Header list of 3grx.pdb file
Complete list - r 14 2 Bytes
HEADER ELECTRON TRANSPORT 17-AUG-98 3GRX
TITLE NMR STRUCTURE OF ESCHERICHIA COLI GLUTAREDOXIN 3-GLUTATHIONE MIXED
TITLE 2 DISULFIDE COMPLEX, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAREDOXIN 3;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 OTHER_DETAILS: COVALENT COMPLEX WITH GLUTATHIONE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 CELL_LINE: BL21;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-24D
KEYWDS ELECTRON TRANSPORT, THIOL-DISULFIDE OXIDOREDUCTASE, THIOLTRANSFERASE,
KEYWDS 2 THIOREDOXIN SUPERFAMILY
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.NORDSTRAND,F.ASLUND,A.HOLMGREN,G.OTTING,K.D.BERNDT
REVDAT 5 14-MAR-18 3GRX 1 SEQADV
REVDAT 4 18-JAN-12 3GRX 1 HETATM HETNAM VERSN
REVDAT 3 24-FEB-09 3GRX 1 VERSN
REVDAT 2 01-APR-03 3GRX 1 JRNL
REVDAT 1 30-MAR-99 3GRX 0
JRNL AUTH K.NORDSTRAND,F.SLUND,A.HOLMGREN,G.OTTING,K.D.BERNDT
JRNL TITL NMR STRUCTURE OF ESCHERICHIA COLI GLUTAREDOXIN 3-GLUTATHIONE
JRNL TITL 2 MIXED DISULFIDE COMPLEX: IMPLICATIONS FOR THE ENZYMATIC
JRNL TITL 3 MECHANISM.
JRNL REF J.MOL.BIOL. V. 286 541 1999
JRNL REFN ISSN 0022-2836
JRNL PMID 9973569
JRNL DOI 10.1006/JMBI.1998.2444
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH F.ASLUND,K.NORDSTRAND,K.D.BERNDT,M.NIKKOLA,T.BERGMAN,
REMARK 1 AUTH 2 H.PONSTINGL,H.JORNVALL,G.OTTING,A.HOLMGREN
REMARK 1 TITL GLUTAREDOXIN-3 FROM ESCHERICHIA COLI. AMINO ACID SEQUENCE,
REMARK 1 TITL 2 1H AND 15N NMR ASSIGNMENTS, AND STRUCTURAL ANALYSIS
REMARK 1 REF J.BIOL.CHEM. V. 271 6736 1996
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : OPAL
REMARK 3 AUTHORS : LUGINBUHL,GUNTERT,BILLETER, WUTHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE 20 CONFORMERS WERE ENERGY-MINIMIZED
REMARK 3 IN A 6 ANGSTROM SHELL OF EXPLICIT WATER.
REMARK 4
REMARK 4 3GRX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000178989.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 301
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 0.05 M
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : H2O/D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 3QF-COSY; SMALL FLIP
REMARK 210 ANGLE COSY; TOCSY; NOESY; OMEGA1-
REMARK 210 DECOUPLED NOESY; 2D HNHB; 15N-
REMARK 210 HSQC; NOESY-15N-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX 600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY, DYANA
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 : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING ONE SAMPLE OF
REMARK 210 RECOMBINANT GRX3[C14S/C65Y] AT NATURAL ABUNDANCE AND ONE SAMPLE
REMARK 210 OF UNIFORMLY 15N-LABELED GRX3[C14S/C65Y] COMPLEXED WITH
REMARK 210 UNLABELED GLUTATHIONE.
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
REMARK 500 REMARK: NULL
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 2 TYR A 65 CB - CG - CD2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 2 TYR A 65 CB - CG - CD1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 3 ARG A 74 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 8 TYR A 65 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 11 ARG A 40 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 18 TYR A 69 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 19 TYR A 65 CB - CG - CD2 ANGL. DEV. = -4.4 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 2 81.89 -154.04
REMARK 500 1 CYS A 11 104.03 -172.40
REMARK 500 1 SER A 27 57.62 -93.25
REMARK 500 1 ASP A 34 -72.29 -71.12
REMARK 500 1 ALA A 38 -72.11 -62.03
REMARK 500 1 ALA A 59 -7.21 65.08
REMARK 500 1 ILE A 62 -77.43 -100.18
REMARK 500 2 ASN A 2 56.86 -167.02
REMARK 500 2 THR A 10 -48.21 75.72
REMARK 500 2 LEU A 20 -70.16 -75.49
REMARK 500 2 ALA A 59 -6.71 70.61
REMARK 500 3 GLU A 9 -73.78 -62.41
REMARK 500 3 CYS A 11 98.75 -164.84
REMARK 500 3 TYR A 13 1.34 -62.66
REMARK 500 3 ALA A 59 -3.26 70.94
REMARK 500 4 ASN A 2 72.39 -104.00
REMARK 500 4 THR A 50 -40.26 -135.98
REMARK 500 5 ASN A 2 65.62 36.55
REMARK 500 5 ILE A 44 -70.29 -54.47
REMARK 500 5 ALA A 59 -4.86 57.98
REMARK 500 5 ILE A 62 -88.98 -86.06
REMARK 500 6 ASN A 2 54.92 -161.73
REMARK 500 6 GLU A 9 -70.70 -53.48
REMARK 500 6 CYS A 11 96.36 -166.83
REMARK 500 6 THR A 50 -13.97 75.41
REMARK 500 6 ALA A 59 -9.27 60.77
REMARK 500 7 GLU A 9 -71.76 -65.89
REMARK 500 7 CYS A 11 92.90 -165.85
REMARK 500 7 ARG A 49 -47.16 -143.37
REMARK 500 7 THR A 50 -19.09 78.31
REMARK 500 7 ALA A 59 -10.24 65.09
REMARK 500 8 ILE A 62 -76.20 -79.74
REMARK 500 9 THR A 10 -8.12 56.64
REMARK 500 9 ALA A 59 -4.34 55.25
REMARK 500 9 ILE A 62 -72.63 -97.33
REMARK 500 9 LEU A 81 35.79 -81.55
REMARK 500 10 ASN A 2 84.08 -155.09
REMARK 500 10 SER A 27 54.93 -96.09
REMARK 500 10 ALA A 38 -72.42 -60.17
REMARK 500 10 SER A 47 -9.40 -144.44
REMARK 500 11 ASN A 2 72.04 -152.52
REMARK 500 11 ALA A 59 -18.62 100.38
REMARK 500 12 ASN A 2 58.31 -102.89
REMARK 500 12 ALA A 59 -3.35 69.41
REMARK 500 13 ASN A 2 83.29 -159.27
REMARK 500 13 CYS A 11 104.37 -161.28
REMARK 500 13 ALA A 59 -1.79 65.18
REMARK 500 14 ASN A 2 72.12 -103.95
REMARK 500 14 GLU A 9 83.66 -66.54
REMARK 500 14 THR A 10 -45.15 166.83
REMARK 500
REMARK 500 THIS ENTRY HAS 67 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 3 TYR A 6 0.07 SIDE CHAIN
REMARK 500 4 ARG A 49 0.08 SIDE CHAIN
REMARK 500 9 TYR A 6 0.11 SIDE CHAIN
REMARK 500 9 TYR A 13 0.09 SIDE CHAIN
REMARK 500 10 ARG A 46 0.08 SIDE CHAIN
REMARK 500 12 TYR A 69 0.08 SIDE CHAIN
REMARK 500 13 ARG A 46 0.11 SIDE CHAIN
REMARK 500 17 ARG A 16 0.11 SIDE CHAIN
REMARK 500 18 ARG A 49 0.08 SIDE CHAIN
REMARK 500 18 ARG A 74 0.09 SIDE CHAIN
REMARK 500 19 TYR A 65 0.08 SIDE CHAIN
REMARK 500 20 TYR A 6 0.07 SIDE CHAIN
REMARK 500 20 ARG A 16 0.08 SIDE CHAIN
REMARK 500 20 TYR A 69 0.09 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 83
DBREF 3GRX A 1 82 UNP P0AC62 GLRX3_ECOLI 1 82
SEQADV 3GRX SER A 14 UNP P0AC62 CYS 14 ENGINEERED MUTATION
SEQADV 3GRX TYR A 65 UNP P0AC62 CYS 65 ENGINEERED MUTATION
SEQRES 1 A 82 ALA ASN VAL GLU ILE TYR THR LYS GLU THR CYS PRO TYR
SEQRES 2 A 82 SER HIS ARG ALA LYS ALA LEU LEU SER SER LYS GLY VAL
SEQRES 3 A 82 SER PHE GLN GLU LEU PRO ILE ASP GLY ASN ALA ALA LYS
SEQRES 4 A 82 ARG GLU GLU MET ILE LYS ARG SER GLY ARG THR THR VAL
SEQRES 5 A 82 PRO GLN ILE PHE ILE ASP ALA GLN HIS ILE GLY GLY TYR
SEQRES 6 A 82 ASP ASP LEU TYR ALA LEU ASP ALA ARG GLY GLY LEU ASP
SEQRES 7 A 82 PRO LEU LEU LYS
HET GSH A 83 35
HETNAM GSH GLUTATHIONE
FORMUL 2 GSH C10 H17 N3 O6 S
HELIX 1 1 PRO A 12 SER A 23 1 12
HELIX 2 2 ALA A 38 SER A 47 1 10
HELIX 3 3 TYR A 65 ALA A 73 1 9
HELIX 4 4 LEU A 77 LEU A 80 1 4
SHEET 1 A 4 PHE A 28 PRO A 32 0
SHEET 2 A 4 VAL A 3 THR A 7 1 N ILE A 5 O GLN A 29
SHEET 3 A 4 GLN A 54 ILE A 57 -1 N PHE A 56 O GLU A 4
SHEET 4 A 4 GLN A 60 HIS A 61 -1 N ILE A 57 O GLN A 60
LINK SG2 GSH A 83 SG CYS A 11 1555 1555 2.03
CISPEP 1 VAL A 52 PRO A 53 1 -11.31
CISPEP 2 VAL A 52 PRO A 53 2 -11.49
CISPEP 3 VAL A 52 PRO A 53 3 -6.55
CISPEP 4 VAL A 52 PRO A 53 4 -7.90
CISPEP 5 VAL A 52 PRO A 53 5 -11.28
CISPEP 6 VAL A 52 PRO A 53 6 -1.61
CISPEP 7 VAL A 52 PRO A 53 7 -2.50
CISPEP 8 VAL A 52 PRO A 53 8 -6.75
CISPEP 9 VAL A 52 PRO A 53 9 -6.80
CISPEP 10 VAL A 52 PRO A 53 10 -11.04
CISPEP 11 VAL A 52 PRO A 53 11 -11.18
CISPEP 12 VAL A 52 PRO A 53 12 -10.82
CISPEP 13 VAL A 52 PRO A 53 13 -9.44
CISPEP 14 VAL A 52 PRO A 53 14 -11.06
CISPEP 15 VAL A 52 PRO A 53 15 -11.40
CISPEP 16 VAL A 52 PRO A 53 16 -3.68
CISPEP 17 VAL A 52 PRO A 53 17 -6.86
CISPEP 18 VAL A 52 PRO A 53 18 -6.21
CISPEP 19 VAL A 52 PRO A 53 19 -11.10
CISPEP 20 VAL A 52 PRO A 53 20 -8.39
SITE 1 AC1 3 CYS A 11 THR A 51 VAL A 52
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 14 2 Bytes