Header list of 1g7o.pdb file
Complete list - b 23 2 Bytes
HEADER OXIDOREDUCTASE 10-NOV-00 1G7O
TITLE NMR SOLUTION STRUCTURE OF REDUCED E. COLI GLUTAREDOXIN 2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAREDOXIN 2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GRX2;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET24A
KEYWDS REDUCED FORM OF GLUTAREDOXIN, OXIDOREDUCTASE
EXPDTA SOLUTION NMR
NUMMDL 21
MDLTYP MINIMIZED AVERAGE
AUTHOR B.XIA,A.VLAMIS-GARDIKAS,A.HOLMGREN,P.E.WRIGHT,H.J.DYSON
REVDAT 3 23-FEB-22 1G7O 1 REMARK
REVDAT 2 24-FEB-09 1G7O 1 VERSN
REVDAT 1 20-JUL-01 1G7O 0
JRNL AUTH B.XIA,A.VLAMIS-GARDIKAS,A.HOLMGREN,P.E.WRIGHT,H.J.DYSON
JRNL TITL SOLUTION STRUCTURE OF ESCHERICHIA COLI GLUTAREDOXIN-2 SHOWS
JRNL TITL 2 SIMILARITY TO MAMMALIAN GLUTATHIONE-S-TRANSFERASES.
JRNL REF J.MOL.BIOL. V. 310 907 2001
JRNL REFN ISSN 0022-2836
JRNL PMID 11453697
JRNL DOI 10.1006/JMBI.2001.4721
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : FELIX 98, AMBER
REMARK 3 AUTHORS :
REMARK 3 PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM,FERGUSON,SEIBEL,SINGH,
REMARK 3 WEINER,KOLLMAN (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1G7O COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-NOV-00.
REMARK 100 THE DEPOSITION ID IS D_1000012336.
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 : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 2MM GLUTAREDOXIN 2; U-15N,13C;
REMARK 210 50MM PHOSPHATE BUFFER;
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 4D_13C/15N-
REMARK 210 SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA, AMBER
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 SIMULATED ANNEALING, MOLECULAR
REMARK 210 DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 21
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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: 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 1 TYR A 96 CB - CG - CD2 ANGL. DEV. = -3.8 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 1 ASN A 23 49.90 71.86
REMARK 500 1 ASP A 54 -66.09 -22.22
REMARK 500 1 ASP A 55 42.27 -77.29
REMARK 500 1 GLU A 61 128.42 73.86
REMARK 500 1 ALA A 109 92.92 -61.62
REMARK 500 1 LYS A 126 -51.72 -129.87
REMARK 500 1 SER A 140 -57.44 -29.52
REMARK 500 1 ILE A 158 107.38 -46.36
REMARK 500 1 ASN A 162 -58.21 -179.21
REMARK 500 2 ASN A 23 52.48 70.84
REMARK 500 2 ASP A 54 -72.08 -7.32
REMARK 500 2 ASP A 55 0.77 -67.25
REMARK 500 2 SER A 56 46.34 84.52
REMARK 500 2 GLU A 61 127.53 75.45
REMARK 500 2 PRO A 76 93.06 -67.50
REMARK 500 2 ALA A 109 81.91 -56.31
REMARK 500 2 GLU A 112 -36.68 -36.25
REMARK 500 2 ILE A 158 108.19 -58.99
REMARK 500 2 ASN A 162 -55.79 179.51
REMARK 500 2 SER A 192 -70.78 -57.87
REMARK 500 3 ASN A 23 44.92 76.08
REMARK 500 3 LYS A 46 86.44 -68.48
REMARK 500 3 ASP A 54 -76.09 -0.80
REMARK 500 3 SER A 56 47.74 127.97
REMARK 500 3 GLU A 61 130.31 72.81
REMARK 500 3 PRO A 76 92.80 -66.89
REMARK 500 3 ALA A 109 85.04 -68.50
REMARK 500 3 GLU A 127 85.24 -18.57
REMARK 500 3 ALA A 130 98.19 -65.28
REMARK 500 3 SER A 140 -62.49 -29.70
REMARK 500 3 ILE A 158 104.94 -48.90
REMARK 500 3 ASN A 162 -56.38 -179.11
REMARK 500 4 ASP A 54 -80.99 0.04
REMARK 500 4 ASP A 55 36.20 -76.09
REMARK 500 4 GLU A 61 124.75 74.96
REMARK 500 4 ALA A 109 89.22 -55.94
REMARK 500 4 SER A 129 40.00 -71.00
REMARK 500 4 ALA A 130 117.24 -25.36
REMARK 500 4 PHE A 133 -16.58 -47.73
REMARK 500 4 SER A 140 -53.81 -28.80
REMARK 500 4 ILE A 158 107.19 -57.85
REMARK 500 4 ASN A 162 -58.93 -177.11
REMARK 500 4 SER A 192 -71.69 -57.95
REMARK 500 5 ASP A 7 -57.26 -29.78
REMARK 500 5 ASN A 23 50.48 72.32
REMARK 500 5 ASP A 54 -79.73 0.44
REMARK 500 5 SER A 56 46.53 129.26
REMARK 500 5 GLU A 61 125.64 74.02
REMARK 500 5 PRO A 76 93.31 -66.21
REMARK 500 5 ALA A 109 96.36 -59.52
REMARK 500
REMARK 500 THIS ENTRY HAS 208 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 VAL A 48 PRO A 49 1 57.26
REMARK 500 VAL A 48 PRO A 49 2 57.72
REMARK 500 VAL A 48 PRO A 49 3 57.06
REMARK 500 VAL A 48 PRO A 49 4 57.75
REMARK 500 VAL A 48 PRO A 49 5 57.66
REMARK 500 VAL A 48 PRO A 49 6 57.51
REMARK 500 VAL A 48 PRO A 49 7 57.48
REMARK 500 VAL A 48 PRO A 49 8 57.18
REMARK 500 VAL A 48 PRO A 49 9 57.23
REMARK 500 VAL A 48 PRO A 49 10 57.09
REMARK 500 VAL A 48 PRO A 49 11 57.26
REMARK 500 VAL A 48 PRO A 49 12 57.51
REMARK 500 VAL A 48 PRO A 49 13 57.56
REMARK 500 VAL A 48 PRO A 49 14 57.90
REMARK 500 VAL A 48 PRO A 49 15 57.66
REMARK 500 VAL A 48 PRO A 49 16 57.26
REMARK 500 VAL A 48 PRO A 49 17 56.86
REMARK 500 VAL A 48 PRO A 49 18 57.23
REMARK 500 VAL A 48 PRO A 49 19 57.24
REMARK 500 VAL A 48 PRO A 49 20 57.56
REMARK 500 VAL A 48 PRO A 49 21 57.58
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 82 0.09 SIDE CHAIN
REMARK 500 1 TYR A 96 0.13 SIDE CHAIN
REMARK 500 2 ARG A 119 0.08 SIDE CHAIN
REMARK 500 2 TYR A 121 0.13 SIDE CHAIN
REMARK 500 3 PHE A 105 0.11 SIDE CHAIN
REMARK 500 4 TYR A 11 0.17 SIDE CHAIN
REMARK 500 4 PHE A 105 0.13 SIDE CHAIN
REMARK 500 5 ARG A 57 0.08 SIDE CHAIN
REMARK 500 5 PHE A 105 0.08 SIDE CHAIN
REMARK 500 5 TYR A 121 0.16 SIDE CHAIN
REMARK 500 5 PHE A 133 0.09 SIDE CHAIN
REMARK 500 5 ARG A 180 0.10 SIDE CHAIN
REMARK 500 6 TYR A 68 0.07 SIDE CHAIN
REMARK 500 6 TYR A 96 0.10 SIDE CHAIN
REMARK 500 6 PHE A 105 0.10 SIDE CHAIN
REMARK 500 6 PHE A 133 0.09 SIDE CHAIN
REMARK 500 7 TYR A 11 0.07 SIDE CHAIN
REMARK 500 7 PHE A 105 0.11 SIDE CHAIN
REMARK 500 7 TYR A 121 0.09 SIDE CHAIN
REMARK 500 7 PHE A 133 0.10 SIDE CHAIN
REMARK 500 8 TYR A 4 0.11 SIDE CHAIN
REMARK 500 8 TYR A 68 0.07 SIDE CHAIN
REMARK 500 8 PHE A 105 0.09 SIDE CHAIN
REMARK 500 9 TYR A 6 0.09 SIDE CHAIN
REMARK 500 10 TYR A 6 0.08 SIDE CHAIN
REMARK 500 10 TYR A 11 0.06 SIDE CHAIN
REMARK 500 10 ARG A 180 0.11 SIDE CHAIN
REMARK 500 11 PHE A 105 0.11 SIDE CHAIN
REMARK 500 12 PHE A 105 0.09 SIDE CHAIN
REMARK 500 13 PHE A 105 0.10 SIDE CHAIN
REMARK 500 13 PHE A 113 0.09 SIDE CHAIN
REMARK 500 13 PHE A 133 0.09 SIDE CHAIN
REMARK 500 14 TYR A 4 0.12 SIDE CHAIN
REMARK 500 14 TYR A 11 0.16 SIDE CHAIN
REMARK 500 14 PHE A 110 0.09 SIDE CHAIN
REMARK 500 14 PHE A 122 0.10 SIDE CHAIN
REMARK 500 15 PHE A 110 0.08 SIDE CHAIN
REMARK 500 15 PHE A 133 0.09 SIDE CHAIN
REMARK 500 16 TYR A 96 0.11 SIDE CHAIN
REMARK 500 17 ARG A 82 0.10 SIDE CHAIN
REMARK 500 17 TYR A 96 0.12 SIDE CHAIN
REMARK 500 17 ARG A 104 0.08 SIDE CHAIN
REMARK 500 17 PHE A 110 0.09 SIDE CHAIN
REMARK 500 18 TYR A 6 0.08 SIDE CHAIN
REMARK 500 18 TYR A 11 0.19 SIDE CHAIN
REMARK 500 18 ARG A 57 0.08 SIDE CHAIN
REMARK 500 18 TYR A 58 0.08 SIDE CHAIN
REMARK 500 18 PHE A 105 0.11 SIDE CHAIN
REMARK 500 18 PHE A 133 0.08 SIDE CHAIN
REMARK 500 19 TYR A 11 0.15 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 59 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1G7O A 1 215 UNP P0AC59 GLRX2_ECOLI 1 215
SEQRES 1 A 215 MET LYS LEU TYR ILE TYR ASP HIS CYS PRO TYR CYS LEU
SEQRES 2 A 215 LYS ALA ARG MET ILE PHE GLY LEU LYS ASN ILE PRO VAL
SEQRES 3 A 215 GLU LEU HIS VAL LEU LEU ASN ASP ASP ALA GLU THR PRO
SEQRES 4 A 215 THR ARG MET VAL GLY GLN LYS GLN VAL PRO ILE LEU GLN
SEQRES 5 A 215 LYS ASP ASP SER ARG TYR MET PRO GLU SER MET ASP ILE
SEQRES 6 A 215 VAL HIS TYR VAL ASP LYS LEU ASP GLY LYS PRO LEU LEU
SEQRES 7 A 215 THR GLY LYS ARG SER PRO ALA ILE GLU GLU TRP LEU ARG
SEQRES 8 A 215 LYS VAL ASN GLY TYR ALA ASN LYS LEU LEU LEU PRO ARG
SEQRES 9 A 215 PHE ALA LYS SER ALA PHE ASP GLU PHE SER THR PRO ALA
SEQRES 10 A 215 ALA ARG LYS TYR PHE VAL ASP LYS LYS GLU ALA SER ALA
SEQRES 11 A 215 GLY ASN PHE ALA ASP LEU LEU ALA HIS SER ASP GLY LEU
SEQRES 12 A 215 ILE LYS ASN ILE SER ASP ASP LEU ARG ALA LEU ASP LYS
SEQRES 13 A 215 LEU ILE VAL LYS PRO ASN ALA VAL ASN GLY GLU LEU SER
SEQRES 14 A 215 GLU ASP ASP ILE GLN LEU PHE PRO LEU LEU ARG ASN LEU
SEQRES 15 A 215 THR LEU VAL ALA GLY ILE ASN TRP PRO SER ARG VAL ALA
SEQRES 16 A 215 ASP TYR ARG ASP ASN MET ALA LYS GLN THR GLN ILE ASN
SEQRES 17 A 215 LEU LEU SER SER MET ALA ILE
HELIX 1 1 CYS A 9 ASN A 23 1 15
HELIX 2 2 ALA A 36 GLY A 44 1 9
HELIX 3 3 GLU A 61 ASP A 73 1 13
HELIX 4 4 SER A 83 SER A 108 1 26
HELIX 5 5 PHE A 110 SER A 114 5 5
HELIX 6 6 THR A 115 ASP A 124 1 10
HELIX 7 7 GLY A 131 ILE A 158 1 28
HELIX 8 8 SER A 169 LEU A 184 1 16
HELIX 9 9 PRO A 191 GLN A 206 1 16
HELIX 10 10 LEU A 210 ALA A 214 5 5
SHEET 1 A 4 GLU A 27 VAL A 30 0
SHEET 2 A 4 LYS A 2 ILE A 5 1 O LEU A 3 N HIS A 29
SHEET 3 A 4 ILE A 50 LYS A 53 -1 O ILE A 50 N TYR A 4
SHEET 4 A 4 ARG A 57 PRO A 60 -1 O ARG A 57 N LYS A 53
CRYST1 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 - b 23 2 Bytes