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PDBsum entry 3ly6

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Transferase PDB id
3ly6
Jmol
Contents
Protein chain
683 a.a.
Ligands
ATP ×3
HEADER    TRANSFERASE                             26-FEB-10   3LY6
TITLE     CRYSTAL STRUCTURE OF HUMAN TRANSGLUTAMINASE 2 COMPLEX WITH ADENOSINE
TITLE    2 5' TRIPHOSPHATE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE 2;
COMPND   3 CHAIN: A, B, C;
COMPND   4 SYNONYM: TGM2, TISSUE TRANSGLUTAMINASE, TGASE C, TGC, TG(C),
COMPND   5 TRANSGLUTAMINASE-2, TGASE-H;
COMPND   6 EC: 2.3.2.13;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: TGM2;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET32 (NOVAGEN)
KEYWDS    TRANSGLUTAMINASE, ACYLTRANSFERASE, DIABETES MELLITUS, DISEASE
KEYWDS   2 MUTATION, METAL-BINDING, PHOSPHOPROTEIN, TRANSFERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    B.G.HAN,B.I.LEE
REVDAT   1   18-AUG-10 3LY6    0
JRNL        AUTH   B.G.HAN,J.W.CHO,Y.D.CHO,K.C.JEONG,S.Y.KIM,B.I.LEE
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN TRANSGLUTAMINASE 2 IN COMPLEX
JRNL        TITL 2 WITH ADENOSINE TRIPHOSPHATE
JRNL        REF    INT.J.BIOL.MACROMOL.          V.  47   190 2010
JRNL        REFN                   ISSN 0141-8130
JRNL        PMID   20450932
JRNL        DOI    10.1016/J.IJBIOMAC.2010.04.023
REMARK   2
REMARK   2 RESOLUTION.    3.14 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.2
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.14
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 38955
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.233
REMARK   3   FREE R VALUE                     : 0.297
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 3927
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 16203
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 93
REMARK   3   SOLVENT ATOMS            : 0
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : NULL
REMARK   3   BOND ANGLES            (DEGREES) : NULL
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : NULL
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 3LY6 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-MAR-10.
REMARK 100 THE RCSB ID CODE IS RCSB057877.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 10-JAN-10
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.6
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : PAL/PLS
REMARK 200  BEAMLINE                       : 6C1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4R
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41905
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.140
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.14
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.26
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.7
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1KV3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 51.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM MES, 200MM NACL, 50MM MGCL2, 6-8%
REMARK 280  PEG3350,5MM DTT, 20% GLYCEROL, PH 6.6, VAPOR DIFFUSION, HANGING
REMARK 280  DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -X,Y,-Z+1/2
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   X+1/2,Y+1/2,Z
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
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       82.97800
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       82.97800
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       67.08750
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      107.87950
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       67.08750
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      107.87950
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       82.97800
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       67.08750
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      107.87950
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       82.97800
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       67.08750
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      107.87950
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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     ALA A     2
REMARK 465     GLU A     3
REMARK 465     GLU A    84
REMARK 465     GLU A    85
REMARK 465     GLU A   689
REMARK 465     HIS A   690
REMARK 465     HIS A   691
REMARK 465     HIS A   692
REMARK 465     HIS A   693
REMARK 465     HIS A   694
REMARK 465     HIS A   695
REMARK 465     HIS A   696
REMARK 465     HIS A   697
REMARK 465     MET B     1
REMARK 465     ALA B     2
REMARK 465     GLU B     3
REMARK 465     GLU B    84
REMARK 465     GLU B    85
REMARK 465     GLU B   689
REMARK 465     HIS B   690
REMARK 465     HIS B   691
REMARK 465     HIS B   692
REMARK 465     HIS B   693
REMARK 465     HIS B   694
REMARK 465     HIS B   695
REMARK 465     HIS B   696
REMARK 465     HIS B   697
REMARK 465     MET C     1
REMARK 465     ALA C     2
REMARK 465     GLU C     3
REMARK 465     GLU C    84
REMARK 465     GLU C    85
REMARK 465     GLU C   689
REMARK 465     HIS C   690
REMARK 465     HIS C   691
REMARK 465     HIS C   692
REMARK 465     HIS C   693
REMARK 465     HIS C   694
REMARK 465     HIS C   695
REMARK 465     HIS C   696
REMARK 465     HIS C   697
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    ASP A  87   N   -  CA  -  C   ANGL. DEV. =  16.7 DEGREES
REMARK 500    ASP B  87   N   -  CA  -  C   ANGL. DEV. =  16.2 DEGREES
REMARK 500    ASP C  87   N   -  CA  -  C   ANGL. DEV. =  17.5 DEGREES
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    LEU A   7      -92.76    -83.27
REMARK 500    GLU A   8       93.29     79.20
REMARK 500    CYS A  10      173.26    164.79
REMARK 500    ASP A  11       77.90   -177.79
REMARK 500    LEU A  14      157.56     53.61
REMARK 500    THR A  23       24.95   -141.81
REMARK 500    LYS A  30      120.06    146.77
REMARK 500    ARG A  35      155.79    -48.31
REMARK 500    LEU A  41       86.13   -170.13
REMARK 500    ASN A  49     -154.10    -87.15
REMARK 500    SER A  53      -84.09    -49.71
REMARK 500    THR A  63      -66.55   -129.84
REMARK 500    PRO A  67      179.70    -46.14
REMARK 500    SER A  68      135.67    174.90
REMARK 500    ALA A  82     -102.00    -94.63
REMARK 500    ASP A  87      -57.83     37.23
REMARK 500    ASP A  94      176.50    179.28
REMARK 500    GLN A  95      124.52    176.03
REMARK 500    ASP A  97      -85.12     72.99
REMARK 500    CYS A  98      -12.75   -147.70
REMARK 500    ASN A 109       13.71   -154.19
REMARK 500    THR A 123       25.32    -72.06
REMARK 500    TYR A 125      -22.97   -146.60
REMARK 500    GLN A 126      -84.41    -96.15
REMARK 500    GLN A 169     -151.89   -126.35
REMARK 500    PHE A 174       74.83   -154.49
REMARK 500    ASP A 187      131.70    -38.33
REMARK 500    PRO A 201      -71.09    -41.67
REMARK 500    LYS A 202      -33.96    -31.80
REMARK 500    ASN A 206       80.67   -178.39
REMARK 500    ARG A 214       20.54    -70.95
REMARK 500    ASN A 229      -73.10   -134.75
REMARK 500    CYS A 230      108.17    -28.96
REMARK 500    ASN A 231       84.78     70.44
REMARK 500    GLN A 234       44.74   -170.28
REMARK 500    ARG A 240      125.10   -172.09
REMARK 500    ASN A 243       34.19     89.22
REMARK 500    ASP A 247       34.71    -98.53
REMARK 500    HIS A 267       41.70   -107.57
REMARK 500    ARG A 271      128.08    -39.14
REMARK 500    LYS A 273       93.80    -60.68
REMARK 500    TYR A 274      124.51     71.48
REMARK 500    ASP A 306      -14.66     68.06
REMARK 500    SER A 309       -1.52    114.57
REMARK 500    LEU A 311        5.66    -67.60
REMARK 500    GLU A 319       31.32    -75.26
REMARK 500    ILE A 323       92.26    -40.85
REMARK 500    ASP A 326      154.94    109.35
REMARK 500    LYS A 327      -17.06     63.89
REMARK 500    ARG A 344       75.26   -117.63
REMARK 500
REMARK 500 THIS ENTRY HAS     227 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    ASP A  87        22.3      L          L   OUTSIDE RANGE
REMARK 500    ASP B  87        22.1      L          L   OUTSIDE RANGE
REMARK 500    ASP C  87        22.4      L          L   OUTSIDE RANGE
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 ATP A 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP C 702
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THIS SEQUENCE IS FROM GENBANK, AAA63261.
REMARK 999 SEE REFERENCE 1 IN UNP DATABASE, P21980.
DBREF  3LY6 A    1   687  UNP    P21980   TGM2_HUMAN       1    687
DBREF  3LY6 B    1   687  UNP    P21980   TGM2_HUMAN       1    687
DBREF  3LY6 C    1   687  UNP    P21980   TGM2_HUMAN       1    687
SEQADV 3LY6 GLY A  224  UNP  P21980    VAL   224 SEE REMARK 999
SEQADV 3LY6 LEU A  688  UNP  P21980              EXPRESSION TAG
SEQADV 3LY6 GLU A  689  UNP  P21980              EXPRESSION TAG
SEQADV 3LY6 HIS A  690  UNP  P21980              EXPRESSION TAG
SEQADV 3LY6 HIS A  691  UNP  P21980              EXPRESSION TAG
SEQADV 3LY6 HIS A  692  UNP  P21980              EXPRESSION TAG
SEQADV 3LY6 HIS A  693  UNP  P21980              EXPRESSION TAG
SEQADV 3LY6 HIS A  694  UNP  P21980              EXPRESSION TAG
SEQADV 3LY6 HIS A  695  UNP  P21980              EXPRESSION TAG
SEQADV 3LY6 HIS A  696  UNP  P21980              EXPRESSION TAG
SEQADV 3LY6 HIS A  697  UNP  P21980              EXPRESSION TAG
SEQADV 3LY6 GLY B  224  UNP  P21980    VAL   224 SEE REMARK 999
SEQADV 3LY6 LEU B  688  UNP  P21980              EXPRESSION TAG
SEQADV 3LY6 GLU B  689  UNP  P21980              EXPRESSION TAG
SEQADV 3LY6 HIS B  690  UNP  P21980              EXPRESSION TAG
SEQADV 3LY6 HIS B  691  UNP  P21980              EXPRESSION TAG
SEQADV 3LY6 HIS B  692  UNP  P21980              EXPRESSION TAG
SEQADV 3LY6 HIS B  693  UNP  P21980              EXPRESSION TAG
SEQADV 3LY6 HIS B  694  UNP  P21980              EXPRESSION TAG
SEQADV 3LY6 HIS B  695  UNP  P21980              EXPRESSION TAG
SEQADV 3LY6 HIS B  696  UNP  P21980              EXPRESSION TAG
SEQADV 3LY6 HIS B  697  UNP  P21980              EXPRESSION TAG
SEQADV 3LY6 GLY C  224  UNP  P21980    VAL   224 SEE REMARK 999
SEQADV 3LY6 LEU C  688  UNP  P21980              EXPRESSION TAG
SEQADV 3LY6 GLU C  689  UNP  P21980              EXPRESSION TAG
SEQADV 3LY6 HIS C  690  UNP  P21980              EXPRESSION TAG
SEQADV 3LY6 HIS C  691  UNP  P21980              EXPRESSION TAG
SEQADV 3LY6 HIS C  692  UNP  P21980              EXPRESSION TAG
SEQADV 3LY6 HIS C  693  UNP  P21980              EXPRESSION TAG
SEQADV 3LY6 HIS C  694  UNP  P21980              EXPRESSION TAG
SEQADV 3LY6 HIS C  695  UNP  P21980              EXPRESSION TAG
SEQADV 3LY6 HIS C  696  UNP  P21980              EXPRESSION TAG
SEQADV 3LY6 HIS C  697  UNP  P21980              EXPRESSION TAG
SEQRES   1 A  697  MET ALA GLU GLU LEU VAL LEU GLU ARG CYS ASP LEU GLU
SEQRES   2 A  697  LEU GLU THR ASN GLY ARG ASP HIS HIS THR ALA ASP LEU
SEQRES   3 A  697  CYS ARG GLU LYS LEU VAL VAL ARG ARG GLY GLN PRO PHE
SEQRES   4 A  697  TRP LEU THR LEU HIS PHE GLU GLY ARG ASN TYR GLU ALA
SEQRES   5 A  697  SER VAL ASP SER LEU THR PHE SER VAL VAL THR GLY PRO
SEQRES   6 A  697  ALA PRO SER GLN GLU ALA GLY THR LYS ALA ARG PHE PRO
SEQRES   7 A  697  LEU ARG ASP ALA VAL GLU GLU GLY ASP TRP THR ALA THR
SEQRES   8 A  697  VAL VAL ASP GLN GLN ASP CYS THR LEU SER LEU GLN LEU
SEQRES   9 A  697  THR THR PRO ALA ASN ALA PRO ILE GLY LEU TYR ARG LEU
SEQRES  10 A  697  SER LEU GLU ALA SER THR GLY TYR GLN GLY SER SER PHE
SEQRES  11 A  697  VAL LEU GLY HIS PHE ILE LEU LEU PHE ASN ALA TRP CYS
SEQRES  12 A  697  PRO ALA ASP ALA VAL TYR LEU ASP SER GLU GLU GLU ARG
SEQRES  13 A  697  GLN GLU TYR VAL LEU THR GLN GLN GLY PHE ILE TYR GLN
SEQRES  14 A  697  GLY SER ALA LYS PHE ILE LYS ASN ILE PRO TRP ASN PHE
SEQRES  15 A  697  GLY GLN PHE GLU ASP GLY ILE LEU ASP ILE CYS LEU ILE
SEQRES  16 A  697  LEU LEU ASP VAL ASN PRO LYS PHE LEU LYS ASN ALA GLY
SEQRES  17 A  697  ARG ASP CYS SER ARG ARG SER SER PRO VAL TYR VAL GLY
SEQRES  18 A  697  ARG VAL GLY SER GLY MET VAL ASN CYS ASN ASP ASP GLN
SEQRES  19 A  697  GLY VAL LEU LEU GLY ARG TRP ASP ASN ASN TYR GLY ASP
SEQRES  20 A  697  GLY VAL SER PRO MET SER TRP ILE GLY SER VAL ASP ILE
SEQRES  21 A  697  LEU ARG ARG TRP LYS ASN HIS GLY CYS GLN ARG VAL LYS
SEQRES  22 A  697  TYR GLY GLN CYS TRP VAL PHE ALA ALA VAL ALA CYS THR
SEQRES  23 A  697  VAL LEU ARG CYS LEU GLY ILE PRO THR ARG VAL VAL THR
SEQRES  24 A  697  ASN TYR ASN SER ALA HIS ASP GLN ASN SER ASN LEU LEU
SEQRES  25 A  697  ILE GLU TYR PHE ARG ASN GLU PHE GLY GLU ILE GLN GLY
SEQRES  26 A  697  ASP LYS SER GLU MET ILE TRP ASN PHE HIS CYS TRP VAL
SEQRES  27 A  697  GLU SER TRP MET THR ARG PRO ASP LEU GLN PRO GLY TYR
SEQRES  28 A  697  GLU GLY TRP GLN ALA LEU ASP PRO THR PRO GLN GLU LYS
SEQRES  29 A  697  SER GLU GLY THR TYR CYS CYS GLY PRO VAL PRO VAL ARG
SEQRES  30 A  697  ALA ILE LYS GLU GLY ASP LEU SER THR LYS TYR ASP ALA
SEQRES  31 A  697  PRO PHE VAL PHE ALA GLU VAL ASN ALA ASP VAL VAL ASP
SEQRES  32 A  697  TRP ILE GLN GLN ASP ASP GLY SER VAL HIS LYS SER ILE
SEQRES  33 A  697  ASN ARG SER LEU ILE VAL GLY LEU LYS ILE SER THR LYS
SEQRES  34 A  697  SER VAL GLY ARG ASP GLU ARG GLU ASP ILE THR HIS THR
SEQRES  35 A  697  TYR LYS TYR PRO GLU GLY SER SER GLU GLU ARG GLU ALA
SEQRES  36 A  697  PHE THR ARG ALA ASN HIS LEU ASN LYS LEU ALA GLU LYS
SEQRES  37 A  697  GLU GLU THR GLY MET ALA MET ARG ILE ARG VAL GLY GLN
SEQRES  38 A  697  SER MET ASN MET GLY SER ASP PHE ASP VAL PHE ALA HIS
SEQRES  39 A  697  ILE THR ASN ASN THR ALA GLU GLU TYR VAL CYS ARG LEU
SEQRES  40 A  697  LEU LEU CYS ALA ARG THR VAL SER TYR ASN GLY ILE LEU
SEQRES  41 A  697  GLY PRO GLU CYS GLY THR LYS TYR LEU LEU ASN LEU ASN
SEQRES  42 A  697  LEU GLU PRO PHE SER GLU LYS SER VAL PRO LEU CYS ILE
SEQRES  43 A  697  LEU TYR GLU LYS TYR ARG ASP CYS LEU THR GLU SER ASN
SEQRES  44 A  697  LEU ILE LYS VAL ARG ALA LEU LEU VAL GLU PRO VAL ILE
SEQRES  45 A  697  ASN SER TYR LEU LEU ALA GLU ARG ASP LEU TYR LEU GLU
SEQRES  46 A  697  ASN PRO GLU ILE LYS ILE ARG ILE LEU GLY GLU PRO LYS
SEQRES  47 A  697  GLN LYS ARG LYS LEU VAL ALA GLU VAL SER LEU GLN ASN
SEQRES  48 A  697  PRO LEU PRO VAL ALA LEU GLU GLY CYS THR PHE THR VAL
SEQRES  49 A  697  GLU GLY ALA GLY LEU THR GLU GLU GLN LYS THR VAL GLU
SEQRES  50 A  697  ILE PRO ASP PRO VAL GLU ALA GLY GLU GLU VAL LYS VAL
SEQRES  51 A  697  ARG MET ASP LEU LEU PRO LEU HIS MET GLY LEU HIS LYS
SEQRES  52 A  697  LEU VAL VAL ASN PHE GLU SER ASP LYS LEU LYS ALA VAL
SEQRES  53 A  697  LYS GLY PHE ARG ASN VAL ILE ILE GLY PRO ALA LEU GLU
SEQRES  54 A  697  HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES   1 B  697  MET ALA GLU GLU LEU VAL LEU GLU ARG CYS ASP LEU GLU
SEQRES   2 B  697  LEU GLU THR ASN GLY ARG ASP HIS HIS THR ALA ASP LEU
SEQRES   3 B  697  CYS ARG GLU LYS LEU VAL VAL ARG ARG GLY GLN PRO PHE
SEQRES   4 B  697  TRP LEU THR LEU HIS PHE GLU GLY ARG ASN TYR GLU ALA
SEQRES   5 B  697  SER VAL ASP SER LEU THR PHE SER VAL VAL THR GLY PRO
SEQRES   6 B  697  ALA PRO SER GLN GLU ALA GLY THR LYS ALA ARG PHE PRO
SEQRES   7 B  697  LEU ARG ASP ALA VAL GLU GLU GLY ASP TRP THR ALA THR
SEQRES   8 B  697  VAL VAL ASP GLN GLN ASP CYS THR LEU SER LEU GLN LEU
SEQRES   9 B  697  THR THR PRO ALA ASN ALA PRO ILE GLY LEU TYR ARG LEU
SEQRES  10 B  697  SER LEU GLU ALA SER THR GLY TYR GLN GLY SER SER PHE
SEQRES  11 B  697  VAL LEU GLY HIS PHE ILE LEU LEU PHE ASN ALA TRP CYS
SEQRES  12 B  697  PRO ALA ASP ALA VAL TYR LEU ASP SER GLU GLU GLU ARG
SEQRES  13 B  697  GLN GLU TYR VAL LEU THR GLN GLN GLY PHE ILE TYR GLN
SEQRES  14 B  697  GLY SER ALA LYS PHE ILE LYS ASN ILE PRO TRP ASN PHE
SEQRES  15 B  697  GLY GLN PHE GLU ASP GLY ILE LEU ASP ILE CYS LEU ILE
SEQRES  16 B  697  LEU LEU ASP VAL ASN PRO LYS PHE LEU LYS ASN ALA GLY
SEQRES  17 B  697  ARG ASP CYS SER ARG ARG SER SER PRO VAL TYR VAL GLY
SEQRES  18 B  697  ARG VAL GLY SER GLY MET VAL ASN CYS ASN ASP ASP GLN
SEQRES  19 B  697  GLY VAL LEU LEU GLY ARG TRP ASP ASN ASN TYR GLY ASP
SEQRES  20 B  697  GLY VAL SER PRO MET SER TRP ILE GLY SER VAL ASP ILE
SEQRES  21 B  697  LEU ARG ARG TRP LYS ASN HIS GLY CYS GLN ARG VAL LYS
SEQRES  22 B  697  TYR GLY GLN CYS TRP VAL PHE ALA ALA VAL ALA CYS THR
SEQRES  23 B  697  VAL LEU ARG CYS LEU GLY ILE PRO THR ARG VAL VAL THR
SEQRES  24 B  697  ASN TYR ASN SER ALA HIS ASP GLN ASN SER ASN LEU LEU
SEQRES  25 B  697  ILE GLU TYR PHE ARG ASN GLU PHE GLY GLU ILE GLN GLY
SEQRES  26 B  697  ASP LYS SER GLU MET ILE TRP ASN PHE HIS CYS TRP VAL
SEQRES  27 B  697  GLU SER TRP MET THR ARG PRO ASP LEU GLN PRO GLY TYR
SEQRES  28 B  697  GLU GLY TRP GLN ALA LEU ASP PRO THR PRO GLN GLU LYS
SEQRES  29 B  697  SER GLU GLY THR TYR CYS CYS GLY PRO VAL PRO VAL ARG
SEQRES  30 B  697  ALA ILE LYS GLU GLY ASP LEU SER THR LYS TYR ASP ALA
SEQRES  31 B  697  PRO PHE VAL PHE ALA GLU VAL ASN ALA ASP VAL VAL ASP
SEQRES  32 B  697  TRP ILE GLN GLN ASP ASP GLY SER VAL HIS LYS SER ILE
SEQRES  33 B  697  ASN ARG SER LEU ILE VAL GLY LEU LYS ILE SER THR LYS
SEQRES  34 B  697  SER VAL GLY ARG ASP GLU ARG GLU ASP ILE THR HIS THR
SEQRES  35 B  697  TYR LYS TYR PRO GLU GLY SER SER GLU GLU ARG GLU ALA
SEQRES  36 B  697  PHE THR ARG ALA ASN HIS LEU ASN LYS LEU ALA GLU LYS
SEQRES  37 B  697  GLU GLU THR GLY MET ALA MET ARG ILE ARG VAL GLY GLN
SEQRES  38 B  697  SER MET ASN MET GLY SER ASP PHE ASP VAL PHE ALA HIS
SEQRES  39 B  697  ILE THR ASN ASN THR ALA GLU GLU TYR VAL CYS ARG LEU
SEQRES  40 B  697  LEU LEU CYS ALA ARG THR VAL SER TYR ASN GLY ILE LEU
SEQRES  41 B  697  GLY PRO GLU CYS GLY THR LYS TYR LEU LEU ASN LEU ASN
SEQRES  42 B  697  LEU GLU PRO PHE SER GLU LYS SER VAL PRO LEU CYS ILE
SEQRES  43 B  697  LEU TYR GLU LYS TYR ARG ASP CYS LEU THR GLU SER ASN
SEQRES  44 B  697  LEU ILE LYS VAL ARG ALA LEU LEU VAL GLU PRO VAL ILE
SEQRES  45 B  697  ASN SER TYR LEU LEU ALA GLU ARG ASP LEU TYR LEU GLU
SEQRES  46 B  697  ASN PRO GLU ILE LYS ILE ARG ILE LEU GLY GLU PRO LYS
SEQRES  47 B  697  GLN LYS ARG LYS LEU VAL ALA GLU VAL SER LEU GLN ASN
SEQRES  48 B  697  PRO LEU PRO VAL ALA LEU GLU GLY CYS THR PHE THR VAL
SEQRES  49 B  697  GLU GLY ALA GLY LEU THR GLU GLU GLN LYS THR VAL GLU
SEQRES  50 B  697  ILE PRO ASP PRO VAL GLU ALA GLY GLU GLU VAL LYS VAL
SEQRES  51 B  697  ARG MET ASP LEU LEU PRO LEU HIS MET GLY LEU HIS LYS
SEQRES  52 B  697  LEU VAL VAL ASN PHE GLU SER ASP LYS LEU LYS ALA VAL
SEQRES  53 B  697  LYS GLY PHE ARG ASN VAL ILE ILE GLY PRO ALA LEU GLU
SEQRES  54 B  697  HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES   1 C  697  MET ALA GLU GLU LEU VAL LEU GLU ARG CYS ASP LEU GLU
SEQRES   2 C  697  LEU GLU THR ASN GLY ARG ASP HIS HIS THR ALA ASP LEU
SEQRES   3 C  697  CYS ARG GLU LYS LEU VAL VAL ARG ARG GLY GLN PRO PHE
SEQRES   4 C  697  TRP LEU THR LEU HIS PHE GLU GLY ARG ASN TYR GLU ALA
SEQRES   5 C  697  SER VAL ASP SER LEU THR PHE SER VAL VAL THR GLY PRO
SEQRES   6 C  697  ALA PRO SER GLN GLU ALA GLY THR LYS ALA ARG PHE PRO
SEQRES   7 C  697  LEU ARG ASP ALA VAL GLU GLU GLY ASP TRP THR ALA THR
SEQRES   8 C  697  VAL VAL ASP GLN GLN ASP CYS THR LEU SER LEU GLN LEU
SEQRES   9 C  697  THR THR PRO ALA ASN ALA PRO ILE GLY LEU TYR ARG LEU
SEQRES  10 C  697  SER LEU GLU ALA SER THR GLY TYR GLN GLY SER SER PHE
SEQRES  11 C  697  VAL LEU GLY HIS PHE ILE LEU LEU PHE ASN ALA TRP CYS
SEQRES  12 C  697  PRO ALA ASP ALA VAL TYR LEU ASP SER GLU GLU GLU ARG
SEQRES  13 C  697  GLN GLU TYR VAL LEU THR GLN GLN GLY PHE ILE TYR GLN
SEQRES  14 C  697  GLY SER ALA LYS PHE ILE LYS ASN ILE PRO TRP ASN PHE
SEQRES  15 C  697  GLY GLN PHE GLU ASP GLY ILE LEU ASP ILE CYS LEU ILE
SEQRES  16 C  697  LEU LEU ASP VAL ASN PRO LYS PHE LEU LYS ASN ALA GLY
SEQRES  17 C  697  ARG ASP CYS SER ARG ARG SER SER PRO VAL TYR VAL GLY
SEQRES  18 C  697  ARG VAL GLY SER GLY MET VAL ASN CYS ASN ASP ASP GLN
SEQRES  19 C  697  GLY VAL LEU LEU GLY ARG TRP ASP ASN ASN TYR GLY ASP
SEQRES  20 C  697  GLY VAL SER PRO MET SER TRP ILE GLY SER VAL ASP ILE
SEQRES  21 C  697  LEU ARG ARG TRP LYS ASN HIS GLY CYS GLN ARG VAL LYS
SEQRES  22 C  697  TYR GLY GLN CYS TRP VAL PHE ALA ALA VAL ALA CYS THR
SEQRES  23 C  697  VAL LEU ARG CYS LEU GLY ILE PRO THR ARG VAL VAL THR
SEQRES  24 C  697  ASN TYR ASN SER ALA HIS ASP GLN ASN SER ASN LEU LEU
SEQRES  25 C  697  ILE GLU TYR PHE ARG ASN GLU PHE GLY GLU ILE GLN GLY
SEQRES  26 C  697  ASP LYS SER GLU MET ILE TRP ASN PHE HIS CYS TRP VAL
SEQRES  27 C  697  GLU SER TRP MET THR ARG PRO ASP LEU GLN PRO GLY TYR
SEQRES  28 C  697  GLU GLY TRP GLN ALA LEU ASP PRO THR PRO GLN GLU LYS
SEQRES  29 C  697  SER GLU GLY THR TYR CYS CYS GLY PRO VAL PRO VAL ARG
SEQRES  30 C  697  ALA ILE LYS GLU GLY ASP LEU SER THR LYS TYR ASP ALA
SEQRES  31 C  697  PRO PHE VAL PHE ALA GLU VAL ASN ALA ASP VAL VAL ASP
SEQRES  32 C  697  TRP ILE GLN GLN ASP ASP GLY SER VAL HIS LYS SER ILE
SEQRES  33 C  697  ASN ARG SER LEU ILE VAL GLY LEU LYS ILE SER THR LYS
SEQRES  34 C  697  SER VAL GLY ARG ASP GLU ARG GLU ASP ILE THR HIS THR
SEQRES  35 C  697  TYR LYS TYR PRO GLU GLY SER SER GLU GLU ARG GLU ALA
SEQRES  36 C  697  PHE THR ARG ALA ASN HIS LEU ASN LYS LEU ALA GLU LYS
SEQRES  37 C  697  GLU GLU THR GLY MET ALA MET ARG ILE ARG VAL GLY GLN
SEQRES  38 C  697  SER MET ASN MET GLY SER ASP PHE ASP VAL PHE ALA HIS
SEQRES  39 C  697  ILE THR ASN ASN THR ALA GLU GLU TYR VAL CYS ARG LEU
SEQRES  40 C  697  LEU LEU CYS ALA ARG THR VAL SER TYR ASN GLY ILE LEU
SEQRES  41 C  697  GLY PRO GLU CYS GLY THR LYS TYR LEU LEU ASN LEU ASN
SEQRES  42 C  697  LEU GLU PRO PHE SER GLU LYS SER VAL PRO LEU CYS ILE
SEQRES  43 C  697  LEU TYR GLU LYS TYR ARG ASP CYS LEU THR GLU SER ASN
SEQRES  44 C  697  LEU ILE LYS VAL ARG ALA LEU LEU VAL GLU PRO VAL ILE
SEQRES  45 C  697  ASN SER TYR LEU LEU ALA GLU ARG ASP LEU TYR LEU GLU
SEQRES  46 C  697  ASN PRO GLU ILE LYS ILE ARG ILE LEU GLY GLU PRO LYS
SEQRES  47 C  697  GLN LYS ARG LYS LEU VAL ALA GLU VAL SER LEU GLN ASN
SEQRES  48 C  697  PRO LEU PRO VAL ALA LEU GLU GLY CYS THR PHE THR VAL
SEQRES  49 C  697  GLU GLY ALA GLY LEU THR GLU GLU GLN LYS THR VAL GLU
SEQRES  50 C  697  ILE PRO ASP PRO VAL GLU ALA GLY GLU GLU VAL LYS VAL
SEQRES  51 C  697  ARG MET ASP LEU LEU PRO LEU HIS MET GLY LEU HIS LYS
SEQRES  52 C  697  LEU VAL VAL ASN PHE GLU SER ASP LYS LEU LYS ALA VAL
SEQRES  53 C  697  LYS GLY PHE ARG ASN VAL ILE ILE GLY PRO ALA LEU GLU
SEQRES  54 C  697  HIS HIS HIS HIS HIS HIS HIS HIS
HET    ATP  A 700      31
HET    ATP  B 701      31
HET    ATP  C 702      31
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE
FORMUL   4  ATP    3(C10 H16 N5 O13 P3)
HELIX    1   1 GLU A   15  HIS A   21  1                                   7
HELIX    2   2 SER A  152  LEU A  161  1                                  10
HELIX    3   3 GLY A  188  ASP A  198  1                                  11
HELIX    4   4 ASN A  200  LYS A  205  1                                   6
HELIX    5   5 ASN A  206  ARG A  214  1                                   9
HELIX    6   6 SER A  216  ASN A  229  1                                  14
HELIX    7   7 SER A  250  TRP A  254  5                                   5
HELIX    8   8 GLY A  256  ASN A  266  1                                  11
HELIX    9   9 GLN A  276  GLY A  292  1                                  17
HELIX   10  10 VAL A  376  GLY A  382  1                                   7
HELIX   11  11 ASP A  389  ALA A  399  1                                  11
HELIX   12  12 THR A  440  TYR A  443  5                                   4
HELIX   13  13 SER A  449  ALA A  459  1                                  11
HELIX   14  14 LEU A  547  TYR A  551  5                                   5
HELIX   15  15 GLU B   15  HIS B   21  1                                   7
HELIX   16  16 SER B  152  LEU B  161  1                                  10
HELIX   17  17 GLY B  188  ASP B  198  1                                  11
HELIX   18  18 ASN B  200  LYS B  205  1                                   6
HELIX   19  19 ASN B  206  ARG B  214  1                                   9
HELIX   20  20 SER B  216  MET B  227  1                                  12
HELIX   21  21 SER B  250  TRP B  254  5                                   5
HELIX   22  22 GLY B  256  ASN B  266  1                                  11
HELIX   23  23 GLN B  276  GLY B  292  1                                  17
HELIX   24  24 VAL B  376  GLY B  382  1                                   7
HELIX   25  25 ASP B  389  ALA B  399  1                                  11
HELIX   26  26 THR B  440  TYR B  443  5                                   4
HELIX   27  27 SER B  449  ALA B  459  1                                  11
HELIX   28  28 LEU B  547  TYR B  551  5                                   5
HELIX   29  29 GLU C   15  HIS C   21  1                                   7
HELIX   30  30 SER C  152  LEU C  161  1                                  10
HELIX   31  31 GLY C  188  ASP C  198  1                                  11
HELIX   32  32 ASN C  200  LYS C  205  1                                   6
HELIX   33  33 ASN C  206  ARG C  214  1                                   9
HELIX   34  34 SER C  216  ASN C  229  1                                  14
HELIX   35  35 SER C  250  TRP C  254  5                                   5
HELIX   36  36 GLY C  256  ASN C  266  1                                  11
HELIX   37  37 GLN C  276  GLY C  292  1                                  17
HELIX   38  38 VAL C  376  GLY C  382  1                                   7
HELIX   39  39 ASP C  389  ALA C  399  1                                  11
HELIX   40  40 THR C  440  TYR C  443  5                                   4
HELIX   41  41 SER C  449  ALA C  459  1                                  11
HELIX   42  42 LEU C  547  TYR C  551  5                                   5
SHEET    1   A 5 LEU A  31  ARG A  34  0
SHEET    2   A 5 SER A 129  LEU A 138  1  O  ILE A 136   N  VAL A  33
SHEET    3   A 5 GLY A 113  SER A 122 -1  N  LEU A 117   O  LEU A 132
SHEET    4   A 5 SER A  56  VAL A  62 -1  N  SER A  60   O  SER A 118
SHEET    5   A 5 LYS A  74  PRO A  78 -1  O  ALA A  75   N  VAL A  61
SHEET    1   B 3 PRO A  38  HIS A  44  0
SHEET    2   B 3 THR A  99  THR A 105 -1  O  LEU A 100   N  LEU A  43
SHEET    3   B 3 THR A  89  VAL A  92 -1  N  THR A  89   O  THR A 105
SHEET    1   C 2 GLN A 164  GLY A 170  0
SHEET    2   C 2 ILE A 175  ASN A 181 -1  O  LYS A 176   N  GLN A 169
SHEET    1   D 2 LEU A 237  GLY A 239  0
SHEET    2   D 2 VAL A 272  GLY A 275  1  O  VAL A 272   N  LEU A 238
SHEET    1   E 6 THR A 368  PRO A 375  0
SHEET    2   E 6 GLY A 353  GLU A 363 -1  N  ALA A 356   O  VAL A 374
SHEET    3   E 6 TRP A 332  MET A 342 -1  N  SER A 340   O  GLN A 355
SHEET    4   E 6 THR A 295  SER A 303 -1  N  VAL A 298   O  TRP A 337
SHEET    5   E 6 LEU A 424  LYS A 429 -1  O  SER A 427   N  THR A 299
SHEET    6   E 6 ARG A 436  ASP A 438 -1  O  GLU A 437   N  THR A 428
SHEET    1   F 3 LEU A 312  ARG A 317  0
SHEET    2   F 3 ASP A 400  GLN A 406  1  O  GLN A 406   N  ARG A 317
SHEET    3   F 3 VAL A 412  LYS A 414 -1  O  HIS A 413   N  ILE A 405
SHEET    1   G 3 MET A 473  ARG A 478  0
SHEET    2   G 3 PHE A 489  ASN A 497 -1  O  PHE A 492   N  ARG A 478
SHEET    3   G 3 SER A 538  ILE A 546 -1  O  LYS A 540   N  ILE A 495
SHEET    1   H 4 LEU A 520  LEU A 534  0
SHEET    2   H 4 TYR A 503  VAL A 514 -1  N  ALA A 511   O  GLY A 525
SHEET    3   H 4 LEU A 560  GLU A 569 -1  O  LYS A 562   N  ARG A 512
SHEET    4   H 4 SER A 574  TYR A 583 -1  O  LEU A 582   N  ILE A 561
SHEET    1   I 3 LYS A 590  LEU A 594  0
SHEET    2   I 3 LEU A 603  GLN A 610 -1  O  GLU A 606   N  ARG A 592
SHEET    3   I 3 GLU A 647  LEU A 654 -1  O  LEU A 654   N  LEU A 603
SHEET    1   J 4 LYS A 634  ILE A 638  0
SHEET    2   J 4 CYS A 620  GLU A 625 -1  N  VAL A 624   O  LYS A 634
SHEET    3   J 4 GLY A 660  GLU A 669 -1  O  GLU A 669   N  THR A 621
SHEET    4   J 4 VAL A 676  ILE A 684 -1  O  ILE A 684   N  GLY A 660
SHEET    1   K 5 LEU B  31  ARG B  34  0
SHEET    2   K 5 SER B 129  LEU B 138  1  O  ILE B 136   N  VAL B  33
SHEET    3   K 5 GLY B 113  GLU B 120 -1  N  LEU B 117   O  LEU B 132
SHEET    4   K 5 THR B  58  VAL B  62 -1  N  SER B  60   O  SER B 118
SHEET    5   K 5 LYS B  74  PRO B  78 -1  O  ALA B  75   N  VAL B  61
SHEET    1   L 3 PRO B  38  HIS B  44  0
SHEET    2   L 3 THR B  99  THR B 105 -1  O  LEU B 100   N  LEU B  43
SHEET    3   L 3 THR B  89  VAL B  92 -1  N  THR B  89   O  THR B 105
SHEET    1   M 2 GLN B 164  GLY B 170  0
SHEET    2   M 2 ILE B 175  ASN B 181 -1  O  LYS B 176   N  GLN B 169
SHEET    1   N 2 LEU B 237  GLY B 239  0
SHEET    2   N 2 VAL B 272  GLY B 275  1  O  VAL B 272   N  LEU B 238
SHEET    1   O 6 THR B 368  PRO B 375  0
SHEET    2   O 6 GLY B 353  GLU B 363 -1  N  ALA B 356   O  VAL B 374
SHEET    3   O 6 TRP B 332  MET B 342 -1  N  SER B 340   O  GLN B 355
SHEET    4   O 6 THR B 295  SER B 303 -1  N  VAL B 298   O  TRP B 337
SHEET    5   O 6 LEU B 424  LYS B 429 -1  O  SER B 427   N  THR B 299
SHEET    6   O 6 ARG B 436  ASP B 438 -1  O  GLU B 437   N  THR B 428
SHEET    1   P 3 LEU B 312  ARG B 317  0
SHEET    2   P 3 ASP B 400  GLN B 406  1  O  GLN B 406   N  ARG B 317
SHEET    3   P 3 VAL B 412  LYS B 414 -1  O  HIS B 413   N  ILE B 405
SHEET    1   Q 3 MET B 473  ARG B 478  0
SHEET    2   Q 3 PHE B 489  ASN B 497 -1  O  PHE B 492   N  ARG B 478
SHEET    3   Q 3 SER B 538  ILE B 546 -1  O  LYS B 540   N  ILE B 495
SHEET    1   R 4 LEU B 520  LEU B 534  0
SHEET    2   R 4 TYR B 503  VAL B 514 -1  N  ALA B 511   O  GLY B 525
SHEET    3   R 4 LEU B 560  GLU B 569 -1  O  LEU B 566   N  LEU B 508
SHEET    4   R 4 SER B 574  TYR B 583 -1  O  LEU B 582   N  ILE B 561
SHEET    1   S 3 LYS B 590  LEU B 594  0
SHEET    2   S 3 LEU B 603  GLN B 610 -1  O  GLU B 606   N  ARG B 592
SHEET    3   S 3 GLU B 647  LEU B 654 -1  O  LEU B 654   N  LEU B 603
SHEET    1   T 4 LYS B 634  ILE B 638  0
SHEET    2   T 4 CYS B 620  GLU B 625 -1  N  VAL B 624   O  LYS B 634
SHEET    3   T 4 GLY B 660  GLU B 669 -1  O  GLU B 669   N  THR B 621
SHEET    4   T 4 VAL B 676  ILE B 684 -1  O  ILE B 684   N  GLY B 660
SHEET    1   U 5 LEU C  31  ARG C  34  0
SHEET    2   U 5 SER C 129  LEU C 138  1  O  ILE C 136   N  VAL C  33
SHEET    3   U 5 GLY C 113  GLU C 120 -1  N  LEU C 117   O  LEU C 132
SHEET    4   U 5 THR C  58  VAL C  62 -1  N  SER C  60   O  SER C 118
SHEET    5   U 5 LYS C  74  PRO C  78 -1  O  ALA C  75   N  VAL C  61
SHEET    1   V 3 PRO C  38  HIS C  44  0
SHEET    2   V 3 THR C  99  THR C 105 -1  O  LEU C 100   N  LEU C  43
SHEET    3   V 3 THR C  89  VAL C  92 -1  N  THR C  89   O  THR C 105
SHEET    1   W 2 GLN C 164  GLY C 170  0
SHEET    2   W 2 ILE C 175  ASN C 181 -1  O  LYS C 176   N  GLN C 169
SHEET    1   X 2 LEU C 237  GLY C 239  0
SHEET    2   X 2 VAL C 272  GLY C 275  1  O  VAL C 272   N  LEU C 238
SHEET    1   Y 6 THR C 368  PRO C 375  0
SHEET    2   Y 6 GLY C 353  GLU C 363 -1  N  ALA C 356   O  VAL C 374
SHEET    3   Y 6 TRP C 332  MET C 342 -1  N  SER C 340   O  GLN C 355
SHEET    4   Y 6 THR C 295  SER C 303 -1  N  VAL C 298   O  TRP C 337
SHEET    5   Y 6 LEU C 424  LYS C 429 -1  O  SER C 427   N  THR C 299
SHEET    6   Y 6 ARG C 436  ASP C 438 -1  O  GLU C 437   N  THR C 428
SHEET    1   Z 3 LEU C 312  ARG C 317  0
SHEET    2   Z 3 ASP C 400  GLN C 406  1  O  GLN C 406   N  ARG C 317
SHEET    3   Z 3 VAL C 412  LYS C 414 -1  O  HIS C 413   N  ILE C 405
SHEET    1  AA 3 MET C 473  ARG C 478  0
SHEET    2  AA 3 PHE C 489  ASN C 497 -1  O  PHE C 492   N  ARG C 478
SHEET    3  AA 3 SER C 538  ILE C 546 -1  O  LYS C 540   N  ILE C 495
SHEET    1  AB 4 LEU C 520  LEU C 534  0
SHEET    2  AB 4 TYR C 503  VAL C 514 -1  N  ALA C 511   O  GLY C 525
SHEET    3  AB 4 LEU C 560  GLU C 569 -1  O  LYS C 562   N  ARG C 512
SHEET    4  AB 4 SER C 574  TYR C 583 -1  O  LEU C 582   N  ILE C 561
SHEET    1  AC 3 LYS C 590  LEU C 594  0
SHEET    2  AC 3 LEU C 603  GLN C 610 -1  O  GLU C 606   N  ARG C 592
SHEET    3  AC 3 GLU C 647  LEU C 654 -1  O  LEU C 654   N  LEU C 603
SHEET    1  AD 4 LYS C 634  ILE C 638  0
SHEET    2  AD 4 CYS C 620  GLU C 625 -1  N  CYS C 620   O  ILE C 638
SHEET    3  AD 4 GLY C 660  GLU C 669 -1  O  GLU C 669   N  THR C 621
SHEET    4  AD 4 VAL C 676  ILE C 684 -1  O  ILE C 684   N  GLY C 660
SSBOND   1 CYS A  230    CYS A  370                          1555   1555  2.03
SSBOND   2 CYS B  230    CYS B  370                          1555   1555  2.03
SSBOND   3 CYS C  230    CYS C  370                          1555   1555  2.03
CISPEP   1 GLY A  372    PRO A  373          0        -0.37
CISPEP   2 GLY B  372    PRO B  373          0        -0.21
CISPEP   3 GLY C  372    PRO C  373          0        -0.20
SITE     1 AC1 11 PHE A 174  ARG A 476  ARG A 478  VAL A 479
SITE     2 AC1 11 GLY A 480  GLN A 481  SER A 482  MET A 483
SITE     3 AC1 11 ARG A 580  LEU A 582  TYR A 583
SITE     1 AC2 13 PHE B 174  ARG B 476  ARG B 478  VAL B 479
SITE     2 AC2 13 GLY B 480  GLN B 481  SER B 482  MET B 483
SITE     3 AC2 13 ARG B 580  LEU B 582  TYR B 583  ARG C 478
SITE     4 AC2 13 ATP C 702
SITE     1 AC3 13 ARG B 478  ATP B 701  PHE C 174  ARG C 476
SITE     2 AC3 13 ARG C 478  VAL C 479  GLY C 480  GLN C 481
SITE     3 AC3 13 SER C 482  MET C 483  ARG C 580  LEU C 582
SITE     4 AC3 13 TYR C 583
CRYST1  134.175  215.759  165.956  90.00  90.00  90.00 C 2 2 21     24
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.007453  0.000000  0.000000        0.00000
SCALE2      0.000000  0.004635  0.000000        0.00000
SCALE3      0.000000  0.000000  0.006026        0.00000
      
PROCHECK
Go to PROCHECK summary
 References