spacer
spacer

PDBsum entry 2qcu

Go to PDB code: 
Top Page protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
2qcu
Jmol
Contents
Protein chains
499 a.a.
Ligands
FAD ×2
BOG ×6
TAM ×3
SO4 ×4
EDO ×30
IMD ×2
PO4 ×2
Waters ×476
HEADER    OXIDOREDUCTASE                          19-JUN-07   2QCU
TITLE     CRYSTAL STRUCTURE OF GLYCEROL-3-PHOSPHATE DEHYDROGENASE
TITLE    2 FROM ESCHERICHIA COLI
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: AEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE;
COMPND   3 CHAIN: A, B;
COMPND   4 EC: 1.1.99.5;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE   3 ORGANISM_TAXID: 562;
SOURCE   4 GENE: GLPD, GLYD;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    GLYCEROL-3-PHOSHATE DEHYDROGENASE, OXIDOREDUCTASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.I.YEH,U.CHINTE,S.DU
REVDAT   2   24-FEB-09 2QCU    1       VERSN
REVDAT   1   15-APR-08 2QCU    0
JRNL        AUTH   J.I.YEH,U.CHINTE,S.DU
JRNL        TITL   STRUCTURE OF GLYCEROL-3-PHOSPHATE DEHYDROGENASE,
JRNL        TITL 2 AN ESSENTIAL MONOTOPIC MEMBRANE ENZYME INVOLVED IN
JRNL        TITL 3 RESPIRATION AND METABOLISM.
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 105  3280 2008
JRNL        REFN                   ISSN 0027-8424
JRNL        PMID   18296637
JRNL        DOI    10.1073/PNAS.0712331105
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    1.75 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0005
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5
REMARK   3   NUMBER OF REFLECTIONS             : 118338
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 + TEST SET) : 0.206
REMARK   3   R VALUE            (WORKING SET) : 0.204
REMARK   3   FREE R VALUE                     : 0.240
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 6272
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.75
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.79
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 8482
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.04
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2620
REMARK   3   BIN FREE R VALUE SET COUNT          : 420
REMARK   3   BIN FREE R VALUE                    : 0.3360
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 7997
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 419
REMARK   3   SOLVENT ATOMS            : 476
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.65
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.01000
REMARK   3    B22 (A**2) : 0.02000
REMARK   3    B33 (A**2) : -0.03000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.119
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.117
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.076
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.320
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8582 ; 0.011 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11552 ; 1.740 ; 1.995
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   998 ;14.085 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   393 ;32.356 ;22.774
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1395 ;18.183 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    78 ;17.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1233 ; 0.251 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6340 ; 0.019 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  4272 ; 0.253 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  5733 ; 0.326 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   552 ; 0.167 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    53 ; 0.288 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    11 ; 0.250 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  5079 ; 2.108 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7970 ; 3.034 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4042 ; 4.344 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3582 ; 6.223 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 1
REMARK   3     CHAIN NAMES                    : A B
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     A      5       A     499      2
REMARK   3           1     B      5       B     499      2
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   1    A    (A):   1980 ;  0.08 ;  0.05
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1982 ;  0.56 ;  0.50
REMARK   3   TIGHT THERMAL      1    A (A**2):   1980 ;  0.28 ;  0.50
REMARK   3   MEDIUM THERMAL     1    A (A**2):   1982 ;  1.19 ;  2.00
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 2QCU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUN-07.
REMARK 100 THE RCSB ID CODE IS RCSB043437.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL; NULL
REMARK 200  TEMPERATURE           (KELVIN) : 100; 100
REMARK 200  PH                             : 8.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y
REMARK 200  RADIATION SOURCE               : SLS; APS
REMARK 200  BEAMLINE                       : X10SA; 22-ID
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9803; 0.97928, 0.97947,
REMARK 200                                   0.97181
REMARK 200  MONOCHROMATOR                  : NULL; NULL
REMARK 200  OPTICS                         : NULL; NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD; CCD
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD;
REMARK 200                                   MARMOSAIC 300 MM CCD
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200  DATA SCALING SOFTWARE          : HKL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 136571
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4
REMARK 200  DATA REDUNDANCY                : 9.000
REMARK 200  R MERGE                    (I) : 0.06100
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 11.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.76
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.1
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.71200
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE, PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 55.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M DI-AMMONIUM HYDROGEN
REMARK 280  PHOSPHATE, 0.1 M TRIS-HCL PH 8.5, 12 % W/V PEG MME 550, VAPOR
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X,Y,-Z
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       56.89550
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       57.04850
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       96.40050
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       56.89550
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       57.04850
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       96.40050
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       56.89550
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       57.04850
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       96.40050
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       56.89550
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       57.04850
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       96.40050
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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     GLU A     2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480   M RES C SSEQI ATOMS
REMARK 480     LEU A   37   C
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    HOH B  1036     O    HOH B  1037              2.19
REMARK 500
REMARK 500 REMARK: NULL
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  35      -94.41   -125.12
REMARK 500    ALA A  40     -116.15   -117.23
REMARK 500    ALA A  78       58.80   -144.50
REMARK 500    LYS A 113       16.52     99.57
REMARK 500    ARG A 114      141.27    -23.80
REMARK 500    SER A 116      -17.58   -152.97
REMARK 500    SER A 120      131.50    124.70
REMARK 500    ASP A 143     -157.02   -149.76
REMARK 500    ALA A 205       51.91   -110.94
REMARK 500    LYS A 253       -1.83     81.38
REMARK 500    ASP A 263      -14.21     64.60
REMARK 500    LEU A 319      116.81     43.05
REMARK 500    TRP A 380      -22.45   -153.82
REMARK 500    ILE A 391     -140.43   -109.33
REMARK 500    GLU A 392       58.76   -174.17
REMARK 500    ASP A 396       17.43    132.25
REMARK 500    THR A 420      -65.62   -109.60
REMARK 500    TRP A 459       18.09     58.76
REMARK 500    LEU A 497      -47.60   -161.49
REMARK 500    LEU A 499      -83.25   -115.06
REMARK 500    GLU B   2       -0.53   -163.83
REMARK 500    GLN B  35      -94.21   -126.08
REMARK 500    ALA B  40     -121.82   -114.86
REMARK 500    HIS B  50      -61.73   -109.96
REMARK 500    ALA B  78       58.39   -147.71
REMARK 500    LYS B 113      -59.37    128.79
REMARK 500    ARG B 114      124.97     54.03
REMARK 500    SER B 116      -18.91   -149.60
REMARK 500    ASP B 143     -159.89   -151.31
REMARK 500    ALA B 205       51.44   -107.13
REMARK 500    ILE B 226      109.74     55.70
REMARK 500    LYS B 253       -1.46     77.29
REMARK 500    ASP B 263      -12.43     64.07
REMARK 500    THR B 270     -147.05   -126.46
REMARK 500    LEU B 319      119.78     37.56
REMARK 500    ILE B 376     -109.04    -52.26
REMARK 500    ALA B 379      157.55    -34.24
REMARK 500    TRP B 380      -21.13   -158.31
REMARK 500    ILE B 391     -101.12   -122.15
REMARK 500    GLU B 392       86.60    136.12
REMARK 500    ASP B 394      -66.68    114.62
REMARK 500    LEU B 497      -70.35   -161.87
REMARK 500    ALA B 500      161.11    172.44
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 ARG A  496     LEU A  497                  116.49
REMARK 500 LEU A  497     SER A  498                  146.84
REMARK 500 SER A  498     LEU A  499                 -124.81
REMARK 500 LEU A  499     ALA A  500                 -132.25
REMARK 500 ARG B  496     LEU B  497                  133.65
REMARK 500 LEU B  497     SER B  498                  146.20
REMARK 500 SER B  498     LEU B  499                 -139.55
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 BOG A 700
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 701
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 801
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG B 700
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG B 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 802
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 803
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 801
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 802
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 804
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 803
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 600
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 600
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAM A 805
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 806
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 807
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 808
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 809
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 810
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 811
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 812
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 813
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 814
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 815
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 816
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 817
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 818
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 819
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 820
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 821
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 822
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAM A 823
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 804
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 805
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 806
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 807
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 808
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 809
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAM B 810
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 811
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 812
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 813
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 814
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 816
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 817
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 819
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 820
DBREF  2QCU A    1   501  UNP    P13035   GLPD_ECOLI       1    501
DBREF  2QCU B    1   501  UNP    P13035   GLPD_ECOLI       1    501
SEQRES   1 A  501  MET GLU THR LYS ASP LEU ILE VAL ILE GLY GLY GLY ILE
SEQRES   2 A  501  ASN GLY ALA GLY ILE ALA ALA ASP ALA ALA GLY ARG GLY
SEQRES   3 A  501  LEU SER VAL LEU MET LEU GLU ALA GLN ASP LEU ALA CYS
SEQRES   4 A  501  ALA THR SER SER ALA SER SER LYS LEU ILE HIS GLY GLY
SEQRES   5 A  501  LEU ARG TYR LEU GLU HIS TYR GLU PHE ARG LEU VAL SER
SEQRES   6 A  501  GLU ALA LEU ALA GLU ARG GLU VAL LEU LEU LYS MET ALA
SEQRES   7 A  501  PRO HIS ILE ALA PHE PRO MET ARG PHE ARG LEU PRO HIS
SEQRES   8 A  501  ARG PRO HIS LEU ARG PRO ALA TRP MET ILE ARG ILE GLY
SEQRES   9 A  501  LEU PHE MET TYR ASP HIS LEU GLY LYS ARG THR SER LEU
SEQRES  10 A  501  PRO GLY SER THR GLY LEU ARG PHE GLY ALA ASN SER VAL
SEQRES  11 A  501  LEU LYS PRO GLU ILE LYS ARG GLY PHE GLU TYR SER ASP
SEQRES  12 A  501  CYS TRP VAL ASP ASP ALA ARG LEU VAL LEU ALA ASN ALA
SEQRES  13 A  501  GLN MET VAL VAL ARG LYS GLY GLY GLU VAL LEU THR ARG
SEQRES  14 A  501  THR ARG ALA THR SER ALA ARG ARG GLU ASN GLY LEU TRP
SEQRES  15 A  501  ILE VAL GLU ALA GLU ASP ILE ASP THR GLY LYS LYS TYR
SEQRES  16 A  501  SER TRP GLN ALA ARG GLY LEU VAL ASN ALA THR GLY PRO
SEQRES  17 A  501  TRP VAL LYS GLN PHE PHE ASP ASP GLY MET HIS LEU PRO
SEQRES  18 A  501  SER PRO TYR GLY ILE ARG LEU ILE LYS GLY SER HIS ILE
SEQRES  19 A  501  VAL VAL PRO ARG VAL HIS THR GLN LYS GLN ALA TYR ILE
SEQRES  20 A  501  LEU GLN ASN GLU ASP LYS ARG ILE VAL PHE VAL ILE PRO
SEQRES  21 A  501  TRP MET ASP GLU PHE SER ILE ILE GLY THR THR ASP VAL
SEQRES  22 A  501  GLU TYR LYS GLY ASP PRO LYS ALA VAL LYS ILE GLU GLU
SEQRES  23 A  501  SER GLU ILE ASN TYR LEU LEU ASN VAL TYR ASN THR HIS
SEQRES  24 A  501  PHE LYS LYS GLN LEU SER ARG ASP ASP ILE VAL TRP THR
SEQRES  25 A  501  TYR SER GLY VAL ARG PRO LEU CYS ASP ASP GLU SER ASP
SEQRES  26 A  501  SER PRO GLN ALA ILE THR ARG ASP TYR THR LEU ASP ILE
SEQRES  27 A  501  HIS ASP GLU ASN GLY LYS ALA PRO LEU LEU SER VAL PHE
SEQRES  28 A  501  GLY GLY LYS LEU THR THR TYR ARG LYS LEU ALA GLU HIS
SEQRES  29 A  501  ALA LEU GLU LYS LEU THR PRO TYR TYR GLN GLY ILE GLY
SEQRES  30 A  501  PRO ALA TRP THR LYS GLU SER VAL LEU PRO GLY GLY ALA
SEQRES  31 A  501  ILE GLU GLY ASP ARG ASP ASP TYR ALA ALA ARG LEU ARG
SEQRES  32 A  501  ARG ARG TYR PRO PHE LEU THR GLU SER LEU ALA ARG HIS
SEQRES  33 A  501  TYR ALA ARG THR TYR GLY SER ASN SER GLU LEU LEU LEU
SEQRES  34 A  501  GLY ASN ALA GLY THR VAL SER ASP LEU GLY GLU ASP PHE
SEQRES  35 A  501  GLY HIS GLU PHE TYR GLU ALA GLU LEU LYS TYR LEU VAL
SEQRES  36 A  501  ASP HIS GLU TRP VAL ARG ARG ALA ASP ASP ALA LEU TRP
SEQRES  37 A  501  ARG ARG THR LYS GLN GLY MET TRP LEU ASN ALA ASP GLN
SEQRES  38 A  501  GLN SER ARG VAL SER GLN TRP LEU VAL GLU TYR THR GLN
SEQRES  39 A  501  GLN ARG LEU SER LEU ALA SER
SEQRES   1 B  501  MET GLU THR LYS ASP LEU ILE VAL ILE GLY GLY GLY ILE
SEQRES   2 B  501  ASN GLY ALA GLY ILE ALA ALA ASP ALA ALA GLY ARG GLY
SEQRES   3 B  501  LEU SER VAL LEU MET LEU GLU ALA GLN ASP LEU ALA CYS
SEQRES   4 B  501  ALA THR SER SER ALA SER SER LYS LEU ILE HIS GLY GLY
SEQRES   5 B  501  LEU ARG TYR LEU GLU HIS TYR GLU PHE ARG LEU VAL SER
SEQRES   6 B  501  GLU ALA LEU ALA GLU ARG GLU VAL LEU LEU LYS MET ALA
SEQRES   7 B  501  PRO HIS ILE ALA PHE PRO MET ARG PHE ARG LEU PRO HIS
SEQRES   8 B  501  ARG PRO HIS LEU ARG PRO ALA TRP MET ILE ARG ILE GLY
SEQRES   9 B  501  LEU PHE MET TYR ASP HIS LEU GLY LYS ARG THR SER LEU
SEQRES  10 B  501  PRO GLY SER THR GLY LEU ARG PHE GLY ALA ASN SER VAL
SEQRES  11 B  501  LEU LYS PRO GLU ILE LYS ARG GLY PHE GLU TYR SER ASP
SEQRES  12 B  501  CYS TRP VAL ASP ASP ALA ARG LEU VAL LEU ALA ASN ALA
SEQRES  13 B  501  GLN MET VAL VAL ARG LYS GLY GLY GLU VAL LEU THR ARG
SEQRES  14 B  501  THR ARG ALA THR SER ALA ARG ARG GLU ASN GLY LEU TRP
SEQRES  15 B  501  ILE VAL GLU ALA GLU ASP ILE ASP THR GLY LYS LYS TYR
SEQRES  16 B  501  SER TRP GLN ALA ARG GLY LEU VAL ASN ALA THR GLY PRO
SEQRES  17 B  501  TRP VAL LYS GLN PHE PHE ASP ASP GLY MET HIS LEU PRO
SEQRES  18 B  501  SER PRO TYR GLY ILE ARG LEU ILE LYS GLY SER HIS ILE
SEQRES  19 B  501  VAL VAL PRO ARG VAL HIS THR GLN LYS GLN ALA TYR ILE
SEQRES  20 B  501  LEU GLN ASN GLU ASP LYS ARG ILE VAL PHE VAL ILE PRO
SEQRES  21 B  501  TRP MET ASP GLU PHE SER ILE ILE GLY THR THR ASP VAL
SEQRES  22 B  501  GLU TYR LYS GLY ASP PRO LYS ALA VAL LYS ILE GLU GLU
SEQRES  23 B  501  SER GLU ILE ASN TYR LEU LEU ASN VAL TYR ASN THR HIS
SEQRES  24 B  501  PHE LYS LYS GLN LEU SER ARG ASP ASP ILE VAL TRP THR
SEQRES  25 B  501  TYR SER GLY VAL ARG PRO LEU CYS ASP ASP GLU SER ASP
SEQRES  26 B  501  SER PRO GLN ALA ILE THR ARG ASP TYR THR LEU ASP ILE
SEQRES  27 B  501  HIS ASP GLU ASN GLY LYS ALA PRO LEU LEU SER VAL PHE
SEQRES  28 B  501  GLY GLY LYS LEU THR THR TYR ARG LYS LEU ALA GLU HIS
SEQRES  29 B  501  ALA LEU GLU LYS LEU THR PRO TYR TYR GLN GLY ILE GLY
SEQRES  30 B  501  PRO ALA TRP THR LYS GLU SER VAL LEU PRO GLY GLY ALA
SEQRES  31 B  501  ILE GLU GLY ASP ARG ASP ASP TYR ALA ALA ARG LEU ARG
SEQRES  32 B  501  ARG ARG TYR PRO PHE LEU THR GLU SER LEU ALA ARG HIS
SEQRES  33 B  501  TYR ALA ARG THR TYR GLY SER ASN SER GLU LEU LEU LEU
SEQRES  34 B  501  GLY ASN ALA GLY THR VAL SER ASP LEU GLY GLU ASP PHE
SEQRES  35 B  501  GLY HIS GLU PHE TYR GLU ALA GLU LEU LYS TYR LEU VAL
SEQRES  36 B  501  ASP HIS GLU TRP VAL ARG ARG ALA ASP ASP ALA LEU TRP
SEQRES  37 B  501  ARG ARG THR LYS GLN GLY MET TRP LEU ASN ALA ASP GLN
SEQRES  38 B  501  GLN SER ARG VAL SER GLN TRP LEU VAL GLU TYR THR GLN
SEQRES  39 B  501  GLN ARG LEU SER LEU ALA SER
HET    BOG  A 700      20
HET    BOG  A 701      20
HET    BOG  A 800      20
HET    BOG  A 801      20
HET    BOG  B 700      20
HET    BOG  B 800      20
HET    SO4  A 802       5
HET    SO4  A 803       5
HET    SO4  B 801       5
HET    SO4  B 802       5
HET    PO4  A 804       5
HET    PO4  B 803       5
HET    FAD  A 600      53
HET    FAD  B 600      53
HET    TAM  A 805      11
HET    EDO  A 806       4
HET    IMD  A 807       5
HET    EDO  A 808       4
HET    EDO  A 809       4
HET    EDO  A 810       4
HET    EDO  A 811       4
HET    EDO  A 812       4
HET    EDO  A 813       4
HET    EDO  A 814       4
HET    EDO  A 815       4
HET    EDO  A 816       4
HET    EDO  A 817       4
HET    EDO  A 818       4
HET    EDO  A 819       4
HET    EDO  A 820       4
HET    IMD  A 821       5
HET    EDO  A 822       4
HET    TAM  A 823      11
HET    EDO  B 804       4
HET    EDO  B 805       4
HET    EDO  B 806       4
HET    EDO  B 807       4
HET    EDO  B 808       4
HET    EDO  B 809       4
HET    TAM  B 810      11
HET    EDO  B 811       4
HET    EDO  B 812       4
HET    EDO  B 813       4
HET    EDO  B 814       4
HET    EDO  B 815       4
HET    EDO  B 816       4
HET    EDO  B 817       4
HET    EDO  B 819       4
HET    EDO  B 820       4
HETNAM     BOG B-OCTYLGLUCOSIDE
HETNAM     SO4 SULFATE ION
HETNAM     PO4 PHOSPHATE ION
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM     TAM TRIS(HYDROXYETHYL)AMINOMETHANE
HETNAM     EDO 1,2-ETHANEDIOL
HETNAM     IMD IMIDAZOLE
HETSYN     EDO ETHYLENE GLYCOL
FORMUL   3  BOG    6(C14 H28 O6)
FORMUL   9  SO4    4(O4 S 2-)
FORMUL  13  PO4    2(O4 P 3-)
FORMUL  15  FAD    2(C27 H33 N9 O15 P2)
FORMUL  17  TAM    3(C7 H17 N O3)
FORMUL  18  EDO    30(C2 H6 O2)
FORMUL  19  IMD    2(C3 H5 N2 1+)
FORMUL  52  HOH   *476(H2 O)
HELIX    1   1 GLY A   12  ARG A   25  1                                  14
HELIX    2   2 ALA A   40  ALA A   44  5                                   5
HELIX    3   3 GLY A   52  TYR A   59  5                                   8
HELIX    4   4 GLU A   60  ALA A   78  1                                  19
HELIX    5   5 PRO A   97  HIS A  110  1                                  14
HELIX    6   6 ASP A  147  LYS A  162  1                                  16
HELIX    7   7 THR A  206  PRO A  208  5                                   3
HELIX    8   8 TRP A  209  GLY A  217  1                                   9
HELIX    9   9 ASP A  278  VAL A  282  5                                   5
HELIX   10  10 GLU A  285  PHE A  300  1                                  16
HELIX   11  11 SER A  305  ILE A  309  5                                   5
HELIX   12  12 SER A  326  ILE A  330  5                                   5
HELIX   13  13 LYS A  354  THR A  356  5                                   3
HELIX   14  14 THR A  357  THR A  370  1                                  14
HELIX   15  15 PRO A  371  TYR A  373  5                                   3
HELIX   16  16 TRP A  380  SER A  384  5                                   5
HELIX   17  17 ASP A  397  TYR A  406  1                                  10
HELIX   18  18 THR A  410  TYR A  421  1                                  12
HELIX   19  19 ASN A  424  GLY A  430  1                                   7
HELIX   20  20 THR A  434  GLY A  439  5                                   6
HELIX   21  21 TYR A  447  GLU A  458  1                                  12
HELIX   22  22 ARG A  462  ARG A  469  1                                   8
HELIX   23  23 LYS A  472  TRP A  476  5                                   5
HELIX   24  24 ASN A  478  GLN A  495  1                                  18
HELIX   25  25 GLY B   12  ARG B   25  1                                  14
HELIX   26  26 ALA B   40  ALA B   44  5                                   5
HELIX   27  27 GLY B   52  TYR B   59  5                                   8
HELIX   28  28 GLU B   60  ALA B   78  1                                  19
HELIX   29  29 PRO B   97  HIS B  110  1                                  14
HELIX   30  30 ASP B  147  LYS B  162  1                                  16
HELIX   31  31 THR B  206  PRO B  208  5                                   3
HELIX   32  32 TRP B  209  GLY B  217  1                                   9
HELIX   33  33 ASP B  278  VAL B  282  5                                   5
HELIX   34  34 GLU B  285  PHE B  300  1                                  16
HELIX   35  35 SER B  305  ILE B  309  5                                   5
HELIX   36  36 SER B  326  ILE B  330  5                                   5
HELIX   37  37 THR B  357  THR B  370  1                                  14
HELIX   38  38 PRO B  371  TYR B  373  5                                   3
HELIX   39  39 TRP B  380  SER B  384  5                                   5
HELIX   40  40 ASP B  397  TYR B  406  1                                  10
HELIX   41  41 THR B  410  TYR B  421  1                                  12
HELIX   42  42 ASN B  424  GLY B  430  1                                   7
HELIX   43  43 THR B  434  GLY B  439  5                                   6
HELIX   44  44 TYR B  447  GLU B  458  1                                  12
HELIX   45  45 ARG B  462  ARG B  469  1                                   8
HELIX   46  46 LYS B  472  TRP B  476  5                                   5
HELIX   47  47 ASN B  478  GLN B  495  1                                  18
SHEET    1   A 6 GLU A 165  LEU A 167  0
SHEET    2   A 6 VAL A  29  LEU A  32  1  N  MET A  31   O  GLU A 165
SHEET    3   A 6 LEU A   6  ILE A   9  1  N  VAL A   8   O  LEU A  30
SHEET    4   A 6 LEU A 202  ASN A 204  1  O  VAL A 203   N  ILE A   9
SHEET    5   A 6 LYS A 344  PHE A 351  1  O  LEU A 348   N  ASN A 204
SHEET    6   A 6 THR A 335  GLU A 341 -1  N  HIS A 339   O  LEU A 347
SHEET    1   B 8 LEU A  48  ILE A  49  0
SHEET    2   B 8 ARG A 137  VAL A 146 -1  O  CYS A 144   N  ILE A  49
SHEET    3   B 8 ALA A  82  PRO A  90 -1  N  PHE A  87   O  TYR A 141
SHEET    4   B 8 ALA A 245  GLN A 249  1  O  ALA A 245   N  ARG A  86
SHEET    5   B 8 ILE A 255  TRP A 261 -1  O  VAL A 256   N  LEU A 248
SHEET    6   B 8 PHE A 265  GLY A 269 -1  O  GLY A 269   N  PHE A 257
SHEET    7   B 8 ILE A 229  PRO A 237 -1  N  ILE A 234   O  ILE A 268
SHEET    8   B 8 VAL A 273  GLU A 274 -1  O  VAL A 273   N  LYS A 230
SHEET    1   C 8 THR A 121  ARG A 124  0
SHEET    2   C 8 ARG A 137  VAL A 146 -1  O  GLU A 140   N  THR A 121
SHEET    3   C 8 ALA A  82  PRO A  90 -1  N  PHE A  87   O  TYR A 141
SHEET    4   C 8 ALA A 245  GLN A 249  1  O  ALA A 245   N  ARG A  86
SHEET    5   C 8 ILE A 255  TRP A 261 -1  O  VAL A 256   N  LEU A 248
SHEET    6   C 8 PHE A 265  GLY A 269 -1  O  GLY A 269   N  PHE A 257
SHEET    7   C 8 ILE A 229  PRO A 237 -1  N  ILE A 234   O  ILE A 268
SHEET    8   C 8 TRP A 311  ARG A 317 -1  O  TRP A 311   N  VAL A 235
SHEET    1   D 3 THR A 170  GLU A 178  0
SHEET    2   D 3 LEU A 181  ASP A 188 -1  O  LEU A 181   N  GLU A 178
SHEET    3   D 3 LYS A 194  ALA A 199 -1  O  TRP A 197   N  VAL A 184
SHEET    1   E 4 THR B   3  LYS B   4  0
SHEET    2   E 4 LYS B 194  ALA B 199  1  O  GLN B 198   N  LYS B   4
SHEET    3   E 4 LEU B 181  ASP B 188 -1  N  TRP B 182   O  ALA B 199
SHEET    4   E 4 THR B 170  GLU B 178 -1  N  GLU B 178   O  LEU B 181
SHEET    1   F 6 GLU B 165  LEU B 167  0
SHEET    2   F 6 VAL B  29  LEU B  32  1  N  MET B  31   O  GLU B 165
SHEET    3   F 6 LEU B   6  ILE B   9  1  N  VAL B   8   O  LEU B  30
SHEET    4   F 6 LEU B 202  ASN B 204  1  O  VAL B 203   N  ILE B   9
SHEET    5   F 6 LYS B 344  PHE B 351  1  O  LEU B 348   N  ASN B 204
SHEET    6   F 6 THR B 335  GLU B 341 -1  N  THR B 335   O  PHE B 351
SHEET    1   G 8 LEU B  48  ILE B  49  0
SHEET    2   G 8 ARG B 137  VAL B 146 -1  O  CYS B 144   N  ILE B  49
SHEET    3   G 8 ALA B  82  PRO B  90 -1  N  LEU B  89   O  PHE B 139
SHEET    4   G 8 ALA B 245  GLN B 249  1  O  ALA B 245   N  ARG B  86
SHEET    5   G 8 ILE B 255  TRP B 261 -1  O  VAL B 256   N  LEU B 248
SHEET    6   G 8 PHE B 265  GLY B 269 -1  O  GLY B 269   N  PHE B 257
SHEET    7   G 8 ILE B 229  PRO B 237 -1  N  ILE B 234   O  ILE B 268
SHEET    8   G 8 VAL B 273  GLU B 274 -1  O  VAL B 273   N  LYS B 230
SHEET    1   H 8 THR B 121  ARG B 124  0
SHEET    2   H 8 ARG B 137  VAL B 146 -1  O  GLU B 140   N  THR B 121
SHEET    3   H 8 ALA B  82  PRO B  90 -1  N  LEU B  89   O  PHE B 139
SHEET    4   H 8 ALA B 245  GLN B 249  1  O  ALA B 245   N  ARG B  86
SHEET    5   H 8 ILE B 255  TRP B 261 -1  O  VAL B 256   N  LEU B 248
SHEET    6   H 8 PHE B 265  GLY B 269 -1  O  GLY B 269   N  PHE B 257
SHEET    7   H 8 ILE B 229  PRO B 237 -1  N  ILE B 234   O  ILE B 268
SHEET    8   H 8 TRP B 311  ARG B 317 -1  O  TRP B 311   N  VAL B 235
CISPEP   1 GLY A  269    THR A  270          0        26.14
CISPEP   2 ARG A  395    ASP A  396          0        -1.63
CISPEP   3 ASP A  396    ASP A  397          0        -1.27
CISPEP   4 GLY B  269    THR B  270          0         0.93
CISPEP   5 ASP B  396    ASP B  397          0         1.32
SITE     1 AC1  1 TRP A  99
SITE     1 AC2  4 TRP A  99  ARG A 102  ARG A 137  BOG A 800
SITE     1 AC3  7 HIS A  91  PRO A  93  PRO A  97  ALA A  98
SITE     2 AC3  7 GLU A 134  LYS A 136  BOG A 701
SITE     1 AC4  9 LEU A  53  ARG A  54  LEU A  56  GLU A  57
SITE     2 AC4  9 TYR A  59  ARG A  96  ILE A 101  GLY A 104
SITE     3 AC4  9 MET A 107
SITE     1 AC5  6 ALA B  98  TRP B  99  ILE B 103  ARG B 137
SITE     2 AC5  6 BOG B 800  EDO B 820
SITE     1 AC6  6 TYR A  59  ARG A  62  ARG B 102  THR B 121
SITE     2 AC6  6 GLY B 122  BOG B 700
SITE     1 AC7  5 VAL A 310  TRP A 311  TRP A 468  GLY A 474
SITE     2 AC7  5 MET A 475
SITE     1 AC8  5 HIS A  80  PHE A  83  ASP A 394  ARG A 419
SITE     2 AC8  5 HOH A1031
SITE     1 AC9  4 VAL B 310  TRP B 468  GLY B 474  MET B 475
SITE     1 BC1  7 ARG A 161  HOH A 942  TYR B 398  ARG B 401
SITE     2 BC1  7 LEU B 402  ARG B 405  GLU B 426
SITE     1 BC2  9 ARG A  54  TYR A  55  ARG A 317  ARG A 332
SITE     2 BC2  9 LYS A 354  HOH A 897  HOH A 973  HOH A 989
SITE     3 BC2  9 HOH A1057
SITE     1 BC3  9 ARG B  54  TYR B  55  ARG B 317  ARG B 332
SITE     2 BC3  9 HOH B 908  HOH B 922  HOH B 943  HOH B1005
SITE     3 BC3  9 HOH B1038
SITE     1 BC4 34 ILE A   9  GLY A  10  GLY A  11  GLY A  12
SITE     2 BC4 34 ILE A  13  ASN A  14  GLU A  33  ALA A  34
SITE     3 BC4 34 CYS A  39  ALA A  40  THR A  41  SER A  42
SITE     4 BC4 34 ALA A  44  SER A  45  SER A  46  LYS A  47
SITE     5 BC4 34 LEU A  48  HIS A  50  ALA A 172  THR A 206
SITE     6 BC4 34 GLY A 207  PRO A 208  PHE A 213  GLY A 231
SITE     7 BC4 34 THR A 270  ARG A 317  GLY A 353  LYS A 354
SITE     8 BC4 34 LEU A 355  THR A 356  EDO A 806  HOH A 824
SITE     9 BC4 34 HOH A 825  HOH A1052
SITE     1 BC5 32 ILE B   9  GLY B  10  GLY B  12  ILE B  13
SITE     2 BC5 32 ASN B  14  LEU B  32  GLU B  33  ALA B  34
SITE     3 BC5 32 CYS B  39  ALA B  40  THR B  41  SER B  42
SITE     4 BC5 32 ALA B  44  SER B  45  SER B  46  LYS B  47
SITE     5 BC5 32 LEU B  48  HIS B  50  ALA B 172  THR B 206
SITE     6 BC5 32 GLY B 207  PRO B 208  GLY B 231  ARG B 317
SITE     7 BC5 32 GLY B 353  LYS B 354  LEU B 355  THR B 356
SITE     8 BC5 32 EDO B 806  HOH B 821  HOH B 822  HOH B1050
SITE     1 BC6  8 ALA A  23  GLY A  24  LYS A 162  HOH A 942
SITE     2 BC6  8 HOH A1056  ARG B 401  ARG B 404  HOH B 971
SITE     1 BC7  4 ALA A  34  ARG A 171  LYS A 280  FAD A 600
SITE     1 BC8  4 HIS A 444  GLU A 445  GLN A 473  EDO A 811
SITE     1 BC9  8 SER A  43  TRP A 311  TRP A 468  EDO A 812
SITE     2 BC9  8 HOH A 826  HOH A 832  HOH A1034  HOH A1035
SITE     1 CC1  5 GLN A 303  EDO A 815  HOH A 964  HOH A1039
SITE     2 CC1  5 EDO B 805
SITE     1 CC2  2 ARG A 306  ILE A 309
SITE     1 CC3  7 HIS A 416  THR A 471  LYS A 472  GLN A 473
SITE     2 CC3  7 TRP A 476  IMD A 807  HOH A 872
SITE     1 CC4  3 TRP A 311  TRP A 468  EDO A 808
SITE     1 CC5  1 GLU A 448
SITE     1 CC6  2 GLU A 440  ASP A 441
SITE     1 CC7  5 ASN A 294  ASN A 297  THR A 298  EDO A 809
SITE     2 CC7  5 HOH A 928
SITE     1 CC8  5 ASN A 294  HOH A 947  SER B 305  ARG B 306
SITE     2 CC8  5 HOH B 839
SITE     1 CC9  4 ARG A 254  THR A 271  ASP A 272  TAM A 823
SITE     1 DC1  8 ALA A  40  THR A  41  PRO A 279  LYS A 280
SITE     2 DC1  8 VAL A 282  GLY A 315  VAL A 316  HOH A1043
SITE     1 DC2  4 ARG A 404  ALA B  23  GLY B  24  HOH B1025
SITE     1 DC3  4 ASP A 397  ARG A 404  HOH A 939  HOH A 969
SITE     1 DC4  7 GLN A 157  ASN A 424  LEU A 427  TYR A 453
SITE     2 DC4  7 EDO A 822  HOH A1066  HOH B 957
SITE     1 DC5  6 GLN A 157  HIS A 457  TRP A 459  IMD A 821
SITE     2 DC5  6 HOH A1063  ARG B 405
SITE     1 DC6 10 ASP A 272  VAL A 273  GLU A 274  GLU A 285
SITE     2 DC6 10 SER A 287  GLU A 288  EDO A 817  GLU B 285
SITE     3 DC6 10 SER B 287  HOH B 924
SITE     1 DC7  3 ARG B 254  THR B 271  ASP B 272
SITE     1 DC8  5 EDO A 809  LEU B 293  ASN B 294  ASN B 297
SITE     2 DC8  5 HOH B 860
SITE     1 DC9  4 ALA B  34  TRP B 209  LYS B 280  FAD B 600
SITE     1 EC1  3 TRP B 311  TRP B 468  EDO B 811
SITE     1 EC2  4 MET B 262  EDO B 817  HOH B1030  HOH B1033
SITE     1 EC3  2 ILE B 289  ARG B 306
SITE     1 EC4  9 ARG A 405  GLU A 426  GLN B 157  VAL B 160
SITE     2 EC4  9 ARG B 161  PRO B 387  ASN B 424  HIS B 457
SITE     3 EC4  9 HOH B1054
SITE     1 EC5  7 SER B  43  ALA B  44  TRP B 311  TRP B 468
SITE     2 EC5  7 EDO B 807  HOH B 830  HOH B 833
SITE     1 EC6  7 ARG B  88  ARG B 124  PHE B 125  SER B 129
SITE     2 EC6  7 VAL B 130  GLN B 242  HOH B1000
SITE     1 EC7  4 PRO B 208  GLN B 212  LEU B 228  PRO B 279
SITE     1 EC8  5 VAL B 455  ASP B 456  HIS B 457  GLU B 458
SITE     2 EC8  5 TRP B 459
SITE     1 EC9  1 ILE B 101
SITE     1 FC1  5 HIS B 416  EDO B 808  EDO B 819  HOH B 826
SITE     2 FC1  5 HOH B1028
SITE     1 FC2  5 HIS B 444  GLU B 445  GLN B 473  EDO B 817
SITE     2 FC2  5 HOH B 866
SITE     1 FC3  5 HIS B  91  PRO B  93  PRO B  97  ALA B  98
SITE     2 FC3  5 BOG B 700
CRYST1  113.791  114.097  192.801  90.00  90.00  90.00 I 2 2 2      16
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      0.008788  0.000000  0.000000        0.00000
SCALE2      0.000000  0.008764  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005187        0.00000
      
PROCHECK
Go to PROCHECK summary
 References