP ILE ASP MET HIS ILE ASP ALA ALA SER GLY
SEQRES  20 C  466  GLY PHE LEU ALA PRO PHE VAL ALA PRO ASP ILE VAL TRP
SEQRES  21 C  466  ASP PHE ARG LEU PRO ARG VAL LYS SER ILE SER ALA SER
SEQRES  22 C  466  GLY HIS LYS PHE GLY LEU ALA PRO LEU GLY CYS GLY TRP
SEQRES  23 C  466  VAL ILE TRP ARG ASP GLU GLU ALA LEU PRO GLN GLU LEU
SEQRES  24 C  466  VAL PHE ASN VAL ASP TYR LEU GLY GLY GLN ILE GLY THR
SEQRES  25 C  466  PHE ALA ILE ASN PHE SER ARG PRO ALA GLY GLN VAL ILE
SEQRES  26 C  466  ALA GLN TYR TYR GLU PHE LEU ARG LEU GLY ARG GLU GLY
SEQRES  27 C  466  TYR THR LYS VAL GLN ASN ALA SER TYR GLN VAL ALA ALA
SEQRES  28 C  466  TYR LEU ALA ASP GLU ILE ALA LYS LEU GLY PRO TYR GLU
SEQRES  29 C  466  PHE ILE CYS THR GLY ARG PRO ASP GLU GLY ILE PRO ALA
SEQRES  30 C  466  VAL CYS PHE LYS LEU LYS ASP GLY GLU ASP PRO GLY TYR
SEQRES  31 C  466  THR LEU TYR ASP LEU SER GLU ARG LEU ARG LEU ARG GLY
SEQRES  32 C  466  TRP GLN VAL PRO ALA PHE THR LEU GLY GLY GLU ALA THR
SEQRES  33 C  466  ASP ILE VAL VAL MET ARG ILE MET CYS ARG ARG GLY PHE
SEQRES  34 C  466  GLU MET ASP PHE ALA GLU LEU LEU LEU GLU ASP TYR LYS
SEQRES  35 C  466  ALA SER LEU LYS TYR LEU SER ASP HIS PRO LYS LEU GLN
SEQRES  36 C  466  GLY ILE ALA GLN GLN ASN SER PHE LYS HIS THR
SEQRES   1 D  466  MET ASP LYS LYS GLN VAL THR ASP LEU ARG SER GLU LEU
SEQRES   2 D  466  LEU ASP SER ARG PHE GLY ALA LYS SER ILE SER THR ILE
SEQRES   3 D  466  ALA GLU SER LYS ARG PHE PRO LEU HIS GLU MET ARG ASP
SEQRES   4 D  466  ASP VAL ALA PHE GLN ILE ILE ASN ASP GLU LEU TYR LEU
SEQRES   5 D  466  ASP GLY ASN ALA ARG GLN ASN LEU ALA THR PHE CYS GLN
SEQRES   6 D  466  THR TRP ASP ASP GLU ASN VAL HIS LYS LEU MET ASP LEU
SEQRES   7 D  466  SER ILE ASN LYS ASN TRP ILE ASP LYS GLU GLU TYR PRO
SEQRES   8 D  466  GLN SER ALA ALA ILE ASP LEU ARG CYS VAL ASN MET VAL
SEQRES   9 D  466  ALA ASP LEU TRP HIS ALA PRO ALA PRO LYS ASN GLY GLN
SEQRES  10 D  466  ALA VAL GLY THR ASN THR ILE GLY SER SER GLU ALA CYS
SEQRES  11 D  466  MET LEU GLY GLY MET ALA MET LYS TRP ARG TRP ARG LYS
SEQRES  12 D  466  ARG MET GLU ALA ALA GLY LYS PRO THR ASP LYS PRO ASN
SEQRES  13 D  466  LEU VAL CYS GLY PRO VAL GLN ILE CYS TRP HIS LYS PHE
SEQRES  14 D  466  ALA ARG TYR TRP ASP VAL GLU LEU ARG GLU ILE PRO MET
SEQRES  15 D  466  ARG PRO GLY GLN LEU PHE MET ASP PRO LYS ARG MET ILE
SEQRES  16 D  466  GLU ALA CYS ASP GLU ASN THR ILE GLY VAL VAL PRO THR
SEQRES  17 D  466  PHE GLY VAL THR TYR THR GLY ASN TYR GLU PHE PRO GLN
SEQRES  18 D  466  PRO LEU HIS ASP ALA LEU ASP LYS PHE GLN ALA ASP THR
SEQRES  19 D  466  GLY ILE ASP ILE ASP MET HIS ILE ASP ALA ALA SER GLY
SEQRES  20 D  466  GLY PHE LEU ALA PRO PHE VAL ALA PRO ASP ILE VAL TRP
SEQRES  21 D  466  ASP PHE ARG LEU PRO ARG VAL LYS SER ILE SER ALA SER
SEQRES  22 D  466  GLY HIS LYS PHE GLY LEU ALA PRO LEU GLY CYS GLY TRP
SEQRES  23 D  466  VAL ILE TRP ARG ASP GLU GLU ALA LEU PRO GLN GLU LEU
SEQRES  24 D  466  VAL PHE ASN VAL ASP TYR LEU GLY GLY GLN ILE GLY THR
SEQRES  25 D  466  PHE ALA ILE ASN PHE SER ARG PRO ALA GLY GLN VAL ILE
SEQRES  26 D  466  ALA GLN TYR TYR GLU PHE LEU ARG LEU GLY ARG GLU GLY
SEQRES  27 D  466  TYR THR LYS VAL GLN ASN ALA SER TYR GLN VAL ALA ALA
SEQRES  28 D  466  TYR LEU ALA ASP GLU ILE ALA LYS LEU GLY PRO TYR GLU
SEQRES  29 D  466  PHE ILE CYS THR GLY ARG PRO ASP GLU GLY ILE PRO ALA
SEQRES  30 D  466  VAL CYS PHE LYS LEU LYS ASP GLY GLU ASP PRO GLY TYR
SEQRES  31 D  466  THR LEU TYR ASP LEU SER GLU ARG LEU ARG LEU ARG GLY
SEQRES  32 D  466  TRP GLN VAL PRO ALA PHE THR LEU GLY GLY GLU ALA THR
SEQRES  33 D  466  ASP ILE VAL VAL MET ARG ILE MET CYS ARG ARG GLY PHE
SEQRES  34 D  466  GLU MET ASP PHE ALA GLU LEU LEU LEU GLU ASP TYR LYS
SEQRES  35 D  466  ALA SER LEU LYS TYR LEU SER ASP HIS PRO LYS LEU GLN
SEQRES  36 D  466  GLY ILE ALA GLN GLN ASN SER PHE LYS HIS THR
SEQRES   1 E  466  MET ASP LYS LYS GLN VAL THR ASP LEU ARG SER GLU LEU
SEQRES   2 E  466  LEU ASP SER ARG PHE GLY ALA LYS SER ILE SER THR ILE
SEQRES   3 E  466  ALA GLU SER LYS ARG PHE PRO LEU HIS GLU MET ARG ASP
SEQRES   4 E  466  ASP VAL ALA PHE GLN ILE ILE ASN ASP GLU LEU TYR LEU
SEQRES   5 E  466  ASP GLY ASN ALA ARG GLN ASN LEU ALA THR PHE CYS GLN
SEQRES   6 E  466  THR TRP ASP ASP GLU ASN VAL HIS LYS LEU MET ASP LEU
SEQRES   7 E  466  SER ILE ASN LYS ASN TRP ILE ASP LYS GLU GLU TYR PRO
SEQRES   8 E  466  GLN SER ALA ALA ILE ASP LEU ARG CYS VAL ASN MET VAL
SEQRES   9 E  466  ALA ASP LEU TRP HIS ALA PRO ALA PRO LYS ASN GLY GLN
SEQRES  10 E  466  ALA VAL GLY THR ASN THR ILE GLY SER SER GLU ALA CYS
SEQRES  11 E  466  MET LEU GLY GLY MET ALA MET LYS TRP ARG TRP ARG LYS
SEQRES  12 E  466  ARG MET GLU ALA ALA GLY LYS PRO THR ASP LYS PRO ASN
SEQRES  13 E  466  LEU VAL CYS GLY PRO VAL GLN ILE CYS TRP HIS LYS PHE
SEQRES  14 E  466  ALA ARG TYR TRP ASP VAL GLU LEU ARG GLU ILE PRO MET
SEQRES  15 E  466  ARG PRO GLY GLN LEU PHE MET ASP PRO LYS ARG MET ILE
SEQRES  16 E  466  GLU ALA CYS ASP GLU ASN THR ILE GLY VAL VAL PRO THR
SEQRES  17 E  466  PHE GLY VAL THR TYR THR GLY ASN TYR GLU PHE PRO GLN
SEQRES  18 E  466  PRO LEU HIS ASP ALA LEU ASP LYS PHE GLN ALA ASP THR
SEQRES  19 E  466  GLY ILE ASP ILE ASP MET HIS ILE ASP ALA ALA SER GLY
SEQRES  20 E  466  GLY PHE LEU ALA PRO PHE VAL ALA PRO ASP ILE VAL TRP
SEQRES  21 E  466  ASP PHE ARG LEU PRO ARG VAL LYS SER ILE SER ALA SER
SEQRES  22 E  466  GLY HIS LYS PHE GLY LEU ALA PRO LEU GLY CYS GLY TRP
SEQRES  23 E  466  VAL ILE TRP ARG ASP GLU GLU ALA LEU PRO GLN GLU LEU
SEQRES  24 E  466  VAL PHE ASN VAL ASP TYR LEU GLY GLY GLN ILE GLY THR
SEQRES  25 E  466  PHE ALA ILE ASN PHE SER ARG PRO ALA GLY GLN VAL ILE
SEQRES  26 E  466  ALA GLN TYR TYR GLU PHE LEU ARG LEU GLY ARG GLU GLY
SEQRES  27 E  466  TYR THR LYS VAL GLN ASN ALA SER TYR GLN VAL ALA ALA
SEQRES  28 E  466  TYR LEU ALA ASP GLU ILE ALA LYS LEU GLY PRO TYR GLU
SEQRES  29 E  466  PHE ILE CYS THR GLY ARG PRO ASP GLU GLY ILE PRO ALA
SEQRES  30 E  466  VAL CYS PHE LYS LEU LYS ASP GLY GLU ASP PRO GLY TYR
SEQRES  31 E  466  THR LEU TYR ASP LEU SER GLU ARG LEU ARG LEU ARG GLY
SEQRES  32 E  466  TRP GLN VAL PRO ALA PHE THR LEU GLY GLY GLU ALA THR
SEQRES  33 E  466  ASP ILE VAL VAL MET ARG ILE MET CYS ARG ARG GLY PHE
SEQRES  34 E  466  GLU MET ASP PHE ALA GLU LEU LEU LEU GLU ASP TYR LYS
SEQRES  35 E  466  ALA SER LEU LYS TYR LEU SER ASP HIS PRO LYS LEU GLN
SEQRES  36 E  466  GLY ILE ALA GLN GLN ASN SER PHE LYS HIS THR
SEQRES   1 F  466  MET ASP LYS LYS GLN VAL THR ASP LEU ARG SER GLU LEU
SEQRES   2 F  466  LEU ASP SER ARG PHE GLY ALA LYS SER ILE SER THR ILE
SEQRES   3 F  466  ALA GLU SER LYS ARG PHE PRO LEU HIS GLU MET ARG ASP
SEQRES   4 F  466  ASP VAL ALA PHE GLN ILE ILE ASN ASP GLU LEU TYR LEU
SEQRES   5 F  466  ASP GLY ASN ALA ARG GLN ASN LEU ALA THR PHE CYS GLN
SEQRES   6 F  466  THR TRP ASP ASP GLU ASN VAL HIS LYS LEU MET ASP LEU
SEQRES   7 F  466  SER ILE ASN LYS ASN TRP ILE ASP LYS GLU GLU TYR PRO
SEQRES   8 F  466  GLN SER ALA ALA ILE ASP LEU ARG CYS VAL ASN MET VAL
SEQRES   9 F  466  ALA ASP LEU TRP HIS ALA PRO ALA PRO LYS ASN GLY GLN
SEQRES  10 F  466  ALA VAL GLY THR ASN THR ILE GLY SER SER GLU ALA CYS
SEQRES  11 F  466  MET LEU GLY GLY MET ALA MET LYS TRP ARG TRP ARG LYS
SEQRES  12 F  466  ARG MET GLU ALA ALA GLY LYS PRO THR ASP LYS PRO ASN
SEQRES  13 F  466  LEU VAL CYS GLY PRO VAL GLN ILE CYS TRP HIS LYS PHE
SEQRES  14 F  466  ALA ARG TYR TRP ASP VAL GLU LEU ARG GLU ILE PRO MET
SEQRES  15 F  466  ARG PRO GLY GLN LEU PHE MET ASP PRO LYS ARG MET ILE
SEQRES  16 F  466  GLU ALA CYS ASP GLU ASN THR ILE GLY VAL VAL PRO THR
SEQRES  17 F  466  PHE GLY VAL THR TYR THR GLY ASN TYR GLU PHE PRO GLN
SEQRES  18 F  466  PRO LEU HIS ASP ALA LEU ASP LYS PHE GLN ALA ASP THR
SEQRES  19 F  466  GLY ILE ASP ILE ASP MET HIS ILE ASP ALA ALA SER GLY
SEQRES  20 F  466  GLY PHE LEU ALA PRO PHE VAL ALA PRO ASP ILE VAL TRP
SEQRES  21 F  466  ASP PHE ARG LEU PRO ARG VAL LYS SER ILE SER ALA SER
SEQRES  22 F  466  GLY HIS LYS PHE GLY LEU ALA PRO LEU GLY CYS GLY TRP
SEQRES  23 F  466  VAL ILE TRP ARG ASP GLU GLU ALA LEU PRO GLN GLU LEU
SEQRES  24 F  466  VAL PHE ASN VAL ASP TYR LEU GLY GLY GLN ILE GLY THR
SEQRES  25 F  466  PHE ALA ILE ASN PHE SER ARG PRO ALA GLY GLN VAL ILE
SEQRES  26 F  466  ALA GLN TYR TYR GLU PHE LEU ARG LEU GLY ARG GLU GLY
SEQRES  27 F  466  TYR THR LYS VAL GLN ASN ALA SER TYR GLN VAL ALA ALA
SEQRES  28 F  466  TYR LEU ALA ASP GLU ILE ALA LYS LEU GLY PRO TYR GLU
SEQRES  29 F  466  PHE ILE CYS THR GLY ARG PRO ASP GLU GLY ILE PRO ALA
SEQRES  30 F  466  VAL CYS PHE LYS LEU LYS ASP GLY GLU ASP PRO GLY TYR
SEQRES  31 F  466  THR LEU TYR ASP LEU SER GLU ARG LEU ARG LEU ARG GLY
SEQRES  32 F  466  TRP GLN VAL PRO ALA PHE THR LEU GLY GLY GLU ALA THR
SEQRES  33 F  466  ASP ILE VAL VAL MET ARG ILE MET CYS ARG ARG GLY PHE
SEQRES  34 F  466  GLU MET ASP PHE ALA GLU LEU LEU LEU GLU ASP TYR LYS
SEQRES  35 F  466  ALA SER LEU LYS TYR LEU SER ASP HIS PRO LYS LEU GLN
SEQRES  36 F  466  GLY ILE ALA GLN GLN ASN SER PHE LYS HIS THR
HET     BR  A 467       1
HET     BR  F 467       1
HET     BR  A 468       1
HET     BR  B 467       1
HET     BR  C 467       1
HET     BR  B 468       1
HET     BR  B 469       1
HET     BR  B 470       1
HET     BR  C 468       1
HET     BR  D 467       1
HET     BR  E 467       1
HET     BR  D 468       1
HET     BR  E 468       1
HET     BR  C 469       1
HET     BR  E 469       1
HET     BR  F 468       1
HET     BR  A 469       1
HET     BR  F 469       1
HET     BR  A 470       1
HET     BR  B 471       1
HET     BR  C 470       1
HET     BR  D 469       1
HET     BR  E 470       1
HET     BR  F 470       1
HET    PLP  A 500      15
HET    PLP  B 500      15
HET    PLP  C 501      15
HET    PLP  D 501      15
HET    PLP  E 502      15
HET    PLP  F 502      15
HET    ACY  E 518       4
HET    ACY  F 528       4
HET    ACY  C 538       4
HET    ACY  C 548       4
HET    ACY  B 558       4
HET    ACY  A 568       4
HETNAM      BR BROMIDE ION
HETNAM     PLP PYRIDOXAL-5'-PHOSPHATE
HETNAM     ACY ACETIC ACID
HETSYN     PLP VITAMIN B6 PHOSPHATE
FORMUL   7   BR    24(BR 1-)
FORMUL  31  PLP    6(C8 H10 N O6 P)
FORMUL  37  ACY    6(C2 H4 O2)
FORMUL  43  HOH   *134(H2 O)
HELIX    1   1 LYS A    3  ASP A   15  1                                  13
HELIX    2   2 ALA A   20  SER A   24  5                                   5
HELIX    3   3 ARG A   38  LEU A   50  1                                  13
HELIX    4   4 TYR A   51  GLY A   54  5                                   4
HELIX    5   5 ASN A   55  ASN A   59  5                                   5
HELIX    6   6 ASP A   69  SER A   79  1                                  11
HELIX    7   7 TYR A   90  TRP A  108  1                                  19
HELIX    8   8 GLY A  125  ALA A  148  1                                  24
HELIX    9   9 GLN A  163  TRP A  173  1                                  11
HELIX   10  10 ASP A  190  GLU A  196  1                                   7
HELIX   11  11 PHE A  219  GLY A  235  1                                  17
HELIX   12  12 SER A  246  PHE A  249  5                                   4
HELIX   13  13 LEU A  250  ALA A  255  1                                   6
HELIX   14  14 PRO A  296  VAL A  300  5                                   5
HELIX   15  15 ALA A  321  LYS A  359  1                                  39
HELIX   16  16 THR A  391  LEU A  401  1                                  11
HELIX   17  17 GLY A  412  THR A  416  5                                   5
HELIX   18  18 GLU A  430  HIS A  451  1                                  22
HELIX   19  19 LYS B    3  ASP B   15  1                                  13
HELIX   20  20 ARG B   38  LEU B   50  1                                  13
HELIX   21  21 TYR B   51  GLY B   54  5                                   4
HELIX   22  22 ASN B   55  ASN B   59  5                                   5
HELIX   23  23 ASP B   69  SER B   79  1                                  11
HELIX   24  24 TYR B   90  TRP B  108  1                                  19
HELIX   25  25 GLY B  125  ALA B  148  1                                  24
HELIX   26  26 GLN B  163  TRP B  173  1                                  11
HELIX   27  27 ASP B  190  GLU B  196  1                                   7
HELIX   28  28 PHE B  219  GLY B  235  1                                  17
HELIX   29  29 SER B  246  PHE B  249  5                                   4
HELIX   30  30 LEU B  250  ALA B  255  1                                   6
HELIX   31  31 PRO B  296  VAL B  300  5                                   5
HELIX   32  32 ALA B  321  LYS B  359  1                                  39
HELIX   33  33 THR B  391  LEU B  401  1                                  11
HELIX   34  34 GLY B  412  THR B  416  5                                   5
HELIX   35  35 GLU B  430  HIS B  451  1                                  22
HELIX   36  36 LYS C    4  ASP C   15  1                                  12
HELIX   37  37 ALA C   20  SER C   24  5                                   5
HELIX   38  38 ARG C   38  LEU C   50  1                                  13
HELIX   39  39 TYR C   51  GLY C   54  5                                   4
HELIX   40  40 ASN C   55  ASN C   59  5                                   5
HELIX   41  41 ASP C   69  SER C   79  1                                  11
HELIX   42  42 TYR C   90  TRP C  108  1                                  19
HELIX   43  43 GLY C  125  ALA C  148  1                                  24
HELIX   44  44 GLN C  163  TRP C  173  1                                  11
HELIX   45  45 ASP C  190  GLU C  196  1                                   7
HELIX   46  46 PHE C  219  GLY C  235  1                                  17
HELIX   47  47 SER C  246  PHE C  249  5                                   4
HELIX   48  48 LEU C  250  ALA C  255  1                                   6
HELIX   49  49 PRO C  296  VAL C  300  5                                   5
HELIX   50  50 ALA C  321  LYS C  359  1                                  39
HELIX   51  51 THR C  391  LEU C  401  1                                  11
HELIX   52  52 GLY C  412  THR C  416  5                                   5
HELIX   53  53 GLU C  430  HIS C  451  1                                  22
HELIX   54  54 LYS D    4  ASP D   15  1                                  12
HELIX   55  55 ARG D   38  LEU D   50  1                                  13
HELIX   56  56 TYR D   51  GLY D   54  5                                   4
HELIX   57  57 ASN D   55  ASN D   59  5                                   5
HELIX   58  58 ASP D   69  SER D   79  1                                  11
HELIX   59  59 TYR D   90  TRP D  108  1                                  19
HELIX   60  60 GLY D  125  ALA D  148  1                                  24
HELIX   61  61 GLN D  163  TRP D  173  1                                  11
HELIX   62  62 ASP D  190  GLU D  196  1                                   7
HELIX   63  63 PHE D  219  GLY D  235  1                                  17
HELIX   64  64 SER D  246  PHE D  249  5                                   4
HELIX   65  65 LEU D  250  ALA D  255  1                                   6
HELIX   66  66 PRO D  296  VAL D  300  5                                   5
HELIX   67  67 ALA D  321  LYS D  359  1                                  39
HELIX   68  68 THR D  391  LEU D  401  1                                  11
HELIX   69  69 GLY D  412  THR D  416  5                                   5
HELIX   70  70 GLU D  430  HIS D  451  1                                  22
HELIX   71  71 LYS E    3  ASP E   15  1                                  13
HELIX   72  72 ALA E   20  SER E   24  5                                   5
HELIX   73  73 ARG E   38  LEU E   50  1                                  13
HELIX   74  74 TYR E   51  GLY E   54  5                                   4
HELIX   75  75 ASN E   55  ASN E   59  5                                   5
HELIX   76  76 ASP E   69  SER E   79  1                                  11
HELIX   77  77 TYR E   90  TRP E  108  1                                  19
HELIX   78  78 GLY E  125  ALA E  148  1                                  24
HELIX   79  79 GLN E  163  TRP E  173  1                                  11
HELIX   80  80 ASP E  190  GLU E  196  1                                   7
HELIX   81  81 PHE E  219  GLY E  235  1                                  17
HELIX   82  82 SER E  246  PHE E  249  5                                   4
HELIX   83  83 LEU E  250  ALA E  255  1                                   6
HELIX   84  84 PRO E  296  VAL E  300  5                                   5
HELIX   85  85 ALA E  321  LYS E  359  1                                  39
HELIX   86  86 THR E  391  LEU E  401  1                                  11
HELIX   87  87 GLY E  412  THR E  416  5                                   5
HELIX   88  88 GLU E  430  HIS E  451  1                                  22
HELIX   89  89 LYS F    3  ASP F   15  1                                  13
HELIX   90  90 ARG F   38  LEU F   50  1                                  13
HELIX   91  91 TYR F   51  GLY F   54  5                                   4
HELIX   92  92 ASN F   55  ASN F   59  5                                   5
HELIX   93  93 ASP F   69  SER F   79  1                                  11
HELIX   94  94 TYR F   90  TRP F  108  1                                  19
HELIX   95  95 GLY F  125  ALA F  148  1                                  24
HELIX   96  96 GLN F  163  TRP F  173  1                                  11
HELIX   97  97 ASP F  190  GLU F  196  1                                   7
HELIX   98  98 PHE F  219  GLY F  235  1                                  17
HELIX   99  99 SER F  246  PHE F  249  5                                   4
HELIX  100 100 LEU F  250  ALA F  255  1                                   6
HELIX  101 101 PRO F  296  VAL F  300  5                                   5
HELIX  102 102 ALA F  321  LYS F  359  1                                  39
HELIX  103 103 THR F  391  LEU F  401  1                                  11
HELIX  104 104 GLY F  412  THR F  416  5                                   5
HELIX  105 105 GLU F  430  HIS F  451  1                                  22
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  MET A 240   O  LYS A 268
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  GLU A 176
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  TYR A 305  0
SHEET    2   C 2 GLY A 308  THR A 312 -1  O  ILE A 310   N  VAL A 303
SHEET    1   D 4 TYR A 363  THR A 368  0
SHEET    2   D 4 ALA A 377  LEU A 382 -1  O  LYS A 381   N  GLU A 364
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  ALA B 272   O  TRP B 286
SHEET    4   E 4 MET B 240  ASP B 243  1  N  MET B 240   O  LYS B 268
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  GLU B 176
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  ASP B 304  0
SHEET    2   G 2 GLN B 309  THR B 312 -1  O  ILE B 310   N  VAL B 303
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  ILE C 270   O  ILE C 288
SHEET    4   I 4 MET C 240  ASP C 243  1  N  MET C 240   O  LYS C 268
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  GLU C 176
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  TYR C 305  0
SHEET    2   K 2 GLY C 308  THR C 312 -1  O  ILE C 310   N  VAL C 303
SHEET    1   L 4 TYR C 363  THR C 368  0
SHEET    2   L 4 ALA C 377  LEU C 382 -1  O  LYS C 381   N  GLU C 364
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  GLY D 285   N  THR D 123
SHEET    3   M 4 VAL D 267  SER D 273 -1  N  ALA D 272   O  TRP D 286
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  GLU D 176
SHEET    3   N 3 THR D 202  VAL D 206  1  O  ILE D 203   N  ASN D 156
SHEET    1   O 2 ASN D 302  TYR D 305  0
SHEET    2   O 2 GLY D 308  GLY D 311 -1  O  GLY D 308   N  TYR D 305
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  MET D 421   N  PHE D 380
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  GLY E 285   N  THR E 123
SHEET    3   Q 4 VAL E 267  SER E 273 -1  N  ILE E 270   O  ILE E 288
SHEET    4   Q 4 MET E 240  ASP E 243  1  N  MET E 240   O  LYS E 268
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  GLU E 176
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  TYR E 305  0
SHEET    2   S 2 GLY E 308  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  LYS E 381   N  GLU E 364
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  MET F 240   O  LYS F 268
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  GLU F 176
SHEET    3   V 3 THR F 202  VAL F 206  1  O  ILE F 203   N  ASN F 156
SHEET    1   W 2 PHE F 301  TYR F 305  0
SHEET    2   W 2 GLY F 308  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  LYS F 381   N  GLU F 364
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 A 500                 NZ  LYS A 276     1555   1555  1.32
LINK         C4A PLP B 500                 NZ  LYS B 276     1555   1555  1.32
LINK         C4A PLP C 501                 NZ  LYS C 276     1555   1555  1.33
LINK         C4A PLP D 501                 NZ  LYS D 276     1555   1555  1.32
LINK         C4A PLP E 502                 NZ  LYS E 276     1555   1555  1.32
LINK         C4A PLP F 502                 NZ  LYS F 276     1555   1555  1.33
SITE     1 AC1  2 SER A  16  ARG F 427
SITE     1 AC2  3 ASN E  81  ASP F  68  HIS F  73
SITE     1 AC3  1 ARG A  17
SITE     1 AC4  2 SER B  16  ARG C 427
SITE     1 AC5  3 TRP C  67  ASP C  68  HIS C  73
SITE     1 AC6  1 ARG B  17
SITE     1 AC7  2 ARG B 427  SER C  16
SITE     1 AC8  3 ASN A  81  ASP B  68  HIS B  73
SITE     1 AC9  1 ARG C  17
SITE     1 BC1  2 SER D  16  ARG E 427
SITE     1 BC2  3 ASP E  68  HIS E  73  ASN F  81
SITE     1 BC3  1 ARG D  17
SITE     1 BC4  2 ARG D 427  SER E  16
SITE     1 BC5  3 ASN C  81  ASP D  68  HIS D  73
SITE     1 BC6  1 ARG E  17
SITE     1 BC7  2 ARG A 427  SER F  16
SITE     1 BC8  3 ASP A  68  HIS A  73  ASN B  81
SITE     1 BC9  1 ARG F  17
SITE     1 CC1  1 ILE A 418
SITE     1 CC2  2 LYS B 381  ILE B 418
SITE     1 CC3  2 LYS C 381  ILE C 418
SITE     1 CC4  1 LYS D 381
SITE     1 CC5  1 ILE E 418
SITE     1 CC6 12 GLY A 125  SER A 126  SER A 127  GLN A 163
SITE     2 CC6 12 THR A 212  ASP A 243  ALA A 245  SER A 273
SITE     3 CC6 12 HIS A 275  LYS A 276  PHE B 317  SER B 318
SITE     1 CC7 13 PHE A 317  SER A 318  GLY B 125  SER B 126
SITE     2 CC7 13 SER B 127  GLN B 163  THR B 212  ASP B 243
SITE     3 CC7 13 ALA B 245  SER B 273  HIS B 275  LYS B 276
SITE     4 CC7 13 HOH B 567
SITE     1 CC8 12 GLY C 125  SER C 126  SER C 127  GLN C 163
SITE     2 CC8 12 THR C 212  ASP C 243  ALA C 245  SER C 273
SITE     3 CC8 12 HIS C 275  LYS C 276  PHE D 317  SER D 318
SITE     1 CC9 12 PHE C 317  SER C 318  SER D 126  SER D 127
SITE     2 CC9 12 GLN D 163  CYS D 165  THR D 212  ASP D 243
SITE     3 CC9 12 ALA D 245  SER D 273  HIS D 275  LYS D 276
SITE     1 DC1 13 GLY E 125  SER E 126  SER E 127  GLN E 163
SITE     2 DC1 13 CYS E 165  THR E 212  ASP E 243  ALA E 245
SITE     3 DC1 13 SER E 273  HIS E 275  LYS E 276  PHE F 317
SITE     4 DC1 13 SER F 318
SITE     1 DC2 14 PHE E 317  SER E 318  HOH E 529  GLY F 125
SITE     2 DC2 14 SER F 126  SER F 127  GLN F 163  THR F 208
SITE     3 DC2 14 THR F 212  ASP F 243  ALA F 245  SER F 273
SITE     4 DC2 14 HIS F 275  LYS F 276
SITE     1 DC3  3 THR E  62  PHE E  63  ASP F  86
SITE     1 DC4  5 ASN E  83  ASP E  86  SER E 318  THR F  62
SITE     2 DC4  5 PHE F  63
SITE     1 DC5  4 THR C  62  PHE C  63  ASP D  86  SER D 318
SITE     1 DC6  7 ASN C  83  ASP C  86  PHE C 317  SER C 318
SITE     2 DC6  7 THR D  62  PHE D  63  CYS D  64
SITE     1 DC7  5 THR A  62  PHE A  63  CYS A  64  ASN B  83
SITE     2 DC7  5 ASP B  86
SITE     1 DC8  5 ASN A  83  ASP A  86  SER A 318  THR B  62
SITE     2 DC8  5 PHE B  63
CRYST1  297.051  297.051  233.731  90.00  90.00 120.00 P 63 2 2     72
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      0.003366  0.001944  0.000000        0.00000
SCALE2      0.000000  0.003887  0.000000        0.00000
SCALE3      0.000000  0.000000  0.004278        0.00000
      
PROCHECK
Go to PROCHECK summary
 References