Header list of 2dcx.pdb file
Complete list - 10 20 Bytes
HEADER ANTIMICROBIAL PROTEIN 17-JAN-06 2DCX TITLE NMR SOLUTION STRUCTURE OF THE DERMASEPTIN ANTIMICROBIAL PEPTIDE ANALOG TITLE 2 NC12-K4S4(1-13)A COMPND MOL_ID: 1; COMPND 2 MOLECULE: DERMASEPTIN-4; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 1-13; COMPND 5 SYNONYM: DS IV; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 OTHER_DETAILS: THIS IS A TRUNCATED, MUTATED SEQUENCE OF A PEPTIDE SOURCE 4 THAT OCCURS NATURALLY IN THE SOUTH AMERICAN TREE FROG, PHYLLOMEDUSA SOURCE 5 SAUVAGEI. KEYWDS ALPHA-HELIX, ANTIMICROBIAL PROTEIN EXPDTA SOLUTION NMR NUMMDL 15 AUTHOR D.E.SHALEV,S.ROTEM,A.FISH,A.MOR REVDAT 4 10-NOV-21 2DCX 1 REMARK SEQADV LINK REVDAT 3 24-FEB-09 2DCX 1 VERSN REVDAT 2 25-APR-06 2DCX 1 JRNL REVDAT 1 28-FEB-06 2DCX 0 JRNL AUTH D.E.SHALEV,S.ROTEM,A.FISH,A.MOR JRNL TITL CONSEQUENCES OF N-ACYLATION ON STRUCTURE AND MEMBRANE JRNL TITL 2 BINDING PROPERTIES OF DERMASEPTIN DERIVATIVE K4-S4-(1-13) JRNL REF J.BIOL.CHEM. V. 281 9432 2006 JRNL REFN ISSN 0021-9258 JRNL PMID 16407175 JRNL DOI 10.1074/JBC.M513051200 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 3.1, X-PLOR 3.856 REMARK 3 AUTHORS : BRUKER (XWINNMR), NILGES, KUSZEWSKI AND BRNGER (X REMARK 3 -PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE DERIVED FROM 241 NOE REMARK 3 CONSTRAINTS; 109 INTRARESIDUAL; 44 I+1; 19 I+2; 39 I+3; 30 LONG- REMARK 3 RANGE. REMARK 4 REMARK 4 2DCX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-JAN-06. REMARK 100 THE DEPOSITION ID IS D_1000025266. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 7.4 REMARK 210 IONIC STRENGTH : 78 MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 2.2MM PEPTIDE; 20:1 MOLAR RATIO REMARK 210 OF DPC-D38 (CAMBRIDGE ISOTOPE REMARK 210 LABORATORIES, INC., USA); 0.02% REMARK 210 NAN3 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D TOCSY; 2D NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWINNMR 3.1, SPARKY 3, X-PLOR REMARK 210 3.856, PROCHECK REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY, STRUCTURES WITH THE REMARK 210 LEAST RESTRAINT VIOLATIONS 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 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 TRP A 3 H LEU A 6 1.47 REMARK 500 O ALA A 13 N NH2 A 14 1.72 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 1 ALA A 13 C ALA A 13 O -0.143 REMARK 500 1 ALA A 13 C NH2 A 14 N -0.189 REMARK 500 2 ALA A 13 C NH2 A 14 N -0.212 REMARK 500 8 ALA A 13 C ALA A 13 O 0.184 REMARK 500 15 ALA A 13 C ALA A 13 O 0.121 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 1 ALA A 13 O - C - N ANGL. DEV. = -21.7 DEGREES REMARK 500 3 ALA A 13 O - C - N ANGL. DEV. = -12.0 DEGREES REMARK 500 5 ALA A 13 O - C - N ANGL. DEV. = 121.4 DEGREES REMARK 500 6 ALA A 13 N - CA - CB ANGL. DEV. = -9.4 DEGREES REMARK 500 6 ALA A 13 O - C - N ANGL. DEV. = -72.1 DEGREES REMARK 500 8 ALA A 13 CB - CA - C ANGL. DEV. = 23.6 DEGREES REMARK 500 8 ALA A 13 N - CA - CB ANGL. DEV. = -8.9 DEGREES REMARK 500 8 ALA A 13 N - CA - C ANGL. DEV. = -17.4 DEGREES REMARK 500 15 ALA A 13 CB - CA - C ANGL. DEV. = 13.0 DEGREES 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 LEU A 2 52.72 89.65 REMARK 500 1 TRP A 3 -42.25 -134.13 REMARK 500 1 LYS A 9 -18.53 169.06 REMARK 500 1 LYS A 12 96.44 57.80 REMARK 500 2 LEU A 2 59.52 81.82 REMARK 500 2 TRP A 3 -43.40 -132.91 REMARK 500 2 LYS A 9 -18.60 167.58 REMARK 500 2 LYS A 12 14.19 58.56 REMARK 500 3 TRP A 3 -45.89 -136.36 REMARK 500 3 LYS A 4 -28.16 -38.05 REMARK 500 3 LEU A 6 -37.29 -39.43 REMARK 500 3 LEU A 7 42.98 -107.67 REMARK 500 3 LYS A 9 -19.55 165.48 REMARK 500 4 LEU A 2 57.93 75.68 REMARK 500 4 LYS A 9 -23.45 171.87 REMARK 500 4 LYS A 12 -68.00 68.28 REMARK 500 5 LEU A 2 59.55 82.06 REMARK 500 5 TRP A 3 -43.92 -132.74 REMARK 500 5 LYS A 9 -18.80 168.68 REMARK 500 5 LYS A 12 -69.54 62.79 REMARK 500 6 TRP A 3 -43.26 -137.00 REMARK 500 6 LYS A 4 -27.40 -38.58 REMARK 500 6 LEU A 6 -36.35 -37.63 REMARK 500 6 LYS A 9 -29.99 164.23 REMARK 500 6 VAL A 10 -89.16 -39.70 REMARK 500 6 LEU A 11 50.05 172.74 REMARK 500 7 LEU A 2 52.77 -111.48 REMARK 500 7 LYS A 9 -21.94 174.09 REMARK 500 7 LYS A 12 91.30 62.58 REMARK 500 8 LEU A 2 74.85 68.78 REMARK 500 8 TRP A 3 -38.35 -147.58 REMARK 500 8 LYS A 9 -20.56 164.13 REMARK 500 8 LYS A 12 96.94 48.37 REMARK 500 9 LEU A 2 54.03 76.23 REMARK 500 9 LYS A 9 -22.12 170.84 REMARK 500 9 LYS A 12 82.87 51.12 REMARK 500 10 LEU A 2 60.22 81.08 REMARK 500 10 TRP A 3 -41.77 -133.76 REMARK 500 10 LYS A 9 -19.13 177.81 REMARK 500 10 LYS A 12 94.21 62.25 REMARK 500 11 LYS A 9 -24.26 -179.79 REMARK 500 11 LYS A 12 89.06 62.03 REMARK 500 12 LYS A 8 -35.98 -39.90 REMARK 500 12 LYS A 9 23.23 -175.55 REMARK 500 12 LYS A 12 -67.74 67.73 REMARK 500 13 LEU A 7 39.18 -84.04 REMARK 500 13 LYS A 9 -19.55 174.83 REMARK 500 13 VAL A 10 12.46 -69.33 REMARK 500 13 LYS A 12 95.17 62.42 REMARK 500 14 LEU A 2 89.16 65.52 REMARK 500 REMARK 500 THIS ENTRY HAS 57 RAMACHANDRAN OUTLIERS. 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 DOA A 0 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2DD6 RELATED DB: PDB REMARK 900 NON-ACYLATED PEPTIDE ANALOG, K4-S4(1-13)A DBREF 2DCX A 1 13 UNP P80280 DMS4_PHYSA 1 13 SEQADV 2DCX LYS A 4 UNP P80280 MET 4 ENGINEERED MUTATION SEQRES 1 A 14 ALA LEU TRP LYS THR LEU LEU LYS LYS VAL LEU LYS ALA SEQRES 2 A 14 NH2 HET NH2 A 14 3 HET DOA A 0 38 HETNAM NH2 AMINO GROUP HETNAM DOA 12-AMINO-DODECANOIC ACID FORMUL 1 NH2 H2 N FORMUL 2 DOA C12 H25 N O2 LINK C DOA A 0 N ALA A 1 1555 1555 1.34 LINK C ALA A 13 N NH2 A 14 1555 1555 1.15 SITE 1 AC1 3 ALA A 1 LEU A 2 TRP A 3 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 - 10 20 Bytes