Header list of 1ju8.pdb file
Complete list - 23 202 Bytes
HEADER HORMONE/GROWTH FACTOR 23-AUG-01 1JU8
TITLE SOLUTION STRUCTURE OF LEGINSULIN, A PLANT HORMON
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LEGINSULIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1-37;
COMPND 5 SYNONYM: ALBUMIN 1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN LEGUMES OF GLYCINE
SOURCE 4 MAX.
KEYWDS T-KNOT, HORMONE-GROWTH FACTOR COMPLEX
EXPDTA SOLUTION NMR
AUTHOR T.YAMAZAKI,M.TAKAOKA,E.KATOH,K.HANADA,M.SAKITA,K.SAKATA,Y.NISHIUCHI,
AUTHOR 2 H.HIRANO
REVDAT 3 23-FEB-22 1JU8 1 REMARK
REVDAT 2 24-FEB-09 1JU8 1 VERSN
REVDAT 1 17-JUN-03 1JU8 0
JRNL AUTH T.YAMAZAKI,M.TAKAOKA,E.KATOH,K.HANADA,M.SAKITA,K.SAKATA,
JRNL AUTH 2 Y.NISHIUCHI,H.HIRANO
JRNL TITL A POSSIBLE PHYSIOLOGICAL FUNCTION AND THE TERTIARY STRUCTURE
JRNL TITL 2 OF A 4-KDA PEPTIDE IN LEGUMES
JRNL REF EUR.J.BIOCHEM. V. 270 1269 2003
JRNL REFN ISSN 0014-2956
JRNL PMID 12631285
JRNL DOI 10.1046/J.1432-1033.2003.03489.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1, X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JU8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-SEP-01.
REMARK 100 THE DEPOSITION ID IS D_1000014191.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 1.8
REMARK 210 IONIC STRENGTH : 0.0
REMARK 210 PRESSURE : AMIENT
REMARK 210 SAMPLE CONTENTS : 4MM LEGINSULIN NON-LABELED; 70%
REMARK 210 H2O, 30% CD3COOD
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; 2D HOHAHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, XWINNMR
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : THE SUBMITTED CONFORMER MODELS
REMARK 210 ARE THE 15 STRUCTURES WITH THE
REMARK 210 LOWEST ENERGY.
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES.
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 ASP A 2 -89.89 -102.26
REMARK 500 VAL A 12 118.63 -160.62
REMARK 500 CYS A 15 -46.78 -141.19
REMARK 500 ARG A 16 -20.31 149.29
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 16 0.08 SIDE CHAIN
REMARK 500 ARG A 18 0.17 SIDE CHAIN
REMARK 500 ARG A 21 0.28 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1JU8 A 1 37 UNP Q39837 ALB1_SOYBN 20 56
SEQRES 1 A 37 ALA ASP CYS ASN GLY ALA CYS SER PRO PHE GLU VAL PRO
SEQRES 2 A 37 PRO CYS ARG SER ARG ASP CYS ARG CYS VAL PRO ILE GLY
SEQRES 3 A 37 LEU PHE VAL GLY PHE CYS ILE HIS PRO THR GLY
SHEET 1 A 3 ALA A 6 CYS A 7 0
SHEET 2 A 3 GLY A 30 ILE A 33 -1 O GLY A 30 N CYS A 7
SHEET 3 A 3 ARG A 21 PRO A 24 -1 N VAL A 23 O PHE A 31
SSBOND 1 CYS A 3 CYS A 20 1555 1555 2.02
SSBOND 2 CYS A 7 CYS A 22 1555 1555 2.02
SSBOND 3 CYS A 15 CYS A 32 1555 1555 2.01
CISPEP 1 VAL A 12 PRO A 13 0 0.25
CRYST1 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 - 23 202 Bytes