Header list of 1kj5.pdb file
Complete list - 23 20 Bytes
HEADER ANTIBIOTIC 04-DEC-01 1KJ5
TITLE SOLUTION STRUCTURE OF HUMAN BETA-DEFENSIN 1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-DEFENSIN 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HBD-1, DEFENSIN, BETA 1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DEFENSIN, ANTIMICROBIAL PROTEIN, HUMAN BETA-DEFENSIN 1, BETA-
KEYWDS 2 DEFENSIN, HBD1, ANTIBIOTIC
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR D.J.SCHIBLI,H.N.HUNTER,V.ASEYEV,T.D.STARNER,J.M.WIENCEK,P.B.MCCRAY
AUTHOR 2 JR.,B.F.TACK,H.J.VOGEL
REVDAT 3 23-FEB-22 1KJ5 1 REMARK
REVDAT 2 24-FEB-09 1KJ5 1 VERSN
REVDAT 1 20-MAR-02 1KJ5 0
JRNL AUTH D.J.SCHIBLI,H.N.HUNTER,V.ASEYEV,T.D.STARNER,J.M.WIENCEK,
JRNL AUTH 2 P.B.MCCRAY JR.,B.F.TACK,H.J.VOGEL
JRNL TITL THE SOLUTION STRUCTURES OF THE HUMAN BETA-DEFENSINS LEAD TO
JRNL TITL 2 A BETTER UNDERSTANDING OF THE POTENT BACTERICIDAL ACTIVITY
JRNL TITL 3 OF HBD3 AGAINST STAPHYLOCOCCUS AUREUS.
JRNL REF J.BIOL.CHEM. V. 277 8279 2002
JRNL REFN ISSN 0021-9258
JRNL PMID 11741980
JRNL DOI 10.1074/JBC.M108830200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CNS 1.0, ARIA 1.0
REMARK 3 AUTHORS : BRUKER (XWINNMR), A.T.BRUNGER, P.D.ADAMS,
REMARK 3 G.M.CLORE, W.L.DELANO, P.GROS, R.W.GROSSE-
REMARK 3 KUNSTLEVE, J.-S.JIANG, J.KUSZEWSKI, M.NILGES,
REMARK 3 N.S.PANNU, R.J.READ, L.M.RICE, T.SIMONSON,
REMARK 3 G.L.WARREN (CNS), J.LINGE, S.O'DONOGHUE, M.NILGES
REMARK 3 (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1KJ5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-DEC-01.
REMARK 100 THE DEPOSITION ID IS D_1000015007.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 3.79
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.5 MM HBD1; 0.5 MM HBD1
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 2D COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 1.8, NMRVIEW 4.1.3
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING, MOLECULAR DYNAMICS
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: 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: 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 ASN A 4 86.08 -66.57
REMARK 500 1 CYS A 5 -74.32 -106.86
REMARK 500 1 PRO A 18 -78.94 -77.06
REMARK 500 1 ILE A 19 -172.10 -56.63
REMARK 500 1 PHE A 20 41.41 -77.94
REMARK 500 1 CYS A 27 -95.39 -83.87
REMARK 500 1 TYR A 28 -156.61 -61.51
REMARK 500 2 CYS A 5 -70.00 -98.30
REMARK 500 2 PRO A 18 -75.39 -91.01
REMARK 500 2 ILE A 19 -176.47 -56.02
REMARK 500 2 PHE A 20 32.15 -74.88
REMARK 500 2 THR A 21 -152.82 -78.86
REMARK 500 2 LYS A 22 94.07 -165.17
REMARK 500 2 CYS A 27 -85.48 -89.64
REMARK 500 2 TYR A 28 -158.23 -61.37
REMARK 500 3 ASN A 4 84.36 -66.11
REMARK 500 3 CYS A 5 -69.21 -102.26
REMARK 500 3 PRO A 18 -70.04 -81.49
REMARK 500 3 ILE A 19 -173.24 -56.59
REMARK 500 3 PHE A 20 25.91 -74.51
REMARK 500 3 THR A 21 -163.04 -76.74
REMARK 500 3 LYS A 22 108.23 -163.60
REMARK 500 3 CYS A 27 -91.30 -83.44
REMARK 500 3 TYR A 28 -156.18 -61.49
REMARK 500 4 ASN A 4 85.63 -68.91
REMARK 500 4 CYS A 5 -79.05 -109.53
REMARK 500 4 PRO A 18 -79.98 -90.80
REMARK 500 4 ILE A 19 -168.30 -56.60
REMARK 500 4 PHE A 20 33.97 -75.69
REMARK 500 4 CYS A 27 -78.06 -95.27
REMARK 500 4 TYR A 28 -164.65 -60.94
REMARK 500 5 PRO A 18 -83.30 -76.43
REMARK 500 5 ILE A 19 -171.18 -56.53
REMARK 500 5 PHE A 20 15.48 -69.96
REMARK 500 5 THR A 21 -172.71 -63.15
REMARK 500 5 CYS A 27 -78.47 -94.37
REMARK 500 5 TYR A 28 -176.92 -60.12
REMARK 500 6 CYS A 5 -72.43 -102.54
REMARK 500 6 PRO A 18 -73.34 -89.75
REMARK 500 6 ILE A 19 -173.45 -56.47
REMARK 500 6 PHE A 20 40.03 -78.10
REMARK 500 6 CYS A 27 -92.71 -93.18
REMARK 500 6 TYR A 28 -160.49 -61.24
REMARK 500 7 PRO A 18 -80.70 -79.05
REMARK 500 7 ILE A 19 -170.34 -56.56
REMARK 500 7 PHE A 20 35.56 -76.00
REMARK 500 7 GLN A 24 -66.98 -107.75
REMARK 500 7 CYS A 27 -84.52 -100.56
REMARK 500 7 TYR A 28 -160.52 -61.12
REMARK 500 8 HIS A 2 96.08 -60.24
REMARK 500
REMARK 500 THIS ENTRY HAS 145 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KJ6 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF HUMAN BETA-DEFENSIN 3
DBREF 1KJ5 A 1 36 UNP P60022 BD01_HUMAN 33 68
SEQRES 1 A 36 ASP HIS TYR ASN CYS VAL SER SER GLY GLY GLN CYS LEU
SEQRES 2 A 36 TYR SER ALA CYS PRO ILE PHE THR LYS ILE GLN GLY THR
SEQRES 3 A 36 CYS TYR ARG GLY LYS ALA LYS CYS CYS LYS
SHEET 1 A 3 GLN A 11 LEU A 13 0
SHEET 2 A 3 LYS A 33 CYS A 35 -1 O LYS A 33 N LEU A 13
SHEET 3 A 3 ILE A 23 THR A 26 -1 N GLY A 25 O CYS A 34
SSBOND 1 CYS A 5 CYS A 34 1555 1555 2.03
SSBOND 2 CYS A 12 CYS A 27 1555 1555 2.03
SSBOND 3 CYS A 17 CYS A 35 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 - 23 20 Bytes