spacer
spacer

PDBsum entry 3hbx

Go to PDB code: 
Top Page protein Protein-protein interface(s) links
Lyase PDB id
3hbx
Jmol
Contents
Protein chains
(+ 0 more) 437 a.a.
Waters ×314
HEADER    LYASE                                   05-MAY-09   3HBX
TITLE     CRYSTAL STRUCTURE OF GAD1 FROM ARABIDOPSIS THALIANA
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: GLUTAMATE DECARBOXYLASE 1;
COMPND   3 CHAIN: A, B, C, D, E, F;
COMPND   4 SYNONYM: GAD 1;
COMPND   5 EC: 4.1.1.15;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE   3 ORGANISM_COMMON: MOUSE-EAR CRESS,THALE-CRESS;
SOURCE   4 ORGANISM_TAXID: 3702;
SOURCE   5 GENE: AT5G17330, GAD, GAD1, GDH1, MKP11.30, MKP11_18;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 DE3 PLYSS;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET12B
KEYWDS    CALMODULIN-BINDING, DECARBOXYLASE, LYASE, PYRIDOXAL
KEYWDS   2 PHOSPHATE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    H.GUT,P.DOMINICI,S.PILATI,M.G.GRUETTER,G.CAPITANI
REVDAT   3   08-DEC-09 3HBX    1       MTRIX1 MTRIX2 MTRIX3
REVDAT   2   15-SEP-09 3HBX    1       JRNL
REVDAT   1   28-JUL-09 3HBX    0
JRNL        AUTH   H.GUT,P.DOMINICI,S.PILATI,A.ASTEGNO,M.V.PETOUKHOV,
JRNL        AUTH 2 D.I.SVERGUN,M.G.GRUTTER,G.CAPITANI
JRNL        TITL   A COMMON STRUCTURAL BASIS FOR PH- AND
JRNL        TITL 2 CALMODULIN-MEDIATED REGULATION IN PLANT GLUTAMATE
JRNL        TITL 3 DECARBOXYLASE.
JRNL        REF    J.MOL.BIOL.                   V. 392   334 2009
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   19580813
JRNL        DOI    10.1016/J.JMB.2009.06.080
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.67 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.4_29)
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK   3               : ZWART
REMARK   3
REMARK   3    REFINEMENT TARGET : ML
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.67
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.09
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.510
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.2
REMARK   3   NUMBER OF REFLECTIONS             : 85127
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.208
REMARK   3   R VALUE            (WORKING SET) : 0.208
REMARK   3   FREE R VALUE                     : 0.221
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.610
REMARK   3   FREE R VALUE TEST SET COUNT      : 2223
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE
REMARK   3     1 29.0927 -  6.7077    0.91     4897   139  0.1612 0.1714
REMARK   3     2  6.7077 -  5.3348    0.94     5062   148  0.1810 0.2145
REMARK   3     3  5.3348 -  4.6636    0.94     5014   166  0.1674 0.1719
REMARK   3     4  4.6636 -  4.2386    0.95     5057   150  0.1643 0.1775
REMARK   3     5  4.2386 -  3.9356    0.96     5158   167  0.1777 0.1781
REMARK   3     6  3.9356 -  3.7040    0.97     5190   133  0.1794 0.2026
REMARK   3     7  3.7040 -  3.5188    0.97     5262   168  0.1993 0.2307
REMARK   3     8  3.5188 -  3.3659    0.98     5253   130  0.2078 0.2269
REMARK   3     9  3.3659 -  3.2365    0.98     5338   150  0.2226 0.2406
REMARK   3    10  3.2365 -  3.1250    0.98     5246   178  0.2415 0.2577
REMARK   3    11  3.1250 -  3.0273    0.98     5278   144  0.2540 0.2659
REMARK   3    12  3.0273 -  2.9409    0.99     5346   117  0.2655 0.3089
REMARK   3    13  2.9409 -  2.8635    0.98     5350   113  0.2756 0.2683
REMARK   3    14  2.8635 -  2.7937    0.98     5333    97  0.2785 0.3089
REMARK   3    15  2.7937 -  2.7303    0.97     5189   126  0.2870 0.3461
REMARK   3    16  2.7303 -  2.6720    0.91     4931    97  0.3029 0.3526
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.11
REMARK   3   SHRINKAGE RADIUS   : 0.90
REMARK   3   K_SOL              : 0.34
REMARK   3   B_SOL              : 28.07
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.290
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.160
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 45.70
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 47.55
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -8.54800
REMARK   3    B22 (A**2) : -8.54800
REMARK   3    B33 (A**2) : 17.09700
REMARK   3    B12 (A**2) : -0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  TWINNING INFORMATION.
REMARK   3   FRACTION: NULL
REMARK   3   OPERATOR: NULL
REMARK   3
REMARK   3  DEVIATIONS FROM IDEAL VALUES.
REMARK   3                 RMSD          COUNT
REMARK   3   BOND      :  0.002          21624
REMARK   3   ANGLE     :  0.606          29356
REMARK   3   CHIRALITY :  0.043           3240
REMARK   3   PLANARITY :  0.002           3788
REMARK   3   DIHEDRAL  : 14.335           7978
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  NCS DETAILS
REMARK   3   NUMBER OF NCS GROUPS : 2
REMARK   3   NCS GROUP : 1
REMARK   3    NCS OPERATOR : 1
REMARK   3     REFERENCE SELECTION: chain A and backbone and resseq 300:314
REMARK   3     SELECTION          : chain B and backbone and resseq 300:314
REMARK   3     ATOM PAIRS NUMBER  : 60
REMARK   3     RMSD               : 0.019
REMARK   3    NCS OPERATOR : 2
REMARK   3     REFERENCE SELECTION: chain A and backbone and resseq 300:314
REMARK   3     SELECTION          : chain C and backbone and resseq 300:314
REMARK   3     ATOM PAIRS NUMBER  : 60
REMARK   3     RMSD               : 0.015
REMARK   3    NCS OPERATOR : 3
REMARK   3     REFERENCE SELECTION: chain A and backbone and resseq 300:314
REMARK   3     SELECTION          : chain D and backbone and resseq 300:314
REMARK   3     ATOM PAIRS NUMBER  : 60
REMARK   3     RMSD               : 0.012
REMARK   3    NCS OPERATOR : 4
REMARK   3     REFERENCE SELECTION: chain A and backbone and resseq 300:314
REMARK   3     SELECTION          : chain E and backbone and resseq 300:314
REMARK   3     ATOM PAIRS NUMBER  : 60
REMARK   3     RMSD               : 0.012
REMARK   3    NCS OPERATOR : 5
REMARK   3     REFERENCE SELECTION: chain A and backbone and resseq 300:314
REMARK   3     SELECTION          : chain F and backbone and resseq 300:314
REMARK   3     ATOM PAIRS NUMBER  : 60
REMARK   3     RMSD               : 0.017
REMARK   3   NCS GROUP : 2
REMARK   3    NCS OPERATOR : 1
REMARK   3     REFERENCE SELECTION: chain A and (resseq 12:111 or resseq
REMARK   3                          117:148 or resseq 150:255 or resseq
REMARK   3                          260:276 or resseq 278:299 or resseq
REMARK   3                          315:404 or resseq 415:447 )
REMARK   3     SELECTION          : chain B and (resseq 12:111 or resseq
REMARK   3                          117:148 or resseq 150:255 or resseq
REMARK   3                          260:276 or resseq 278:299 or resseq
REMARK   3                          315:404 or resseq 415:447 )
REMARK   3     ATOM PAIRS NUMBER  : 3202
REMARK   3     RMSD               : 0.009
REMARK   3    NCS OPERATOR : 2
REMARK   3     REFERENCE SELECTION: chain A and (resseq 12:111 or resseq
REMARK   3                          117:148 or resseq 150:255 or resseq
REMARK   3                          260:276 or resseq 278:299 or resseq
REMARK   3                          315:404 or resseq 415:447 )
REMARK   3     SELECTION          : chain C and (resseq 12:111 or resseq
REMARK   3                          117:148 or resseq 150:255 or resseq
REMARK   3                          260:276 or resseq 278:299 or resseq
REMARK   3                          315:404 or resseq 415:447 )
REMARK   3     ATOM PAIRS NUMBER  : 3202
REMARK   3     RMSD               : 0.008
REMARK   3    NCS OPERATOR : 3
REMARK   3     REFERENCE SELECTION: chain A and (resseq 12:111 or resseq
REMARK   3                          117:148 or resseq 150:255 or resseq
REMARK   3                          260:276 or resseq 278:299 or resseq
REMARK   3                          315:404 or resseq 415:447 )
REMARK   3     SELECTION          : chain D and (resseq 12:111 or resseq
REMARK   3                          117:148 or resseq 150:255 or resseq
REMARK   3                          260:276 or resseq 278:299 or resseq
REMARK   3                          315:404 or resseq 415:447 )
REMARK   3     ATOM PAIRS NUMBER  : 3202
REMARK   3     RMSD               : 0.008
REMARK   3    NCS OPERATOR : 4
REMARK   3     REFERENCE SELECTION: chain A and (resseq 12:111 or resseq
REMARK   3                          117:148 or resseq 150:255 or resseq
REMARK   3                          260:276 or resseq 278:299 or resseq
REMARK   3                          315:404 or resseq 415:447 )
REMARK   3     SELECTION          : chain E and (resseq 12:111 or resseq
REMARK   3                          117:148 or resseq 150:255 or resseq
REMARK   3                          260:276 or resseq 278:299 or resseq
REMARK   3                          315:404 or resseq 415:447 )
REMARK   3     ATOM PAIRS NUMBER  : 3202
REMARK   3     RMSD               : 0.007
REMARK   3    NCS OPERATOR : 5
REMARK   3     REFERENCE SELECTION: chain A and (resseq 12:111 or resseq
REMARK   3                          117:148 or resseq 150:255 or resseq
REMARK   3                          260:276 or resseq 278:299 or resseq
REMARK   3                          315:404 or resseq 415:447 )
REMARK   3     SELECTION          : chain F and (resseq 12:111 or resseq
REMARK   3                          117:148 or resseq 150:255 or resseq
REMARK   3                          260:276 or resseq 278:299 or resseq
REMARK   3                          315:404 or resseq 415:447 )
REMARK   3     ATOM PAIRS NUMBER  : 3202
REMARK   3     RMSD               : 0.009
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 3HBX COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAY-09.
REMARK 100 THE RCSB ID CODE IS RCSB052945.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 26-FEB-05
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : NULL
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) : 0.90002
REMARK 200  MONOCHROMATOR                  : LN2 COOLED FIXED-EXIT SI(111)
REMARK 200  OPTICS                         : DYNAMICALLY BENDABLE MIRROR
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 85232
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.650
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.4
REMARK 200  DATA REDUNDANCY                : 2.000
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.07700
REMARK 200   FOR THE DATA SET  : 8.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.74
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.1
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.45900
REMARK 200   FOR SHELL         : 1.700
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 (E. COLI GADB)
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 47.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2 UL PROTEIN SOLUTION (1.9 MG/ML
REMARK 280  GAD1, 50 MM HEPES PH 7.2, 150 MM NACL AND 10 UM PLP) + 1 UL
REMARK 280  RESERVOIR SOLUTION (100 MM NA ACETATE PH 5.5, 720 MM NA
REMARK 280  FORMATE, 9 % PEG 8000 AND 9 % PEG 1000), VAPOR DIFFUSION,
REMARK 280  SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+2/3
REMARK 290       3555   -X+Y,-X,Z+1/3
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      133.71733
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       66.85867
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 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     VAL A     2
REMARK 465     LEU A     3
REMARK 465     SER A     4
REMARK 465     HIS A     5
REMARK 465     ALA A     6
REMARK 465     VAL A     7
REMARK 465     SER A     8
REMARK 465     GLU A     9
REMARK 465     SER A    10
REMARK 465     ASP A    11
REMARK 465     SER A   449
REMARK 465     ARG A   450
REMARK 465     VAL A   451
REMARK 465     ILE A   452
REMARK 465     HIS A   453
REMARK 465     LYS A   454
REMARK 465     ILE A   455
REMARK 465     SER A   456
REMARK 465     LEU A   457
REMARK 465     GLY A   458
REMARK 465     GLN A   459
REMARK 465     GLU A   460
REMARK 465     LYS A   461
REMARK 465     SER A   462
REMARK 465     GLU A   463
REMARK 465     SER A   464
REMARK 465     ASN A   465
REMARK 465     SER A   466
REMARK 465     ASP A   467
REMARK 465     ASN A   468
REMARK 465     LEU A   469
REMARK 465     MET A   470
REMARK 465     VAL A   471
REMARK 465     THR A   472
REMARK 465     VAL A   473
REMARK 465     LYS A   474
REMARK 465     LYS A   475
REMARK 465     SER A   476
REMARK 465     ASP A   477
REMARK 465     ILE A   478
REMARK 465     ASP A   479
REMARK 465     LYS A   480
REMARK 465     GLN A   481
REMARK 465     ARG A   482
REMARK 465     ASP A   483
REMARK 465     ILE A   484
REMARK 465     ILE A   485
REMARK 465     THR A   486
REMARK 465     GLY A   487
REMARK 465     TRP A   488
REMARK 465     LYS A   489
REMARK 465     LYS A   490
REMARK 465     PHE A   491
REMARK 465     VAL A   492
REMARK 465     ALA A   493
REMARK 465     ASP A   494
REMARK 465     ARG A   495
REMARK 465     LYS A   496
REMARK 465     LYS A   497
REMARK 465     THR A   498
REMARK 465     SER A   499
REMARK 465     GLY A   500
REMARK 465     ILE A   501
REMARK 465     CYS A   502
REMARK 465     MET B     1
REMARK 465     VAL B     2
REMARK 465     LEU B     3
REMARK 465     SER B     4
REMARK 465     HIS B     5
REMARK 465     ALA B     6
REMARK 465     VAL B     7
REMARK 465     SER B     8
REMARK 465     GLU B     9
REMARK 465     SER B    10
REMARK 465     ASP B    11
REMARK 465     SER B   449
REMARK 465     ARG B   450
REMARK 465     VAL B   451
REMARK 465     ILE B   452
REMARK 465     HIS B   453
REMARK 465     LYS B   454
REMARK 465     ILE B   455
REMARK 465     SER B   456
REMARK 465     LEU B   457
REMARK 465     GLY B   458
REMARK 465     GLN B   459
REMARK 465     GLU B   460
REMARK 465     LYS B   461
REMARK 465     SER B   462
REMARK 465     GLU B   463
REMARK 465     SER B   464
REMARK 465     ASN B   465
REMARK 465     SER B   466
REMARK 465     ASP B   467
REMARK 465     ASN B   468
REMARK 465     LEU B   469
REMARK 465     MET B   470
REMARK 465     VAL B   471
REMARK 465     THR B   472
REMARK 465     VAL B   473
REMARK 465     LYS B   474
REMARK 465     LYS B   475
REMARK 465     SER B   476
REMARK 465     ASP B   477
REMARK 465     ILE B   478
REMARK 465     ASP B   479
REMARK 465     LYS B   480
REMARK 465     GLN B   481
REMARK 465     ARG B   482
REMARK 465     ASP B   483
REMARK 465     ILE B   484
REMARK 465     ILE B   485
REMARK 465     THR B   486
REMARK 465     GLY B   487
REMARK 465     TRP B   488
REMARK 465     LYS B   489
REMARK 465     LYS B   490
REMARK 465     PHE B   491
REMARK 465     VAL B   492
REMARK 465     ALA B   493
REMARK 465     ASP B   494
REMARK 465     ARG B   495
REMARK 465     LYS B   496
REMARK 465     LYS B   497
REMARK 465     THR B   498
REMARK 465     SER B   499
REMARK 465     GLY B   500
REMARK 465     ILE B   501
REMARK 465     CYS B   502
REMARK 465     MET C     1
REMARK 465     VAL C     2
REMARK 465     LEU C     3
REMARK 465     SER C     4
REMARK 465     HIS C     5
REMARK 465     ALA C     6
REMARK 465     VAL C     7
REMARK 465     SER C     8
REMARK 465     GLU C     9
REMARK 465     SER C    10
REMARK 465     ASP C    11
REMARK 465     SER C   449
REMARK 465     ARG C   450
REMARK 465     VAL C   451
REMARK 465     ILE C   452
REMARK 465     HIS C   453
REMARK 465     LYS C   454
REMARK 465     ILE C   455
REMARK 465     SER C   456
REMARK 465     LEU C   457
REMARK 465     GLY C   458
REMARK 465     GLN C   459
REMARK 465     GLU C   460
REMARK 465     LYS C   461
REMARK 465     SER C   462
REMARK 465     GLU C   463
REMARK 465     SER C   464
REMARK 465     ASN C   465
REMARK 465     SER C   466
REMARK 465     ASP C   467
REMARK 465     ASN C   468
REMARK 465     LEU C   469
REMARK 465     MET C   470
REMARK 465     VAL C   471
REMARK 465     THR C   472
REMARK 465     VAL C   473
REMARK 465     LYS C   474
REMARK 465     LYS C   475
REMARK 465     SER C   476
REMARK 465     ASP C   477
REMARK 465     ILE C   478
REMARK 465     ASP C   479
REMARK 465     LYS C   480
REMARK 465     GLN C   481
REMARK 465     ARG C   482
REMARK 465     ASP C   483
REMARK 465     ILE C   484
REMARK 465     ILE C   485
REMARK 465     THR C   486
REMARK 465     GLY C   487
REMARK 465     TRP C   488
REMARK 465     LYS C   489
REMARK 465     LYS C   490
REMARK 465     PHE C   491
REMARK 465     VAL C   492
REMARK 465     ALA C   493
REMARK 465     ASP C   494
REMARK 465     ARG C   495
REMARK 465     LYS C   496
REMARK 465     LYS C   497
REMARK 465     THR C   498
REMARK 465     SER C   499
REMARK 465     GLY C   500
REMARK 465     ILE C   501
REMARK 465     CYS C   502
REMARK 465     MET D     1
REMARK 465     VAL D     2
REMARK 465     LEU D     3
REMARK 465     SER D     4
REMARK 465     HIS D     5
REMARK 465     ALA D     6
REMARK 465     VAL D     7
REMARK 465     SER D     8
REMARK 465     GLU D     9
REMARK 465     SER D    10
REMARK 465     ASP D    11
REMARK 465     PRO D   448
REMARK 465     SER D   449
REMARK 465     ARG D   450
REMARK 465     VAL D   451
REMARK 465     ILE D   452
REMARK 465     HIS D   453
REMARK 465     LYS D   454
REMARK 465     ILE D   455
REMARK 465     SER D   456
REMARK 465     LEU D   457
REMARK 465     GLY D   458
REMARK 465     GLN D   459
REMARK 465     GLU D   460
REMARK 465     LYS D   461
REMARK 465     SER D   462
REMARK 465     GLU D   463
REMARK 465     SER D   464
REMARK 465     ASN D   465
REMARK 465     SER D   466
REMARK 465     ASP D   467
REMARK 465     ASN D   468
REMARK 465     LEU D   469
REMARK 465     MET D   470
REMARK 465     VAL D   471
REMARK 465     THR D   472
REMARK 465     VAL D   473
REMARK 465     LYS D   474
REMARK 465     LYS D   475
REMARK 465     SER D   476
REMARK 465     ASP D   477
REMARK 465     ILE D   478
REMARK 465     ASP D   479
REMARK 465     LYS D   480
REMARK 465     GLN D   481
REMARK 465     ARG D   482
REMARK 465     ASP D   483
REMARK 465     ILE D   484
REMARK 465     ILE D   485
REMARK 465     THR D   486
REMARK 465     GLY D   487
REMARK 465     TRP D   488
REMARK 465     LYS D   489
REMARK 465     LYS D   490
REMARK 465     PHE D   491
REMARK 465     VAL D   492
REMARK 465     ALA D   493
REMARK 465     ASP D   494
REMARK 465     ARG D   495
REMARK 465     LYS D   496
REMARK 465     LYS D   497
REMARK 465     THR D   498
REMARK 465     SER D   499
REMARK 465     GLY D   500
REMARK 465     ILE D   501
REMARK 465     CYS D   502
REMARK 465     MET E     1
REMARK 465     VAL E     2
REMARK 465     LEU E     3
REMARK 465     SER E     4
REMARK 465     HIS E     5
REMARK 465     ALA E     6
REMARK 465     VAL E     7
REMARK 465     SER E     8
REMARK 465     GLU E     9
REMARK 465     SER E    10
REMARK 465     ASP E    11
REMARK 465     PRO E   448
REMARK 465     SER E   449
REMARK 465     ARG E   450
REMARK 465     VAL E   451
REMARK 465     ILE E   452
REMARK 465     HIS E   453
REMARK 465     LYS E   454
REMARK 465     ILE E   455
REMARK 465     SER E   456
REMARK 465     LEU E   457
REMARK 465     GLY E   458
REMARK 465     GLN E   459
REMARK 465     GLU E   460
REMARK 465     LYS E   461
REMARK 465     SER E   462
REMARK 465     GLU E   463
REMARK 465     SER E   464
REMARK 465     ASN E   465
REMARK 465     SER E   466
REMARK 465     ASP E   467
REMARK 465     ASN E   468
REMARK 465     LEU E   469
REMARK 465     MET E   470
REMARK 465     VAL E   471
REMARK 465     THR E   472
REMARK 465     VAL E   473
REMARK 465     LYS E   474
REMARK 465     LYS E   475
REMARK 465     SER E   476
REMARK 465     ASP E   477
REMARK 465     ILE E   478
REMARK 465     ASP E   479
REMARK 465     LYS E   480
REMARK 465     GLN E   481
REMARK 465     ARG E   482
REMARK 465     ASP E   483
REMARK 465     ILE E   484
REMARK 465     ILE E   485
REMARK 465     THR E   486
REMARK 465     GLY E   487
REMARK 465     TRP E   488
REMARK 465     LYS E   489
REMARK 465     LYS E   490
REMARK 465     PHE E   491
REMARK 465     VAL E   492
REMARK 465     ALA E   493
REMARK 465     ASP E   494
REMARK 465     ARG E   495
REMARK 465     LYS E   496
REMARK 465     LYS E   497
REMARK 465     THR E   498
REMARK 465     SER E   499
REMARK 465     GLY E   500
REMARK 465     ILE E   501
REMARK 465     CYS E   502
REMARK 465     MET F     1
REMARK 465     VAL F     2
REMARK 465     LEU F     3
REMARK 465     SER F     4
REMARK 465     HIS F     5
REMARK 465     ALA F     6
REMARK 465     VAL F     7
REMARK 465     SER F     8
REMARK 465     GLU F     9
REMARK 465     SER F    10
REMARK 465     ASP F    11
REMARK 465     SER F   449
REMARK 465     ARG F   450
REMARK 465     VAL F   451
REMARK 465     ILE F   452
REMARK 465     HIS F   453
REMARK 465     LYS F   454
REMARK 465     ILE F   455
REMARK 465     SER F   456
REMARK 465     LEU F   457
REMARK 465     GLY F   458
REMARK 465     GLN F   459
REMARK 465     GLU F   460
REMARK 465     LYS F   461
REMARK 465     SER F   462
REMARK 465     GLU F   463
REMARK 465     SER F   464
REMARK 465     ASN F   465
REMARK 465     SER F   466
REMARK 465     ASP F   467
REMARK 465     ASN F   468
REMARK 465     LEU F   469
REMARK 465     MET F   470
REMARK 465     VAL F   471
REMARK 465     THR F   472
REMARK 465     VAL F   473
REMARK 465     LYS F   474
REMARK 465     LYS F   475
REMARK 465     SER F   476
REMARK 465     ASP F   477
REMARK 465     ILE F   478
REMARK 465     ASP F   479
REMARK 465     LYS F   480
REMARK 465     GLN F   481
REMARK 465     ARG F   482
REMARK 465     ASP F   483
REMARK 465     ILE F   484
REMARK 465     ILE F   485
REMARK 465     THR F   486
REMARK 465     GLY F   487
REMARK 465     TRP F   488
REMARK 465     LYS F   489
REMARK 465     LYS F   490
REMARK 465     PHE F   491
REMARK 465     VAL F   492
REMARK 465     ALA F   493
REMARK 465     ASP F   494
REMARK 465     ARG F   495
REMARK 465     LYS F   496
REMARK 465     LYS F   497
REMARK 465     THR F   498
REMARK 465     SER F   499
REMARK 465     GLY F   500
REMARK 465     ILE F   501
REMARK 465     CYS F   502
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    PHE A  30      -53.52   -122.22
REMARK 500    PRO A 111       86.87    -69.72
REMARK 500    GLU A 113     -159.55    -74.57
REMARK 500    ASN A 215       14.69   -148.56
REMARK 500    ASP A 238       58.00   -107.52
REMARK 500    ILE A 251      -51.04   -120.09
REMARK 500    TRP A 261      -15.10   -141.01
REMARK 500    ASP A 262     -146.70    -99.94
REMARK 500    ASN A 305       22.09   -152.54
REMARK 500    PHE A 318      -95.16   -125.05
REMARK 500    PRO A 374       87.37    -63.14
REMARK 500    ASP A 382       81.19     67.03
REMARK 500    SER A 383       42.98    -83.58
REMARK 500    SER A 384      -78.18    -79.60
REMARK 500    ASN A 410       56.98    -95.48
REMARK 500    GLN A 412        0.85    -67.31
REMARK 500    PHE B  30      -53.45   -121.62
REMARK 500    ASN B 215       15.19   -148.61
REMARK 500    ASP B 238       57.99   -106.97
REMARK 500    ALA B 245       40.34   -104.62
REMARK 500    TRP B 261      -15.45   -140.96
REMARK 500    ASP B 262     -146.55    -99.74
REMARK 500    ASN B 305       15.51   -150.97
REMARK 500    PHE B 318      -94.94   -125.08
REMARK 500    PRO B 374       87.09    -63.30
REMARK 500    ASP B 382       81.40     67.20
REMARK 500    SER B 383       42.86    -83.69
REMARK 500    SER B 384      -78.19    -79.57
REMARK 500    ASN B 410       59.07   -103.10
REMARK 500    PHE C  30      -53.73   -122.01
REMARK 500    PRO C 111       84.87    -69.66
REMARK 500    GLU C 113       55.80    -98.98
REMARK 500    GLU C 114      -72.04     68.59
REMARK 500    ASN C 215       14.86   -148.49
REMARK 500    ASP C 238       57.74   -107.63
REMARK 500    TRP C 261      -15.53   -141.31
REMARK 500    ASP C 262     -146.83    -99.99
REMARK 500    ASN C 305       26.82   -153.67
REMARK 500    PHE C 318      -95.05   -125.67
REMARK 500    PRO C 374       87.53    -63.39
REMARK 500    ASP C 382       81.34     66.97
REMARK 500    SER C 383       42.97    -83.61
REMARK 500    SER C 384      -78.36    -79.67
REMARK 500    ALA C 411       30.76   -158.23
REMARK 500    PHE D  30      -53.37   -122.24
REMARK 500    GLU D 113       46.49   -100.16
REMARK 500    GLU D 114      -55.24     72.98
REMARK 500    ASN D 215       15.10   -148.51
REMARK 500    ASP D 238       58.28   -107.34
REMARK 500    TRP D 261      -15.11   -141.23
REMARK 500
REMARK 500 THIS ENTRY HAS      84 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF  3HBX A    1   502  UNP    Q42521   DCE1_ARATH      12    513
DBREF  3HBX B    1   502  UNP    Q42521   DCE1_ARATH      12    513
DBREF  3HBX C    1   502  UNP    Q42521   DCE1_ARATH      12    513
DBREF  3HBX D    1   502  UNP    Q42521   DCE1_ARATH      12    513
DBREF  3HBX E    1   502  UNP    Q42521   DCE1_ARATH      12    513
DBREF  3HBX F    1   502  UNP    Q42521   DCE1_ARATH      12    513
SEQRES   1 A  502  MET VAL LEU SER HIS ALA VAL SER GLU SER ASP VAL SER
SEQRES   2 A  502  VAL HIS SER THR PHE ALA SER ARG TYR VAL ARG THR SER
SEQRES   3 A  502  LEU PRO ARG PHE LYS MET PRO GLU ASN SER ILE PRO LYS
SEQRES   4 A  502  GLU ALA ALA TYR GLN ILE ILE ASN ASP GLU LEU MET LEU
SEQRES   5 A  502  ASP GLY ASN PRO ARG LEU ASN LEU ALA SER PHE VAL THR
SEQRES   6 A  502  THR TRP MET GLU PRO GLU CYS ASP LYS LEU ILE MET SER
SEQRES   7 A  502  SER ILE ASN LYS ASN TYR VAL ASP MET ASP GLU TYR PRO
SEQRES   8 A  502  VAL THR THR GLU LEU GLN ASN ARG CYS VAL ASN MET ILE
SEQRES   9 A  502  ALA HIS LEU PHE ASN ALA PRO LEU GLU GLU ALA GLU THR
SEQRES  10 A  502  ALA VAL GLY VAL GLY THR VAL GLY SER SER GLU ALA ILE
SEQRES  11 A  502  MET LEU ALA GLY LEU ALA PHE LYS ARG LYS TRP GLN ASN
SEQRES  12 A  502  LYS ARG LYS ALA GLU GLY LYS PRO VAL ASP LYS PRO ASN
SEQRES  13 A  502  ILE VAL THR GLY ALA ASN VAL GLN VAL CYS TRP GLU LYS
SEQRES  14 A  502  PHE ALA ARG TYR PHE GLU VAL GLU LEU LYS GLU VAL LYS
SEQRES  15 A  502  LEU SER GLU GLY TYR TYR VAL MET ASP PRO GLN GLN ALA
SEQRES  16 A  502  VAL ASP MET VAL ASP GLU ASN THR ILE CYS VAL ALA ALA
SEQRES  17 A  502  ILE LEU GLY SER THR LEU ASN GLY GLU PHE GLU ASP VAL
SEQRES  18 A  502  LYS LEU LEU ASN ASP LEU LEU VAL GLU LYS ASN LYS GLU
SEQRES  19 A  502  THR GLY TRP ASP THR PRO ILE HIS VAL ASP ALA ALA SER
SEQRES  20 A  502  GLY GLY PHE ILE ALA PRO PHE LEU TYR PRO GLU LEU GLU
SEQRES  21 A  502  TRP ASP PHE ARG LEU PRO LEU VAL LYS SER ILE ASN VAL
SEQRES  22 A  502  SER GLY HIS LLP TYR GLY LEU VAL TYR ALA GLY ILE GLY
SEQRES  23 A  502  TRP VAL ILE TRP ARG ASN LYS GLU ASP LEU PRO GLU GLU
SEQRES  24 A  502  LEU ILE PHE HIS ILE ASN TYR LEU GLY ALA ASP GLN PRO
SEQRES  25 A  502  THR PHE THR LEU ASN PHE SER LYS GLY SER SER GLN VAL
SEQRES  26 A  502  ILE ALA GLN TYR TYR GLN LEU ILE ARG LEU GLY HIS GLU
SEQRES  27 A  502  GLY TYR ARG ASN VAL MET GLU ASN CYS ARG GLU ASN MET
SEQRES  28 A  502  ILE VAL LEU ARG GLU GLY LEU GLU LYS THR GLU ARG PHE
SEQRES  29 A  502  ASN ILE VAL SER LYS ASP GLU GLY VAL PRO LEU VAL ALA
SEQRES  30 A  502  PHE SER LEU LYS ASP SER SER CYS HIS THR GLU PHE GLU
SEQRES  31 A  502  ILE SER ASP MET LEU ARG ARG TYR GLY TRP ILE VAL PRO
SEQRES  32 A  502  ALA TYR THR MET PRO PRO ASN ALA GLN HIS ILE THR VAL
SEQRES  33 A  502  LEU ARG VAL VAL ILE ARG GLU ASP PHE SER ARG THR LEU
SEQRES  34 A  502  ALA GLU ARG LEU VAL ILE ASP ILE GLU LYS VAL MET ARG
SEQRES  35 A  502  GLU LEU ASP GLU LEU PRO SER ARG VAL ILE HIS LYS ILE
SEQRES  36 A  502  SER LEU GLY GLN GLU LYS SER GLU SER ASN SER ASP ASN
SEQRES  37 A  502  LEU MET VAL THR VAL LYS LYS SER ASP ILE ASP LYS GLN
SEQRES  38 A  502  ARG ASP ILE ILE THR GLY TRP LYS LYS PHE VAL ALA ASP
SEQRES  39 A  502  ARG LYS LYS THR SER GLY ILE CYS
SEQRES   1 B  502  MET VAL LEU SER HIS ALA VAL SER GLU SER ASP VAL SER
SEQRES   2 B  502  VAL HIS SER THR PHE ALA SER ARG TYR VAL ARG THR SER
SEQRES   3 B  502  LEU PRO ARG PHE LYS MET PRO GLU ASN SER ILE PRO LYS
SEQRES   4 B  502  GLU ALA ALA TYR GLN ILE ILE ASN ASP GLU LEU MET LEU
SEQRES   5 B  502  ASP GLY ASN PRO ARG LEU ASN LEU ALA SER PHE VAL THR
SEQRES   6 B  502  THR TRP MET GLU PRO GLU CYS ASP LYS LEU ILE MET SER
SEQRES   7 B  502  SER ILE ASN LYS ASN TYR VAL ASP MET ASP GLU TYR PRO
SEQRES   8 B  502  VAL THR THR GLU LEU GLN ASN ARG CYS VAL ASN MET ILE
SEQRES   9 B  502  ALA HIS LEU PHE ASN ALA PRO LEU GLU GLU ALA GLU THR
SEQRES  10 B  502  ALA VAL GLY VAL GLY THR VAL GLY SER SER GLU ALA ILE
SEQRES  11 B  502  MET LEU ALA GLY LEU ALA PHE LYS ARG LYS TRP GLN ASN
SEQRES  12 B  502  LYS ARG LYS ALA GLU GLY LYS PRO VAL ASP LYS PRO ASN
SEQRES  13 B  502  ILE VAL THR GLY ALA ASN VAL GLN VAL CYS TRP GLU LYS
SEQRES  14 B  502  PHE ALA ARG TYR PHE GLU VAL GLU LEU LYS GLU VAL LYS
SEQRES  15 B  502  LEU SER GLU GLY TYR TYR VAL MET ASP PRO GLN GLN ALA
SEQRES  16 B  502  VAL ASP MET VAL ASP GLU ASN THR ILE CYS VAL ALA ALA
SEQRES  17 B  502  ILE LEU GLY SER THR LEU ASN GLY GLU PHE GLU ASP VAL
SEQRES  18 B  502  LYS LEU LEU ASN ASP LEU LEU VAL GLU LYS ASN LYS GLU
SEQRES  19 B  502  THR GLY TRP ASP THR PRO ILE HIS VAL ASP ALA ALA SER
SEQRES  20 B  502  GLY GLY PHE ILE ALA PRO PHE LEU TYR PRO GLU LEU GLU
SEQRES  21 B  502  TRP ASP PHE ARG LEU PRO LEU VAL LYS SER ILE ASN VAL
SEQRES  22 B  502  SER GLY HIS LLP TYR GLY LEU VAL TYR ALA GLY ILE GLY
SEQRES  23 B  502  TRP VAL ILE TRP ARG ASN LYS GLU ASP LEU PRO GLU GLU
SEQRES  24 B  502  LEU ILE PHE HIS ILE ASN TYR LEU GLY ALA ASP GLN PRO
SEQRES  25 B  502  THR PHE THR LEU ASN PHE SER LYS GLY SER SER GLN VAL
SEQRES  26 B  502  ILE ALA GLN TYR TYR GLN LEU ILE ARG LEU GLY HIS GLU
SEQRES  27 B  502  GLY TYR ARG ASN VAL MET GLU ASN CYS ARG GLU ASN MET
SEQRES  28 B  502  ILE VAL LEU ARG GLU GLY LEU GLU LYS THR GLU ARG PHE
SEQRES  29 B  502  ASN ILE VAL SER LYS ASP GLU GLY VAL PRO LEU VAL ALA
SEQRES  30 B  502  PHE SER LEU LYS ASP SER SER CYS HIS THR GLU PHE GLU
SEQRES  31 B  502  ILE SER ASP MET LEU ARG ARG TYR GLY TRP ILE VAL PRO
SEQRES  32 B  502  ALA TYR THR MET PRO PRO ASN ALA GLN HIS ILE THR VAL
SEQRES  33 B  502  LEU ARG VAL VAL ILE ARG GLU ASP PHE SER ARG THR LEU
SEQRES  34 B  502  ALA GLU ARG LEU VAL ILE ASP ILE GLU LYS VAL MET ARG
SEQRES  35 B  502  GLU LEU ASP GLU LEU PRO SER ARG VAL ILE HIS LYS ILE
SEQRES  36 B  502  SER LEU GLY GLN GLU LYS SER GLU SER ASN SER ASP ASN
SEQRES  37 B  502  LEU MET VAL THR VAL LYS LYS SER ASP ILE ASP LYS GLN
SEQRES  38 B  502  ARG ASP ILE ILE THR GLY TRP LYS LYS PHE VAL ALA ASP
SEQRES  39 B  502  ARG LYS LYS THR SER GLY ILE CYS
SEQRES   1 C  502  MET VAL LEU SER HIS ALA VAL SER GLU SER ASP VAL SER
SEQRES   2 C  502  VAL HIS SER THR PHE ALA SER ARG TYR VAL ARG THR SER
SEQRES   3 C  502  LEU PRO ARG PHE LYS MET PRO GLU ASN SER ILE PRO LYS
SEQRES   4 C  502  GLU ALA ALA TYR GLN ILE ILE ASN ASP GLU LEU MET LEU
SEQRES   5 C  502  ASP GLY ASN PRO ARG LEU ASN LEU ALA SER PHE VAL THR
SEQRES   6 C  502  THR TRP MET GLU PRO GLU CYS ASP LYS LEU ILE MET SER
SEQRES   7 C  502  SER ILE ASN LYS ASN TYR VAL ASP MET ASP GLU TYR PRO
SEQRES   8 C  502  VAL THR THR GLU LEU GLN ASN ARG CYS VAL ASN MET ILE
SEQRES   9 C  502  ALA HIS LEU PHE ASN ALA PRO LEU GLU GLU ALA GLU THR
SEQRES  10 C  502  ALA VAL GLY VAL GLY THR VAL GLY SER SER GLU ALA ILE
SEQRES  11 C  502  MET LEU ALA GLY LEU ALA PHE LYS ARG LYS TRP GLN ASN
SEQRES  12 C  502  LYS ARG LYS ALA GLU GLY LYS PRO VAL ASP LYS PRO ASN
SEQRES  13 C  502  ILE VAL THR GLY ALA ASN VAL GLN VAL CYS TRP GLU LYS
SEQRES  14 C  502  PHE ALA ARG TYR PHE GLU VAL GLU LEU LYS GLU VAL LYS
SEQRES  15 C  502  LEU SER GLU GLY TYR TYR VAL MET ASP PRO GLN GLN ALA
SEQRES  16 C  502  VAL ASP MET VAL ASP GLU ASN THR ILE CYS VAL ALA ALA
SEQRES  17 C  502  ILE LEU GLY SER THR LEU ASN GLY GLU PHE GLU ASP VAL
SEQRES  18 C  502  LYS LEU LEU ASN ASP LEU LEU VAL GLU LYS ASN LYS GLU
SEQRES  19 C  502  THR GLY TRP ASP THR PRO ILE HIS VAL ASP ALA ALA SER
SEQRES  20 C  502  GLY GLY PHE ILE ALA PRO PHE LEU TYR PRO GLU LEU GLU
SEQRES  21 C  502  TRP ASP PHE ARG LEU PRO LEU VAL LYS SER ILE ASN VAL
SEQRES  22 C  502  SER GLY HIS LLP TYR GLY LEU VAL TYR ALA GLY ILE GLY
SEQRES  23 C  502  TRP VAL ILE TRP ARG ASN LYS GLU ASP LEU PRO GLU GLU
SEQRES  24 C  502  LEU ILE PHE HIS ILE ASN TYR LEU GLY ALA ASP GLN PRO
SEQRES  25 C  502  THR PHE THR LEU ASN PHE SER LYS GLY SER SER GLN VAL
SEQRES  26 C  502  ILE ALA GLN TYR TYR GLN LEU ILE ARG LEU GLY HIS GLU
SEQRES  27 C  502  GLY TYR ARG ASN VAL MET GLU ASN CYS ARG GLU ASN MET
SEQRES  28 C  502  ILE VAL LEU ARG GLU GLY LEU GLU LYS THR GLU ARG PHE
SEQRES  29 C  502  ASN ILE VAL SER LYS ASP GLU GLY VAL PRO LEU VAL ALA
SEQRES  30 C  502  PHE SER LEU LYS ASP SER SER CYS HIS THR GLU PHE GLU
SEQRES  31 C  502  ILE SER ASP MET LEU ARG ARG TYR GLY TRP ILE VAL PRO
SEQRES  32 C  502  ALA TYR THR MET PRO PRO ASN ALA GLN HIS ILE THR VAL
SEQRES  33 C  502  LEU ARG VAL VAL ILE ARG GLU ASP PHE SER ARG THR LEU
SEQRES  34 C  502  ALA GLU ARG LEU VAL ILE ASP ILE GLU LYS VAL MET ARG
SEQRES  35 C  502  GLU LEU ASP GLU LEU PRO SER ARG VAL ILE HIS LYS ILE
SEQRES  36 C  502  SER LEU GLY GLN GLU LYS SER GLU SER ASN SER ASP ASN
SEQRES  37 C  502  LEU MET VAL THR VAL LYS LYS SER ASP ILE ASP LYS GLN
SEQRES  38 C  502  ARG ASP ILE ILE THR GLY TRP LYS LYS PHE VAL ALA ASP
SEQRES  39 C  502  ARG LYS LYS THR SER GLY ILE CYS
SEQRES   1 D  502  MET VAL LEU SER HIS ALA VAL SER GLU SER ASP VAL SER
SEQRES   2 D  502  VAL HIS SER THR PHE ALA SER ARG TYR VAL ARG THR SER
SEQRES   3 D  502  LEU PRO ARG PHE LYS MET PRO GLU ASN SER ILE PRO LYS
SEQRES   4 D  502  GLU ALA ALA TYR GLN ILE ILE ASN ASP GLU LEU MET LEU
SEQRES   5 D  502  ASP GLY ASN PRO ARG LEU ASN LEU ALA SER PHE VAL THR
SEQRES   6 D  502  THR TRP MET GLU PRO GLU CYS ASP LYS LEU ILE MET SER
SEQRES   7 D  502  SER ILE ASN LYS ASN TYR VAL ASP MET ASP GLU TYR PRO
SEQRES   8 D  502  VAL THR THR GLU LEU GLN ASN ARG CYS VAL ASN MET ILE
SEQRES   9 D  502  ALA HIS LEU PHE ASN ALA PRO LEU GLU GLU ALA GLU THR
SEQRES  10 D  502  ALA VAL GLY VAL GLY THR VAL GLY SER SER GLU ALA ILE
SEQRES  11 D  502  MET LEU ALA GLY LEU ALA PHE LYS ARG LYS TRP GLN ASN
SEQRES  12 D  502  LYS ARG LYS ALA GLU GLY LYS PRO VAL ASP LYS PRO ASN
SEQRES  13 D  502  ILE VAL THR GLY ALA ASN VAL GLN VAL CYS TRP GLU LYS
SEQRES  14 D  502  PHE ALA ARG TYR PHE GLU VAL GLU LEU LYS GLU VAL LYS
SEQRES  15 D  502  LEU SER GLU GLY TYR TYR VAL MET ASP PRO GLN GLN ALA
SEQRES  16 D  502  VAL ASP MET VAL ASP GLU ASN THR ILE CYS VAL ALA ALA
SEQRES  17 D  502  ILE LEU GLY SER THR LEU ASN GLY GLU PHE GLU ASP VAL
SEQRES  18 D  502  LYS LEU LEU ASN ASP LEU LEU VAL GLU LYS ASN LYS GLU
SEQRES  19 D  502  THR GLY TRP ASP THR PRO ILE HIS VAL ASP ALA ALA SER
SEQRES  20 D  502  GLY GLY PHE ILE ALA PRO PHE LEU TYR PRO GLU LEU GLU
SEQRES  21 D  502  TRP ASP PHE ARG LEU PRO LEU VAL LYS SER ILE ASN VAL
SEQRES  22 D  502  SER GLY HIS LLP TYR GLY LEU VAL TYR ALA GLY ILE GLY
SEQRES  23 D  502  TRP VAL ILE TRP ARG ASN LYS GLU ASP LEU PRO GLU GLU
SEQRES  24 D  502  LEU ILE PHE HIS ILE ASN TYR LEU GLY ALA ASP GLN PRO
SEQRES  25 D  502  THR PHE THR LEU ASN PHE SER LYS GLY SER SER GLN VAL
SEQRES  26 D  502  ILE ALA GLN TYR TYR GLN LEU ILE ARG LEU GLY HIS GLU
SEQRES  27 D  502  GLY TYR ARG ASN VAL MET GLU ASN CYS ARG GLU ASN MET
SEQRES  28 D  502  ILE VAL LEU ARG GLU GLY LEU GLU LYS THR GLU ARG PHE
SEQRES  29 D  502  ASN ILE VAL SER LYS ASP GLU GLY VAL PRO LEU VAL ALA
SEQRES  30 D  502  PHE SER LEU LYS ASP SER SER CYS HIS THR GLU PHE GLU
SEQRES  31 D  502  ILE SER ASP MET LEU ARG ARG TYR GLY TRP ILE VAL PRO
SEQRES  32 D  502  ALA TYR THR MET PRO PRO ASN ALA GLN HIS ILE THR VAL
SEQRES  33 D  502  LEU ARG VAL VAL ILE ARG GLU ASP PHE SER ARG THR LEU
SEQRES  34 D  502  ALA GLU ARG LEU VAL ILE ASP ILE GLU LYS VAL MET ARG
SEQRES  35 D  502  GLU LEU ASP GLU LEU PRO SER ARG VAL ILE HIS LYS ILE
SEQRES  36 D  502  SER LEU GLY GLN GLU LYS SER GLU SER ASN SER ASP ASN
SEQRES  37 D  502  LEU MET VAL THR VAL LYS LYS SER ASP ILE ASP LYS GLN
SEQRES  38 D  502  ARG ASP ILE ILE THR GLY TRP LYS LYS PHE VAL ALA ASP
SEQRES  39 D  502  ARG LYS LYS THR SER GLY ILE CYS
SEQRES   1 E  502  MET VAL LEU SER HIS ALA VAL SER GLU SER ASP VAL SER
SEQRES   2 E  502  VAL HIS SER THR PHE ALA SER ARG TYR VAL ARG THR SER
SEQRES   3 E  502  LEU PRO ARG PHE LYS MET PRO GLU ASN SER ILE PRO LYS
SEQRES   4 E  502  GLU ALA ALA TYR GLN ILE ILE ASN ASP GLU LEU MET LEU
SEQRES   5 E  502  ASP GLY ASN PRO ARG LEU ASN LEU ALA SER PHE VAL THR
SEQRES   6 E  502  THR TRP MET GLU PRO GLU CYS ASP LYS LEU ILE MET SER
SEQRES   7 E  502  SER ILE ASN LYS ASN TYR VAL ASP MET ASP GLU TYR PRO
SEQRES   8 E  502  VAL THR THR GLU LEU GLN ASN ARG CYS VAL ASN MET ILE
SEQRES   9 E  502  ALA HIS LEU PHE ASN ALA PRO LEU GLU GLU ALA GLU THR
SEQRES  10 E  502  ALA VAL GLY VAL GLY THR VAL GLY SER SER GLU ALA ILE
SEQRES  11 E  502  MET LEU ALA GLY LEU ALA PHE LYS ARG LYS TRP GLN ASN
SEQRES  12 E  502  LYS ARG LYS ALA GLU GLY LYS PRO VAL ASP LYS PRO ASN
SEQRES  13 E  502  ILE VAL THR GLY ALA ASN VAL GLN VAL CYS TRP GLU LYS
SEQRES  14 E  502  PHE ALA ARG TYR PHE GLU VAL GLU LEU LYS GLU VAL LYS
SEQRES  15 E  502  LEU SER GLU GLY TYR TYR VAL MET ASP PRO GLN GLN ALA
SEQRES  16 E  502  VAL ASP MET VAL ASP GLU ASN THR ILE CYS VAL ALA ALA
SEQRES  17 E  502  ILE LEU GLY SER THR LEU ASN GLY GLU PHE GLU ASP VAL
SEQRES  18 E  502  LYS LEU LEU ASN ASP LEU LEU VAL GLU LYS ASN LYS GLU
SEQRES  19 E  502  THR GLY TRP ASP THR PRO ILE HIS VAL ASP ALA ALA SER
SEQRES  20 E  502  GLY GLY PHE ILE ALA PRO PHE LEU TYR PRO GLU LEU GLU
SEQRES  21 E  502  TRP ASP PHE ARG LEU PRO LEU VAL LYS SER ILE ASN VAL
SEQRES  22 E  502  SER GLY HIS LLP TYR GLY LEU VAL TYR ALA GLY ILE GLY
SEQRES  23 E  502  TRP VAL ILE TRP ARG ASN LYS GLU ASP LEU PRO GLU GLU
SEQRES  24 E  502  LEU ILE PHE HIS ILE ASN TYR LEU GLY ALA ASP GLN PRO
SEQRES  25 E  502  THR PHE THR LEU ASN PHE SER LYS GLY SER SER GLN VAL
SEQRES  26 E  502  ILE ALA GLN TYR TYR GLN LEU ILE ARG LEU GLY HIS GLU
SEQRES  27 E  502  GLY TYR ARG ASN VAL MET GLU ASN CYS ARG GLU ASN MET
SEQRES  28 E  502  ILE VAL LEU ARG GLU GLY LEU GLU LYS THR GLU ARG PHE
SEQRES  29 E  502  ASN ILE VAL SER LYS ASP GLU GLY VAL PRO LEU VAL ALA
SEQRES  30 E  502  PHE SER LEU LYS ASP SER SER CYS HIS THR GLU PHE GLU
SEQRES  31 E  502  ILE SER ASP MET LEU ARG ARG TYR GLY TRP ILE VAL PRO
SEQRES  32 E  502  ALA TYR THR MET PRO PRO ASN ALA GLN HIS ILE THR VAL
SEQRES  33 E  502  LEU ARG VAL VAL ILE ARG GLU ASP PHE SER ARG THR LEU
SEQRES  34 E  502  ALA GLU ARG LEU VAL ILE ASP ILE GLU LYS VAL MET ARG
SEQRES  35 E  502  GLU LEU ASP GLU LEU PRO SER ARG VAL ILE HIS LYS ILE
SEQRES  36 E  502  SER LEU GLY GLN GLU LYS SER GLU SER ASN SER ASP ASN
SEQRES  37 E  502  LEU MET VAL THR VAL LYS LYS SER ASP ILE ASP LYS GLN
SEQRES  38 E  502  ARG ASP ILE ILE THR GLY TRP LYS LYS PHE VAL ALA ASP
SEQRES  39 E  502  ARG LYS LYS THR SER GLY ILE CYS
SEQRES   1 F  502  MET VAL LEU SER HIS ALA VAL SER GLU SER ASP VAL SER
SEQRES   2 F  502  VAL HIS SER THR PHE ALA SER ARG TYR VAL ARG THR SER
SEQRES   3 F  502  LEU PRO ARG PHE LYS MET PRO GLU ASN SER ILE PRO LYS
SEQRES   4 F  502  GLU ALA ALA TYR GLN ILE ILE ASN ASP GLU LEU MET LEU
SEQRES   5 F  502  ASP GLY ASN PRO ARG LEU ASN LEU ALA SER PHE VAL THR
SEQRES   6 F  502  THR TRP MET GLU PRO GLU CYS ASP LYS LEU ILE MET SER
SEQRES   7 F  502  SER ILE ASN LYS ASN TYR VAL ASP MET ASP GLU TYR PRO
SEQRES   8 F  502  VAL THR THR GLU LEU GLN ASN ARG CYS VAL ASN MET ILE
SEQRES   9 F  502  ALA HIS LEU PHE ASN ALA PRO LEU GLU GLU ALA GLU THR
SEQRES  10 F  502  ALA VAL GLY VAL GLY THR VAL GLY SER SER GLU ALA ILE
SEQRES  11 F  502  MET LEU ALA GLY LEU ALA PHE LYS ARG LYS TRP GLN ASN
SEQRES  12 F  502  LYS ARG LYS ALA GLU GLY LYS PRO VAL ASP LYS PRO ASN
SEQRES  13 F  502  ILE VAL THR GLY ALA ASN VAL GLN VAL CYS TRP GLU LYS
SEQRES  14 F  502  PHE ALA ARG TYR PHE GLU VAL GLU LEU LYS GLU VAL LYS
SEQRES  15 F  502  LEU SER GLU GLY TYR TYR VAL MET ASP PRO GLN GLN ALA
SEQRES  16 F  502  VAL ASP MET VAL ASP GLU ASN THR ILE CYS VAL ALA ALA
SEQRES  17 F  502  ILE LEU GLY SER THR LEU ASN GLY GLU PHE GLU ASP VAL
SEQRES  18 F  502  LYS LEU LEU ASN ASP LEU LEU VAL GLU LYS ASN LYS GLU
SEQRES  19 F  502  THR GLY TRP ASP THR PRO ILE HIS VAL ASP ALA ALA SER
SEQRES  20 F  502  GLY GLY PHE ILE ALA PRO PHE LEU TYR PRO GLU LEU GLU
SEQRES  21 F  502  TRP ASP PHE ARG LEU PRO LEU VAL LYS SER ILE ASN VAL
SEQRES  22 F  502  SER GLY HIS LLP TYR GLY LEU VAL TYR ALA GLY ILE GLY
SEQRES  23 F  502  TRP VAL ILE TRP ARG ASN LYS GLU ASP LEU PRO GLU GLU
SEQRES  24 F  502  LEU ILE PHE HIS ILE ASN TYR LEU GLY ALA ASP GLN PRO
SEQRES  25 F  502  THR PHE THR LEU ASN PHE SER LYS GLY SER SER GLN VAL
SEQRES  26 F  502  ILE ALA GLN TYR TYR GLN LEU ILE ARG LEU GLY HIS GLU
SEQRES  27 F  502  GLY TYR ARG ASN VAL MET GLU ASN CYS ARG GLU ASN MET
SEQRES  28 F  502  ILE VAL LEU ARG GLU GLY LEU GLU LYS THR GLU ARG PHE
SEQRES  29 F  502  ASN ILE VAL SER LYS ASP GLU GLY VAL PRO LEU VAL ALA
SEQRES  30 F  502  PHE SER LEU LYS ASP SER SER CYS HIS THR GLU PHE GLU
SEQRES  31 F  502  ILE SER ASP MET LEU ARG ARG TYR GLY TRP ILE VAL PRO
SEQRES  32 F  502  ALA TYR THR MET PRO PRO ASN ALA GLN HIS ILE THR VAL
SEQRES  33 F  502  LEU ARG VAL VAL ILE ARG GLU ASP PHE SER ARG THR LEU
SEQRES  34 F  502  ALA GLU ARG LEU VAL ILE ASP ILE GLU LYS VAL MET ARG
SEQRES  35 F  502  GLU LEU ASP GLU LEU PRO SER ARG VAL ILE HIS LYS ILE
SEQRES  36 F  502  SER LEU GLY GLN GLU LYS SER GLU SER ASN SER ASP ASN
SEQRES  37 F  502  LEU MET VAL THR VAL LYS LYS SER ASP ILE ASP LYS GLN
SEQRES  38 F  502  ARG ASP ILE ILE THR GLY TRP LYS LYS PHE VAL ALA ASP
SEQRES  39 F  502  ARG LYS LYS THR SER GLY ILE CYS
MODRES 3HBX LLP A  277  LYS
MODRES 3HBX LLP B  277  LYS
MODRES 3HBX LLP C  277  LYS
MODRES 3HBX LLP D  277  LYS
MODRES 3HBX LLP E  277  LYS
MODRES 3HBX LLP F  277  LYS
HET    LLP  A 277      24
HET    LLP  B 277      24
HET    LLP  C 277      24
HET    LLP  D 277      24
HET    LLP  E 277      24
HET    LLP  F 277      24
HETNAM     LLP 2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-
HETNAM   2 LLP  PYRIDIN-4-YLMETHANE)
HETSYN     LLP N'-PYRIDOXYL-LYSINE-5'-MONOPHOSPHATE
FORMUL   1  LLP    6(C14 H24 N3 O7 P)
FORMUL   7  HOH   *314(H2 O)
HELIX    1   1 ARG A   21  THR A   25  5                                   5
HELIX    2   2 PRO A   38  LEU A   50  1                                  13
HELIX    3   3 MET A   51  ASP A   53  5                                   3
HELIX    4   4 ASN A   55  ASN A   59  5                                   5
HELIX    5   5 GLU A   69  SER A   79  1                                  11
HELIX    6   6 TYR A   90  PHE A  108  1                                  19
HELIX    7   7 GLY A  125  GLU A  148  1                                  24
HELIX    8   8 GLN A  164  PHE A  174  1                                  11
HELIX    9   9 ASP A  191  VAL A  199  1                                   9
HELIX   10  10 ASP A  220  GLY A  236  1                                  17
HELIX   11  11 SER A  247  PHE A  250  5                                   4
HELIX   12  12 ILE A  251  TYR A  256  1                                   6
HELIX   13  13 ASN A  292  LEU A  296  5                                   5
HELIX   14  14 PRO A  297  ILE A  301  5                                   5
HELIX   15  15 SER A  322  LYS A  360  1                                  39
HELIX   16  16 THR A  387  ARG A  397  1                                  11
HELIX   17  17 SER A  426  GLU A  446  1                                  21
HELIX   18  18 ARG B   21  THR B   25  5                                   5
HELIX   19  19 PRO B   38  LEU B   50  1                                  13
HELIX   20  20 MET B   51  ASP B   53  5                                   3
HELIX   21  21 ASN B   55  ASN B   59  5                                   5
HELIX   22  22 GLU B   69  SER B   79  1                                  11
HELIX   23  23 TYR B   90  PHE B  108  1                                  19
HELIX   24  24 GLY B  125  GLU B  148  1                                  24
HELIX   25  25 GLN B  164  PHE B  174  1                                  11
HELIX   26  26 ASP B  191  VAL B  199  1                                   9
HELIX   27  27 ASP B  220  GLY B  236  1                                  17
HELIX   28  28 SER B  247  PHE B  250  5                                   4
HELIX   29  29 ILE B  251  TYR B  256  1                                   6
HELIX   30  30 ASN B  292  LEU B  296  5                                   5
HELIX   31  31 PRO B  297  ILE B  301  5                                   5
HELIX   32  32 SER B  322  LYS B  360  1                                  39
HELIX   33  33 THR B  387  ARG B  397  1                                  11
HELIX   34  34 SER B  426  GLU B  446  1                                  21
HELIX   35  35 ARG C   21  THR C   25  5                                   5
HELIX   36  36 PRO C   38  LEU C   50  1                                  13
HELIX   37  37 MET C   51  ASP C   53  5                                   3
HELIX   38  38 ASN C   55  ASN C   59  5                                   5
HELIX   39  39 GLU C   69  SER C   79  1                                  11
HELIX   40  40 TYR C   90  PHE C  108  1                                  19
HELIX   41  41 GLY C  125  GLU C  148  1                                  24
HELIX   42  42 GLN C  164  PHE C  174  1                                  11
HELIX   43  43 ASP C  191  VAL C  199  1                                   9
HELIX   44  44 ASP C  220  GLY C  236  1                                  17
HELIX   45  45 SER C  247  PHE C  250  5                                   4
HELIX   46  46 ILE C  251  TYR C  256  1                                   6
HELIX   47  47 ASN C  292  LEU C  296  5                                   5
HELIX   48  48 PRO C  297  ILE C  301  5                                   5
HELIX   49  49 SER C  322  LYS C  360  1                                  39
HELIX   50  50 THR C  387  ARG C  397  1                                  11
HELIX   51  51 SER C  426  GLU C  446  1                                  21
HELIX   52  52 ARG D   21  THR D   25  5                                   5
HELIX   53  53 PRO D   38  LEU D   50  1                                  13
HELIX   54  54 MET D   51  ASP D   53  5                                   3
HELIX   55  55 ASN D   55  ASN D   59  5                                   5
HELIX   56  56 GLU D   69  SER D   79  1                                  11
HELIX   57  57 TYR D   90  PHE D  108  1                                  19
HELIX   58  58 GLY D  125  GLU D  148  1                                  24
HELIX   59  59 GLN D  164  PHE D  174  1                                  11
HELIX   60  60 ASP D  191  VAL D  199  1                                   9
HELIX   61  61 ASP D  220  GLY D  236  1                                  17
HELIX   62  62 SER D  247  PHE D  250  5                                   4
HELIX   63  63 ILE D  251  TYR D  256  1                                   6
HELIX   64  64 ASN D  292  LEU D  296  5                                   5
HELIX   65  65 PRO D  297  ILE D  301  5                                   5
HELIX   66  66 SER D  322  LYS D  360  1                                  39
HELIX   67  67 THR D  387  ARG D  397  1                                  11
HELIX   68  68 SER D  426  GLU D  446  1                                  21
HELIX   69  69 ARG E   21  THR E   25  5                                   5
HELIX   70  70 PRO E   38  LEU E   50  1                                  13
HELIX   71  71 MET E   51  ASP E   53  5                                   3
HELIX   72  72 ASN E   55  ASN E   59  5                                   5
HELIX   73  73 GLU E   69  SER E   79  1                                  11
HELIX   74  74 TYR E   90  PHE E  108  1                                  19
HELIX   75  75 GLY E  125  GLU E  148  1                                  24
HELIX   76  76 GLN E  164  PHE E  174  1                                  11
HELIX   77  77 ASP E  191  VAL E  199  1                                   9
HELIX   78  78 ASP E  220  GLY E  236  1                                  17
HELIX   79  79 SER E  247  PHE E  250  5                                   4
HELIX   80  80 ILE E  251  TYR E  256  1                                   6
HELIX   81  81 ASN E  292  LEU E  296  5                                   5
HELIX   82  82 PRO E  297  ILE E  301  5                                   5
HELIX   83  83 SER E  322  LYS E  360  1                                  39
HELIX   84  84 THR E  387  ARG E  397  1                                  11
HELIX   85  85 SER E  426  GLU E  446  1                                  21
HELIX   86  86 ARG F   21  THR F   25  5                                   5
HELIX   87  87 PRO F   38  LEU F   50  1                                  13
HELIX   88  88 MET F   51  ASP F   53  5                                   3
HELIX   89  89 ASN F   55  ASN F   59  5                                   5
HELIX   90  90 GLU F   69  SER F   79  1                                  11
HELIX   91  91 TYR F   90  PHE F  108  1                                  19
HELIX   92  92 GLY F  125  GLU F  148  1                                  24
HELIX   93  93 GLN F  164  PHE F  174  1                                  11
HELIX   94  94 ASP F  191  VAL F  199  1                                   9
HELIX   95  95 ASP F  220  GLY F  236  1                                  17
HELIX   96  96 SER F  247  PHE F  250  5                                   4
HELIX   97  97 ILE F  251  TYR F  256  1                                   6
HELIX   98  98 ASN F  292  LEU F  296  5                                   5
HELIX   99  99 PRO F  297  ILE F  301  5                                   5
HELIX  100 100 SER F  322  LYS F  360  1                                  39
HELIX  101 101 THR F  387  ARG F  397  1                                  11
HELIX  102 102 SER F  426  GLU F  446  1                                  21
SHEET    1   A 7 VAL A 119  THR A 123  0
SHEET    2   A 7 GLY A 286  TRP A 290 -1  O  GLY A 286   N  THR A 123
SHEET    3   A 7 VAL A 268  SER A 274 -1  N  ILE A 271   O  ILE A 289
SHEET    4   A 7 ILE A 241  ASP A 244  1  N  ILE A 241   O  LYS A 269
SHEET    5   A 7 THR A 203  ILE A 209  1  N  ALA A 208   O  ASP A 244
SHEET    6   A 7 ASN A 156  GLY A 160  1  N  ASN A 156   O  ILE A 204
SHEET    7   A 7 GLU A 177  VAL A 181  1  O  LYS A 179   N  ILE A 157
SHEET    1   B 2 PHE A 302  ILE A 304  0
SHEET    2   B 2 GLN A 311  THR A 313 -1  O  THR A 313   N  PHE A 302
SHEET    1   C 4 PHE A 364  ILE A 366  0
SHEET    2   C 4 LEU A 375  LEU A 380 -1  O  SER A 379   N  ASN A 365
SHEET    3   C 4 THR A 415  VAL A 420 -1  O  LEU A 417   N  PHE A 378
SHEET    4   C 4 ALA A 404  THR A 406 -1  N  TYR A 405   O  VAL A 416
SHEET    1   D 7 VAL B 119  THR B 123  0
SHEET    2   D 7 GLY B 286  TRP B 290 -1  O  GLY B 286   N  THR B 123
SHEET    3   D 7 VAL B 268  SER B 274 -1  N  ILE B 271   O  ILE B 289
SHEET    4   D 7 ILE B 241  ASP B 244  1  N  ILE B 241   O  LYS B 269
SHEET    5   D 7 THR B 203  ILE B 209  1  N  ALA B 208   O  ASP B 244
SHEET    6   D 7 ASN B 156  GLY B 160  1  N  ASN B 156   O  ILE B 204
SHEET    7   D 7 GLU B 177  VAL B 181  1  O  LYS B 179   N  ILE B 157
SHEET    1   E 2 PHE B 302  ILE B 304  0
SHEET    2   E 2 GLN B 311  THR B 313 -1  O  THR B 313   N  PHE B 302
SHEET    1   F 4 PHE B 364  ILE B 366  0
SHEET    2   F 4 LEU B 375  LEU B 380 -1  O  SER B 379   N  ASN B 365
SHEET    3   F 4 THR B 415  VAL B 420 -1  O  LEU B 417   N  PHE B 378
SHEET    4   F 4 ALA B 404  THR B 406 -1  N  TYR B 405   O  VAL B 416
SHEET    1   G 7 VAL C 119  THR C 123  0
SHEET    2   G 7 GLY C 286  TRP C 290 -1  O  TRP C 290   N  VAL C 119
SHEET    3   G 7 VAL C 268  SER C 274 -1  N  ILE C 271   O  ILE C 289
SHEET    4   G 7 ILE C 241  ASP C 244  1  N  ILE C 241   O  LYS C 269
SHEET    5   G 7 THR C 203  ILE C 209  1  N  ALA C 208   O  ASP C 244
SHEET    6   G 7 ASN C 156  GLY C 160  1  N  ASN C 156   O  ILE C 204
SHEET    7   G 7 GLU C 177  VAL C 181  1  O  LYS C 179   N  ILE C 157
SHEET    1   H 2 PHE C 302  ILE C 304  0
SHEET    2   H 2 GLN C 311  THR C 313 -1  O  THR C 313   N  PHE C 302
SHEET    1   I 4 PHE C 364  ILE C 366  0
SHEET    2   I 4 LEU C 375  LEU C 380 -1  O  SER C 379   N  ASN C 365
SHEET    3   I 4 THR C 415  VAL C 420 -1  O  LEU C 417   N  PHE C 378
SHEET    4   I 4 ALA C 404  THR C 406 -1  N  TYR C 405   O  VAL C 416
SHEET    1   J 7 VAL D 119  THR D 123  0
SHEET    2   J 7 GLY D 286  TRP D 290 -1  O  GLY D 286   N  THR D 123
SHEET    3   J 7 VAL D 268  SER D 274 -1  N  ILE D 271   O  ILE D 289
SHEET    4   J 7 ILE D 241  ASP D 244  1  N  ILE D 241   O  LYS D 269
SHEET    5   J 7 THR D 203  ILE D 209  1  N  ALA D 208   O  ASP D 244
SHEET    6   J 7 ASN D 156  GLY D 160  1  N  ASN D 156   O  ILE D 204
SHEET    7   J 7 GLU D 177  VAL D 181  1  O  LYS D 179   N  ILE D 157
SHEET    1   K 2 PHE D 302  ILE D 304  0
SHEET    2   K 2 GLN D 311  THR D 313 -1  O  THR D 313   N  PHE D 302
SHEET    1   L 4 PHE D 364  ILE D 366  0
SHEET    2   L 4 LEU D 375  LEU D 380 -1  O  SER D 379   N  ASN D 365
SHEET    3   L 4 THR D 415  VAL D 420 -1  O  LEU D 417   N  PHE D 378
SHEET    4   L 4 ALA D 404  THR D 406 -1  N  TYR D 405   O  VAL D 416
SHEET    1   M 7 VAL E 119  THR E 123  0
SHEET    2   M 7 GLY E 286  TRP E 290 -1  O  GLY E 286   N  THR E 123
SHEET    3   M 7 VAL E 268  SER E 274 -1  N  ILE E 271   O  ILE E 289
SHEET    4   M 7 ILE E 241  ASP E 244  1  N  ILE E 241   O  LYS E 269
SHEET    5   M 7 THR E 203  ILE E 209  1  N  ALA E 208   O  ASP E 244
SHEET    6   M 7 ASN E 156  GLY E 160  1  N  ASN E 156   O  ILE E 204
SHEET    7   M 7 GLU E 177  VAL E 181  1  O  LYS E 179   N  ILE E 157
SHEET    1   N 2 PHE E 302  ILE E 304  0
SHEET    2   N 2 GLN E 311  THR E 313 -1  O  THR E 313   N  PHE E 302
SHEET    1   O 4 PHE E 364  ILE E 366  0
SHEET    2   O 4 LEU E 375  LEU E 380 -1  O  SER E 379   N  ASN E 365
SHEET    3   O 4 THR E 415  VAL E 420 -1  O  LEU E 417   N  PHE E 378
SHEET    4   O 4 ALA E 404  THR E 406 -1  N  TYR E 405   O  VAL E 416
SHEET    1   P 7 VAL F 119  THR F 123  0
SHEET    2   P 7 GLY F 286  TRP F 290 -1  O  GLY F 286   N  THR F 123
SHEET    3   P 7 VAL F 268  SER F 274 -1  N  ILE F 271   O  ILE F 289
SHEET    4   P 7 ILE F 241  ASP F 244  1  N  ILE F 241   O  LYS F 269
SHEET    5   P 7 THR F 203  ILE F 209  1  N  ALA F 208   O  ASP F 244
SHEET    6   P 7 ASN F 156  GLY F 160  1  N  ASN F 156   O  ILE F 204
SHEET    7   P 7 GLU F 177  VAL F 181  1  O  LYS F 179   N  ILE F 157
SHEET    1   Q 2 PHE F 302  ILE F 304  0
SHEET    2   Q 2 GLN F 311  THR F 313 -1  O  THR F 313   N  PHE F 302
SHEET    1   R 4 PHE F 364  ILE F 366  0
SHEET    2   R 4 LEU F 375  LEU F 380 -1  O  SER F 379   N  ASN F 365
SHEET    3   R 4 THR F 415  VAL F 420 -1  O  LEU F 417   N  PHE F 378
SHEET    4   R 4 ALA F 404  THR F 406 -1  N  TYR F 405   O  VAL F 416
LINK         C   HIS A 276                 N   LLP A 277     1555   1555  1.33
LINK         C   LLP A 277                 N   TYR A 278     1555   1555  1.33
LINK         C   HIS B 276                 N   LLP B 277     1555   1555  1.33
LINK         C   LLP B 277                 N   TYR B 278     1555   1555  1.33
LINK         C   HIS C 276                 N   LLP C 277     1555   1555  1.33
LINK         C   LLP C 277                 N   TYR C 278     1555   1555  1.33
LINK         C   HIS D 276                 N   LLP D 277     1555   1555  1.33
LINK         C   LLP D 277                 N   TYR D 278     1555   1555  1.33
LINK         C   HIS E 276                 N   LLP E 277     1555   1555  1.33
LINK         C   LLP E 277                 N   TYR E 278     1555   1555  1.33
LINK         C   HIS F 276                 N   LLP F 277     1555   1555  1.33
LINK         C   LLP F 277                 N   TYR F 278     1555   1555  1.33
CISPEP   1 GLU A  114    ALA A  115          0         0.13
CISPEP   2 PRO A  409    ASN A  410          0        -0.17
CISPEP   3 PRO B  409    ASN B  410          0         0.93
CISPEP   4 PRO C  409    ASN C  410          0         0.17
CISPEP   5 PRO D  409    ASN D  410          0         0.80
CISPEP   6 PRO E  409    ASN E  410          0        -0.33
CISPEP   7 PRO F  409    ASN F  410          0         0.44
CRYST1  118.098  118.098  200.576  90.00  90.00 120.00 P 32         18
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      0.008468  0.004889  0.000000        0.00000
SCALE2      0.000000  0.009777  0.000000        0.00000
SCALE3      0.000000  0.000000  0.004986        0.00000
MTRIX1   1  0.318302  0.947977  0.004831      -54.36670    1
MTRIX2   1  0.947233 -0.317841 -0.041559       75.45140    1
MTRIX3   1 -0.037861  0.017805 -0.999124       -1.46108    1
MTRIX1   2 -0.503232  0.864004  0.015946      -48.50860    1
MTRIX2   2 -0.864137 -0.503243 -0.003575       88.45970    1
MTRIX3   2  0.004936 -0.015578  0.999866        1.23684    1
MTRIX1   3 -0.979238 -0.202103  0.015704       13.92040    1
MTRIX2   3 -0.202182  0.979341 -0.003624        1.35622    1
MTRIX3   3 -0.014647 -0.006724 -0.999870        0.68996    1
MTRIX1   4 -0.497458 -0.867314  0.017358       52.35720    1
MTRIX2   4  0.867356 -0.497632 -0.007499       86.29350    1
MTRIX3   4  0.015142  0.011325  0.999821       -0.80090    1
MTRIX1   5  0.667823 -0.744318  0.001814       43.75040    1
MTRIX2   5 -0.744144 -0.667715 -0.020149       97.96570    1
MTRIX3   5  0.016208  0.012106 -0.999795       -1.02356    1
MTRIX1   6  0.317723  0.948059 -0.015386      -54.46810    1
MTRIX2   6  0.948068 -0.317896 -0.010433       75.69090    1
MTRIX3   6 -0.014782 -0.011273 -0.999827        0.62471    1
MTRIX1   7 -0.500290  0.865677  0.017686      -48.81490    1
MTRIX2   7 -0.865653 -0.500512  0.011547       88.35250    1
MTRIX3   7  0.018848 -0.009533  0.999777        0.40187    1
MTRIX1   8 -0.979966 -0.199142  0.002942       13.77390    1
MTRIX2   8 -0.199138  0.979970  0.001718        1.29489    1
MTRIX3   8 -0.003225  0.001098 -0.999994        0.05058    1
MTRIX1   9 -0.499153 -0.866332  0.017746       52.19540    1
MTRIX2   9  0.866352 -0.499351 -0.009100       86.47640    1
MTRIX3   9  0.016745  0.010832  0.999801       -0.71221    1
MTRIX1  10  0.664267 -0.747260 -0.018753       44.00390    1
MTRIX2  10 -0.747290 -0.664464  0.006800       97.82600    1
MTRIX3  10 -0.017542  0.009497 -0.999801       -0.54785    1
      
PROCHECK
Go to PROCHECK summary
 References