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PDBsum entry 3ezg

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Chaperone PDB id
3ezg
Jmol
Contents
Protein chain
187 a.a.
Waters ×288
HEADER    CHAPERONE                               22-OCT-08   3EZG
TITLE     CRYSTAL STRUCTURE OF E18Q DJ-1 WITH OXIDIZED C106
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;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLSMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET21A
KEYWDS    CYSTEINE OXIDATION, SULFINIC ACID, CHAPERONE, CYTOPLASM,
KEYWDS   2 DISEASE MUTATION, NUCLEUS, ONCOGENE, OXIDATION, PARKINSON
KEYWDS   3 DISEASE, PHOSPHOPROTEIN, POLYMORPHISM, UBL CONJUGATION
EXPDTA    X-RAY DIFFRACTION
AUTHOR    M.LAKSHMINARASIMHAN,M.A.WILSON
REVDAT   2   17-MAR-09 3EZG    1       JRNL
REVDAT   1   30-DEC-08 3EZG    0
JRNL        AUTH   J.BLACKINTON,M.LAKSHMINARASIMHAN,K.J.THOMAS,
JRNL        AUTH 2 R.AHMAD,E.GREGGIO,A.S.RAZA,M.R.COOKSON,M.A.WILSON
JRNL        TITL   FORMATION OF A STABILIZED CYSTEINE SULFINIC ACID
JRNL        TITL 2 IS CRITICAL FOR THE MITOCHONDRIAL FUNCTION OF THE
JRNL        TITL 3 PARKINSONISM PROTEIN DJ-1.
JRNL        REF    J.BIOL.CHEM.                  V. 284  6476 2009
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   19124468
JRNL        DOI    10.1074/JBC.M806599200
REMARK   1
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) : 30.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8
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) : 0.116
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.116
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.145
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 4279
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 85756
REMARK   3
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.010
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.010
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.136
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 3859
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 77074
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS      : 1439
REMARK   3   NUCLEIC ACID ATOMS : 0
REMARK   3   HETEROGEN ATOMS    : 0
REMARK   3   SOLVENT ATOMS      : 288
REMARK   3
REMARK   3  MODEL REFINEMENT.
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 1638.00
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 1406.00
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 7
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 15553
REMARK   3   NUMBER OF RESTRAINTS                     : 19134
REMARK   3
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK   3   BOND LENGTHS                         (A) : 0.015
REMARK   3   ANGLE DISTANCES                      (A) : 0.030
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.030
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.086
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.095
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.032
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.005
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.048
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.107
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED: MOEWS & KRETSINGER, J.MOL.BIOL.91(1973)201-228
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 3EZG COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-OCT-08.
REMARK 100 THE RCSB ID CODE IS RCSB049955.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 14-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) : 0.9
REMARK 200  MONOCHROMATOR                  : BENT GE(111) MONOCHROMATOR
REMARK 200  OPTICS                         : BENT CONICAL RH-COATED SI
REMARK 200                                   MIRROR
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
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   : 88152
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     (%) : 99.8
REMARK 200  DATA REDUNDANCY                : 10.000
REMARK 200  R MERGE                    (I) : 0.09200
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 25.7000
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) : 1.18
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.80
REMARK 200  R MERGE FOR SHELL          (I) : 0.37900
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 6.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: SHELX
REMARK 200 STARTING MODEL: PDB ENTRY 1P5F
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 57.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG400, 50 MM HEPES, 125 MM
REMARK 280  SODIUM CITRATE, PH 7.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280  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       24.93000
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       49.86000
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       49.86000
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       24.93000
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: 2710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
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      -49.86000
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     ASP A   189
REMARK 465     LEU A   190
REMARK 465     GLU A   191
REMARK 465     HIS A   192
REMARK 465     HIS A   193
REMARK 465     HIS A   194
REMARK 465     HIS A   195
REMARK 465     HIS A   196
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   CD  -  NE  -  CZ  ANGL. DEV. =  10.2 DEGREES
REMARK 500    ARG A   5   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES
REMARK 500    LYS A  12   CD  -  CE  -  NZ  ANGL. DEV. =  17.0 DEGREES
REMARK 500    LYS A  89   CD  -  CE  -  NZ  ANGL. DEV. =  15.2 DEGREES
REMARK 500    ARG A  98   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES
REMARK 500    ARG A  98   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.3 DEGREES
REMARK 500    ARG A 145   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES
REMARK 500    ARG A 145   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES
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 465        DISTANCE =  5.91 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1SOA   RELATED DB: PDB
REMARK 900 HUMAN DJ-1 WITH SULFINIC ACID
REMARK 900 RELATED ID: 3CY6   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF E18Q DJ-1
DBREF  3EZG A    1   189  UNP    Q99497   PARK7_HUMAN      1    189
SEQADV 3EZG GLN A   18  UNP  Q99497    GLU    18 ENGINEERED
SEQADV 3EZG LEU A  190  UNP  Q99497              EXPRESSION TAG
SEQADV 3EZG GLU A  191  UNP  Q99497              EXPRESSION TAG
SEQADV 3EZG HIS A  192  UNP  Q99497              EXPRESSION TAG
SEQADV 3EZG HIS A  193  UNP  Q99497              EXPRESSION TAG
SEQADV 3EZG HIS A  194  UNP  Q99497              EXPRESSION TAG
SEQADV 3EZG HIS A  195  UNP  Q99497              EXPRESSION TAG
SEQADV 3EZG HIS A  196  UNP  Q99497              EXPRESSION TAG
SEQRES   1 A  196  MET ALA SER LYS ARG ALA LEU VAL ILE LEU ALA LYS GLY
SEQRES   2 A  196  ALA GLU GLU MET GLN THR VAL ILE PRO VAL ASP VAL MET
SEQRES   3 A  196  ARG ARG ALA GLY ILE LYS VAL THR VAL ALA GLY LEU ALA
SEQRES   4 A  196  GLY LYS ASP PRO VAL GLN CYS SER ARG ASP VAL VAL ILE
SEQRES   5 A  196  CYS PRO ASP ALA SER LEU GLU ASP ALA LYS LYS GLU GLY
SEQRES   6 A  196  PRO TYR ASP VAL VAL VAL LEU PRO GLY GLY ASN LEU GLY
SEQRES   7 A  196  ALA GLN ASN LEU SER GLU SER ALA ALA VAL LYS GLU ILE
SEQRES   8 A  196  LEU LYS GLU GLN GLU ASN ARG LYS GLY LEU ILE ALA ALA
SEQRES   9 A  196  ILE CSW ALA GLY PRO THR ALA LEU LEU ALA HIS GLU ILE
SEQRES  10 A  196  GLY PHE GLY SER LYS VAL THR THR HIS PRO LEU ALA LYS
SEQRES  11 A  196  ASP LYS MET MET ASN GLY GLY HIS TYR THR TYR SER GLU
SEQRES  12 A  196  ASN ARG VAL GLU LYS ASP GLY LEU ILE LEU THR SER ARG
SEQRES  13 A  196  GLY PRO GLY THR SER PHE GLU PHE ALA LEU ALA ILE VAL
SEQRES  14 A  196  GLU ALA LEU ASN GLY LYS GLU VAL ALA ALA GLN VAL LYS
SEQRES  15 A  196  ALA PRO LEU VAL LEU LYS ASP LEU GLU HIS HIS HIS HIS
SEQRES  16 A  196  HIS
MODRES 3EZG CSW A  106  CYS  CYSTEINE-S-DIOXIDE
HET    CSW  A 106       8
HETNAM     CSW CYSTEINE-S-DIOXIDE
HETSYN     CSW CYSTEINE SULFINIC ACID
FORMUL   1  CSW    C3 H7 N O4 S
FORMUL   2  HOH   *288(H2 O)
HELIX    1   1 GLU A   15  ALA A   29  1                                  15
HELIX    2   2 LEU A   58  GLU A   64  1                                   7
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  VAL A   8   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   CSW A 106     1555   1555  1.36
LINK         C   CSW A 106                 N   ALA A 107     1555   1555  1.34
CISPEP   1 GLY A   65    PRO A   66          0        -1.40
CRYST1   74.770   74.770   74.790  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      0.013374  0.007722  0.000000        0.00000
SCALE2      0.000000  0.015443  0.000000        0.00000
SCALE3      0.000000  0.000000  0.013371        0.00000
      
PROCHECK
Go to PROCHECK summary
 References