Header list of 1gur.pdb file
Complete list - 25 20 Bytes
HEADER SWEET TASTE-SUPPRESSING PROTEIN 12-MAR-96 1GUR TITLE GURMARIN, A SWEET TASTE-SUPPRESSING POLYPEPTIDE, NMR, 10 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: GURMARIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: GYMNEMA SYLVESTRE; SOURCE 3 ORGANISM_TAXID: 4068; SOURCE 4 ORGAN: LEAF KEYWDS SWEET-TASTE, SUPPRESSING PROTEIN, SWEET TASTE-SUPPRESSING PROTEIN EXPDTA SOLUTION NMR NUMMDL 10 AUTHOR K.ARAI,R.ISHIMA,S.MORIKAWA,T.IMOTO,S.YOSHIMURA,S.AIMOTO,K.AKASAKA REVDAT 3 25-DEC-19 1GUR 1 REMARK SEQRES LINK REVDAT 2 24-FEB-09 1GUR 1 VERSN REVDAT 1 01-AUG-96 1GUR 0 JRNL AUTH K.ARAI,R.ISHIMA,S.MORIKAWA,A.MIYASAKA,T.IMOTO,S.YOSHIMURA, JRNL AUTH 2 S.AIMOTO,K.AKASAKA JRNL TITL THREE-DIMENSIONAL STRUCTURE OF GURMARIN, A SWEET JRNL TITL 2 TASTE-SUPPRESSING POLYPEPTIDE. JRNL REF J.BIOMOL.NMR V. 5 297 1995 JRNL REFN ISSN 0925-2738 JRNL PMID 7787425 JRNL DOI 10.1007/BF00211756 REMARK 1 REMARK 1 REFERENCE 1 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 2 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 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : AMBER REMARK 3 AUTHORS : NAKAI,KIDERA,NAKAMURA REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1GUR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000173719. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : NULL REMARK 210 PH : NULL REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : NULL REMARK 210 SPECTROMETER MODEL : NULL REMARK 210 SPECTROMETER MANUFACTURER : NULL REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : NULL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL 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 1 VAL A 4 102.81 -179.75 REMARK 500 1 LYS A 6 109.21 73.16 REMARK 500 1 TYR A 14 70.68 -156.08 REMARK 500 1 LEU A 15 -86.80 -154.45 REMARK 500 1 ASP A 16 109.75 77.60 REMARK 500 1 CYS A 17 169.05 -44.05 REMARK 500 1 CYS A 18 -176.07 -66.37 REMARK 500 1 GLU A 22 -160.26 -126.30 REMARK 500 1 ILE A 34 -90.33 -129.34 REMARK 500 2 GLN A 2 79.03 57.89 REMARK 500 2 VAL A 4 154.78 179.72 REMARK 500 2 LYS A 5 135.02 175.32 REMARK 500 2 LYS A 6 109.14 73.38 REMARK 500 2 ILE A 11 58.73 -158.90 REMARK 500 2 PRO A 12 -81.27 -39.45 REMARK 500 2 TYR A 13 -77.79 -110.01 REMARK 500 2 CYS A 17 165.60 -48.76 REMARK 500 2 GLU A 22 -159.65 -91.59 REMARK 500 2 CYS A 23 113.16 -171.63 REMARK 500 2 ASP A 30 174.08 178.69 REMARK 500 2 LYS A 32 163.64 178.49 REMARK 500 2 CYS A 33 -178.40 -55.22 REMARK 500 2 ILE A 34 -61.56 -133.84 REMARK 500 3 VAL A 4 119.70 -179.66 REMARK 500 3 LYS A 6 109.38 73.27 REMARK 500 3 ASP A 7 18.19 58.42 REMARK 500 3 PRO A 12 178.50 -45.26 REMARK 500 3 TYR A 13 -91.27 57.98 REMARK 500 3 TYR A 14 55.71 -94.29 REMARK 500 3 ASP A 16 73.76 179.63 REMARK 500 3 GLU A 22 -151.76 -116.06 REMARK 500 3 CYS A 23 119.65 -161.28 REMARK 500 3 ASP A 30 160.94 168.66 REMARK 500 3 ILE A 34 -70.42 -100.84 REMARK 500 4 GLN A 2 63.75 -107.15 REMARK 500 4 VAL A 4 105.68 179.07 REMARK 500 4 LYS A 6 108.85 75.49 REMARK 500 4 GLU A 8 -168.33 -105.36 REMARK 500 4 TYR A 14 27.18 43.55 REMARK 500 4 CYS A 17 161.15 -46.91 REMARK 500 4 GLU A 22 -152.56 -132.92 REMARK 500 4 ASP A 30 175.95 166.93 REMARK 500 5 GLN A 2 71.32 48.50 REMARK 500 5 CYS A 3 -169.20 79.53 REMARK 500 5 VAL A 4 105.39 179.38 REMARK 500 5 LYS A 6 108.60 67.38 REMARK 500 5 CYS A 10 161.62 -45.85 REMARK 500 5 TYR A 13 107.00 74.86 REMARK 500 5 ASP A 16 83.65 179.85 REMARK 500 5 GLU A 22 -148.08 -104.16 REMARK 500 REMARK 500 THIS ENTRY HAS 101 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 CYS A 3 VAL A 4 1 -148.50 REMARK 500 CYS A 3 VAL A 4 2 -148.37 REMARK 500 CYS A 3 VAL A 4 3 -148.52 REMARK 500 CYS A 3 VAL A 4 4 -148.44 REMARK 500 CYS A 3 VAL A 4 5 -148.46 REMARK 500 CYS A 3 VAL A 4 6 -148.36 REMARK 500 CYS A 3 VAL A 4 7 -148.39 REMARK 500 CYS A 3 VAL A 4 8 -148.49 REMARK 500 CYS A 3 VAL A 4 9 -148.45 REMARK 500 CYS A 3 VAL A 4 10 -148.52 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 HIS A 31 0.11 SIDE CHAIN REMARK 500 5 HIS A 31 0.10 SIDE CHAIN REMARK 500 6 HIS A 31 0.10 SIDE CHAIN REMARK 500 8 HIS A 31 0.11 SIDE CHAIN REMARK 500 10 HIS A 31 0.10 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 1 CYS A 3 17.18 REMARK 500 2 CYS A 3 17.17 REMARK 500 3 CYS A 3 17.13 REMARK 500 4 CYS A 3 17.35 REMARK 500 5 CYS A 3 17.28 REMARK 500 6 CYS A 3 17.27 REMARK 500 7 CYS A 3 17.14 REMARK 500 7 LYS A 5 -10.42 REMARK 500 7 ASP A 30 -10.94 REMARK 500 8 CYS A 3 17.03 REMARK 500 8 TRP A 28 -10.18 REMARK 500 9 CYS A 3 17.44 REMARK 500 10 CYS A 3 17.31 REMARK 500 REMARK 500 REMARK: NULL DBREF 1GUR A 2 35 UNP P25810 GUR_GYMSY 2 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 1GUR PCA A 1 GLN PYROGLUTAMIC ACID HET PCA A 1 14 HETNAM PCA PYROGLUTAMIC ACID FORMUL 1 PCA C5 H7 N O3 SHEET 1 A 2 LYS A 24 ASN A 27 0 SHEET 2 A 2 ASP A 30 LYS A 32 -1 N ASP A 30 O ASN A 27 LINK C PCA A 1 N GLN A 2 1555 1555 1.34 CISPEP 1 GLU A 19 PRO A 20 1 18.66 CISPEP 2 GLU A 19 PRO A 20 2 16.41 CISPEP 3 GLU A 19 PRO A 20 3 19.69 CISPEP 4 GLU A 19 PRO A 20 4 16.80 CISPEP 5 GLU A 19 PRO A 20 5 20.13 CISPEP 6 GLU A 19 PRO A 20 6 19.86 CISPEP 7 GLU A 19 PRO A 20 7 17.59 CISPEP 8 GLU A 19 PRO A 20 8 19.85 CISPEP 9 GLU A 19 PRO A 20 9 15.15 CISPEP 10 GLU A 19 PRO A 20 10 18.09 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