Header list of 1tv0.pdb file
Complete list - 2 20 Bytes
HEADER ANTIMICROBIAL PROTEIN 25-JUN-04 1TV0
TITLE SOLUTION STRUCTURE OF CRYPTDIN-4, THE MOST POTENT ALPHA-DEFENSIN FROM
TITLE 2 MOUSE PANETH CELLS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CRYPTDIN-4;
COMPND 3 CHAIN: A;
COMPND 4 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_CELL_LINE: BL21(DE3)-CODON-PLUS-RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET-28A
KEYWDS BETA SHEET, BETA HAIRPIN, ANTIMICROBIAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR W.JING,H.N.HUNTER,H.TANABE,A.J.OUELLETTE,H.J.VOGEL
REVDAT 3 02-MAR-22 1TV0 1 REMARK
REVDAT 2 24-FEB-09 1TV0 1 VERSN
REVDAT 1 04-JAN-05 1TV0 0
JRNL AUTH W.JING,H.N.HUNTER,H.TANABE,A.J.OUELLETTE,H.J.VOGEL
JRNL TITL SOLUTION STRUCTURE OF CRYPTDIN-4, A MOUSE PANETH CELL
JRNL TITL 2 ALPHA-DEFENSIN.
JRNL REF BIOCHEMISTRY V. 43 15759 2004
JRNL REFN ISSN 0006-2960
JRNL PMID 15595831
JRNL DOI 10.1021/BI048645P
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE
REMARK 3 -KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE,
REMARK 3 SIMONSON,WARREN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1TV0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000022925.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 4.2
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 3.2 MG PROTEIN H2O/D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; NOESY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 700 MHZ
REMARK 210 SPECTROMETER MODEL : BRUKER ADVANCE 700
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW 4.1.3, ARIA 1.2
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: BRUCKER MODEL EQUIPPED WITH TRIPPLE RESONANCE PROBE
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 51.04 -100.75
REMARK 500 1 ARG A 13 122.71 -172.48
REMARK 500 1 ILE A 23 -61.78 -91.45
REMARK 500 2 PRO A 30 -170.31 -56.01
REMARK 500 2 ARG A 31 -78.54 -63.22
REMARK 500 3 ARG A 13 120.28 -174.62
REMARK 500 3 ILE A 23 -70.31 -94.26
REMARK 500 4 ARG A 13 115.57 -173.61
REMARK 500 4 THR A 20 164.50 179.50
REMARK 500 4 ILE A 23 -76.88 -64.78
REMARK 500 4 ARG A 31 33.16 -83.97
REMARK 500 5 ARG A 13 132.62 -173.57
REMARK 500 6 ARG A 13 128.71 -171.11
REMARK 500 6 THR A 20 151.25 -44.99
REMARK 500 6 PRO A 30 45.97 -81.08
REMARK 500 7 ARG A 13 47.01 -152.42
REMARK 500 8 LEU A 2 74.60 -101.98
REMARK 500 8 LYS A 12 -86.04 -65.22
REMARK 500 8 PRO A 30 94.09 -64.29
REMARK 500 9 LEU A 2 -167.08 -110.07
REMARK 500 9 LEU A 3 -177.66 -66.48
REMARK 500 9 ARG A 13 115.15 -172.31
REMARK 500 9 ARG A 31 92.79 -66.00
REMARK 500 10 ARG A 13 57.91 -172.37
REMARK 500 10 THR A 20 164.29 179.57
REMARK 500 11 CYS A 4 -177.16 -68.33
REMARK 500 11 ARG A 13 71.57 -176.73
REMARK 500 12 ARG A 13 110.21 -177.58
REMARK 500 12 PRO A 30 -175.05 -56.66
REMARK 500 13 LEU A 2 79.89 -102.72
REMARK 500 13 ILE A 23 -68.56 -90.46
REMARK 500 13 PRO A 30 -179.81 -56.82
REMARK 500 13 ARG A 31 91.04 -64.12
REMARK 500 14 ARG A 13 130.01 -175.55
REMARK 500 14 ILE A 23 -75.01 -82.41
REMARK 500 14 CYS A 29 118.13 -165.63
REMARK 500 15 LEU A 2 89.10 -150.55
REMARK 500 15 LEU A 3 43.81 -148.28
REMARK 500 15 ARG A 13 129.95 -173.74
REMARK 500 15 THR A 20 170.08 179.56
REMARK 500 15 ILE A 23 -71.06 -68.39
REMARK 500 16 THR A 20 158.45 178.96
REMARK 500 16 ILE A 23 -62.56 -92.06
REMARK 500 17 PRO A 30 152.72 -41.84
REMARK 500 18 LYS A 12 -80.75 -64.26
REMARK 500 18 CYS A 29 91.86 -161.47
REMARK 500 19 LEU A 2 47.49 -98.00
REMARK 500 19 LEU A 3 61.01 -114.09
REMARK 500 19 THR A 20 160.41 179.19
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1TV0 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 CYS A 28 -1 O CYS A 28 N TYR A 5
SHEET 3 A 3 GLU A 15 ARG A 16 -1 N ARG A 16 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
Complete list - 2 20 Bytes