Header list of 2ga5.pdb file
Complete list - r 9 2 Bytes
HEADER CHAPERONE 07-MAR-06 2GA5
TITLE YEAST FRATAXIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FRATAXIN HOMOLOG, MITOCHONDRIAL;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: YFH1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: YFH1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS YFH1, CHAPERONE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR Y.HE,S.L.ALAM,S.V.PROTEASA,Y.ZHANG,E.LESUISSE,A.DANCIS
REVDAT 3 09-MAR-22 2GA5 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2GA5 1 VERSN
REVDAT 1 21-MAR-06 2GA5 0
SPRSDE 21-MAR-06 2GA5 1XAQ
JRNL AUTH Y.HE,S.L.ALAM,S.V.PROTEASA,Y.ZHANG,E.LESUISSE,E.DANCID,
JRNL AUTH 2 T.L.STEMMLER
JRNL TITL YEAST FRATAXIN SOLUTION STRUCTURE, IRON BINDING AND
JRNL TITL 2 FERROCHELATASE INTERACTION
JRNL REF BIOCHEMISTRY V. 43 16254 2004
JRNL REFN ISSN 0006-2960
JRNL PMID 15610019
JRNL DOI 10.1021/BI0488193
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA 2.1
REMARK 3 AUTHORS : P.GUNTERT ET AL.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2GA5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-MAR-06.
REMARK 100 THE DEPOSITION ID IS D_1000036880.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM PROTEIN
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; 3D_15N-SEPARATED_NOESY;
REMARK 210 4D_13C-SEPARATED_NOESY; 4D_13C/
REMARK 210 15N-SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CYANA 2.1
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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: MONOMERIC
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 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 1 GLU A 2 -28.24 172.92
REMARK 500 1 VAL A 10 147.83 69.67
REMARK 500 1 PRO A 11 66.75 -69.79
REMARK 500 1 ASN A 16 -161.98 -121.29
REMARK 500 1 LEU A 17 153.67 -49.30
REMARK 500 1 PRO A 18 72.21 -69.76
REMARK 500 1 HIS A 44 75.19 -171.76
REMARK 500 1 PRO A 45 -91.40 -69.81
REMARK 500 1 ASP A 46 -46.68 167.84
REMARK 500 1 CYS A 47 -62.79 -138.48
REMARK 500 1 ILE A 48 61.54 -178.80
REMARK 500 1 HIS A 55 92.97 -57.87
REMARK 500 1 PRO A 63 64.23 -69.79
REMARK 500 1 ALA A 64 -39.51 -169.08
REMARK 500 1 LYS A 72 47.94 -144.03
REMARK 500 1 PRO A 75 3.64 -69.79
REMARK 500 1 ASN A 76 -91.40 -140.91
REMARK 500 1 LYS A 77 94.12 -170.71
REMARK 500 1 PRO A 84 3.26 -69.69
REMARK 500 1 LEU A 85 -54.52 -123.18
REMARK 500 1 SER A 86 58.42 159.69
REMARK 500 1 ASN A 95 39.37 36.16
REMARK 500 1 LEU A 101 54.79 80.47
REMARK 500 1 ARG A 102 49.99 36.36
REMARK 500 1 ASN A 103 78.75 80.85
REMARK 500 1 LEU A 107 -77.20 -60.53
REMARK 500 2 GLU A 2 95.52 43.18
REMARK 500 2 ASP A 6 75.68 59.60
REMARK 500 2 PRO A 11 65.08 -69.81
REMARK 500 2 ASN A 16 -71.87 -91.43
REMARK 500 2 LEU A 17 80.90 165.33
REMARK 500 2 PRO A 18 82.52 -69.77
REMARK 500 2 HIS A 44 90.45 169.41
REMARK 500 2 PRO A 45 -90.96 -69.81
REMARK 500 2 ASP A 46 -38.53 171.91
REMARK 500 2 CYS A 47 -61.71 -147.46
REMARK 500 2 ILE A 48 59.88 178.48
REMARK 500 2 HIS A 55 92.79 -56.86
REMARK 500 2 PRO A 63 64.77 -69.74
REMARK 500 2 ALA A 64 -39.92 -170.29
REMARK 500 2 GLN A 73 43.99 -150.93
REMARK 500 2 PRO A 75 3.08 -69.76
REMARK 500 2 ASN A 76 -91.55 -134.01
REMARK 500 2 LYS A 77 85.94 -177.99
REMARK 500 2 PRO A 84 3.00 -69.72
REMARK 500 2 SER A 86 72.87 57.62
REMARK 500 2 LEU A 101 113.39 82.74
REMARK 500 2 ARG A 102 98.21 -34.25
REMARK 500 2 LEU A 107 -82.32 -63.89
REMARK 500 3 GLU A 2 176.55 174.86
REMARK 500
REMARK 500 THIS ENTRY HAS 475 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2GA5 A 2 123 UNP Q07540 FRDA_YEAST 53 174
SEQADV 2GA5 MET A 1 UNP Q07540 CLONING ARTIFACT
SEQRES 1 A 123 MET GLU SER SER THR ASP GLY GLN VAL VAL PRO GLN GLU
SEQRES 2 A 123 VAL LEU ASN LEU PRO LEU GLU LYS TYR HIS GLU GLU ALA
SEQRES 3 A 123 ASP ASP TYR LEU ASP HIS LEU LEU ASP SER LEU GLU GLU
SEQRES 4 A 123 LEU SER GLU ALA HIS PRO ASP CYS ILE PRO ASP VAL GLU
SEQRES 5 A 123 LEU SER HIS GLY VAL MET THR LEU GLU ILE PRO ALA PHE
SEQRES 6 A 123 GLY THR TYR VAL ILE ASN LYS GLN PRO PRO ASN LYS GLN
SEQRES 7 A 123 ILE TRP LEU ALA SER PRO LEU SER GLY PRO ASN ARG PHE
SEQRES 8 A 123 ASP LEU LEU ASN GLY GLU TRP VAL SER LEU ARG ASN GLY
SEQRES 9 A 123 THR LYS LEU THR ASP ILE LEU THR GLU GLU VAL GLU LYS
SEQRES 10 A 123 ALA ILE SER LYS SER GLN
HELIX 1 1 PRO A 18 HIS A 44 1 27
HELIX 2 2 LEU A 107 SER A 120 1 14
SHEET 1 A 7 ASP A 50 SER A 54 0
SHEET 2 A 7 VAL A 57 ILE A 62 -1 O GLU A 61 N ASP A 50
SHEET 3 A 7 GLY A 66 ASN A 71 -1 O TYR A 68 N LEU A 60
SHEET 4 A 7 ILE A 79 ALA A 82 -1 O TRP A 80 N ASN A 71
SHEET 5 A 7 ARG A 90 LEU A 94 -1 O PHE A 91 N ILE A 79
SHEET 6 A 7 GLU A 97 SER A 100 -1 O VAL A 99 N ASP A 92
SHEET 7 A 7 THR A 105 LYS A 106 -1 O THR A 105 N SER A 100
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - r 9 2 Bytes