spacer
spacer

PDBsum entry 3bwe

Go to PDB code: 
Top Page protein ligands Protein-protein interface(s) links
Chaperone PDB id
3bwe
Jmol
Contents
Protein chain
(+ 1 more) 188 a.a.
Ligands
PO4 ×7
Waters ×283
HEADER    CHAPERONE                               09-JAN-08   3BWE
TITLE     CRYSTAL STRUCTURE OF AGGREGATED FORM OF DJ1
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROTEIN DJ-1;
COMPND   3 CHAIN: A, B, C, D, E, F, G;
COMPND   4 SYNONYM: ONCOGENE DJ1, PARKINSON DISEASE PROTEIN 7;
COMPND   5 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: PARK7;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    CRYSTAL STRUCTURE, DJ-1, FILAMENTOUS AGGREGATES, CHAPERONE,
KEYWDS   2 CYTOPLASM, DISEASE MUTATION, NUCLEUS, ONCOGENE, OXIDATION,
KEYWDS   3 PARKINSON DISEASE, PHOSPHOPROTEIN, POLYMORPHISM, UBL
KEYWDS   4 CONJUGATION
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.S.CHA
REVDAT   3   14-APR-09 3BWE    1       JRNL
REVDAT   2   24-FEB-09 3BWE    1       VERSN
REVDAT   1   14-OCT-08 3BWE    0
JRNL        AUTH   S.S.CHA,H.I.JUNG,H.JEON,Y.J.AN,I.K.KIM,S.YUN,
JRNL        AUTH 2 H.J.AHN,K.C.CHUNG,S.H.LEE,P.G.SUH,S.O.KANG
JRNL        TITL   CRYSTAL STRUCTURE OF FILAMENTOUS AGGREGATES OF
JRNL        TITL 2 HUMAN DJ-1 FORMED IN AN INORGANIC
JRNL        TITL 3 PHOSPHATE-DEPENDENT MANNER.
JRNL        REF    J.BIOL.CHEM.                  V. 283 34069 2008
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   18922803
JRNL        DOI    10.1074/JBC.M804243200
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.1
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.99
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 58196.920
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 94.5
REMARK   3   NUMBER OF REFLECTIONS             : 56652
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.232
REMARK   3   FREE R VALUE                     : 0.282
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.200
REMARK   3   FREE R VALUE TEST SET COUNT      : 5760
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 6
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.55
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.30
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 8338
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3300
REMARK   3   BIN FREE R VALUE                    : 0.3560
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.20
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 951
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.012
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 9490
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 35
REMARK   3   SOLVENT ATOMS            : 283
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) : -3.78000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : 0.00000
REMARK   3    B12 (A**2) : 1.71000
REMARK   3    B13 (A**2) : 2.06000
REMARK   3    B23 (A**2) : 3.36000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.32
REMARK   3   ESD FROM SIGMAA              (A) : 0.41
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.012
REMARK   3   BOND ANGLES            (DEGREES) : 1.70
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 3BWE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-JAN-08.
REMARK 100 THE RCSB ID CODE IS RCSB046039.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 04-NOV-04
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               : PHOTON FACTORY
REMARK 200  BEAMLINE                       : BL-5A
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.12714
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 56724
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6
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) : 2.40
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.40
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.8
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: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1J42
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 55.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: EVAPORATION
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,Y,-Z
REMARK 290       3555   X+1/2,Y+1/2,Z
REMARK 290       4555   -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       96.80800
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       51.29100
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       96.80800
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       51.29100
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.4 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.5 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.9 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G
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   BIOMT1   2 -1.000000  0.000000  0.000000      193.61600
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     ASP A   189
REMARK 465     MSE B   201
REMARK 465     ASP B   389
REMARK 465     ASP C   589
REMARK 465     MSE D   601
REMARK 465     ALA D   602
REMARK 465     ASP D   789
REMARK 465     MSE E   801
REMARK 465     MSE F  1001
REMARK 465     ALA F  1002
REMARK 465     ASP F  1189
REMARK 465     MSE G  1201
REMARK 465     ALA G  1202
REMARK 465     ASP G  1389
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     MSE A   1    CG  SE    CE
REMARK 470     LYS A  41    CG   CD   CE   NZ
REMARK 470     LYS A  63    CG   CD   CE   NZ
REMARK 470     LYS A  99    CG   CD   CE   NZ
REMARK 470     LYS B 241    CG   CD   CE   NZ
REMARK 470     GLU B 259    CG   CD   OE1  OE2
REMARK 470     LYS B 263    CG   CD   CE   NZ
REMARK 470     MSE C 401    CG  SE    CE
REMARK 470     LYS C 441    CG   CD   CE   NZ
REMARK 470     LYS C 532    CG   CD   CE   NZ
REMARK 470     LYS C 588    CG   CD   CE   NZ
REMARK 470     LYS D 663    CG   CD   CE   NZ
REMARK 470     GLU D 694    CG   CD   OE1  OE2
REMARK 470     LYS D 788    CG   CD   CE   NZ
REMARK 470     GLU E 859    CG   CD   OE1  OE2
REMARK 470     LYS E 863    CG   CD   CE   NZ
REMARK 470     GLU E 894    CG   CD   OE1  OE2
REMARK 470     LYS E 899    CG   CD   CE   NZ
REMARK 470     GLU E 916    CG   CD   OE1  OE2
REMARK 470     VAL E 923    CG1  CG2
REMARK 470     GLU E 976    CG   CD   OE1  OE2
REMARK 470     LYS E 988    CG   CD   CE   NZ
REMARK 470     ASP E 989    CG   OD1  OD2
REMARK 470     LYS F1041    CG   CD   CE   NZ
REMARK 470     GLU F1059    CG   CD   OE1  OE2
REMARK 470     LYS F1063    CG   CD   CE   NZ
REMARK 470     GLU F1090    CG   CD   OE1  OE2
REMARK 470     LYS F1188    CG   CD   CE   NZ
REMARK 470     LYS G1241    CG   CD   CE   NZ
REMARK 470     GLU G1259    CG   CD   OE1  OE2
REMARK 470     LYS G1263    CG   CD   CE   NZ
REMARK 470     GLU G1290    CG   CD   OE1  OE2
REMARK 470     GLU G1294    CG   CD   OE1  OE2
REMARK 470     ARG G1298    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS G1299    CG   CD   CE   NZ
REMARK 470     LYS G1332    CG   CD   CE   NZ
REMARK 470     LYS G1388    CG   CD   CE   NZ
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    CYS D 653   CA  -  CB  -  SG  ANGL. DEV. =   8.6 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    CYS A 106     -105.60     70.46
REMARK 500    THR A 110        0.41    -67.40
REMARK 500    PRO B 273      170.03    -59.42
REMARK 500    ASN B 276      -76.44    -49.15
REMARK 500    CYS B 306     -106.55     69.83
REMARK 500    ALA C 456      175.33    176.67
REMARK 500    CYS C 506     -108.18     65.08
REMARK 500    PHE C 519      120.08    -38.28
REMARK 500    ASP C 531      -77.70    -47.67
REMARK 500    HIS C 538       -3.34    -48.77
REMARK 500    PRO D 654      155.30    -49.57
REMARK 500    CYS D 706     -114.54     63.13
REMARK 500    PRO D 709       -7.54    -59.94
REMARK 500    GLU E 864       63.11    -44.48
REMARK 500    LEU E 892        6.95    -68.72
REMARK 500    GLU E 896      -32.26     96.67
REMARK 500    CYS E 906     -107.64     73.34
REMARK 500    PRO E 909        1.58    -64.17
REMARK 500    GLU E 916       70.54     42.64
REMARK 500    CYS F1106      -89.88     65.72
REMARK 500    VAL F1186       62.31     66.23
REMARK 500    ASP G1249       -6.98     74.11
REMARK 500    GLU G1264       97.47    -52.80
REMARK 500    PRO G1266     -161.53    -67.15
REMARK 500    VAL G1269      136.38    176.24
REMARK 500    ASN G1276      -65.79     77.09
REMARK 500    CYS G1306     -110.47     62.15
REMARK 500    GLU G1316       59.69     33.36
REMARK 500    THR G1325     -167.76   -119.07
REMARK 500    LYS G1330      -71.09    -48.76
REMARK 500    ASP G1331      -71.34    -28.81
REMARK 500    ARG G1356     -136.83    -71.31
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH E 104        DISTANCE =  5.78 ANGSTROMS
REMARK 525    HOH D 106        DISTANCE =  5.14 ANGSTROMS
REMARK 525    HOH A 219        DISTANCE =  5.87 ANGSTROMS
REMARK 525    HOH D 122        DISTANCE =  5.10 ANGSTROMS
REMARK 525    HOH E 234        DISTANCE =  5.35 ANGSTROMS
REMARK 525    HOH D 124        DISTANCE =  7.57 ANGSTROMS
REMARK 525    HOH A 227        DISTANCE =  5.96 ANGSTROMS
REMARK 525    HOH E 274        DISTANCE =  6.91 ANGSTROMS
REMARK 525    HOH E 275        DISTANCE =  5.11 ANGSTROMS
REMARK 525    HOH C 230        DISTANCE =  8.52 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 190
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 191
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 3
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 1
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 E 6
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 F 4
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 F 5
DBREF  3BWE A    1   189  UNP    Q99497   PARK7_HUMAN      1    189
DBREF  3BWE B  201   389  UNP    Q99497   PARK7_HUMAN      1    189
DBREF  3BWE C  401   589  UNP    Q99497   PARK7_HUMAN      1    189
DBREF  3BWE D  601   789  UNP    Q99497   PARK7_HUMAN      1    189
DBREF  3BWE E  801   989  UNP    Q99497   PARK7_HUMAN      1    189
DBREF  3BWE F 1001  1189  UNP    Q99497   PARK7_HUMAN      1    189
DBREF  3BWE G 1201  1389  UNP    Q99497   PARK7_HUMAN      1    189
SEQRES   1 A  189  MSE ALA SER LYS ARG ALA LEU VAL ILE LEU ALA LYS GLY
SEQRES   2 A  189  ALA GLU GLU MSE GLU THR VAL ILE PRO VAL ASP VAL MSE
SEQRES   3 A  189  ARG ARG ALA GLY ILE LYS VAL THR VAL ALA GLY LEU ALA
SEQRES   4 A  189  GLY LYS ASP PRO VAL GLN CYS SER ARG ASP VAL VAL ILE
SEQRES   5 A  189  CYS PRO ASP ALA SER LEU GLU ASP ALA LYS LYS GLU GLY
SEQRES   6 A  189  PRO TYR ASP VAL VAL VAL LEU PRO GLY GLY ASN LEU GLY
SEQRES   7 A  189  ALA GLN ASN LEU SER GLU SER ALA ALA VAL LYS GLU ILE
SEQRES   8 A  189  LEU LYS GLU GLN GLU ASN ARG LYS GLY LEU ILE ALA ALA
SEQRES   9 A  189  ILE CYS ALA GLY PRO THR ALA LEU LEU ALA HIS GLU ILE
SEQRES  10 A  189  GLY PHE GLY SER LYS VAL THR THR HIS PRO LEU ALA LYS
SEQRES  11 A  189  ASP LYS MSE MSE ASN GLY GLY HIS TYR THR TYR SER GLU
SEQRES  12 A  189  ASN ARG VAL GLU LYS ASP GLY LEU ILE LEU THR SER ARG
SEQRES  13 A  189  GLY PRO GLY THR SER PHE GLU PHE ALA LEU ALA ILE VAL
SEQRES  14 A  189  GLU ALA LEU ASN GLY LYS GLU VAL ALA ALA GLN VAL LYS
SEQRES  15 A  189  ALA PRO LEU VAL LEU LYS ASP
SEQRES   1 B  189  MSE ALA SER LYS ARG ALA LEU VAL ILE LEU ALA LYS GLY
SEQRES   2 B  189  ALA GLU GLU MSE GLU THR VAL ILE PRO VAL ASP VAL MSE
SEQRES   3 B  189  ARG ARG ALA GLY ILE LYS VAL THR VAL ALA GLY LEU ALA
SEQRES   4 B  189  GLY LYS ASP PRO VAL GLN CYS SER ARG ASP VAL VAL ILE
SEQRES   5 B  189  CYS PRO ASP ALA SER LEU GLU ASP ALA LYS LYS GLU GLY
SEQRES   6 B  189  PRO TYR ASP VAL VAL VAL LEU PRO GLY GLY ASN LEU GLY
SEQRES   7 B  189  ALA GLN ASN LEU SER GLU SER ALA ALA VAL LYS GLU ILE
SEQRES   8 B  189  LEU LYS GLU GLN GLU ASN ARG LYS GLY LEU ILE ALA ALA
SEQRES   9 B  189  ILE CYS ALA GLY PRO THR ALA LEU LEU ALA HIS GLU ILE
SEQRES  10 B  189  GLY PHE GLY SER LYS VAL THR THR HIS PRO LEU ALA LYS
SEQRES  11 B  189  ASP LYS MSE MSE ASN GLY GLY HIS TYR THR TYR SER GLU
SEQRES  12 B  189  ASN ARG VAL GLU LYS ASP GLY LEU ILE LEU THR SER ARG
SEQRES  13 B  189  GLY PRO GLY THR SER PHE GLU PHE ALA LEU ALA ILE VAL
SEQRES  14 B  189  GLU ALA LEU ASN GLY LYS GLU VAL ALA ALA GLN VAL LYS
SEQRES  15 B  189  ALA PRO LEU VAL LEU LYS ASP
SEQRES   1 C  189  MSE ALA SER LYS ARG ALA LEU VAL ILE LEU ALA LYS GLY
SEQRES   2 C  189  ALA GLU GLU MSE GLU THR VAL ILE PRO VAL ASP VAL MSE
SEQRES   3 C  189  ARG ARG ALA GLY ILE LYS VAL THR VAL ALA GLY LEU ALA
SEQRES   4 C  189  GLY LYS ASP PRO VAL GLN CYS SER ARG ASP VAL VAL ILE
SEQRES   5 C  189  CYS PRO ASP ALA SER LEU GLU ASP ALA LYS LYS GLU GLY
SEQRES   6 C  189  PRO TYR ASP VAL VAL VAL LEU PRO GLY GLY ASN LEU GLY
SEQRES   7 C  189  ALA GLN ASN LEU SER GLU SER ALA ALA VAL LYS GLU ILE
SEQRES   8 C  189  LEU LYS GLU GLN GLU ASN ARG LYS GLY LEU ILE ALA ALA
SEQRES   9 C  189  ILE CYS ALA GLY PRO THR ALA LEU LEU ALA HIS GLU ILE
SEQRES  10 C  189  GLY PHE GLY SER LYS VAL THR THR HIS PRO LEU ALA LYS
SEQRES  11 C  189  ASP LYS MSE MSE ASN GLY GLY HIS TYR THR TYR SER GLU
SEQRES  12 C  189  ASN ARG VAL GLU LYS ASP GLY LEU ILE LEU THR SER ARG
SEQRES  13 C  189  GLY PRO GLY THR SER PHE GLU PHE ALA LEU ALA ILE VAL
SEQRES  14 C  189  GLU ALA LEU ASN GLY LYS GLU VAL ALA ALA GLN VAL LYS
SEQRES  15 C  189  ALA PRO LEU VAL LEU LYS ASP
SEQRES   1 D  189  MSE ALA SER LYS ARG ALA LEU VAL ILE LEU ALA LYS GLY
SEQRES   2 D  189  ALA GLU GLU MSE GLU THR VAL ILE PRO VAL ASP VAL MSE
SEQRES   3 D  189  ARG ARG ALA GLY ILE LYS VAL THR VAL ALA GLY LEU ALA
SEQRES   4 D  189  GLY LYS ASP PRO VAL GLN CYS SER ARG ASP VAL VAL ILE
SEQRES   5 D  189  CYS PRO ASP ALA SER LEU GLU ASP ALA LYS LYS GLU GLY
SEQRES   6 D  189  PRO TYR ASP VAL VAL VAL LEU PRO GLY GLY ASN LEU GLY
SEQRES   7 D  189  ALA GLN ASN LEU SER GLU SER ALA ALA VAL LYS GLU ILE
SEQRES   8 D  189  LEU LYS GLU GLN GLU ASN ARG LYS GLY LEU ILE ALA ALA
SEQRES   9 D  189  ILE CYS ALA GLY PRO THR ALA LEU LEU ALA HIS GLU ILE
SEQRES  10 D  189  GLY PHE GLY SER LYS VAL THR THR HIS PRO LEU ALA LYS
SEQRES  11 D  189  ASP LYS MSE MSE ASN GLY GLY HIS TYR THR TYR SER GLU
SEQRES  12 D  189  ASN ARG VAL GLU LYS ASP GLY LEU ILE LEU THR SER ARG
SEQRES  13 D  189  GLY PRO GLY THR SER PHE GLU PHE ALA LEU ALA ILE VAL
SEQRES  14 D  189  GLU ALA LEU ASN GLY LYS GLU VAL ALA ALA GLN VAL LYS
SEQRES  15 D  189  ALA PRO LEU VAL LEU LYS ASP
SEQRES   1 E  189  MSE ALA SER LYS ARG ALA LEU VAL ILE LEU ALA LYS GLY
SEQRES   2 E  189  ALA GLU GLU MSE GLU THR VAL ILE PRO VAL ASP VAL MSE
SEQRES   3 E  189  ARG ARG ALA GLY ILE LYS VAL THR VAL ALA GLY LEU ALA
SEQRES   4 E  189  GLY LYS ASP PRO VAL GLN CYS SER ARG ASP VAL VAL ILE
SEQRES   5 E  189  CYS PRO ASP ALA SER LEU GLU ASP ALA LYS LYS GLU GLY
SEQRES   6 E  189  PRO TYR ASP VAL VAL VAL LEU PRO GLY GLY ASN LEU GLY
SEQRES   7 E  189  ALA GLN ASN LEU SER GLU SER ALA ALA VAL LYS GLU ILE
SEQRES   8 E  189  LEU LYS GLU GLN GLU ASN ARG LYS GLY LEU ILE ALA ALA
SEQRES   9 E  189  ILE CYS ALA GLY PRO THR ALA LEU LEU ALA HIS GLU ILE
SEQRES  10 E  189  GLY PHE GLY SER LYS VAL THR THR HIS PRO LEU ALA LYS
SEQRES  11 E  189  ASP LYS MSE MSE ASN GLY GLY HIS TYR THR TYR SER GLU
SEQRES  12 E  189  ASN ARG VAL GLU LYS ASP GLY LEU ILE LEU THR SER ARG
SEQRES  13 E  189  GLY PRO GLY THR SER PHE GLU PHE ALA LEU ALA ILE VAL
SEQRES  14 E  189  GLU ALA LEU ASN GLY LYS GLU VAL ALA ALA GLN VAL LYS
SEQRES  15 E  189  ALA PRO LEU VAL LEU LYS ASP
SEQRES   1 F  189  MSE ALA SER LYS ARG ALA LEU VAL ILE LEU ALA LYS GLY
SEQRES   2 F  189  ALA GLU GLU MSE GLU THR VAL ILE PRO VAL ASP VAL MSE
SEQRES   3 F  189  ARG ARG ALA GLY ILE LYS VAL THR VAL ALA GLY LEU ALA
SEQRES   4 F  189  GLY LYS ASP PRO VAL GLN CYS SER ARG ASP VAL VAL ILE
SEQRES   5 F  189  CYS PRO ASP ALA SER LEU GLU ASP ALA LYS LYS GLU GLY
SEQRES   6 F  189  PRO TYR ASP VAL VAL VAL LEU PRO GLY GLY ASN LEU GLY
SEQRES   7 F  189  ALA GLN ASN LEU SER GLU SER ALA ALA VAL LYS GLU ILE
SEQRES   8 F  189  LEU LYS GLU GLN GLU ASN ARG LYS GLY LEU ILE ALA ALA
SEQRES   9 F  189  ILE CYS ALA GLY PRO THR ALA LEU LEU ALA HIS GLU ILE
SEQRES  10 F  189  GLY PHE GLY SER LYS VAL THR THR HIS PRO LEU ALA LYS
SEQRES  11 F  189  ASP LYS MSE MSE ASN GLY GLY HIS TYR THR TYR SER GLU
SEQRES  12 F  189  ASN ARG VAL GLU LYS ASP GLY LEU ILE LEU THR SER ARG
SEQRES  13 F  189  GLY PRO GLY THR SER PHE GLU PHE ALA LEU ALA ILE VAL
SEQRES  14 F  189  GLU ALA LEU ASN GLY LYS GLU VAL ALA ALA GLN VAL LYS
SEQRES  15 F  189  ALA PRO LEU VAL LEU LYS ASP
SEQRES   1 G  189  MSE ALA SER LYS ARG ALA LEU VAL ILE LEU ALA LYS GLY
SEQRES   2 G  189  ALA GLU GLU MSE GLU THR VAL ILE PRO VAL ASP VAL MSE
SEQRES   3 G  189  ARG ARG ALA GLY ILE LYS VAL THR VAL ALA GLY LEU ALA
SEQRES   4 G  189  GLY LYS ASP PRO VAL GLN CYS SER ARG ASP VAL VAL ILE
SEQRES   5 G  189  CYS PRO ASP ALA SER LEU GLU ASP ALA LYS LYS GLU GLY
SEQRES   6 G  189  PRO TYR ASP VAL VAL VAL LEU PRO GLY GLY ASN LEU GLY
SEQRES   7 G  189  ALA GLN ASN LEU SER GLU SER ALA ALA VAL LYS GLU ILE
SEQRES   8 G  189  LEU LYS GLU GLN GLU ASN ARG LYS GLY LEU ILE ALA ALA
SEQRES   9 G  189  ILE CYS ALA GLY PRO THR ALA LEU LEU ALA HIS GLU ILE
SEQRES  10 G  189  GLY PHE GLY SER LYS VAL THR THR HIS PRO LEU ALA LYS
SEQRES  11 G  189  ASP LYS MSE MSE ASN GLY GLY HIS TYR THR TYR SER GLU
SEQRES  12 G  189  ASN ARG VAL GLU LYS ASP GLY LEU ILE LEU THR SER ARG
SEQRES  13 G  189  GLY PRO GLY THR SER PHE GLU PHE ALA LEU ALA ILE VAL
SEQRES  14 G  189  GLU ALA LEU ASN GLY LYS GLU VAL ALA ALA GLN VAL LYS
SEQRES  15 G  189  ALA PRO LEU VAL LEU LYS ASP
MODRES 3BWE MSE A    1  MET  SELENOMETHIONINE
MODRES 3BWE MSE A   17  MET  SELENOMETHIONINE
MODRES 3BWE MSE A   26  MET  SELENOMETHIONINE
MODRES 3BWE MSE A  133  MET  SELENOMETHIONINE
MODRES 3BWE MSE A  134  MET  SELENOMETHIONINE
MODRES 3BWE MSE B  217  MET  SELENOMETHIONINE
MODRES 3BWE MSE B  226  MET  SELENOMETHIONINE
MODRES 3BWE MSE B  333  MET  SELENOMETHIONINE
MODRES 3BWE MSE B  334  MET  SELENOMETHIONINE
MODRES 3BWE MSE C  401  MET  SELENOMETHIONINE
MODRES 3BWE MSE C  417  MET  SELENOMETHIONINE
MODRES 3BWE MSE C  426  MET  SELENOMETHIONINE
MODRES 3BWE MSE C  533  MET  SELENOMETHIONINE
MODRES 3BWE MSE C  534  MET  SELENOMETHIONINE
MODRES 3BWE MSE D  617  MET  SELENOMETHIONINE
MODRES 3BWE MSE D  626  MET  SELENOMETHIONINE
MODRES 3BWE MSE D  733  MET  SELENOMETHIONINE
MODRES 3BWE MSE D  734  MET  SELENOMETHIONINE
MODRES 3BWE MSE E  817  MET  SELENOMETHIONINE
MODRES 3BWE MSE E  826  MET  SELENOMETHIONINE
MODRES 3BWE MSE E  933  MET  SELENOMETHIONINE
MODRES 3BWE MSE E  934  MET  SELENOMETHIONINE
MODRES 3BWE MSE F 1017  MET  SELENOMETHIONINE
MODRES 3BWE MSE F 1026  MET  SELENOMETHIONINE
MODRES 3BWE MSE F 1133  MET  SELENOMETHIONINE
MODRES 3BWE MSE F 1134  MET  SELENOMETHIONINE
MODRES 3BWE MSE G 1217  MET  SELENOMETHIONINE
MODRES 3BWE MSE G 1226  MET  SELENOMETHIONINE
MODRES 3BWE MSE G 1333  MET  SELENOMETHIONINE
MODRES 3BWE MSE G 1334  MET  SELENOMETHIONINE
HET    MSE  A   1       5
HET    MSE  A  17       8
HET    MSE  A  26       8
HET    MSE  A 133       8
HET    MSE  A 134       8
HET    MSE  B 217       8
HET    MSE  B 226       8
HET    MSE  B 333       8
HET    MSE  B 334       8
HET    MSE  C 401       5
HET    MSE  C 417       8
HET    MSE  C 426       8
HET    MSE  C 533       8
HET    MSE  C 534       8
HET    MSE  D 617       8
HET    MSE  D 626       8
HET    MSE  D 733       8
HET    MSE  D 734       8
HET    MSE  E 817       8
HET    MSE  E 826       8
HET    MSE  E 933       8
HET    MSE  E 934       8
HET    MSE  F1017       8
HET    MSE  F1026       8
HET    MSE  F1133       8
HET    MSE  F1134       8
HET    MSE  G1217       8
HET    MSE  G1226       8
HET    MSE  G1333       8
HET    MSE  G1334       8
HET    PO4  A 190       5
HET    PO4  A 191       5
HET    PO4  C   3       5
HET    PO4  D   1       5
HET    PO4  E   6       5
HET    PO4  F   4       5
HET    PO4  F   5       5
HETNAM     MSE SELENOMETHIONINE
HETNAM     PO4 PHOSPHATE ION
FORMUL   1  MSE    30(C5 H11 N O2 SE)
FORMUL   8  PO4    7(O4 P 3-)
FORMUL  15  HOH   *283(H2 O)
HELIX    1   1 GLU A   15  ALA A   29  1                                  15
HELIX    2   2 LEU A   58  LYS A   62  1                                   5
HELIX    3   3 GLY A   75  GLU A   84  1                                  10
HELIX    4   4 SER A   85  ARG A   98  1                                  14
HELIX    5   5 PRO A  109  HIS A  115  1                                   7
HELIX    6   6 HIS A  126  LEU A  128  5                                   3
HELIX    7   7 ALA A  129  MSE A  134  1                                   6
HELIX    8   8 GLY A  157  GLY A  159  5                                   3
HELIX    9   9 THR A  160  GLY A  174  1                                  15
HELIX   10  10 GLY A  174  ALA A  183  1                                  10
HELIX   11  11 PRO A  184  VAL A  186  5                                   3
HELIX   12  12 GLU B  215  ALA B  229  1                                  15
HELIX   13  13 LEU B  258  LYS B  262  1                                   5
HELIX   14  14 GLY B  275  GLU B  284  1                                  10
HELIX   15  15 SER B  285  ARG B  298  1                                  14
HELIX   16  16 GLY B  308  HIS B  315  1                                   8
HELIX   17  17 HIS B  326  LEU B  328  5                                   3
HELIX   18  18 ALA B  329  ASN B  335  1                                   7
HELIX   19  19 GLY B  357  GLY B  359  5                                   3
HELIX   20  20 THR B  360  GLY B  374  1                                  15
HELIX   21  21 GLY B  374  VAL B  386  1                                  13
HELIX   22  22 GLU C  415  ALA C  429  1                                  15
HELIX   23  23 LEU C  458  GLU C  464  1                                   7
HELIX   24  24 GLY C  475  GLU C  484  1                                  10
HELIX   25  25 SER C  485  ARG C  498  1                                  14
HELIX   26  26 GLY C  508  HIS C  515  1                                   8
HELIX   27  27 HIS C  526  LEU C  528  5                                   3
HELIX   28  28 ALA C  529  ASN C  535  1                                   7
HELIX   29  29 GLY C  557  GLY C  559  5                                   3
HELIX   30  30 THR C  560  GLY C  574  1                                  15
HELIX   31  31 GLY C  574  ALA C  583  1                                  10
HELIX   32  32 PRO C  584  VAL C  586  5                                   3
HELIX   33  33 GLU D  615  ALA D  629  1                                  15
HELIX   34  34 LEU D  658  LYS D  662  1                                   5
HELIX   35  35 GLY D  675  SER D  685  1                                  11
HELIX   36  36 SER D  685  ARG D  698  1                                  14
HELIX   37  37 GLY D  708  HIS D  715  1                                   8
HELIX   38  38 HIS D  726  LEU D  728  5                                   3
HELIX   39  39 ALA D  729  MSE D  734  1                                   6
HELIX   40  40 GLY D  757  GLY D  759  5                                   3
HELIX   41  41 THR D  760  ALA D  783  1                                  24
HELIX   42  42 PRO D  784  VAL D  786  5                                   3
HELIX   43  43 GLU E  815  ALA E  829  1                                  15
HELIX   44  44 LEU E  858  GLU E  864  1                                   7
HELIX   45  45 GLY E  875  SER E  885  1                                  11
HELIX   46  46 SER E  885  ARG E  898  1                                  14
HELIX   47  47 PRO E  909  HIS E  915  1                                   7
HELIX   48  48 HIS E  926  LEU E  928  5                                   3
HELIX   49  49 ALA E  929  MSE E  934  1                                   6
HELIX   50  50 GLY E  957  GLY E  959  5                                   3
HELIX   51  51 THR E  960  GLY E  974  1                                  15
HELIX   52  52 GLY E  974  ALA E  983  1                                  10
HELIX   53  53 PRO E  984  VAL E  986  5                                   3
HELIX   54  54 GLU F 1015  ALA F 1029  1                                  15
HELIX   55  55 LEU F 1058  GLU F 1064  1                                   7
HELIX   56  56 GLY F 1075  SER F 1085  1                                  11
HELIX   57  57 SER F 1085  ARG F 1098  1                                  14
HELIX   58  58 GLY F 1108  HIS F 1115  1                                   8
HELIX   59  59 HIS F 1126  LEU F 1128  5                                   3
HELIX   60  60 ALA F 1129  ASN F 1135  1                                   7
HELIX   61  61 GLY F 1157  GLY F 1159  5                                   3
HELIX   62  62 THR F 1160  GLY F 1174  1                                  15
HELIX   63  63 GLY F 1174  ALA F 1183  1                                  10
HELIX   64  64 PRO F 1184  VAL F 1186  5                                   3
HELIX   65  65 GLU G 1215  ALA G 1229  1                                  15
HELIX   66  66 LEU G 1258  GLU G 1264  1                                   7
HELIX   67  67 ASN G 1276  SER G 1285  1                                  10
HELIX   68  68 SER G 1285  ARG G 1298  1                                  14
HELIX   69  69 GLY G 1308  HIS G 1315  1                                   8
HELIX   70  70 HIS G 1326  LEU G 1328  5                                   3
HELIX   71  71 ALA G 1329  MSE G 1334  1                                   6
HELIX   72  72 ASN G 1335  HIS G 1338  5                                   4
HELIX   73  73 GLY G 1357  GLY G 1359  5                                   3
HELIX   74  74 THR G 1360  GLY G 1374  1                                  15
HELIX   75  75 GLY G 1374  ALA G 1383  1                                  10
HELIX   76  76 PRO G 1384  VAL G 1386  5                                   3
SHEET    1   A 7 ALA A  56  SER A  57  0
SHEET    2   A 7 LYS A  32  GLY A  37  1  N  GLY A  37   O  ALA A  56
SHEET    3   A 7 ARG A   5  LEU A  10  1  N  ALA A   6   O  LYS A  32
SHEET    4   A 7 VAL A  69  LEU A  72  1  O  VAL A  71   N  LEU A   7
SHEET    5   A 7 LEU A 101  ILE A 105  1  O  ALA A 103   N  VAL A  70
SHEET    6   A 7 ILE A 152  SER A 155  1  O  LEU A 153   N  ILE A 102
SHEET    7   A 7 VAL A 146  ASP A 149 -1  N  GLU A 147   O  THR A 154
SHEET    1   B 4 VAL A  44  GLN A  45  0
SHEET    2   B 4 VAL A  51  CYS A  53 -1  O  ILE A  52   N  VAL A  44
SHEET    3   B 4 VAL B 251  CYS B 253 -1  O  CYS B 253   N  VAL A  51
SHEET    4   B 4 VAL B 244  GLN B 245 -1  N  VAL B 244   O  ILE B 252
SHEET    1   C 2 LYS A 122  VAL A 123  0
SHEET    2   C 2 THR A 140  TYR A 141  1  O  THR A 140   N  VAL A 123
SHEET    1   D 7 ALA B 256  SER B 257  0
SHEET    2   D 7 LYS B 232  GLY B 237  1  N  GLY B 237   O  ALA B 256
SHEET    3   D 7 ARG B 205  LEU B 210  1  N  LEU B 210   O  ALA B 236
SHEET    4   D 7 VAL B 269  LEU B 272  1  O  VAL B 271   N  LEU B 207
SHEET    5   D 7 LEU B 301  ILE B 305  1  O  ALA B 303   N  LEU B 272
SHEET    6   D 7 ILE B 352  SER B 355  1  O  LEU B 353   N  ILE B 302
SHEET    7   D 7 VAL B 346  ASP B 349 -1  N  GLU B 347   O  THR B 354
SHEET    1   E 2 LYS B 322  VAL B 323  0
SHEET    2   E 2 THR B 340  TYR B 341  1  O  THR B 340   N  VAL B 323
SHEET    1   F 7 ALA C 456  SER C 457  0
SHEET    2   F 7 LYS C 432  GLY C 437  1  N  GLY C 437   O  ALA C 456
SHEET    3   F 7 ARG C 405  LEU C 410  1  N  VAL C 408   O  ALA C 436
SHEET    4   F 7 VAL C 469  LEU C 472  1  O  VAL C 471   N  LEU C 407
SHEET    5   F 7 LEU C 501  ILE C 505  1  O  ALA C 503   N  VAL C 470
SHEET    6   F 7 ILE C 552  SER C 555  1  O  LEU C 553   N  ILE C 502
SHEET    7   F 7 VAL C 546  ASP C 549 -1  N  GLU C 547   O  THR C 554
SHEET    1   G 4 VAL C 444  GLN C 445  0
SHEET    2   G 4 VAL C 451  CYS C 453 -1  O  ILE C 452   N  VAL C 444
SHEET    3   G 4 VAL D 651  ILE D 652 -1  O  VAL D 651   N  CYS C 453
SHEET    4   G 4 VAL D 644  GLN D 645 -1  N  VAL D 644   O  ILE D 652
SHEET    1   H 2 LYS C 522  VAL C 523  0
SHEET    2   H 2 THR C 540  TYR C 541  1  O  THR C 540   N  VAL C 523
SHEET    1   I 7 ALA D 656  SER D 657  0
SHEET    2   I 7 LYS D 632  GLY D 637  1  N  GLY D 637   O  ALA D 656
SHEET    3   I 7 ARG D 605  LEU D 610  1  N  LEU D 610   O  ALA D 636
SHEET    4   I 7 VAL D 669  LEU D 672  1  O  VAL D 671   N  LEU D 607
SHEET    5   I 7 LEU D 701  ILE D 705  1  O  ALA D 703   N  LEU D 672
SHEET    6   I 7 ILE D 752  SER D 755  1  O  LEU D 753   N  ILE D 702
SHEET    7   I 7 VAL D 746  ASP D 749 -1  N  GLU D 747   O  THR D 754
SHEET    1   J 2 LYS D 722  VAL D 723  0
SHEET    2   J 2 THR D 740  TYR D 741  1  O  THR D 740   N  VAL D 723
SHEET    1   K 7 ALA E 856  SER E 857  0
SHEET    2   K 7 LYS E 832  GLY E 837  1  N  GLY E 837   O  ALA E 856
SHEET    3   K 7 ARG E 805  LEU E 810  1  N  VAL E 808   O  ALA E 836
SHEET    4   K 7 VAL E 869  LEU E 872  1  O  VAL E 869   N  LEU E 807
SHEET    5   K 7 LEU E 901  ILE E 905  1  O  ALA E 903   N  LEU E 872
SHEET    6   K 7 ILE E 952  SER E 955  1  O  LEU E 953   N  ILE E 902
SHEET    7   K 7 VAL E 946  ASP E 949 -1  N  GLU E 947   O  THR E 954
SHEET    1   L 4 VAL E 844  GLN E 845  0
SHEET    2   L 4 VAL E 851  CYS E 853 -1  O  ILE E 852   N  VAL E 844
SHEET    3   L 4 VAL F1051  CYS F1053 -1  O  VAL F1051   N  CYS E 853
SHEET    4   L 4 VAL F1044  GLN F1045 -1  N  VAL F1044   O  ILE F1052
SHEET    1   M 2 LYS E 922  VAL E 923  0
SHEET    2   M 2 THR E 940  TYR E 941  1  O  THR E 940   N  VAL E 923
SHEET    1   N 7 ALA F1056  SER F1057  0
SHEET    2   N 7 LYS F1032  GLY F1037  1  N  GLY F1037   O  ALA F1056
SHEET    3   N 7 ARG F1005  LEU F1010  1  N  VAL F1008   O  THR F1034
SHEET    4   N 7 VAL F1069  LEU F1072  1  O  VAL F1071   N  LEU F1007
SHEET    5   N 7 LEU F1101  ILE F1105  1  O  ALA F1103   N  LEU F1072
SHEET    6   N 7 ILE F1152  SER F1155  1  O  LEU F1153   N  ALA F1104
SHEET    7   N 7 VAL F1146  ASP F1149 -1  N  GLU F1147   O  THR F1154
SHEET    1   O 2 LYS F1122  VAL F1123  0
SHEET    2   O 2 THR F1140  TYR F1141  1  O  THR F1140   N  VAL F1123
SHEET    1   P 7 ALA G1256  SER G1257  0
SHEET    2   P 7 LYS G1232  GLY G1237  1  N  GLY G1237   O  ALA G1256
SHEET    3   P 7 ARG G1205  LEU G1210  1  N  LEU G1210   O  ALA G1236
SHEET    4   P 7 VAL G1269  LEU G1272  1  O  VAL G1269   N  LEU G1207
SHEET    5   P 7 LEU G1301  ILE G1305  1  O  ALA G1303   N  LEU G1272
SHEET    6   P 7 ILE G1352  SER G1355  1  O  LEU G1353   N  ILE G1302
SHEET    7   P 7 VAL G1346  ASP G1349 -1  N  ASP G1349   O  ILE G1352
SHEET    1   Q 2 VAL G1244  GLN G1245  0
SHEET    2   Q 2 VAL G1251  ILE G1252 -1  O  ILE G1252   N  VAL G1244
SHEET    1   R 2 LYS G1322  VAL G1323  0
SHEET    2   R 2 THR G1340  TYR G1341  1  O  THR G1340   N  VAL G1323
SSBOND   1 CYS C  453    CYS D  653                          1555   1555  2.07
SSBOND   2 CYS E  853    CYS F 1053                          1555   1555  3.00
LINK         C   MSE A   1                 N   ALA A   2     1555   1555  1.34
LINK         C   GLU A  16                 N   MSE A  17     1555   1555  1.33
LINK         C   MSE A  17                 N   GLU A  18     1555   1555  1.32
LINK         C   VAL A  25                 N   MSE A  26     1555   1555  1.33
LINK         C   MSE A  26                 N   ARG A  27     1555   1555  1.33
LINK         C   LYS A 132                 N   MSE A 133     1555   1555  1.33
LINK         C   MSE A 133                 N   MSE A 134     1555   1555  1.33
LINK         C   MSE A 134                 N   ASN A 135     1555   1555  1.32
LINK         C   GLU B 216                 N   MSE B 217     1555   1555  1.33
LINK         C   MSE B 217                 N   GLU B 218     1555   1555  1.33
LINK         C   VAL B 225                 N   MSE B 226     1555   1555  1.33
LINK         C   MSE B 226                 N   ARG B 227     1555   1555  1.33
LINK         C   LYS B 332                 N   MSE B 333     1555   1555  1.32
LINK         C   MSE B 333                 N   MSE B 334     1555   1555  1.32
LINK         C   MSE B 334                 N   ASN B 335     1555   1555  1.32
LINK         C   MSE C 401                 N   ALA C 402     1555   1555  1.33
LINK         C   GLU C 416                 N   MSE C 417     1555   1555  1.33
LINK         C   MSE C 417                 N   GLU C 418     1555   1555  1.33
LINK         C   VAL C 425                 N   MSE C 426     1555   1555  1.33
LINK         C   MSE C 426                 N   ARG C 427     1555   1555  1.33
LINK         C   LYS C 532                 N   MSE C 533     1555   1555  1.32
LINK         C   MSE C 533                 N   MSE C 534     1555   1555  1.33
LINK         C   MSE C 534                 N   ASN C 535     1555   1555  1.32
LINK         C   GLU D 616                 N   MSE D 617     1555   1555  1.33
LINK         C   MSE D 617                 N   GLU D 618     1555   1555  1.33
LINK         C   VAL D 625                 N   MSE D 626     1555   1555  1.33
LINK         C   MSE D 626                 N   ARG D 627     1555   1555  1.33
LINK         C   LYS D 732                 N   MSE D 733     1555   1555  1.33
LINK         C   MSE D 733                 N   MSE D 734     1555   1555  1.33
LINK         C   MSE D 734                 N   ASN D 735     1555   1555  1.33
LINK         C   GLU E 816                 N   MSE E 817     1555   1555  1.32
LINK         C   MSE E 817                 N   GLU E 818     1555   1555  1.33
LINK         C   VAL E 825                 N   MSE E 826     1555   1555  1.33
LINK         C   MSE E 826                 N   ARG E 827     1555   1555  1.33
LINK         C   LYS E 932                 N   MSE E 933     1555   1555  1.33
LINK         C   MSE E 933                 N   MSE E 934     1555   1555  1.33
LINK         C   MSE E 934                 N   ASN E 935     1555   1555  1.33
LINK         C   GLU F1016                 N   MSE F1017     1555   1555  1.32
LINK         C   MSE F1017                 N   GLU F1018     1555   1555  1.33
LINK         C   VAL F1025                 N   MSE F1026     1555   1555  1.33
LINK         C   MSE F1026                 N   ARG F1027     1555   1555  1.33
LINK         C   LYS F1132                 N   MSE F1133     1555   1555  1.32
LINK         C   MSE F1133                 N   MSE F1134     1555   1555  1.33
LINK         C   MSE F1134                 N   ASN F1135     1555   1555  1.32
LINK         C   GLU G1216                 N   MSE G1217     1555   1555  1.33
LINK         C   MSE G1217                 N   GLU G1218     1555   1555  1.33
LINK         C   VAL G1225                 N   MSE G1226     1555   1555  1.33
LINK         C   MSE G1226                 N   ARG G1227     1555   1555  1.33
LINK         C   LYS G1332                 N   MSE G1333     1555   1555  1.33
LINK         C   MSE G1333                 N   MSE G1334     1555   1555  1.33
LINK         C   MSE G1334                 N   ASN G1335     1555   1555  1.33
SITE     1 AC1  4 ARG A  48  ASN A  76  HOH C  95  GLN C 580
SITE     1 AC2  6 GLN A 180  HOH A 228  SER B 247  ARG B 248
SITE     2 AC2  6 GLY B 275  ASN B 276
SITE     1 AC3  4 ARG C 448  ASN C 476  ARG D 628  GLN E 980
SITE     1 AC4  5 GLN B 380  ARG C 428  ARG D 648  GLY D 675
SITE     2 AC4  5 ASN D 676
SITE     1 AC5  4 ARG E 848  ASN E 876  HOH G 174  GLN G1380
SITE     1 AC6  4 HOH D 126  GLN D 780  ARG F1048  ASN F1076
SITE     1 AC7  6 GLN F1180  GLU G1215  ARG G1248  GLY G1275
SITE     2 AC7  6 ASN G1276  LEU G1277
CRYST1  193.616  102.582   85.535  90.00 113.69  90.00 C 1 2 1      28
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      0.005165  0.000000  0.002266        0.00000
SCALE2      0.000000  0.009748  0.000000        0.00000
SCALE3      0.000000  0.000000  0.012767        0.00000
      
PROCHECK
Go to PROCHECK summary
 References