Header list of 1xkm.pdb file
Complete list - r 2 2 Bytes
HEADER ANTIBIOTIC 29-SEP-04 1XKM TITLE NMR STRUCTURE OF ANTIMICROBIAL PEPTIDE DISTINCTIN IN WATER COMPND MOL_ID: 1; COMPND 2 MOLECULE: DISTINCTIN CHAIN A; COMPND 3 CHAIN: A, C; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: DISTINCTIN CHAIN B; COMPND 7 CHAIN: B, D; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS PREPARED BY SOLID-PHASE SYNTHESIS. SOURCE 4 THIS SEQUENCE OCCURS NATURALLY IN THE TREE-FROG PHYLLOMEDUSA SOURCE 5 DISTINCTA; SOURCE 6 MOL_ID: 2; SOURCE 7 SYNTHETIC: YES; SOURCE 8 OTHER_DETAILS: THE PEPTIDE WAS PREPARED BY SOLID-PHASE SYNTHESIS. SOURCE 9 THIS SEQUENCE OCCURS NATURALLY IN THE TREE-FROG PHYLLOMEDUSA SOURCE 10 DISTINCTA KEYWDS PORE-FORMING PEPTIDE, HETERODIMER, HOMODIMER, DISULFIDE, FOUR-HELIX KEYWDS 2 BUNDLE, ANTIBIOTIC EXPDTA SOLUTION NMR NUMMDL 24 AUTHOR P.AMODEO,D.RAIMONDO,G.ANDREOTTI,A.MOTTA,A.SCALONI REVDAT 4 02-MAR-22 1XKM 1 REMARK REVDAT 3 24-FEB-09 1XKM 1 VERSN REVDAT 2 21-JUN-05 1XKM 1 JRNL REVDAT 1 05-APR-05 1XKM 0 JRNL AUTH D.RAIMONDO,G.ANDREOTTI,N.SAINT,P.AMODEO,G.RENZONE, JRNL AUTH 2 M.SANSEVERINO,I.ZOCCHI,G.MOLLE,A.MOTTA,A.SCALONI JRNL TITL A FOLDING-DEPENDENT MECHANISM OF ANTIMICROBIAL PEPTIDE JRNL TITL 2 RESISTANCE TO DEGRADATION UNVEILED BY SOLUTION STRUCTURE OF JRNL TITL 3 DISTINCTIN. JRNL REF PROC.NATL.ACAD.SCI.USA V. 102 6309 2005 JRNL REFN ISSN 0027-8424 JRNL PMID 15840728 JRNL DOI 10.1073/PNAS.0409004102 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH C.V.BATISTA,A.SCALONI,D.J.RIGDEN,L.R.SILVA, REMARK 1 AUTH 2 A.RODRIGUES ROMERO,R.DUKOR,A.SEBBEN,F.TALAMO,C.BLOCH REMARK 1 TITL A NOVEL HETERODIMERIC ANTIMICROBIAL PEPTIDE FROM THE REMARK 1 TITL 2 TREE-FROG PHYLLOMEDUSA DISTINCTA REMARK 1 REF FEBS LETT. V. 494 85 2001 REMARK 1 REFN ISSN 0014-5793 REMARK 1 PMID 11297740 REMARK 1 DOI 10.1016/S0014-5793(01)02324-9 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : AMBER 5, AMBER 5 REMARK 3 AUTHORS : KOLLMAN, CASE (AMBER), KOLLMAN, CASE (AMBER) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF REMARK 3 636 RESTRAINTS, 548 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 88 REMARK 3 DISTANCE RESTRAINTS FROM HYDROGEN BONDS. REMARK 4 REMARK 4 1XKM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-OCT-04. REMARK 100 THE DEPOSITION ID IS D_1000030461. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 310; 300; 310; 300; 310; 300; REMARK 210 310; 300 REMARK 210 PH : 6.8; 6.8; 6.4; 6.4; 5.4; 5.4; REMARK 210 5.0; 5.0 REMARK 210 IONIC STRENGTH : NULL; NULL; NULL; NULL; NULL; REMARK 210 NULL; NULL; NULL REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT; REMARK 210 AMBIENT; AMBIENT; AMBIENT; REMARK 210 AMBIENT; AMBIENT REMARK 210 SAMPLE CONTENTS : 3.8MM NATURAL ABUNDANCE REMARK 210 DISTINCTIN; NAN3; 0.05MM NATURAL REMARK 210 ABUNDANCE DISTINCTIN; NAN3; REMARK 210 3.8MM NATURAL ABUNDANCE REMARK 210 DISTINCTIN; NAN3; 0.05MM NATURAL REMARK 210 ABUNDANCE DISTINCTIN; NAN3 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : MOLMOL 2K.2, XWINNMR 2.0 REMARK 210 METHOD USED : SIMULATED ANNEALING WITH REMARK 210 CARTESIAN COORDINATE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 150 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 24 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITHIN A PREFIXED REMARK 210 THRESHOLD OF AMBER ENERGY, REMARK 210 SOLVENT ACCESSIBLE SURFACE AREA REMARK 210 AND SYMMETRY-BASED PENALTY REMARK 210 FUNCTIONS (SEE JRNL) REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 20 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: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D 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: 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 11 CYS B 23 CA - CB - SG ANGL. DEV. = 7.9 DEGREES REMARK 500 12 CYS B 23 CA - CB - SG ANGL. DEV. = 7.4 DEGREES REMARK 500 19 CYS D 23 CA - CB - SG ANGL. DEV. = 7.5 DEGREES REMARK 500 23 ARG B 10 NE - CZ - NH1 ANGL. DEV. = 3.1 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 ARG A 3 65.33 -117.17 REMARK 500 1 VAL A 5 90.86 66.19 REMARK 500 1 ILE A 21 -56.94 71.46 REMARK 500 1 LYS B 24 -56.70 70.49 REMARK 500 1 ASN C 2 26.13 -155.60 REMARK 500 1 ARG C 3 -73.04 -130.90 REMARK 500 1 SER D 4 170.18 71.03 REMARK 500 1 LEU D 6 -64.96 -28.28 REMARK 500 1 LYS D 24 -48.33 62.21 REMARK 500 2 ASN A 2 -39.93 68.80 REMARK 500 2 ILE A 21 -51.80 69.28 REMARK 500 2 LEU B 2 -70.24 -76.68 REMARK 500 2 LYS B 24 -57.47 69.51 REMARK 500 2 GLU C 4 -53.86 66.47 REMARK 500 2 SER D 4 -60.79 168.99 REMARK 500 2 CYS D 23 -70.84 -57.92 REMARK 500 2 LYS D 24 41.69 32.04 REMARK 500 3 VAL A 5 107.74 -42.11 REMARK 500 3 ILE A 21 -57.79 68.27 REMARK 500 3 LEU B 2 -68.27 65.17 REMARK 500 3 VAL B 3 -70.45 -62.96 REMARK 500 3 GLU C 4 -71.12 -92.20 REMARK 500 3 ILE C 21 -62.88 67.71 REMARK 500 3 LYS D 24 -39.60 -151.71 REMARK 500 4 ASN A 2 -52.05 67.60 REMARK 500 4 ARG A 3 -55.15 75.85 REMARK 500 4 ILE A 21 -59.01 71.15 REMARK 500 4 LEU B 2 -72.55 63.45 REMARK 500 4 SER B 4 -133.88 -167.30 REMARK 500 4 LYS B 24 -52.82 72.93 REMARK 500 4 ASN C 2 90.40 -65.30 REMARK 500 4 GLU C 4 -66.66 64.60 REMARK 500 4 ILE C 21 -55.23 67.43 REMARK 500 4 LYS D 24 -54.29 68.54 REMARK 500 5 ASN A 2 45.28 -70.09 REMARK 500 5 ARG A 3 -58.58 66.98 REMARK 500 5 ILE A 21 -57.77 67.04 REMARK 500 5 LEU B 2 -89.26 31.36 REMARK 500 5 LYS B 24 -73.38 59.86 REMARK 500 5 ASN C 2 -177.74 67.62 REMARK 500 5 ARG C 3 99.73 -9.29 REMARK 500 5 ILE C 21 -62.20 68.91 REMARK 500 5 SER D 4 -44.93 -133.35 REMARK 500 5 LYS D 24 65.77 -68.17 REMARK 500 6 ARG A 3 -42.44 69.21 REMARK 500 6 GLU A 4 -59.49 68.54 REMARK 500 6 ILE A 21 -53.50 70.67 REMARK 500 6 SER B 4 74.23 -63.53 REMARK 500 6 LYS B 24 25.08 -161.78 REMARK 500 6 ASN C 2 -58.04 64.66 REMARK 500 REMARK 500 THIS ENTRY HAS 202 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 2 ARG A 3 0.08 SIDE CHAIN REMARK 500 2 ARG A 17 0.08 SIDE CHAIN REMARK 500 2 ARG D 10 0.08 SIDE CHAIN REMARK 500 3 TYR B 12 0.06 SIDE CHAIN REMARK 500 5 TYR B 12 0.15 SIDE CHAIN REMARK 500 6 ARG A 3 0.10 SIDE CHAIN REMARK 500 6 ARG B 10 0.10 SIDE CHAIN REMARK 500 6 TYR D 12 0.12 SIDE CHAIN REMARK 500 7 TYR B 12 0.07 SIDE CHAIN REMARK 500 8 TYR D 12 0.06 SIDE CHAIN REMARK 500 9 TYR B 12 0.07 SIDE CHAIN REMARK 500 10 TYR D 12 0.07 SIDE CHAIN REMARK 500 11 TYR D 12 0.12 SIDE CHAIN REMARK 500 13 TYR B 12 0.07 SIDE CHAIN REMARK 500 14 ARG D 10 0.09 SIDE CHAIN REMARK 500 16 ARG C 3 0.09 SIDE CHAIN REMARK 500 17 TYR B 12 0.08 SIDE CHAIN REMARK 500 18 TYR D 12 0.09 SIDE CHAIN REMARK 500 19 TYR B 12 0.07 SIDE CHAIN REMARK 500 21 TYR B 12 0.18 SIDE CHAIN REMARK 500 23 ARG A 3 0.14 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 650 REMARK 650 HELIX REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED DBREF 1XKM A 1 22 PDB 1XKM 1XKM 1 22 DBREF 1XKM B 1 25 PDB 1XKM 1XKM 1 25 DBREF 1XKM C 1 22 PDB 1XKM 1XKM 1 22 DBREF 1XKM D 1 25 PDB 1XKM 1XKM 1 25 SEQRES 1 A 22 GLU ASN ARG GLU VAL PRO PRO GLY PHE THR ALA LEU ILE SEQRES 2 A 22 LYS THR LEU ARG LYS CYS LYS ILE ILE SEQRES 1 B 25 ASN LEU VAL SER GLY LEU ILE GLU ALA ARG LYS TYR LEU SEQRES 2 B 25 GLU GLN LEU HIS ARG LYS LEU LYS ASN CYS LYS VAL SEQRES 1 C 22 GLU ASN ARG GLU VAL PRO PRO GLY PHE THR ALA LEU ILE SEQRES 2 C 22 LYS THR LEU ARG LYS CYS LYS ILE ILE SEQRES 1 D 25 ASN LEU VAL SER GLY LEU ILE GLU ALA ARG LYS TYR LEU SEQRES 2 D 25 GLU GLN LEU HIS ARG LYS LEU LYS ASN CYS LYS VAL HELIX 1 1 PRO A 7 CYS A 19 1 13 HELIX 2 2 LEU B 6 LYS B 21 1 16 HELIX 3 3 PRO C 7 CYS C 19 1 13 HELIX 4 4 LEU D 6 LYS D 21 1 16 SSBOND 1 CYS A 19 CYS B 23 1555 1555 2.11 SSBOND 2 CYS C 19 CYS D 23 1555 1555 2.12 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 - r 2 2 Bytes