Header list of 1c4e.pdb file
Complete list - 25 20 Bytes
HEADER PLANT PROTEIN 27-JUL-99 1C4E
TITLE GURMARIN FROM GYMNEMA SYLVESTRE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (GURMARIN);
COMPND 3 CHAIN: A;
COMPND 4 OTHER_DETAILS: SYNTHETIC
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GYMNEMA SYLVESTRE;
SOURCE 3 ORGANISM_TAXID: 4068;
SOURCE 4 TISSUE: LEAVES;
SOURCE 5 OTHER_DETAILS: CHEMICALLY SYNTHESIZED
KEYWDS GURMARIN, SWEET TASTE SUPPRESSION, CYSTINE KNOT, SWEET TASTE
KEYWDS 2 TRANSDUCTION, PLANT PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.I.FLETCHER,A.J.DINGLEY,G.F.KING
REVDAT 7 25-DEC-19 1C4E 1 SEQADV SEQRES LINK
REVDAT 6 29-NOV-17 1C4E 1 REMARK HELIX
REVDAT 5 07-APR-09 1C4E 1 REVDAT
REVDAT 4 24-FEB-09 1C4E 1 VERSN
REVDAT 3 01-APR-03 1C4E 1 JRNL
REVDAT 2 23-DEC-99 1C4E 1 JRNL
REVDAT 1 27-AUG-99 1C4E 0
SPRSDE 27-AUG-99 1C4E 2GUR
JRNL AUTH J.I.FLETCHER,A.J.DINGLEY,R.SMITH,M.CONNOR,M.J.CHRISTIE,
JRNL AUTH 2 G.F.KING
JRNL TITL HIGH-RESOLUTION SOLUTION STRUCTURE OF GURMARIN, A
JRNL TITL 2 SWEET-TASTE-SUPPRESSING PLANT POLYPEPTIDE.
JRNL REF EUR.J.BIOCHEM. V. 264 525 1999
JRNL REFN ISSN 0014-2956
JRNL PMID 10491100
JRNL DOI 10.1046/J.1432-1327.1999.00659.X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH K.ARAI,R.ISHIMA,S.MORIKAWA,A.MIYASAKA,T.IMOTO,S.YOSHIMURA,
REMARK 1 AUTH 2 S.AIMOTO,K.AKASAKA
REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF GURMARIN, A SWEET
REMARK 1 TITL 2 TASTE-SUPPRESSING POLYPEPTIDE
REMARK 1 REF J.BIOMOL.NMR V. 5 297 1995
REMARK 1 REFN ISSN 0925-2738
REMARK 1 REFERENCE 2
REMARK 1 AUTH K.KAMEI,R.TAKANO,A.MIYASAKA,T.IMOTO,S.HARA
REMARK 1 TITL AMINO ACID SEQUENCE OF SWEET-TASTE-SUPPRESSING PEPTIDE
REMARK 1 TITL 2 (GURMARIN) FROM THE LEAVES OF GYMNEMA SYLVESTRE
REMARK 1 REF J.BIOCHEM.(TOKYO) V. 111 109 1992
REMARK 1 REFN ISSN 0021-924X
REMARK 1 REFERENCE 3
REMARK 1 AUTH T.IMOTO,A.MIYASAKA,R.ISHIMA,K.AKASAKA
REMARK 1 TITL A NOVEL PEPTIDE ISOLATED FROM THE LEAVES OF GYMNEMA
REMARK 1 TITL 2 SYLVESTRE-I. CHARACTERIZATION AND ITS SUPPRESSIVE EFFECT ON
REMARK 1 TITL 3 THE NEURAL RESPONSES TO SWEET TASTE STIMULI IN THE RAT
REMARK 1 REF COMP.BIOCHEM.PHYSIOL. A: V. 100 309 1991
REMARK 1 REF 2 PHYSIOL.
REMARK 1 REFN ISSN 0300-9629
REMARK 1 DOI 10.1016/0300-9629(91)90475-R
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5, X-PLOR 3.843
REMARK 3 AUTHORS : GUENTERT (DYANA), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: SEE PRIMARY REFERENCE ABOVE.
REMARK 4
REMARK 4 1C4E COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-AUG-99.
REMARK 100 THE DEPOSITION ID IS D_1000001249.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 2.9
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : ATMOSPHERIC ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; DQFCOSY; TOCSY; ECOSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA, X-PLOR
REMARK 210 METHOD USED : DISTANCE GEOMETRY AND DYNAMICAL
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING STANDARD 2D HOMONUCLEAR
REMARK 210 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: 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 HG2 GLU A 19 HA PRO A 20 1.18
REMARK 500 HB2 ASN A 27 H TRP A 28 1.23
REMARK 500 HD22 LEU A 9 HG2 LYS A 32 1.25
REMARK 500 HB ILE A 34 H GLY A 35 1.27
REMARK 500 HD3 PRO A 12 HD2 HIS A 31 1.32
REMARK 500 OD1 ASN A 27 O ASP A 30 2.16
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 3 -159.90 -79.41
REMARK 500 1 ASP A 7 -14.24 93.76
REMARK 500 1 LEU A 9 -176.47 -63.33
REMARK 500 1 CYS A 10 -173.79 178.71
REMARK 500 1 TYR A 13 20.92 89.60
REMARK 500 1 TYR A 14 -77.88 -137.25
REMARK 500 1 CYS A 18 -91.05 -59.62
REMARK 500 1 GLU A 19 145.31 170.72
REMARK 500 1 CYS A 23 84.59 -64.35
REMARK 500 1 ASN A 27 -118.24 -140.67
REMARK 500 1 TRP A 29 -33.42 -133.67
REMARK 500 1 LYS A 32 -148.00 -145.91
REMARK 500 1 ILE A 34 -136.92 -124.27
REMARK 500 2 CYS A 3 -158.91 -68.93
REMARK 500 2 ASP A 7 -16.86 93.82
REMARK 500 2 LEU A 9 -173.63 -58.16
REMARK 500 2 CYS A 10 -170.57 169.32
REMARK 500 2 PRO A 12 29.63 -64.98
REMARK 500 2 TYR A 13 24.54 -169.05
REMARK 500 2 TYR A 14 -31.03 -150.10
REMARK 500 2 CYS A 18 -80.87 -52.22
REMARK 500 2 GLU A 19 142.33 161.53
REMARK 500 2 LEU A 21 170.45 -37.14
REMARK 500 2 ASN A 27 -99.21 -138.17
REMARK 500 2 TRP A 28 -20.58 -141.83
REMARK 500 2 TRP A 29 -32.67 -130.15
REMARK 500 2 LYS A 32 -147.20 -144.44
REMARK 500 2 ILE A 34 -151.24 -122.26
REMARK 500 3 CYS A 3 -154.77 -67.64
REMARK 500 3 ASP A 7 -2.02 84.67
REMARK 500 3 CYS A 10 -177.12 -172.22
REMARK 500 3 PRO A 12 21.30 -60.86
REMARK 500 3 TYR A 13 25.62 -155.45
REMARK 500 3 TYR A 14 -32.93 -153.96
REMARK 500 3 CYS A 18 -99.93 -57.27
REMARK 500 3 GLU A 19 144.64 179.89
REMARK 500 3 LEU A 21 172.97 -43.20
REMARK 500 3 ASN A 27 -109.59 -141.39
REMARK 500 3 LYS A 32 -152.50 -144.67
REMARK 500 3 ILE A 34 -160.49 -126.74
REMARK 500 4 GLN A 2 137.98 -26.76
REMARK 500 4 CYS A 3 -156.25 -62.92
REMARK 500 4 ASP A 7 -16.33 91.03
REMARK 500 4 LEU A 9 -173.99 -61.68
REMARK 500 4 CYS A 10 176.83 163.03
REMARK 500 4 PRO A 12 22.62 -65.86
REMARK 500 4 TYR A 13 32.89 -151.41
REMARK 500 4 TYR A 14 -61.58 -162.67
REMARK 500 4 CYS A 18 -84.21 -62.46
REMARK 500 4 GLU A 19 142.72 164.78
REMARK 500
REMARK 500 THIS ENTRY HAS 277 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2GUR RELATED DB: PDB
REMARK 900 HIGHER RESOLUTION STRUCTURE IS BEING PRESENTED IN THE CURRENT ENTRY
DBREF 1C4E A 1 35 UNP P25810 GUR_GYMSY 1 35
SEQRES 1 A 35 PCA GLN CYS VAL LYS LYS ASP GLU LEU CYS ILE PRO TYR
SEQRES 2 A 35 TYR LEU ASP CYS CYS GLU PRO LEU GLU CYS LYS LYS VAL
SEQRES 3 A 35 ASN TRP TRP ASP HIS LYS CYS ILE GLY
MODRES 1C4E PCA A 1 GLN PYROGLUTAMIC ACID
HET PCA A 1 14
HETNAM PCA PYROGLUTAMIC ACID
FORMUL 1 PCA C5 H7 N O3
SHEET 1 B1 1 GLU A 22 LYS A 25 0
SHEET 1 B2 1 HIS A 31 ILE A 34 0
SSBOND 1 CYS A 3 CYS A 18 1555 1555 2.03
SSBOND 2 CYS A 10 CYS A 23 1555 1555 2.03
SSBOND 3 CYS A 17 CYS A 33 1555 1555 2.03
LINK C PCA A 1 N GLN A 2 1555 1555 1.34
CISPEP 1 GLU A 19 PRO A 20 1 0.02
CISPEP 2 GLU A 19 PRO A 20 2 0.10
CISPEP 3 GLU A 19 PRO A 20 3 0.10
CISPEP 4 GLU A 19 PRO A 20 4 0.09
CISPEP 5 GLU A 19 PRO A 20 5 0.10
CISPEP 6 GLU A 19 PRO A 20 6 0.10
CISPEP 7 GLU A 19 PRO A 20 7 0.03
CISPEP 8 GLU A 19 PRO A 20 8 0.01
CISPEP 9 GLU A 19 PRO A 20 9 0.14
CISPEP 10 GLU A 19 PRO A 20 10 0.06
CISPEP 11 GLU A 19 PRO A 20 11 0.00
CISPEP 12 GLU A 19 PRO A 20 12 0.07
CISPEP 13 GLU A 19 PRO A 20 13 0.02
CISPEP 14 GLU A 19 PRO A 20 14 0.10
CISPEP 15 GLU A 19 PRO A 20 15 0.06
CISPEP 16 GLU A 19 PRO A 20 16 0.25
CISPEP 17 GLU A 19 PRO A 20 17 0.17
CISPEP 18 GLU A 19 PRO A 20 18 0.09
CISPEP 19 GLU A 19 PRO A 20 19 0.10
CISPEP 20 GLU A 19 PRO A 20 20 0.10
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 - 25 20 Bytes