Header list of 1fyc.pdb file
Complete list - 29 20 Bytes
HEADER TRANSFERASE 21-FEB-97 1FYC
TITLE INNER LIPOYL DOMAIN FROM HUMAN PYRUVATE DEHYDROGENASE (PDH) COMPLEX,
TITLE 2 NMR, 1 STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIHYDROLIPOAMIDE ACETYLTRANSFERASE (E2P);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: LIPOYL DOMAIN;
COMPND 5 EC: 2.3.1.12;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: DIHYDROLIPOAMIDE ACETYLTRANSFERASE SUBUNIT OF THE
COMPND 8 PYRUVATE DEHYDROGENASE (PDH) MULTIENZYME COMPLEX (UNLIPOYLATED
COMPND 9 DOMAIN)
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 ORGAN: LIVER;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: HLIP;
SOURCE 10 OTHER_DETAILS: EXPRESSED AS A GST FUSION PROTEIN
KEYWDS TRANSFERASE, ACYLTRANSFERASE DIHYDROLIPOAMIDE, SUBUNIT, UNLIPOYLATED
EXPDTA SOLUTION NMR
AUTHOR M.J.HOWARD,C.FULLER,R.W.BROADHURST,J.QUINN,S.J.YEAMAN,R.N.PERHAM
REVDAT 3 29-NOV-17 1FYC 1 REMARK HELIX
REVDAT 2 24-FEB-09 1FYC 1 VERSN
REVDAT 1 04-SEP-97 1FYC 0
JRNL AUTH M.J.HOWARD,C.FULLER,R.W.BROADHURST,R.N.PERHAM,J.G.TANG,
JRNL AUTH 2 J.QUINN,A.G.DIAMOND,S.J.YEAMAN
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF THE MAJOR AUTOANTIGEN IN
JRNL TITL 2 PRIMARY BILIARY CIRRHOSIS.
JRNL REF GASTROENTEROLOGY V. 115 139 1998
JRNL REFN ISSN 0016-5085
JRNL PMID 9649469
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAM BE FOUND IN P.M.
REMARK 3 RICAUD ET AL., JOURNAL OF MOLECULAR BIOLOGY, 264, 179-190, 1996
REMARK 4
REMARK 4 1FYC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000173462.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; COSY; TCOSY; HSQC-NOESY;
REMARK 210 HSQC-TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AM500
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : ANSIG 3.3
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 80
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : MEAN STRUCTURE FROM 26 CHOSEN
REMARK 210 HAVING LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
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 SER A 2 -165.61 -56.03
REMARK 500 TYR A 6 151.58 59.89
REMARK 500 HIS A 9 82.83 177.82
REMARK 500 ALA A 16 -75.62 -109.42
REMARK 500 LEU A 17 5.18 80.61
REMARK 500 SER A 18 59.00 -175.05
REMARK 500 THR A 22 27.17 -150.51
REMARK 500 MET A 23 75.32 -161.48
REMARK 500 TRP A 29 44.92 -172.46
REMARK 500 GLU A 30 94.95 -67.87
REMARK 500 VAL A 33 137.81 -22.76
REMARK 500 GLU A 35 -139.20 -69.34
REMARK 500 LYS A 36 97.68 158.76
REMARK 500 GLU A 39 20.97 -149.65
REMARK 500 LEU A 42 -169.75 -67.46
REMARK 500 ALA A 44 95.89 -47.57
REMARK 500 THR A 48 -41.57 -143.78
REMARK 500 ASP A 49 -24.56 161.81
REMARK 500 GLU A 56 107.01 -42.57
REMARK 500 GLU A 59 78.97 42.19
REMARK 500 GLU A 60 -164.63 172.57
REMARK 500 LEU A 63 72.50 55.75
REMARK 500 VAL A 75 168.65 168.55
REMARK 500 LEU A 77 -91.49 -150.70
REMARK 500 THR A 79 88.75 -29.14
REMARK 500 LEU A 81 -43.47 -132.23
REMARK 500 VAL A 85 -33.35 -170.37
REMARK 500 GLU A 86 28.83 81.69
REMARK 500 LYS A 87 153.38 -43.16
REMARK 500 ALA A 89 138.28 75.17
REMARK 500 ASP A 90 103.35 -178.09
REMARK 500 SER A 92 103.35 165.33
REMARK 500 ALA A 93 -72.06 -50.42
REMARK 500 PHE A 94 75.82 55.86
REMARK 500 PRO A 99 -168.47 -78.44
REMARK 500 THR A 100 -77.86 -124.05
REMARK 500 ASP A 104 99.31 -66.76
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 ARG A 28 0.27 SIDE CHAIN
REMARK 500 ARG A 73 0.14 SIDE CHAIN
REMARK 500 ARG A 98 0.21 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1FYC A 1 106 UNP P10515 ODP2_HUMAN 179 282
SEQADV 1FYC ASN A 3 UNP P10515 INSERTION
SEQADV 1FYC MET A 4 UNP P10515 INSERTION
SEQRES 1 A 106 GLY SER ASN MET SER TYR PRO PRO HIS MET GLN VAL LEU
SEQRES 2 A 106 LEU PRO ALA LEU SER PRO THR MET THR MET GLY THR VAL
SEQRES 3 A 106 GLN ARG TRP GLU LYS LYS VAL GLY GLU LYS LEU SER GLU
SEQRES 4 A 106 GLY ASP LEU LEU ALA GLU ILE GLU THR ASP LYS ALA THR
SEQRES 5 A 106 ILE GLY PHE GLU VAL GLN GLU GLU GLY TYR LEU ALA LYS
SEQRES 6 A 106 ILE LEU VAL PRO GLU GLY THR ARG ASP VAL PRO LEU GLY
SEQRES 7 A 106 THR PRO LEU CYS ILE ILE VAL GLU LYS GLU ALA ASP ILE
SEQRES 8 A 106 SER ALA PHE ALA ASP TYR ARG PRO THR GLU VAL THR ASP
SEQRES 9 A 106 LEU LYS
SHEET 1 S1 4 MET A 10 LEU A 13 0
SHEET 2 S1 4 PRO A 80 VAL A 85 -1
SHEET 3 S1 4 GLU A 60 ILE A 66 -1
SHEET 4 S1 4 GLY A 34 SER A 38 -1
SHEET 1 S2 4 THR A 52 VAL A 57 0
SHEET 2 S2 4 ASP A 41 THR A 48 -1
SHEET 3 S2 4 THR A 25 TRP A 29 -1
SHEET 4 S2 4 THR A 72 VAL A 75 -1
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
Complete list - 29 20 Bytes