Header list of 1yt6.pdb file
Complete list - 2 20 Bytes
HEADER DE NOVO PROTEIN 10-FEB-05 1YT6 TITLE NMR STRUCTURE OF PEPTIDE SD COMPND MOL_ID: 1; COMPND 2 MOLECULE: PEPTIDE SD; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 OTHER_DETAILS: CHEMICALLY SYNTHESIZED KEYWDS GIBBERELLIN, MIMIC, STD-NMR, DE NOVO PROTEIN EXPDTA SOLUTION NMR NUMMDL 50 AUTHOR T.MURATA,H.HEMMI,S.NAKAMURA,K.SHIMIZU,Y.SUZUKI,I.YAMAGUCHI REVDAT 3 02-MAR-22 1YT6 1 REMARK REVDAT 2 24-FEB-09 1YT6 1 VERSN REVDAT 1 27-SEP-05 1YT6 0 JRNL AUTH T.MURATA,H.HEMMI,S.NAKAMURA,K.SHIMIZU,Y.SUZUKI,I.YAMAGUCHI JRNL TITL STRUCTURE, EPITOPE MAPPING, AND DOCKING SIMULATION OF A JRNL TITL 2 GIBBERELLIN MIMIC PEPTIDE AS A PEPTIDYL MIMOTOPE FOR A JRNL TITL 3 HYDROPHOBIC LIGAND. JRNL REF FEBS J. V. 272 4938 2005 JRNL REFN ISSN 1742-464X JRNL PMID 16176267 JRNL DOI 10.1111/J.1742-4658.2005.04902.X REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 2.6, CNS 1.0 REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1YT6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-FEB-05. REMARK 100 THE DEPOSITION ID IS D_1000031902. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 5.0 REMARK 210 IONIC STRENGTH : NA REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 5MM PEPTIDE SD; 50MM PHOSPHATE REMARK 210 BUFFER; 90% H2O, 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY; 2D REMARK 210 ROESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWINNMR 2.6, SPARKY 3 REMARK 210 METHOD USED : SIMULATED ANNEALING, TORSION REMARK 210 ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 50 REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES REMARK 210 SUBMITTED REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 36 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 1 CYS A 2 151.24 -35.76 REMARK 500 1 SER A 6 63.51 -165.98 REMARK 500 1 ASP A 7 -70.99 -44.94 REMARK 500 2 SER A 6 41.12 72.65 REMARK 500 2 PRO A 9 63.04 -69.06 REMARK 500 3 CYS A 2 -77.35 -86.11 REMARK 500 3 SER A 6 116.19 61.87 REMARK 500 3 ASP A 7 129.60 -177.67 REMARK 500 3 PRO A 9 88.96 -52.11 REMARK 500 4 CYS A 2 -168.68 -53.21 REMARK 500 4 SER A 6 108.34 62.11 REMARK 500 4 ASP A 7 125.10 -174.10 REMARK 500 5 CYS A 2 -78.26 -83.24 REMARK 500 5 SER A 6 -144.67 -164.45 REMARK 500 5 ASP A 7 -142.91 -127.35 REMARK 500 6 CYS A 2 101.66 -43.94 REMARK 500 6 SER A 6 76.35 -158.27 REMARK 500 6 ASP A 7 -122.50 -57.24 REMARK 500 7 SER A 6 -143.59 -146.73 REMARK 500 7 ASP A 7 -82.52 -111.51 REMARK 500 7 PRO A 9 -169.67 -77.13 REMARK 500 8 TRP A 5 31.38 -144.75 REMARK 500 8 SER A 6 -142.86 -173.86 REMARK 500 8 ASP A 7 -81.61 -118.71 REMARK 500 9 SER A 6 -145.20 -159.88 REMARK 500 9 ASP A 7 -85.77 -124.20 REMARK 500 10 SER A 6 101.02 60.63 REMARK 500 10 ASP A 7 118.63 -171.39 REMARK 500 11 SER A 6 50.83 -179.28 REMARK 500 11 ASP A 7 -82.76 -28.07 REMARK 500 12 CYS A 2 150.56 -36.04 REMARK 500 12 SER A 6 58.92 175.06 REMARK 500 13 SER A 6 99.99 -164.37 REMARK 500 14 CYS A 2 -36.69 -38.38 REMARK 500 14 TRP A 5 33.17 -144.11 REMARK 500 14 SER A 6 -144.57 -163.40 REMARK 500 14 ASP A 7 -69.34 -120.07 REMARK 500 15 SER A 6 -144.82 -162.63 REMARK 500 15 ASP A 7 -79.90 -145.96 REMARK 500 16 CYS A 2 152.28 -35.20 REMARK 500 16 SER A 6 21.52 -173.42 REMARK 500 16 ASP A 7 72.35 179.20 REMARK 500 17 SER A 6 -146.10 -130.31 REMARK 500 17 ASP A 7 -139.46 -133.56 REMARK 500 17 PRO A 9 91.58 -62.94 REMARK 500 18 CYS A 2 138.46 -36.28 REMARK 500 18 SER A 6 77.20 -159.40 REMARK 500 18 ASP A 7 -99.45 -52.31 REMARK 500 19 TRP A 5 34.66 -156.74 REMARK 500 19 SER A 6 -140.98 -168.05 REMARK 500 REMARK 500 THIS ENTRY HAS 135 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1YT6 A 1 10 PDB 1YT6 1YT6 1 10 SEQRES 1 A 10 ALA CYS LEU PRO TRP SER ASP GLY PRO CYS SSBOND 1 CYS A 2 CYS A 10 1555 1555 2.03 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 - 2 20 Bytes