Header list of 1e4r.pdb file
Complete list - 20 20 Bytes
HEADER DEFENSIN 12-JUL-00 1E4R
TITLE SOLUTION STRUCTURE OF THE MOUSE DEFENSIN MBD-8
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-DEFENSIN 8;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MBD-8,DEFENSIN,BETA 8,DEFENSIN-RELATED PEPTIDE,DEFR1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 4 ORGANISM_COMMON: MOUSE;
SOURCE 5 ORGANISM_TAXID: 10090
KEYWDS DEFENSIN, MOUSE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR F.BAUER,K.SCHWEIMER,E.KLUVER,K.ADERMANN,W.G.FORSSMANN,P.ROESCH,
AUTHOR 2 H.STICHT
REVDAT 5 20-JUN-18 1E4R 1 COMPND SOURCE JRNL DBREF
REVDAT 4 24-FEB-09 1E4R 1 VERSN
REVDAT 3 26-NOV-01 1E4R 1 REVDAT JRNL
REVDAT 2 23-AUG-01 1E4R 1 TITLE COMPND REMARK DBREF
REVDAT 1 12-JUL-01 1E4R 0
JRNL AUTH F.BAUER,K.SCHWEIMER,E.KLUVER,J.R.CONEJO-GARCIA,
JRNL AUTH 2 W.G.FORSSMANN,P.ROSCH,K.ADERMANN,H.STICHT
JRNL TITL STRUCTURE DETERMINATION OF HUMAN AND MURINE BETA-DEFENSINS
JRNL TITL 2 REVEALS STRUCTURAL CONSERVATION IN THE ABSENCE OF
JRNL TITL 3 SIGNIFICANT SEQUENCE SIMILARITY.
JRNL REF PROTEIN SCI. V. 10 2470 2001
JRNL REFN ISSN 0961-8368
JRNL PMID 11714914
JRNL DOI 10.1110/PS.24401
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE.
REMARK 4
REMARK 4 1E4R COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-JUL-00.
REMARK 100 THE DEPOSITION ID IS D_1290005055.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 4.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : COSY; TOCSY; NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 400 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NDEE, X-PLOR
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 60
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY, LEAST RESTRAINT
REMARK 210 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 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
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 VAL A 4 173.67 56.00
REMARK 500 2 VAL A 4 173.49 51.69
REMARK 500 6 VAL A 4 -161.55 38.50
REMARK 500 6 ILE A 7 -28.16 -175.06
REMARK 500 7 PRO A 3 -155.26 -76.24
REMARK 500 10 PRO A 3 -155.18 -73.55
REMARK 500 14 PRO A 3 -154.71 -78.64
REMARK 500 17 PRO A 3 -156.41 -78.16
REMARK 500 17 HIS A 22 37.01 -99.77
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 8 0.10 SIDE CHAIN
REMARK 500 1 ARG A 16 0.30 SIDE CHAIN
REMARK 500 1 ARG A 21 0.20 SIDE CHAIN
REMARK 500 2 ARG A 8 0.30 SIDE CHAIN
REMARK 500 2 ARG A 16 0.27 SIDE CHAIN
REMARK 500 2 ARG A 21 0.14 SIDE CHAIN
REMARK 500 3 ARG A 8 0.15 SIDE CHAIN
REMARK 500 3 ARG A 16 0.19 SIDE CHAIN
REMARK 500 3 ARG A 21 0.31 SIDE CHAIN
REMARK 500 4 ARG A 8 0.11 SIDE CHAIN
REMARK 500 4 ARG A 16 0.20 SIDE CHAIN
REMARK 500 4 ARG A 21 0.25 SIDE CHAIN
REMARK 500 5 ARG A 8 0.26 SIDE CHAIN
REMARK 500 5 ARG A 16 0.32 SIDE CHAIN
REMARK 500 5 ARG A 21 0.27 SIDE CHAIN
REMARK 500 6 ARG A 8 0.21 SIDE CHAIN
REMARK 500 6 ARG A 16 0.17 SIDE CHAIN
REMARK 500 6 ARG A 21 0.27 SIDE CHAIN
REMARK 500 7 ARG A 8 0.11 SIDE CHAIN
REMARK 500 7 ARG A 16 0.30 SIDE CHAIN
REMARK 500 7 ARG A 21 0.22 SIDE CHAIN
REMARK 500 8 ARG A 8 0.29 SIDE CHAIN
REMARK 500 8 ARG A 16 0.27 SIDE CHAIN
REMARK 500 8 ARG A 21 0.20 SIDE CHAIN
REMARK 500 9 ARG A 8 0.09 SIDE CHAIN
REMARK 500 9 ARG A 16 0.16 SIDE CHAIN
REMARK 500 9 ARG A 21 0.27 SIDE CHAIN
REMARK 500 10 ARG A 8 0.31 SIDE CHAIN
REMARK 500 10 ARG A 16 0.32 SIDE CHAIN
REMARK 500 10 ARG A 21 0.30 SIDE CHAIN
REMARK 500 11 ARG A 8 0.28 SIDE CHAIN
REMARK 500 11 ARG A 16 0.32 SIDE CHAIN
REMARK 500 11 ARG A 21 0.32 SIDE CHAIN
REMARK 500 12 ARG A 8 0.31 SIDE CHAIN
REMARK 500 12 ARG A 16 0.26 SIDE CHAIN
REMARK 500 12 ARG A 21 0.32 SIDE CHAIN
REMARK 500 13 ARG A 8 0.31 SIDE CHAIN
REMARK 500 13 ARG A 16 0.29 SIDE CHAIN
REMARK 500 13 ARG A 21 0.25 SIDE CHAIN
REMARK 500 14 ARG A 8 0.32 SIDE CHAIN
REMARK 500 14 ARG A 21 0.16 SIDE CHAIN
REMARK 500 15 ARG A 8 0.28 SIDE CHAIN
REMARK 500 15 ARG A 16 0.26 SIDE CHAIN
REMARK 500 15 ARG A 21 0.32 SIDE CHAIN
REMARK 500 16 ARG A 8 0.13 SIDE CHAIN
REMARK 500 16 ARG A 16 0.11 SIDE CHAIN
REMARK 500 16 ARG A 21 0.31 SIDE CHAIN
REMARK 500 17 ARG A 8 0.23 SIDE CHAIN
REMARK 500 17 ARG A 16 0.17 SIDE CHAIN
REMARK 500 17 ARG A 21 0.31 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 57 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1E4R A 1 35 UNP Q91V82 DEFB8_MOUSE 26 60
SEQRES 1 A 35 ASN GLU PRO VAL SER CYS ILE ARG ASN GLY GLY ILE CYS
SEQRES 2 A 35 GLN TYR ARG CYS ILE GLY LEU ARG HIS LYS ILE GLY THR
SEQRES 3 A 35 CYS GLY SER PRO PHE LYS CYS CYS LYS
HELIX 1 1 SER A 5 GLY A 10 5 6
SHEET 1 A 2 ILE A 12 GLN A 14 0
SHEET 2 A 2 LYS A 32 CYS A 34 -1 N CYS A 34 O ILE A 12
SHEET 3 A 2 HIS A 22 THR A 26 -1 N GLY A 25 O CYS A 33
SSBOND 1 CYS A 6 CYS A 33 1555 1555 2.02
SSBOND 2 CYS A 13 CYS A 27 1555 1555 2.02
SSBOND 3 CYS A 17 CYS A 34 1555 1555 2.02
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 - 20 20 Bytes