HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 19-MAY-05 2CQ9
TITLE SOLUTION STRUCTURE OF RSGI RUH-044, AN N-TERMINAL DOMAIN OF
TITLE 2 GLUTAREDOXIN 2 FROM HUMAN CDNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLRX2 PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN;
COMPND 5 SYNONYM: GLUTAREDOXIN 2;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 6 EXPRESSION_SYSTEM_PLASMID: P041115-06;
SOURCE 7 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS GLUTAREDOXIN, GLUTAREDOXIN 2, GLUTATHIONE-S-TRANSFERASE, STRUCTURAL
KEYWDS 2 GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND
KEYWDS 3 FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 4 INITIATIVE, RSGI, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.ABE,H.HIROTA,F.HAYASHI,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2CQ9 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2CQ9 1 VERSN
REVDAT 1 19-NOV-05 2CQ9 0
JRNL AUTH T.ABE,H.HIROTA,F.HAYASHI,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF RSGI RUH-044, AN N-TERMINAL DOMAIN OF
JRNL TITL 2 GLUTAREDOXIN 2 FROM HUMAN CDNA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1C, CYANA 2.0.17
REMARK 3 AUTHORS : VARIAN (VNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2CQ9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024500.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.43MM RSGI RUH-044 U-15,13C;
REMARK 210 20MM D-TRIS-HCL; 100MM NACL; 1MM
REMARK 210 D-DTT; 0.02% NAN3; 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 900 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20031121, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9295
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 : TARGET FUNCTION, STRUCTURES WITH
REMARK 210 THE LOWEST ENERGY, STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: SPECTROMETER_ID 1 FOR 3D_15N-SEPARATED_NOESY;
REMARK 210 SPECTROMETER_ID 2 FOR 3D_13C-SEPARATED_NOESY
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 SER A 5 42.39 38.78
REMARK 500 1 SER A 8 116.15 -168.28
REMARK 500 1 ALA A 15 152.51 -48.04
REMARK 500 1 ASN A 53 112.24 -39.63
REMARK 500 1 TYR A 64 38.61 -94.75
REMARK 500 1 GLN A 67 -71.64 -79.85
REMARK 500 1 PRO A 82 -179.19 -69.77
REMARK 500 1 PHE A 90 75.29 -69.51
REMARK 500 1 LYS A 117 -50.40 -122.55
REMARK 500 1 SER A 118 141.07 -36.64
REMARK 500 1 LYS A 121 83.58 -65.38
REMARK 500 1 SER A 129 -60.32 -127.20
REMARK 500 2 THR A 14 51.64 39.51
REMARK 500 2 THR A 35 49.51 33.69
REMARK 500 2 SER A 36 -44.45 -133.74
REMARK 500 2 ASN A 53 116.73 -34.42
REMARK 500 2 ASP A 60 -38.09 -37.58
REMARK 500 2 TYR A 64 40.99 -98.68
REMARK 500 2 GLN A 67 -70.50 -78.16
REMARK 500 2 THR A 95 -70.04 -55.17
REMARK 500 2 LYS A 116 -174.95 -53.99
REMARK 500 2 PRO A 127 98.08 -69.79
REMARK 500 3 SER A 2 -59.52 -133.03
REMARK 500 3 THR A 14 37.64 39.85
REMARK 500 3 ALA A 15 165.34 -42.84
REMARK 500 3 THR A 35 47.00 34.75
REMARK 500 3 ASN A 53 114.44 -35.17
REMARK 500 3 GLN A 67 -72.42 -74.44
REMARK 500 3 ARG A 79 50.32 -110.62
REMARK 500 3 GLN A 112 -34.51 -34.40
REMARK 500 3 LYS A 116 155.12 -37.64
REMARK 500 3 LYS A 117 43.88 71.08
REMARK 500 3 LYS A 119 148.82 -36.93
REMARK 500 3 LYS A 121 130.09 -173.93
REMARK 500 3 GLU A 122 79.25 -101.77
REMARK 500 3 SER A 125 41.32 34.71
REMARK 500 3 PRO A 127 -176.18 -69.73
REMARK 500 4 THR A 35 44.99 30.76
REMARK 500 4 ASN A 53 112.08 -35.26
REMARK 500 4 GLN A 67 -72.53 -79.27
REMARK 500 4 PRO A 82 -178.51 -69.73
REMARK 500 4 LYS A 117 138.94 -34.68
REMARK 500 4 SER A 118 34.60 -91.32
REMARK 500 4 PRO A 127 93.28 -69.75
REMARK 500 5 SER A 6 150.72 -44.98
REMARK 500 5 THR A 14 45.41 34.29
REMARK 500 5 ALA A 15 152.10 -46.24
REMARK 500 5 THR A 35 46.23 33.61
REMARK 500 5 LEU A 46 -73.75 -52.69
REMARK 500 5 ASN A 53 110.58 -34.24
REMARK 500
REMARK 500 THIS ENTRY HAS 233 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSI002021569.1 RELATED DB: TARGETDB
DBREF 2CQ9 A 8 124 UNP Q9NS18 GLRX2_HUMAN 8 124
SEQADV 2CQ9 GLY A 1 UNP Q9NS18 CLONING ARTIFACT
SEQADV 2CQ9 SER A 2 UNP Q9NS18 CLONING ARTIFACT
SEQADV 2CQ9 SER A 3 UNP Q9NS18 CLONING ARTIFACT
SEQADV 2CQ9 GLY A 4 UNP Q9NS18 CLONING ARTIFACT
SEQADV 2CQ9 SER A 5 UNP Q9NS18 CLONING ARTIFACT
SEQADV 2CQ9 SER A 6 UNP Q9NS18 CLONING ARTIFACT
SEQADV 2CQ9 GLY A 7 UNP Q9NS18 CLONING ARTIFACT
SEQADV 2CQ9 SER A 125 UNP Q9NS18 CLONING ARTIFACT
SEQADV 2CQ9 GLY A 126 UNP Q9NS18 CLONING ARTIFACT
SEQADV 2CQ9 PRO A 127 UNP Q9NS18 CLONING ARTIFACT
SEQADV 2CQ9 SER A 128 UNP Q9NS18 CLONING ARTIFACT
SEQADV 2CQ9 SER A 129 UNP Q9NS18 CLONING ARTIFACT
SEQADV 2CQ9 GLY A 130 UNP Q9NS18 CLONING ARTIFACT
SEQRES 1 A 130 GLY SER SER GLY SER SER GLY SER LEU GLU ASN LEU ALA
SEQRES 2 A 130 THR ALA PRO VAL ASN GLN ILE GLN GLU THR ILE SER ASP
SEQRES 3 A 130 ASN CYS VAL VAL ILE PHE SER LYS THR SER CYS SER TYR
SEQRES 4 A 130 CYS THR MET ALA LYS LYS LEU PHE HIS ASP MET ASN VAL
SEQRES 5 A 130 ASN TYR LYS VAL VAL GLU LEU ASP LEU LEU GLU TYR GLY
SEQRES 6 A 130 ASN GLN PHE GLN ASP ALA LEU TYR LYS MET THR GLY GLU
SEQRES 7 A 130 ARG THR VAL PRO ARG ILE PHE VAL ASN GLY THR PHE ILE
SEQRES 8 A 130 GLY GLY ALA THR ASP THR HIS ARG LEU HIS LYS GLU GLY
SEQRES 9 A 130 LYS LEU LEU PRO LEU VAL HIS GLN CYS TYR LEU LYS LYS
SEQRES 10 A 130 SER LYS ARG LYS GLU PHE GLN SER GLY PRO SER SER GLY
HELIX 1 1 ALA A 15 ASN A 27 1 13
HELIX 2 2 SER A 38 ASN A 51 1 14
HELIX 3 3 TYR A 64 GLY A 77 1 14
HELIX 4 4 ALA A 94 GLY A 104 1 11
HELIX 5 5 LEU A 106 TYR A 114 1 9
SHEET 1 A 4 LYS A 55 GLU A 58 0
SHEET 2 A 4 VAL A 29 SER A 33 1 N ILE A 31 O LYS A 55
SHEET 3 A 4 ARG A 83 VAL A 86 -1 O PHE A 85 N VAL A 30
SHEET 4 A 4 THR A 89 GLY A 93 -1 O THR A 89 N VAL A 86
SSBOND 1 CYS A 28 CYS A 113 1555 1555 2.00
CISPEP 1 VAL A 81 PRO A 82 1 -0.02
CISPEP 2 VAL A 81 PRO A 82 2 -0.12
CISPEP 3 VAL A 81 PRO A 82 3 -0.06
CISPEP 4 VAL A 81 PRO A 82 4 -0.09
CISPEP 5 VAL A 81 PRO A 82 5 -0.11
CISPEP 6 VAL A 81 PRO A 82 6 -0.02
CISPEP 7 VAL A 81 PRO A 82 7 -0.04
CISPEP 8 VAL A 81 PRO A 82 8 -0.06
CISPEP 9 VAL A 81 PRO A 82 9 -0.06
CISPEP 10 VAL A 81 PRO A 82 10 -0.10
CISPEP 11 VAL A 81 PRO A 82 11 -0.10
CISPEP 12 VAL A 81 PRO A 82 12 -0.02
CISPEP 13 VAL A 81 PRO A 82 13 0.04
CISPEP 14 VAL A 81 PRO A 82 14 -0.04
CISPEP 15 VAL A 81 PRO A 82 15 -0.11
CISPEP 16 VAL A 81 PRO A 82 16 -0.05
CISPEP 17 VAL A 81 PRO A 82 17 -0.08
CISPEP 18 VAL A 81 PRO A 82 18 -0.04
CISPEP 19 VAL A 81 PRO A 82 19 -0.04
CISPEP 20 VAL A 81 PRO A 82 20 -0.05
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
(ATOM LINES ARE NOT SHOWN.)
END
