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PDBsum entry 2rk6

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Chaperone PDB id
2rk6
Jmol
Contents
Protein chain
186 a.a.
Waters ×190
HEADER    CHAPERONE                               16-OCT-07   2RK6
TITLE     STRUCTURE OF E163K DJ-1
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROTEIN DJ-1;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: ONCOGENE DJ1, PARKINSON DISEASE PROTEIN 7;
COMPND   5 ENGINEERED: YES;
COMPND   6 MUTATION: 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 BL21(DE3);
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS    PARKINSON'S DISEASE, THIJ, PFPI, CHAPERONE, DISEASE MUTATION,
KEYWDS   2 NUCLEUS, ONCOGENE, OXIDATION, PARKINSON DISEASE, PHOSPHORYLATION
EXPDTA    X-RAY DIFFRACTION
AUTHOR    M.LAKSHMINARASIMHAN,M.T.MALDONADO,W.ZHOU,A.L.FINK,M.A.WILSON
REVDAT   4   19-NOV-14 2RK6    1       HET    HETATM HETNAM VERSN
REVDAT   3   24-FEB-09 2RK6    1       VERSN
REVDAT   2   19-FEB-08 2RK6    1       JRNL
REVDAT   1   15-JAN-08 2RK6    0
JRNL        AUTH   M.LAKSHMINARASIMHAN,M.T.MALDONADO,W.ZHOU,A.L.FINK,M.A.WILSON
JRNL        TITL   STRUCTURAL IMPACT OF THREE PARKINSONISM-ASSOCIATED MISSENSE
JRNL        TITL 2 MUTATIONS ON HUMAN DJ-1.
JRNL        REF    BIOCHEMISTRY                  V.  47  1381 2008
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   18181649
JRNL        DOI    10.1021/BI701189C
REMARK   2
REMARK   2 RESOLUTION.    1.15 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : SHELXL-97
REMARK   3   AUTHORS     : G.M.SHELDRICK
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.15
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0
REMARK   3   CROSS-VALIDATION METHOD           : FREE R
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.150
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.149
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.175
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 4331
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 86744
REMARK   3
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.122
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.121
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.143
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 3317
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 66376
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS      : 1368
REMARK   3   NUCLEIC ACID ATOMS : 0
REMARK   3   HETEROGEN ATOMS    : 0
REMARK   3   SOLVENT ATOMS      : 190
REMARK   3
REMARK   3  MODEL REFINEMENT.
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 1556.80
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 1385.00
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 10
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 14801
REMARK   3   NUMBER OF RESTRAINTS                     : 18983
REMARK   3
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK   3   BOND LENGTHS                         (A) : 0.013
REMARK   3   ANGLE DISTANCES                      (A) : 0.029
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.029
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.075
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.087
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.029
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.005
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.055
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.106
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED: BABINET
REMARK   3
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER
REMARK   3   SPECIAL CASE: NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2RK6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-DEC-07.
REMARK 100 THE RCSB ID CODE IS RCSB044958.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 12-MAR-06
REMARK 200  TEMPERATURE           (KELVIN) : 110
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 14-BM-C
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.90
REMARK 200  MONOCHROMATOR                  : SINGLE CRYSTAL BENT GE(111)
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   : 86963
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.150
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     (%) : 100.0
REMARK 200  DATA REDUNDANCY                : 10.700
REMARK 200  R MERGE                    (I) : 0.07900
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 34.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.15
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.19
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.40
REMARK 200  R MERGE FOR SHELL          (I) : 0.81900
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: SHELXL
REMARK 200 STARTING MODEL: 1P5F
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 59.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 M SODIUM CITRATE, 20 MM HEPES, PH
REMARK 280  7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+1/3
REMARK 290       3555   -X+Y,-X,Z+2/3
REMARK 290       4555   Y,X,-Z
REMARK 290       5555   X-Y,-Y,-Z+2/3
REMARK 290       6555   -X,-X+Y,-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       25.04900
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       50.09800
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   4  0.866025  0.500000  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        0.00000
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       50.09800
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       25.04900
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2540 ANGSTROM**2
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   BIOMT1   2 -0.500000 -0.866025  0.000000        0.00000
REMARK 350   BIOMT2   2 -0.866025  0.500000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       25.04900
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     GLY A    -2
REMARK 465     SER A    -1
REMARK 465     HIS A     0
REMARK 465     MET A     1
REMARK 465     LYS A   188
REMARK 465     ASP A   189
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    ARG A   5   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES
REMARK 500    ARG A   5   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES
REMARK 500    GLY A  65   C   -  N   -  CA  ANGL. DEV. = -12.8 DEGREES
REMARK 500    ARG A  98   NE  -  CZ  -  NH1 ANGL. DEV. =   5.0 DEGREES
REMARK 500    ARG A  98   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.7 DEGREES
REMARK 500    ARG A 145   NE  -  CZ  -  NH1 ANGL. DEV. =   5.1 DEGREES
REMARK 500    ARG A 145   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 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    CSD A 106     -107.80     72.87
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 A 374        DISTANCE =  7.08 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2RK3   RELATED DB: PDB
REMARK 900 STRUCTURE OF A104T DJ-1
REMARK 900 RELATED ID: 2RK4   RELATED DB: PDB
REMARK 900 STRUCTURE OF M26I DJ-1
DBREF  2RK6 A    1   189  UNP    Q99497   PARK7_HUMAN      1    189
SEQADV 2RK6 GLY A   -2  UNP  Q99497              EXPRESSION TAG
SEQADV 2RK6 SER A   -1  UNP  Q99497              EXPRESSION TAG
SEQADV 2RK6 HIS A    0  UNP  Q99497              EXPRESSION TAG
SEQADV 2RK6 LYS A  163  UNP  Q99497    GLU   163 ENGINEERED
SEQRES   1 A  192  GLY SER HIS MET ALA SER LYS ARG ALA LEU VAL ILE LEU
SEQRES   2 A  192  ALA LYS GLY ALA GLU GLU MET GLU THR VAL ILE PRO VAL
SEQRES   3 A  192  ASP VAL MET ARG ARG ALA GLY ILE LYS VAL THR VAL ALA
SEQRES   4 A  192  GLY LEU ALA GLY LYS ASP PRO VAL GLN CYS SER ARG ASP
SEQRES   5 A  192  VAL VAL ILE CYS PRO ASP ALA SER LEU GLU ASP ALA LYS
SEQRES   6 A  192  LYS GLU GLY PRO TYR ASP VAL VAL VAL LEU PRO GLY GLY
SEQRES   7 A  192  ASN LEU GLY ALA GLN ASN LEU SER GLU SER ALA ALA VAL
SEQRES   8 A  192  LYS GLU ILE LEU LYS GLU GLN GLU ASN ARG LYS GLY LEU
SEQRES   9 A  192  ILE ALA ALA ILE CSD ALA GLY PRO THR ALA LEU LEU ALA
SEQRES  10 A  192  HIS GLU ILE GLY PHE GLY SER LYS VAL THR THR HIS PRO
SEQRES  11 A  192  LEU ALA LYS ASP LYS MET MET ASN GLY GLY HIS TYR THR
SEQRES  12 A  192  TYR SER GLU ASN ARG VAL GLU LYS ASP GLY LEU ILE LEU
SEQRES  13 A  192  THR SER ARG GLY PRO GLY THR SER PHE LYS PHE ALA LEU
SEQRES  14 A  192  ALA ILE VAL GLU ALA LEU ASN GLY LYS GLU VAL ALA ALA
SEQRES  15 A  192  GLN VAL LYS ALA PRO LEU VAL LEU LYS ASP
MODRES 2RK6 CSD A  106  CYS  3-SULFINOALANINE
HET    CSD  A 106       8
HETNAM     CSD 3-SULFINOALANINE
HETSYN     CSD S-CYSTEINESULFINIC ACID; S-SULFINOCYSTEINE
FORMUL   1  CSD    C3 H7 N O4 S
FORMUL   2  HOH   *190(H2 O)
HELIX    1   1 GLU A   15  ALA A   29  1                                  15
HELIX    2   2 LEU A   58  LYS A   63  1                                   6
HELIX    3   3 GLY A   75  SER A   85  1                                  11
HELIX    4   4 SER A   85  ARG A   98  1                                  14
HELIX    5   5 GLY A  108  HIS A  115  1                                   8
HELIX    6   6 HIS A  126  LEU A  128  5                                   3
HELIX    7   7 ALA A  129  MET 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
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  LEU A  10   O  ALA A  36
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 2 VAL A  44  GLN A  45  0
SHEET    2   B 2 VAL A  51  ILE A  52 -1  O  ILE A  52   N  VAL A  44
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
LINK         C   ILE A 105                 N   CSD A 106     1555   1555  1.36
LINK         C   CSD A 106                 N   ALA A 107     1555   1555  1.34
CISPEP   1 GLY A   65    PRO A   66          0         1.54
CRYST1   74.928   74.928   75.147  90.00  90.00 120.00 P 31 2 1      6
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      0.013346  0.007705  0.000000        0.00000
SCALE2      0.000000  0.015411  0.000000        0.00000
SCALE3      0.000000  0.000000  0.013307        0.00000
      
PROCHECK
Go to PROCHECK summary
 References