Header list of 1b4q.pdb file
Complete list - v 3 2 Bytes
HEADER OXIDOREDUCTASE 25-DEC-98 1B4Q
TITLE SOLUTION STRUCTURE OF HUMAN THIOLTRANSFERASE COMPLEX WITH GLUTATHIONE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (HUMAN THIOLTRANSFERASE);
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 OTHER_DETAILS: COMPLEXED WITH GLUTATHIONE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HUMAN THIOLTRANSFERASE, DISULFIDE INTERMEDIATE, GLUTATHIONE,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA SOLUTION NMR
NUMMDL 21
AUTHOR Y.YANG,S.C.JAO,S.NANDURI,D.W.STARKE,J.J.MIEYAL,J.QIN
REVDAT 5 03-NOV-21 1B4Q 1 REMARK SEQADV
REVDAT 4 21-DEC-11 1B4Q 1 HETATM VERSN
REVDAT 3 24-FEB-09 1B4Q 1 VERSN
REVDAT 2 01-APR-03 1B4Q 1 JRNL
REVDAT 1 23-DEC-99 1B4Q 0
JRNL AUTH Y.YANG,S.JAO,S.NANDURI,D.W.STARKE,J.J.MIEYAL,J.QIN
JRNL TITL REACTIVITY OF THE HUMAN THIOLTRANSFERASE (GLUTAREDOXIN) C7S,
JRNL TITL 2 C25S, C78S, C82S MUTANT AND NMR SOLUTION STRUCTURE OF ITS
JRNL TITL 3 GLUTATHIONYL MIXED DISULFIDE INTERMEDIATE REFLECT CATALYTIC
JRNL TITL 4 SPECIFICITY.
JRNL REF BIOCHEMISTRY V. 37 17145 1998
JRNL REFN ISSN 0006-2960
JRNL PMID 9860827
JRNL DOI 10.1021/BI9806504
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.2
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1B4Q COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-AUG-99.
REMARK 100 THE DEPOSITION ID IS D_1000007342.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D-NCNOESY; HNCACB; CBCACONH;
REMARK 210 CCC-TOCSY; HCCH-TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : VARIAN INOVA-500
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 95
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK:
REMARK 210 THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY ON 13C,
REMARK 210 15N-LABELED HUMAN THIOLTRANSFERASE MUTANT (C7S,C25S,C78S,C82S).
REMARK 210 THE STRUCTURE
REMARK 210 CALCULATION IS BASED ON A TOTAL OF 2658 EXPERIMENTAL CONSTRAINTS
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: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O VAL A 16 H VAL A 45 1.52
REMARK 500 O GLN A 39 H LEU A 41 1.55
REMARK 500 O ILE A 56 H LEU A 60 1.57
REMARK 500 SG CYS A 22 SG2 GSH A 106 2.02
REMARK 500 O VAL A 69 OE1 GSH A 106 2.12
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 GLN A 2 -75.26 -111.84
REMARK 500 1 PHE A 4 -71.18 -61.11
REMARK 500 1 PRO A 20 82.57 -48.32
REMARK 500 1 THR A 21 -36.46 -177.78
REMARK 500 1 PRO A 36 70.14 -69.49
REMARK 500 1 LYS A 38 -168.11 -54.36
REMARK 500 1 GLN A 39 -129.08 -54.76
REMARK 500 1 ILE A 47 2.54 -62.05
REMARK 500 1 ALA A 49 28.81 -78.81
REMARK 500 1 THR A 50 -3.55 -144.49
REMARK 500 1 ASN A 51 -179.14 69.94
REMARK 500 2 GLN A 2 -83.37 -166.24
REMARK 500 2 GLU A 3 -6.99 -58.84
REMARK 500 2 PRO A 20 80.28 -46.87
REMARK 500 2 THR A 21 -37.31 -175.39
REMARK 500 2 PRO A 36 68.58 -64.99
REMARK 500 2 LYS A 38 -171.75 -53.41
REMARK 500 2 GLN A 39 -128.35 -50.64
REMARK 500 2 THR A 50 -2.96 -144.39
REMARK 500 2 ASN A 51 -176.97 74.88
REMARK 500 2 THR A 64 -70.62 -112.35
REMARK 500 2 ARG A 67 33.02 -99.99
REMARK 500 3 GLN A 2 -77.29 -151.78
REMARK 500 3 GLU A 3 -7.60 -58.43
REMARK 500 3 PRO A 20 80.83 -47.14
REMARK 500 3 THR A 21 -34.10 -175.68
REMARK 500 3 PRO A 36 67.90 -68.06
REMARK 500 3 LYS A 38 -167.40 -53.65
REMARK 500 3 GLN A 39 -133.40 -52.65
REMARK 500 3 ILE A 47 1.61 -61.98
REMARK 500 3 THR A 50 -0.48 -143.68
REMARK 500 3 ASN A 51 -172.56 65.63
REMARK 500 3 PRO A 70 -165.02 -77.03
REMARK 500 3 ARG A 71 89.92 -151.03
REMARK 500 4 GLN A 2 -70.43 -95.34
REMARK 500 4 PHE A 4 -73.07 -62.18
REMARK 500 4 PRO A 20 75.69 -47.26
REMARK 500 4 THR A 21 -34.57 -170.74
REMARK 500 4 PRO A 36 65.37 -67.35
REMARK 500 4 LYS A 38 -169.44 -55.60
REMARK 500 4 GLN A 39 -129.45 -52.50
REMARK 500 4 THR A 50 -12.30 -142.63
REMARK 500 4 ASN A 51 -172.92 82.71
REMARK 500 4 THR A 64 -74.02 -114.05
REMARK 500 5 GLN A 2 -74.36 -140.39
REMARK 500 5 PRO A 20 66.91 -49.22
REMARK 500 5 THR A 21 -35.89 -162.62
REMARK 500 5 PRO A 36 63.55 -65.05
REMARK 500 5 LYS A 38 -174.42 -53.46
REMARK 500 5 GLN A 39 -128.90 -49.81
REMARK 500
REMARK 500 THIS ENTRY HAS 224 RAMACHANDRAN OUTLIERS.
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 20 ARG A 67 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH A 106
DBREF 1B4Q A 1 105 UNP P35754 GLRX_HUMAN 1 105
SEQADV 1B4Q SER A 7 UNP P35754 CYS 7 ENGINEERED MUTATION
SEQADV 1B4Q SER A 25 UNP P35754 CYS 25 ENGINEERED MUTATION
SEQADV 1B4Q SER A 78 UNP P35754 CYS 78 ENGINEERED MUTATION
SEQADV 1B4Q SER A 82 UNP P35754 CYS 82 ENGINEERED MUTATION
SEQRES 1 A 105 ALA GLN GLU PHE VAL ASN SER LYS ILE GLN PRO GLY LYS
SEQRES 2 A 105 VAL VAL VAL PHE ILE LYS PRO THR CYS PRO TYR SER ARG
SEQRES 3 A 105 ARG ALA GLN GLU ILE LEU SER GLN LEU PRO ILE LYS GLN
SEQRES 4 A 105 GLY LEU LEU GLU PHE VAL ASP ILE THR ALA THR ASN HIS
SEQRES 5 A 105 THR ASN GLU ILE GLN ASP TYR LEU GLN GLN LEU THR GLY
SEQRES 6 A 105 ALA ARG THR VAL PRO ARG VAL PHE ILE GLY LYS ASP SER
SEQRES 7 A 105 ILE GLY GLY SER SER ASP LEU VAL SER LEU GLN GLN SER
SEQRES 8 A 105 GLY GLU LEU LEU THR ARG LEU LYS GLN ILE GLY ALA LEU
SEQRES 9 A 105 GLN
HET GSH A 106 35
HETNAM GSH GLUTATHIONE
FORMUL 2 GSH C10 H17 N3 O6 S
HELIX 1 H1 GLN A 2 LYS A 8 1 7
HELIX 2 H3 THR A 53 THR A 64 1 12
HELIX 3 H4 SER A 82 GLN A 90 1 9
HELIX 4 H5 GLU A 93 ILE A 101 1 9
SHEET 1 A 4 LEU A 42 ASP A 46 0
SHEET 2 A 4 VAL A 14 ILE A 18 1 O VAL A 14 N GLU A 43
SHEET 3 A 4 ARG A 71 ILE A 74 -1 O ARG A 71 N PHE A 17
SHEET 4 A 4 ASP A 77 GLY A 80 -1 N ASP A 77 O ILE A 74
CISPEP 1 VAL A 69 PRO A 70 1 -0.48
CISPEP 2 VAL A 69 PRO A 70 2 0.01
CISPEP 3 VAL A 69 PRO A 70 3 0.83
CISPEP 4 VAL A 69 PRO A 70 4 -1.04
CISPEP 5 VAL A 69 PRO A 70 5 -0.19
CISPEP 6 VAL A 69 PRO A 70 6 -0.21
CISPEP 7 VAL A 69 PRO A 70 7 -0.12
CISPEP 8 VAL A 69 PRO A 70 8 -1.40
CISPEP 9 VAL A 69 PRO A 70 9 -1.13
CISPEP 10 VAL A 69 PRO A 70 10 -0.35
CISPEP 11 VAL A 69 PRO A 70 11 1.26
CISPEP 12 VAL A 69 PRO A 70 12 -0.03
CISPEP 13 VAL A 69 PRO A 70 13 0.48
CISPEP 14 VAL A 69 PRO A 70 14 -0.83
CISPEP 15 VAL A 69 PRO A 70 15 0.76
CISPEP 16 VAL A 69 PRO A 70 16 -0.44
CISPEP 17 VAL A 69 PRO A 70 17 -0.91
CISPEP 18 VAL A 69 PRO A 70 18 -0.64
CISPEP 19 VAL A 69 PRO A 70 19 1.35
CISPEP 20 VAL A 69 PRO A 70 20 -0.64
CISPEP 21 VAL A 69 PRO A 70 21 -0.14
SITE 1 AC1 8 CYS A 22 TYR A 24 ARG A 67 THR A 68
SITE 2 AC1 8 VAL A 69 GLY A 81 SER A 82 SER A 83
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 - v 3 2 Bytes