Header list of 1feo.pdb file
Complete list - 3 20 Bytes
HEADER TOXIN 21-JUL-00 1FEO
TITLE SOLUTION STRUCTURE OF OMEGA-CONOTOXIN MVIIA WITH C-TERMINAL GLY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OMEGA-CONOTOXIN MVIIA-GLY;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: CHEMICALLY SYNTHESIZED SEQUENCE BASED ON C-DNA FROM
SOURCE 4 CONUS MAGUS. 15N-LABELED SAMPLE WAS PRODUCED IN ESCHERICHIA COLI
SOURCE 5 USING A SYNTHETIC GENE.
KEYWDS BETA SHEET, DISULFIDE KNOT, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR D.P.GOLDENBERG,R.E.KOEHN,D.E.GILBERT,G.WAGNER
REVDAT 4 03-NOV-21 1FEO 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1FEO 1 VERSN
REVDAT 2 31-MAY-05 1FEO 3 ATOM JRNL
REVDAT 1 23-AUG-00 1FEO 0
JRNL AUTH D.P.GOLDENBERG,R.E.KOEHN,D.E.GILBERT,G.WAGNER
JRNL TITL SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF AN
JRNL TITL 2 OMEGA-CONOTOXIN PRECURSOR
JRNL REF PROTEIN SCI. V. 10 538 2001
JRNL REFN ISSN 0961-8368
JRNL PMID 11344322
JRNL DOI 10.1110/PS.30701
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.PRICE-CARTER,W.R.GRAY,D.P.GOLDENBERG
REMARK 1 TITL FOLDING OF OMEGA-CONOTOXINS. 2. INFLUENCE OF PRECURSOR
REMARK 1 TITL 2 SEQUENCES AND PROTEIN DISULFIDE ISOMERASE
REMARK 1 REF BIOCHEMISTRY V. 35 15547 1996
REMARK 1 REFN ISSN 0006-2960
REMARK 1 DOI 10.1021/BI9615755
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE, DYANA 1.3
REMARK 3 AUTHORS : DELAGLIO ET AL. (NMRPIPE), GUNTERT ET AL (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 249 NON
REMARK 3 -REDUNCANT NOE-DERIVED DISTANCE RESTRAINTS, 9 DISTANCE
REMARK 3 RESTRAINTS FROM THE THREE DISULFIDE BONDS, 16 DISTANCE
REMARK 3 RESTRAINTS FROM HYDROGEN BONDS, 19 DIHEDRAL ANGLE RESTRAINTS.
REMARK 4
REMARK 4 1FEO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-AUG-00.
REMARK 100 THE DEPOSITION ID IS D_1000011519.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 283
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2 MM OMEGA-MVIIA-GLY; 2 MM OMEGA
REMARK 210 -MVIIA-GLY U-15N
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA; HNHB
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS; AMX
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.2, DYANA 1.3
REMARK 210 METHOD USED : SIMULATED ANNEALING IN TORSION
REMARK 210 ANGLE SPACE
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 9
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: 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: 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 CYS A 8 -163.48 -112.00
REMARK 500 1 LEU A 11 103.29 174.75
REMARK 500 1 MET A 12 16.91 -144.64
REMARK 500 1 TYR A 13 83.81 36.67
REMARK 500 1 THR A 17 -67.84 -90.63
REMARK 500 1 SER A 19 -160.04 -113.71
REMARK 500 2 LYS A 4 142.98 -39.68
REMARK 500 2 CYS A 8 -164.20 -107.07
REMARK 500 2 ARG A 10 -40.38 177.92
REMARK 500 2 LEU A 11 71.05 174.06
REMARK 500 2 TYR A 13 84.55 37.77
REMARK 500 2 THR A 17 -67.29 -93.47
REMARK 500 3 LYS A 4 128.14 -39.76
REMARK 500 3 CYS A 8 -163.67 -105.35
REMARK 500 3 SER A 9 -64.02 -97.74
REMARK 500 3 ARG A 10 36.85 -173.95
REMARK 500 3 LEU A 11 63.25 85.59
REMARK 500 3 TYR A 13 78.94 38.22
REMARK 500 3 THR A 17 -68.40 -94.52
REMARK 500 4 LYS A 4 123.95 -39.77
REMARK 500 4 CYS A 8 -163.77 -115.43
REMARK 500 4 LEU A 11 104.43 174.53
REMARK 500 4 MET A 12 17.22 -146.70
REMARK 500 4 TYR A 13 83.95 36.19
REMARK 500 4 SER A 19 -158.56 -112.15
REMARK 500 5 CYS A 8 -163.79 -112.43
REMARK 500 5 ARG A 10 -50.51 -176.53
REMARK 500 5 LEU A 11 57.88 -174.92
REMARK 500 5 TYR A 13 84.58 37.83
REMARK 500 5 THR A 17 -67.55 -92.62
REMARK 500 6 LYS A 4 141.19 -39.68
REMARK 500 6 CYS A 8 -165.38 -106.01
REMARK 500 6 ARG A 10 -54.67 179.89
REMARK 500 6 LEU A 11 60.09 -173.94
REMARK 500 6 TYR A 13 82.54 39.57
REMARK 500 6 THR A 17 -67.59 -93.10
REMARK 500 6 SER A 19 -164.58 -117.09
REMARK 500 7 LYS A 4 129.98 -39.94
REMARK 500 7 LEU A 11 84.38 54.51
REMARK 500 7 TYR A 13 80.84 43.98
REMARK 500 7 ASP A 14 20.15 -140.90
REMARK 500 7 THR A 17 -68.59 -94.99
REMARK 500 8 LYS A 4 125.48 -39.66
REMARK 500 8 CYS A 8 -163.13 -103.17
REMARK 500 8 ARG A 10 -48.21 177.56
REMARK 500 8 LEU A 11 56.75 176.62
REMARK 500 8 TYR A 13 84.57 38.08
REMARK 500 8 THR A 17 -67.78 -92.97
REMARK 500 8 CYS A 25 150.64 -47.48
REMARK 500 9 LYS A 4 127.60 -39.85
REMARK 500
REMARK 500 THIS ENTRY HAS 114 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1OMG RELATED DB: PDB
REMARK 900 MATURE FORM OF OMEGA-CONOTOXIN MVIIA, WITH AMIDATED C-TERMINUS
REMARK 900 RELATED ID: 1MVI RELATED DB: PDB
REMARK 900 MATURE FORM OF OMEGA-CONOTOXIN MVIIA, WITH AMIDATED C-TERMINUS
REMARK 900 RELATED ID: 1DW4 RELATED DB: PDB
REMARK 900 MATURE FORM OF OMEGA-CONOTOXIN MVIIA, WITH AMIDATED C-TERMINUS
DBREF 1FEO A 1 25 UNP P05484 CXO7A_CONMA 1 25
SEQADV 1FEO GLY A 26 UNP P05484 ENGINEERED MUTATION
SEQRES 1 A 26 CYS LYS GLY LYS GLY ALA LYS CYS SER ARG LEU MET TYR
SEQRES 2 A 26 ASP CYS CYS THR GLY SER CYS ARG SER GLY LYS CYS GLY
SHEET 1 A 2 SER A 19 ARG A 21 0
SHEET 2 A 2 LYS A 24 GLY A 26 -1 O LYS A 24 N ARG A 21
SSBOND 1 CYS A 1 CYS A 16 1555 1555 1.92
SSBOND 2 CYS A 8 CYS A 20 1555 1555 2.00
SSBOND 3 CYS A 15 CYS A 25 1555 1555 2.20
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 - 3 20 Bytes