Header list of 1dx8.pdb file
Complete list - n 17 2 Bytes
HEADER ELECTRON TRANSPORT 23-DEC-99 1DX8
TITLE RUBREDOXIN FROM GUILLARDIA THETA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RUBREDOXIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GUILLARDIA THETA;
SOURCE 3 ORGANISM_TAXID: 55529;
SOURCE 4 ATCC: NCBI 55529;
SOURCE 5 ORGANELLE: NUCLEOMORPH;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A;
SOURCE 11 OTHER_DETAILS: THE RBX-GENE IS ENCODED ON THE G.THETA NUCLEOMORPH
SOURCE 12 (CHROMOSOME II)
KEYWDS ELECTRON TRANSPORT, RUBREDOXIN, GUILLARDIA THETA, ZINC-SUBSTITUTION
EXPDTA SOLUTION NMR
NUMMDL 21
AUTHOR K.SCHWEIMER,S.HOFFMANN,J.WASTL,U.G.MAIER,P.ROESCH,H.STICHT
REVDAT 5 17-JAN-18 1DX8 1 JRNL
REVDAT 4 24-FEB-09 1DX8 1 VERSN
REVDAT 3 04-APR-05 1DX8 1 ATOM
REVDAT 2 12-SEP-00 1DX8 1 JRNL
REVDAT 1 04-JAN-00 1DX8 0
JRNL AUTH K.SCHWEIMER,S.HOFFMANN,J.WASTL,U.G.MAIER,P.ROSCH,H.STICHT
JRNL TITL SOLUTION STRUCTURE OF A ZINC SUBSTITUTED EUKARYOTIC
JRNL TITL 2 RUBREDOXIN FROM THE CRYPTOMONAD ALGA GUILLARDIA THETA.
JRNL REF PROTEIN SCI. V. 9 1474 2000
JRNL REFN ISSN 0961-8368
JRNL PMID 10975569
JRNL DOI 10.1110/PS.9.8.1474
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE.
REMARK 4
REMARK 4 1DX8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-DEC-99.
REMARK 100 THE DEPOSITION ID IS D_1290004397.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.4
REMARK 210 IONIC STRENGTH : 10
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 10% WATER/90% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 1H-1H NOESY; 1H-1H TOCSY 1H-15N
REMARK 210 HSQC; 1H-13C CT-HSQC 15N-EDITED
REMARK 210 NOESY(3D); 13C-EDITED NOESY(3D)
REMARK 210 HNCO; HNCA; HNCACB; CBCA(CO)NH
REMARK 210 HBHA(CO)NH; HNHA; HCCH-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW, NDEE
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 60
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION,
REMARK 210 LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY ON 13C, 15N-LABELED, ZINC-SUBSTITUTED RUBREDOXIN
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 400
REMARK 400 COMPOUND
REMARK 400 THE IRON-ATOM PRESENT IN THE NATIVE RUBREDOXIN WAS REPLACED
REMARK 400 BY ZINC IN ORDER TO AVOID PARAMAGNETIC EFFECTS.
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 ASP A 4 -24.88 174.02
REMARK 500 1 GLU A 5 61.44 -69.68
REMARK 500 1 PRO A 19 -70.04 -68.77
REMARK 500 1 PRO A 30 -163.38 -70.90
REMARK 500 1 LEU A 37 178.97 -56.61
REMARK 500 1 ARG A 47 18.17 57.65
REMARK 500 1 ILE A 56 77.63 -159.99
REMARK 500 1 LYS A 57 65.76 -100.71
REMARK 500 1 ALA A 61 127.16 -176.20
REMARK 500 1 GLU A 65 79.01 -154.36
REMARK 500 1 ASN A 66 53.16 -90.74
REMARK 500 2 GLU A 2 96.38 -61.88
REMARK 500 2 GLU A 5 -148.47 -90.57
REMARK 500 2 PRO A 19 -76.66 -68.58
REMARK 500 2 PRO A 30 -164.87 -72.19
REMARK 500 2 SER A 55 -178.44 -68.15
REMARK 500 2 ILE A 56 88.12 -160.00
REMARK 500 2 LYS A 57 64.55 -101.66
REMARK 500 2 GLN A 67 62.89 -103.54
REMARK 500 3 GLU A 5 -146.95 -91.38
REMARK 500 3 PRO A 19 -72.24 -68.99
REMARK 500 3 PRO A 30 -163.59 -73.01
REMARK 500 3 LEU A 37 -179.25 -53.19
REMARK 500 3 ILE A 56 69.93 -157.60
REMARK 500 3 LYS A 58 148.59 -170.47
REMARK 500 3 ALA A 61 23.23 -153.36
REMARK 500 3 GLU A 65 79.38 53.46
REMARK 500 3 ASN A 66 46.38 -146.92
REMARK 500 4 ASP A 4 -32.02 178.06
REMARK 500 4 GLU A 5 78.03 -66.66
REMARK 500 4 PRO A 30 -164.14 -69.54
REMARK 500 4 SER A 38 164.86 -49.57
REMARK 500 4 ARG A 47 17.73 52.95
REMARK 500 4 LYS A 57 66.46 -108.69
REMARK 500 4 ALA A 64 127.70 -174.19
REMARK 500 4 GLN A 67 -167.31 -116.68
REMARK 500 5 GLU A 2 71.46 53.68
REMARK 500 5 ASP A 4 10.53 -146.70
REMARK 500 5 PRO A 19 -74.04 -68.81
REMARK 500 5 PRO A 30 -163.54 -70.84
REMARK 500 5 ARG A 47 16.32 57.30
REMARK 500 5 ILE A 56 81.51 -160.03
REMARK 500 5 ALA A 61 -56.74 -176.80
REMARK 500 5 LYS A 68 173.75 55.32
REMARK 500 5 TYR A 69 -72.90 -147.09
REMARK 500 6 ASP A 4 -30.70 -176.35
REMARK 500 6 GLU A 5 -142.04 -78.59
REMARK 500 6 PRO A 30 -163.83 -71.42
REMARK 500 6 ARG A 47 17.60 57.66
REMARK 500 6 ILE A 56 89.19 -158.78
REMARK 500
REMARK 500 THIS ENTRY HAS 197 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 1 ARG A 47 0.23 SIDE CHAIN
REMARK 500 2 ARG A 47 0.29 SIDE CHAIN
REMARK 500 3 ARG A 47 0.32 SIDE CHAIN
REMARK 500 4 ARG A 47 0.21 SIDE CHAIN
REMARK 500 5 ARG A 47 0.20 SIDE CHAIN
REMARK 500 6 ARG A 47 0.32 SIDE CHAIN
REMARK 500 7 ARG A 47 0.17 SIDE CHAIN
REMARK 500 8 ARG A 47 0.29 SIDE CHAIN
REMARK 500 9 ARG A 47 0.30 SIDE CHAIN
REMARK 500 10 ARG A 47 0.28 SIDE CHAIN
REMARK 500 11 ARG A 47 0.16 SIDE CHAIN
REMARK 500 12 ARG A 47 0.21 SIDE CHAIN
REMARK 500 13 ARG A 47 0.22 SIDE CHAIN
REMARK 500 14 ARG A 47 0.31 SIDE CHAIN
REMARK 500 15 ARG A 47 0.26 SIDE CHAIN
REMARK 500 16 ARG A 47 0.26 SIDE CHAIN
REMARK 500 17 ARG A 47 0.25 SIDE CHAIN
REMARK 500 18 ARG A 47 0.15 SIDE CHAIN
REMARK 500 19 ARG A 47 0.21 SIDE CHAIN
REMARK 500 20 ARG A 47 0.21 SIDE CHAIN
REMARK 500 21 ARG A 47 0.32 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 71 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 43 SG
REMARK 620 2 CYS A 13 SG 109.6
REMARK 620 3 CYS A 46 SG 108.9 110.6
REMARK 620 4 CYS A 10 SG 108.7 109.5 109.6
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 71
DBREF 1DX8 A 1 70 UNP Q9XG40 Q9XG40 57 126
SEQRES 1 A 70 MET GLU ILE ASP GLU GLY LYS TYR GLU CYS GLU ALA CYS
SEQRES 2 A 70 GLY TYR ILE TYR GLU PRO GLU LYS GLY ASP LYS PHE ALA
SEQRES 3 A 70 GLY ILE PRO PRO GLY THR PRO PHE VAL ASP LEU SER ASP
SEQRES 4 A 70 SER PHE MET CYS PRO ALA CYS ARG SER PRO LYS ASN GLN
SEQRES 5 A 70 PHE LYS SER ILE LYS LYS VAL ILE ALA GLY PHE ALA GLU
SEQRES 6 A 70 ASN GLN LYS TYR GLY
HET ZN A 71 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 1 PRO A 33 LEU A 37 5 5
SHEET 1 A 3 TYR A 15 TYR A 17 0
SHEET 2 A 3 TYR A 8 CYS A 10 -1 N CYS A 10 O TYR A 15
SHEET 3 A 3 PHE A 53 SER A 55 -1 N LYS A 54 O GLU A 9
LINK ZN ZN A 71 SG CYS A 43 1555 1555 2.35
LINK ZN ZN A 71 SG CYS A 13 1555 1555 2.35
LINK ZN ZN A 71 SG CYS A 46 1555 1555 2.35
LINK ZN ZN A 71 SG CYS A 10 1555 1555 2.35
SITE 1 AC1 4 CYS A 10 CYS A 13 CYS A 43 CYS A 46
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 - n 17 2 Bytes