Header list of 1ut3.pdb file
Complete list - 25 20 Bytes
HEADER ANTIBIOTIC 02-DEC-03 1UT3 TITLE SOLUTION STRUCTURE OF SPHENISCIN-2, A BETA-DEFENSIN FROM TITLE 2 PENGUIN STOMACH PRESERVING FOOD COMPND MOL_ID: 1; COMPND 2 MOLECULE: SPHENISCIN-2; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: SPHE-2, PBD-2; COMPND 5 OTHER_DETAILS: ANTIMICROBIAL PEPTIDE BELONGING TO THE COMPND 6 DEFENSIN FAMILY. SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 ORGANISM_SCIENTIFIC: APTENODYTES PATAGONICUS; SOURCE 4 ORGANISM_COMMON: KING PENGUIN; SOURCE 5 ORGANISM_TAXID: 9234; SOURCE 6 TISSUE: STOMACHAL CONTENT; SOURCE 7 OTHER_DETAILS: THE STUDIES ON THE KING PENGUINS WERE SOURCE 8 CARRIED OUT ON POSSESSION ISLAND, CROZET ARCHIPELAGO. KEYWDS ANTIMICROBIAL PEPTIDE, PENGUIN, DEFENSIN, NMR STRUCTURE, KEYWDS 2 GASTROINTESTINAL IMMUNITY, ANTIBIOTIC, FUNGICIDE EXPDTA SOLUTION NMR NUMMDL 10 AUTHOR C.LANDON,H.LABBE,C.THOUZEAU,P.BULET,F.VOVELLE REVDAT 3 24-FEB-09 1UT3 1 VERSN REVDAT 2 16-JUL-04 1UT3 1 JRNL REVDAT 1 06-MAY-04 1UT3 0 JRNL AUTH C.LANDON,C.THOUZEAU,H.LABBE,P.BULET,F.VOVELLE JRNL TITL SOLUTION STRUCTURE OF SPHENISCIN, A JRNL TITL 2 {BETA}-DEFENSIN FROM THE PENGUIN STOMACH JRNL REF J.BIOL.CHEM. V. 279 30433 2004 JRNL REFN ISSN 0021-9258 JRNL PMID 15123713 JRNL DOI 10.1074/JBC.M401338200 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH C.THOUZEAU,Y.LE MAHO,G.FROGET,L.SABATIER, REMARK 1 AUTH 2 C.LE BOHEC,J.A.HOFFMANN,P.BULET REMARK 1 TITL SPHENISCINS, AVIAN BETA-DEFENSINS IN PRESERVED REMARK 1 TITL 2 STOMACH CONTENTS OF THE KING PENGUIN, APTENODYTES REMARK 1 TITL 3 PATAGONICUS. REMARK 1 REF J.BIOL.CHEM. V. 278 51053 2003 REMARK 1 REFN ISSN 0021-9258 REMARK 1 PMID 14525994 REMARK 1 DOI 10.1074/JBC.M306839200 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : ARIA1.1/CNS1.1 REMARK 3 AUTHORS : LINGE REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1UT3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-DEC-03. REMARK 100 THE PDBE ID CODE IS EBI-14072. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 293 REMARK 210 PH : 4.3 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D-1H-COSY,2D-1H-TOCSY, REMARK 210 2D-1H-NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 REMARK 210 SPECTROMETER MODEL : INOVA600 REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : ARIA/CNS REMARK 210 METHOD USED : NULL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10 REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY, LEAST REMARK 210 RESTRAINT VIOLATION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 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 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT 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 HE2 PHE A 11 - HG2 ARG A 36 1.50 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 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 5 -157.67 -137.58 REMARK 500 1 PRO A 20 46.87 -86.53 REMARK 500 1 SER A 28 -141.85 -146.61 REMARK 500 1 CYS A 33 69.14 -103.98 REMARK 500 2 ARG A 18 45.88 -90.45 REMARK 500 2 PHE A 19 146.62 -171.47 REMARK 500 2 PRO A 20 60.44 -63.24 REMARK 500 2 SER A 28 -140.44 -147.55 REMARK 500 2 VAL A 37 44.13 -79.03 REMARK 500 3 ARG A 16 149.22 69.61 REMARK 500 3 PRO A 20 46.12 -75.06 REMARK 500 3 ARG A 29 -60.91 -172.83 REMARK 500 3 VAL A 37 60.25 -108.36 REMARK 500 4 ARG A 18 56.83 -154.93 REMARK 500 4 PHE A 19 -66.90 -166.39 REMARK 500 5 LEU A 4 75.66 -160.07 REMARK 500 5 LEU A 7 -45.12 72.25 REMARK 500 5 PRO A 20 83.98 -53.99 REMARK 500 5 SER A 28 -147.98 -114.55 REMARK 500 6 LEU A 4 41.40 -108.24 REMARK 500 6 PHE A 11 138.59 -175.39 REMARK 500 6 PRO A 20 40.88 -72.49 REMARK 500 6 SER A 28 -57.02 -141.15 REMARK 500 6 ARG A 29 -66.47 -172.24 REMARK 500 7 LEU A 7 -33.09 -151.23 REMARK 500 7 SER A 28 -146.61 -138.77 REMARK 500 7 VAL A 37 37.90 -75.89 REMARK 500 8 ARG A 6 -37.16 68.96 REMARK 500 8 ARG A 18 46.32 -163.08 REMARK 500 8 PHE A 19 -61.89 -172.84 REMARK 500 8 SER A 21 148.72 179.52 REMARK 500 9 LEU A 4 52.66 -114.10 REMARK 500 9 ARG A 6 -19.19 71.11 REMARK 500 9 LEU A 7 -28.62 72.26 REMARK 500 9 ARG A 18 57.03 -162.56 REMARK 500 9 PHE A 19 -63.01 -159.79 REMARK 500 9 ARG A 26 140.79 -170.99 REMARK 500 9 VAL A 37 65.96 -114.87 REMARK 500 10 LEU A 4 38.75 -88.72 REMARK 500 10 ARG A 6 -35.69 70.24 REMARK 500 10 ARG A 8 -22.61 72.72 REMARK 500 10 ARG A 16 112.20 -161.31 REMARK 500 10 ARG A 18 52.05 -163.38 REMARK 500 10 PHE A 19 -65.27 -167.05 REMARK 500 10 VAL A 37 42.27 -152.68 REMARK 500 REMARK 500 REMARK: NULL REMARK 700 REMARK 700 SHEET REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED. DBREF 1UT3 A 1 38 UNP P83430 SHE2_APTPA 1 38 SEQRES 1 A 38 SER PHE GLY LEU CYS ARG LEU ARG ARG GLY PHE CYS ALA SEQRES 2 A 38 ARG GLY ARG CYS ARG PHE PRO SER ILE PRO ILE GLY ARG SEQRES 3 A 38 CYS SER ARG PHE VAL GLN CYS CYS ARG ARG VAL TRP SHEET 1 AA 3 PHE A 11 ALA A 13 0 SHEET 2 AA 3 VAL A 31 ARG A 36 -1 O GLN A 32 N ALA A 13 SHEET 3 AA 3 SER A 21 CYS A 27 -1 O ILE A 22 N ARG A 35 SSBOND 1 CYS A 5 CYS A 33 1555 1555 2.02 SSBOND 2 CYS A 12 CYS A 27 1555 1555 2.03 SSBOND 3 CYS A 17 CYS A 34 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 - 25 20 Bytes