HEADER ANTIBIOTIC 04-MAY-06 2GW9
TITLE HIGH-RESOLUTION SOLUTION STRUCTURE OF THE MOUSE DEFENSIN CRYPTDIN4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DEFENSIN-RELATED CRYPTDIN 4;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CRYPTDIN4;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: DEFCR4;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-CODON-PLUS-RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-28A
KEYWDS TRIPLE STRANDED BETA SHEET, BETA HAIRPIN, ANTIBIOTIC
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.J.ROSENGREN,D.J.CRAIK,H.J.VOGEL,N.L.DALY,A.J.OUELLETTE
REVDAT 4 09-MAR-22 2GW9 1 REMARK
REVDAT 3 24-FEB-09 2GW9 1 VERSN
REVDAT 2 10-OCT-06 2GW9 1 JRNL
REVDAT 1 25-JUL-06 2GW9 0
JRNL AUTH K.J.ROSENGREN,N.L.DALY,L.M.FORNANDER,Y.SHIRAFUJI,X.QU,
JRNL AUTH 2 H.J.VOGEL,A.J.OUELLETTE,D.J.CRAIK
JRNL TITL STRUCTURAL AND FUNCTIONAL CHARACTERIZATION OF THE CONSERVED
JRNL TITL 2 SALT BRIDGE IN MAMMALIAN PANETH CELL ALPHA-DEFENSINS:
JRNL TITL 3 SOLUTION STRUCTURES OF MOUSE CRYPTDIN-4 AND
JRNL TITL 4 (E15D)-CRYPTDIN-4.
JRNL REF J.BIOL.CHEM. V. 281 28068 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16857681
JRNL DOI 10.1074/JBC.M604992200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 1.3.5, CNS 1.0
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER, A.T. ET AL. (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2GW9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAY-06.
REMARK 100 THE DEPOSITION ID IS D_1000037625.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 288; 293; 298; 303; 308
REMARK 210 PH : 4.6; 4.6; 4.6; 4.6; 4.6
REMARK 210 IONIC STRENGTH : 0; 0; 0; 0; 0
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT;
REMARK 210 AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.5 MM CRYPTDIN4; 90% H2O, 10%
REMARK 210 D2O; 1.5 MM CRYPTDIN4; 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CARA 1.0, CYANA 2.0
REMARK 210 METHOD USED : SIMULATED ANNEALING USING
REMARK 210 TORSION ANGLE DYNAMICS FOLLOWED
REMARK 210 BY REFINEMENT IN EXPLICIT
REMARK 210 SOLVENT USING CARTESIAN DYNAMICS
REMARK 210 WITHIN CNS.
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST 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: 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 HH21 ARG A 7 OE2 GLU A 15 1.59
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 13 70.40 -66.72
REMARK 500 1 ARG A 31 42.40 -86.13
REMARK 500 3 ARG A 13 78.53 -67.93
REMARK 500 3 ILE A 23 99.83 -62.12
REMARK 500 4 LEU A 3 137.55 178.57
REMARK 500 4 PRO A 30 151.77 -45.57
REMARK 500 5 LEU A 2 40.61 -80.69
REMARK 500 5 LEU A 3 133.40 -172.01
REMARK 500 5 ARG A 13 105.34 -48.42
REMARK 500 6 ARG A 13 69.97 -65.87
REMARK 500 7 ARG A 13 105.29 -46.05
REMARK 500 8 LEU A 3 117.56 -167.82
REMARK 500 8 ARG A 13 70.13 -66.00
REMARK 500 9 LEU A 2 38.67 -86.98
REMARK 500 9 LEU A 3 130.89 -176.12
REMARK 500 10 LEU A 3 133.03 179.47
REMARK 500 10 ARG A 13 101.87 -54.09
REMARK 500 11 ARG A 13 92.39 -56.14
REMARK 500 12 LEU A 3 129.31 179.09
REMARK 500 12 ARG A 13 53.86 -69.15
REMARK 500 13 ARG A 13 62.17 -67.63
REMARK 500 14 ARG A 13 69.64 -65.20
REMARK 500 14 ARG A 24 15.44 81.41
REMARK 500 15 ARG A 13 102.24 -50.83
REMARK 500 16 LEU A 3 118.64 178.86
REMARK 500 16 ARG A 13 62.28 -68.48
REMARK 500 17 LEU A 3 54.04 -163.43
REMARK 500 17 ARG A 13 67.29 -67.52
REMARK 500 17 ARG A 31 47.80 -80.65
REMARK 500 18 ARG A 13 75.96 -64.40
REMARK 500 19 LEU A 3 56.35 -159.43
REMARK 500 20 HIS A 10 163.02 179.40
REMARK 500 20 ARG A 13 96.97 -58.21
REMARK 500 20 ILE A 23 108.23 -58.97
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2GW9 A 1 32 UNP P28311 DEF4_MOUSE 61 92
SEQRES 1 A 32 GLY LEU LEU CYS TYR CYS ARG LYS GLY HIS CYS LYS ARG
SEQRES 2 A 32 GLY GLU ARG VAL ARG GLY THR CYS GLY ILE ARG PHE LEU
SEQRES 3 A 32 TYR CYS CYS PRO ARG ARG
SHEET 1 A 3 TYR A 5 LYS A 8 0
SHEET 2 A 3 PHE A 25 PRO A 30 -1 O CYS A 28 N TYR A 5
SHEET 3 A 3 GLU A 15 GLY A 22 -1 N ARG A 18 O TYR A 27
SSBOND 1 CYS A 4 CYS A 29 1555 1555 2.03
SSBOND 2 CYS A 6 CYS A 21 1555 1555 2.03
SSBOND 3 CYS A 11 CYS A 28 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
(ATOM LINES ARE NOT SHOWN.)
END
