Header list of 1ru5.pdb file
Complete list - 2 20 Bytes
HEADER HORMONE/GROWTH FACTOR 11-DEC-03 1RU5 TITLE SOLUTION STRUCTURE OF PORCINE PEPTIDE YY (PPYY) COMPND MOL_ID: 1; COMPND 2 MOLECULE: PEPTIDE YY; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: PYY, PEPTIDE TYROSINE TYROSINE; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA; SOURCE 3 ORGANISM_COMMON: PIG; SOURCE 4 ORGANISM_TAXID: 9823; SOURCE 5 GENE: PYY; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PUBK19 KEYWDS ALPHA-HELICAL, PP-FOLD, HORMONE-GROWTH FACTOR COMPLEX EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR M.LERCH,M.MAYRHOFER,O.ZERBE REVDAT 3 02-MAR-22 1RU5 1 REMARK LINK REVDAT 2 24-FEB-09 1RU5 1 VERSN REVDAT 1 08-JUN-04 1RU5 0 JRNL AUTH M.LERCH,M.MAYRHOFER,O.ZERBE JRNL TITL STRUCTURAL SIMILARITIES OF MICELLE-BOUND PEPTIDE YY (PYY) JRNL TITL 2 AND NEUROPEPTIDE Y (NPY) ARE RELATED TO THEIR AFFINITY JRNL TITL 3 PROFILES AT THE Y RECEPTORS. JRNL REF J.MOL.BIOL. V. 339 1153 2004 JRNL REFN ISSN 0022-2836 JRNL PMID 15178255 JRNL DOI 10.1016/J.JMB.2004.04.032 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 3.0, AMBER6 6 REMARK 3 AUTHORS : BRUKER (XWINNMR), KOLLMAN ET AL. (AMBER6) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1RU5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-DEC-03. REMARK 100 THE DEPOSITION ID IS D_1000021040. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 301 REMARK 210 PH : 4.2 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 2MM PPYY, PH=4.2; 2MM PPYY, REMARK 210 PH=4.2; 1MM U-15N-PPYY, PH=4.2 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; 2D TOCSY; REMARK 210 15N{1H}-NOE REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 700 MHZ REMARK 210 SPECTROMETER MODEL : DRX; AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XEASY 2.51, DYANA 1.5 REMARK 210 METHOD USED : CALCULATION OF STRUCTURE BY REMARK 210 TORSION ANGLE DYNAMICS REMARK 210 REFINEMENT BY ENERGY REMARK 210 MINIMIZATION WITH FULL REMARK 210 FORCEFIELD IN EXPLICIT WATER REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: REMARK 210 BACKBONE DYNAMICS INFORMATION WAS USED TO VERIFY STRUCTURES. REMARK 210 REMARK 210 STRUCTURE DEVIATES FROM PREVIOUSLY PUBLISHED STRUCTURE BY KEIRE ET REMARK 210 AL., PDB ENTRY 1QBF 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 O GLU A 15 HG SER A 18 1.53 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 ALA A 3 49.58 -160.16 REMARK 500 1 ALA A 12 92.51 47.43 REMARK 500 1 TYR A 21 -54.49 -154.50 REMARK 500 1 ARG A 33 36.44 -157.50 REMARK 500 2 GLU A 10 78.78 42.16 REMARK 500 2 ASP A 11 91.73 67.50 REMARK 500 2 THR A 32 15.62 52.48 REMARK 500 2 ARG A 33 16.80 -155.13 REMARK 500 3 GLU A 10 74.10 44.39 REMARK 500 3 ASP A 11 102.39 69.10 REMARK 500 3 THR A 32 26.88 47.74 REMARK 500 3 ARG A 33 47.10 -175.77 REMARK 500 4 LYS A 4 153.58 -40.61 REMARK 500 4 GLU A 10 -32.40 71.42 REMARK 500 4 ALA A 12 69.54 -68.25 REMARK 500 4 THR A 32 7.03 -68.02 REMARK 500 4 ARG A 33 45.15 -155.01 REMARK 500 4 ARG A 35 85.83 48.93 REMARK 500 5 GLU A 10 25.11 -70.31 REMARK 500 5 ALA A 12 71.30 -61.72 REMARK 500 5 ARG A 33 36.01 -147.27 REMARK 500 6 ALA A 12 82.58 39.54 REMARK 500 6 ARG A 33 35.40 -159.20 REMARK 500 7 ALA A 3 50.27 -150.33 REMARK 500 7 LYS A 4 84.50 -158.40 REMARK 500 7 ARG A 33 31.22 -159.45 REMARK 500 8 GLU A 10 -35.88 73.98 REMARK 500 8 ALA A 12 119.52 -176.61 REMARK 500 8 ARG A 33 27.25 -152.36 REMARK 500 8 ARG A 35 145.85 -171.51 REMARK 500 9 ALA A 3 105.76 -163.30 REMARK 500 9 ALA A 7 91.15 -164.00 REMARK 500 9 GLU A 10 -21.69 73.65 REMARK 500 9 ALA A 12 118.35 -175.61 REMARK 500 9 ARG A 33 34.32 -156.10 REMARK 500 9 ARG A 35 76.88 46.04 REMARK 500 10 ALA A 3 165.76 179.38 REMARK 500 10 LYS A 4 166.10 58.79 REMARK 500 10 GLU A 10 71.09 71.80 REMARK 500 10 ALA A 12 82.12 40.97 REMARK 500 10 ARG A 33 33.86 -154.72 REMARK 500 11 ASP A 11 72.40 -157.29 REMARK 500 11 SER A 13 175.75 79.77 REMARK 500 11 ARG A 33 42.81 -149.57 REMARK 500 12 ALA A 3 63.36 -162.92 REMARK 500 12 GLU A 10 5.72 100.05 REMARK 500 12 ASP A 11 77.42 61.43 REMARK 500 12 ALA A 12 49.52 -72.53 REMARK 500 12 SER A 13 173.27 91.55 REMARK 500 12 ARG A 33 37.89 -156.55 REMARK 500 REMARK 500 THIS ENTRY HAS 89 RAMACHANDRAN OUTLIERS. 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 TYR A 36 0.08 SIDE CHAIN REMARK 500 5 TYR A 27 0.07 SIDE CHAIN REMARK 500 6 TYR A 27 0.07 SIDE CHAIN REMARK 500 12 TYR A 27 0.09 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 A 37 DBREF 1RU5 A 1 36 UNP P68005 PYY_PIG 1 36 SEQRES 1 A 37 TYR PRO ALA LYS PRO GLU ALA PRO GLY GLU ASP ALA SER SEQRES 2 A 37 PRO GLU GLU LEU SER ARG TYR TYR ALA SER LEU ARG HIS SEQRES 3 A 37 TYR LEU ASN LEU VAL THR ARG GLN ARG TYR NH2 HET NH2 A 37 3 HETNAM NH2 AMINO GROUP FORMUL 1 NH2 H2 N HELIX 1 1 SER A 13 THR A 32 1 20 LINK C TYR A 36 N NH2 A 37 1555 1555 1.32 SITE 1 AC1 1 TYR A 36 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