Header list of 1bnb.pdb file
Complete list - 16 20 Bytes
HEADER BETA-DEFENSIN 12 08-MAR-95 1BNB
TITLE SOLUTION STRUCTURE OF BOVINE NEUTROPHIL BETA-DEFENSIN 12: THE PEPTIDE
TITLE 2 FOLD OF THE BETA-DEFENSINS IS IDENTICAL TO THAT OF THE CLASSICAL
TITLE 3 DEFENSINS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BOVINE NEUTROPHIL BETA-DEFENSIN 12;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 ORGAN: NEUTROPHILS;
SOURCE 6 CELL: POLYMORPHONUCLEOCYTE
KEYWDS BETA-DEFENSIN 12
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR G.R.ZIMMERMANN,P.LEGAULT,M.E.SELSTED,A.PARDI
REVDAT 3 16-FEB-22 1BNB 1 REMARK
REVDAT 2 24-FEB-09 1BNB 1 VERSN
REVDAT 1 15-OCT-95 1BNB 0
JRNL AUTH G.R.ZIMMERMANN,P.LEGAULT,M.E.SELSTED,A.PARDI
JRNL TITL SOLUTION STRUCTURE OF BOVINE NEUTROPHIL BETA-DEFENSIN-12:
JRNL TITL 2 THE PEPTIDE FOLD OF THE BETA-DEFENSINS IS IDENTICAL TO THAT
JRNL TITL 3 OF THE CLASSICAL DEFENSINS.
JRNL REF BIOCHEMISTRY V. 34 13663 1995
JRNL REFN ISSN 0006-2960
JRNL PMID 7577957
JRNL DOI 10.1021/BI00041A048
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.E.SELSTED,Y.-Q.TANG,W.L.MORRIS,P.A.MCGUIRE,M.J.NOVOTNY,
REMARK 1 AUTH 2 A.H.HENSCHEN,J.S.CULLOR
REMARK 1 TITL PURIFICATION, PRIMARY STRUCTURES, AND ANTIBACTERIAL
REMARK 1 TITL 2 ACTIVITIES OF BETA-DEFENSINS, A NEW FAMILY OF ANTI-MICROBIAL
REMARK 1 TITL 3 PEPTIDES FROM BOVINE NEUTROPHILS
REMARK 1 REF J.BIOL.CHEM. V. 268 6641 1993
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 2
REMARK 1 AUTH Y.-Q.TANG,M.E.SELSTED
REMARK 1 TITL CHARACTERIZATION OF THE DISULFIDE MOTIF IN BNDB-12, AN
REMARK 1 TITL 2 ANTIMICROBIAL BETA-DEFENSIN PEPTIDE FROM BOVINE NEUTROPHILS
REMARK 1 REF J.BIOL.CHEM. V. 268 6649 1993
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1BNB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000171934.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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: 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 3 -79.33 66.82
REMARK 500 1 SER A 4 -167.62 63.75
REMARK 500 1 ILE A 15 -93.56 61.84
REMARK 500 2 CYS A 5 -62.44 73.07
REMARK 500 2 ILE A 15 -126.75 53.49
REMARK 500 3 ILE A 15 -136.82 51.05
REMARK 500 3 MET A 21 77.04 63.18
REMARK 500 4 PRO A 2 -167.42 -77.35
REMARK 500 4 ILE A 15 -129.79 51.37
REMARK 500 5 ILE A 15 -94.03 61.46
REMARK 500 5 MET A 21 84.44 58.89
REMARK 500 6 ILE A 15 -93.51 58.85
REMARK 500 6 MET A 21 65.19 60.84
REMARK 500 7 ILE A 15 -92.98 60.48
REMARK 500 8 SER A 4 43.54 -91.40
REMARK 500 8 CYS A 5 44.42 -149.45
REMARK 500 8 ILE A 15 -92.90 61.89
REMARK 500 8 MET A 21 63.71 62.64
REMARK 500 9 ILE A 15 -116.78 54.92
REMARK 500 10 ILE A 15 -121.84 54.84
REMARK 500 11 CYS A 5 40.18 -97.40
REMARK 500 11 ILE A 15 -99.10 61.49
REMARK 500 12 LEU A 3 70.77 54.35
REMARK 500 12 PRO A 14 31.20 -80.32
REMARK 500 12 ILE A 15 -153.95 -146.23
REMARK 500 12 ILE A 24 44.49 -148.38
REMARK 500 13 CYS A 5 45.60 -104.75
REMARK 500 13 ILE A 15 -101.80 61.29
REMARK 500 14 CYS A 5 49.18 -97.43
REMARK 500 14 ILE A 15 -94.96 61.42
REMARK 500 14 MET A 21 65.70 61.85
REMARK 500 15 PRO A 14 38.26 -79.65
REMARK 500 15 ILE A 15 -83.68 -157.31
REMARK 500 16 ILE A 15 -119.22 54.21
REMARK 500 17 ILE A 15 -95.21 63.02
REMARK 500 17 ILE A 24 42.16 -145.33
REMARK 500 18 LEU A 3 132.61 70.69
REMARK 500 18 ILE A 15 -98.49 59.68
REMARK 500 18 PRO A 18 -165.13 -78.53
REMARK 500 18 ILE A 24 49.29 -142.03
REMARK 500 19 SER A 4 -171.03 57.46
REMARK 500 19 ILE A 15 -107.38 56.88
REMARK 500 20 ARG A 7 89.81 -69.45
REMARK 500 20 ILE A 15 -120.59 53.75
REMARK 500 20 MET A 21 86.19 61.68
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 ARG A 7 0.28 SIDE CHAIN
REMARK 500 1 ARG A 16 0.29 SIDE CHAIN
REMARK 500 1 ARG A 22 0.32 SIDE CHAIN
REMARK 500 1 ARG A 30 0.30 SIDE CHAIN
REMARK 500 1 ARG A 36 0.13 SIDE CHAIN
REMARK 500 2 ARG A 7 0.31 SIDE CHAIN
REMARK 500 2 ARG A 16 0.32 SIDE CHAIN
REMARK 500 2 ARG A 22 0.23 SIDE CHAIN
REMARK 500 2 ARG A 30 0.31 SIDE CHAIN
REMARK 500 2 ARG A 36 0.23 SIDE CHAIN
REMARK 500 3 ARG A 7 0.30 SIDE CHAIN
REMARK 500 3 ARG A 16 0.32 SIDE CHAIN
REMARK 500 3 ARG A 22 0.32 SIDE CHAIN
REMARK 500 3 ARG A 30 0.29 SIDE CHAIN
REMARK 500 3 ARG A 36 0.27 SIDE CHAIN
REMARK 500 4 ARG A 7 0.31 SIDE CHAIN
REMARK 500 4 ARG A 16 0.32 SIDE CHAIN
REMARK 500 4 ARG A 22 0.29 SIDE CHAIN
REMARK 500 4 ARG A 30 0.30 SIDE CHAIN
REMARK 500 4 ARG A 36 0.29 SIDE CHAIN
REMARK 500 5 ARG A 7 0.28 SIDE CHAIN
REMARK 500 5 ARG A 16 0.32 SIDE CHAIN
REMARK 500 5 ARG A 22 0.28 SIDE CHAIN
REMARK 500 5 ARG A 30 0.30 SIDE CHAIN
REMARK 500 5 ARG A 36 0.32 SIDE CHAIN
REMARK 500 6 ARG A 7 0.30 SIDE CHAIN
REMARK 500 6 ARG A 16 0.30 SIDE CHAIN
REMARK 500 6 ARG A 22 0.32 SIDE CHAIN
REMARK 500 6 ARG A 30 0.28 SIDE CHAIN
REMARK 500 6 ARG A 36 0.18 SIDE CHAIN
REMARK 500 7 ARG A 7 0.32 SIDE CHAIN
REMARK 500 7 ARG A 16 0.28 SIDE CHAIN
REMARK 500 7 ARG A 22 0.26 SIDE CHAIN
REMARK 500 7 ARG A 30 0.31 SIDE CHAIN
REMARK 500 7 ARG A 36 0.31 SIDE CHAIN
REMARK 500 8 ARG A 7 0.31 SIDE CHAIN
REMARK 500 8 ARG A 16 0.30 SIDE CHAIN
REMARK 500 8 ARG A 22 0.31 SIDE CHAIN
REMARK 500 8 ARG A 30 0.30 SIDE CHAIN
REMARK 500 8 ARG A 36 0.17 SIDE CHAIN
REMARK 500 9 ARG A 7 0.31 SIDE CHAIN
REMARK 500 9 ARG A 16 0.32 SIDE CHAIN
REMARK 500 9 ARG A 22 0.30 SIDE CHAIN
REMARK 500 9 ARG A 30 0.32 SIDE CHAIN
REMARK 500 10 ARG A 7 0.26 SIDE CHAIN
REMARK 500 10 ARG A 16 0.32 SIDE CHAIN
REMARK 500 10 ARG A 22 0.22 SIDE CHAIN
REMARK 500 10 ARG A 30 0.30 SIDE CHAIN
REMARK 500 10 ARG A 36 0.15 SIDE CHAIN
REMARK 500 11 ARG A 7 0.29 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 98 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1BNB A 2 38 UNP P46170 BD12_BOVIN 2 38
SEQRES 1 A 38 ALA PRO LEU SER CYS GLY ARG ASN GLY GLY VAL CYS ILE
SEQRES 2 A 38 PRO ILE ARG CYS PRO VAL PRO MET ARG GLN ILE GLY THR
SEQRES 3 A 38 CYS PHE GLY ARG PRO VAL LYS CYS CYS ARG SER TRP
SHEET 1 A 3 GLY A 10 ILE A 13 0
SHEET 2 A 3 VAL A 32 ARG A 36 -1 N CYS A 35 O VAL A 11
SHEET 3 A 3 ARG A 22 CYS A 27 -1 N CYS A 27 O VAL A 32
SSBOND 1 CYS A 5 CYS A 34 1555 1555 2.02
SSBOND 2 CYS A 12 CYS A 27 1555 1555 2.02
SSBOND 3 CYS A 17 CYS A 35 1555 1555 2.02
CISPEP 1 VAL A 19 PRO A 20 1 -0.16
CISPEP 2 VAL A 19 PRO A 20 2 -0.22
CISPEP 3 VAL A 19 PRO A 20 3 -0.30
CISPEP 4 VAL A 19 PRO A 20 4 -0.05
CISPEP 5 VAL A 19 PRO A 20 5 0.05
CISPEP 6 VAL A 19 PRO A 20 6 0.06
CISPEP 7 VAL A 19 PRO A 20 7 0.02
CISPEP 8 VAL A 19 PRO A 20 8 -0.42
CISPEP 9 VAL A 19 PRO A 20 9 -0.22
CISPEP 10 VAL A 19 PRO A 20 10 -0.31
CISPEP 11 VAL A 19 PRO A 20 11 0.14
CISPEP 12 VAL A 19 PRO A 20 12 -0.15
CISPEP 13 VAL A 19 PRO A 20 13 -0.05
CISPEP 14 VAL A 19 PRO A 20 14 0.10
CISPEP 15 VAL A 19 PRO A 20 15 0.04
CISPEP 16 VAL A 19 PRO A 20 16 -0.23
CISPEP 17 VAL A 19 PRO A 20 17 0.01
CISPEP 18 VAL A 19 PRO A 20 18 -1.20
CISPEP 19 VAL A 19 PRO A 20 19 0.08
CISPEP 20 VAL A 19 PRO A 20 20 -0.08
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 - 16 20 Bytes