Header list of 1y04.pdb file
Complete list - 2 20 Bytes
HEADER ANTIFREEZE PROTEIN 14-NOV-04 1Y04
TITLE SOLUTION STRUCTURE OF A RECOMBINANT TYPE I SCULPIN ANTIFREEZE PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANTIFREEZE PEPTIDE SS-3;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: RSS3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYOXOCEPHALUS SCORPIUS;
SOURCE 3 ORGANISM_COMMON: SHORTHORN SCULPIN;
SOURCE 4 ORGANISM_TAXID: 8097;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX-2T
KEYWDS TYPE I ANTIFREEZE PROTEIN, SCULPIN, NMR SPECTROSCOPY, SOLUTION
KEYWDS 2 STRUCTURE, A-HELIX, ANTIFREEZE PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.H.Y.KWAN,K.FAIRLEY,P.I.ANDERBERG,C.W.LIEW,M.M.HARDING,J.P.MACKAY
REVDAT 3 02-MAR-22 1Y04 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1Y04 1 VERSN
REVDAT 1 15-MAR-05 1Y04 0
JRNL AUTH A.H.Y.KWAN,K.FAIRLEY,P.I.ANDERBERG,C.W.LIEW,M.M.HARDING,
JRNL AUTH 2 J.P.MACKAY
JRNL TITL SOLUTION STRUCTURE OF A RECOMBINANT TYPE I SCULPIN
JRNL TITL 2 ANTIFREEZE PROTEIN
JRNL REF BIOCHEMISTRY V. 44 1980 2005
JRNL REFN ISSN 0006-2960
JRNL PMID 15697223
JRNL DOI 10.1021/BI047782J
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.5, ARIA 1.2
REMARK 3 AUTHORS : BRUKER (XWINNMR), LINGE ET AL (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURE CALCULATIONS WERE PERFORMED
REMARK 3 USING THE PACKAGE ARIA 1.2. FINAL STUCTURES ARE BASED ON 452
REMARK 3 UNAMBIGUOUS RESTRAINTS, 31 SETS OF AMBIGUOUS RESTRAINTS AND 52
REMARK 3 DIHEDRAL ANGLE RESTRAINTS.
REMARK 4
REMARK 4 1Y04 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-NOV-04.
REMARK 100 THE DEPOSITION ID IS D_1000030947.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 268
REMARK 210 PH : 5.0
REMARK 210 IONIC STRENGTH : LOW
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM RSS3; PH ADJUSTED TO 5.0
REMARK 210 USING NAOH.; 1MM RSS3 U-15N,13C;
REMARK 210 PH ADJUSTED TO 5.0 USING NAOH
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; 2D NOESY; DQF-COSY;
REMARK 210 HNHA; HNCA; HNCACB; CBCA(CO)NH;
REMARK 210 HNCO; HNCA-ECOSY; HET-NOE
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.3.13, SPARKY 3, ARIA 1.2
REMARK 210 METHOD USED : SIMULATED ANNEALING, MOLECULAR
REMARK 210 DYNAMICS, TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 500
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: THE STRUCTURE WAS DETERMINED USING STANDARD TRIPLE
REMARK 210 -RESONANCE NMR SPECTROSCOPY.
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 2 ALA A 32 46.49 -94.13
REMARK 500 3 ALA A 32 60.54 -100.54
REMARK 500 4 MET A 3 105.85 73.78
REMARK 500 5 SER A 2 -152.24 59.09
REMARK 500 5 MET A 3 47.43 -106.69
REMARK 500 7 SER A 2 49.60 -94.17
REMARK 500 7 ALA A 32 49.17 -87.08
REMARK 500 9 SER A 2 58.78 -102.88
REMARK 500 10 ALA A 32 40.26 -84.90
REMARK 500 11 ALA A 32 50.13 -100.37
REMARK 500 12 ALA A 34 33.34 -97.85
REMARK 500 13 MET A 3 51.36 -119.47
REMARK 500 14 ALA A 33 95.19 -58.22
REMARK 500 16 ALA A 34 45.37 -99.49
REMARK 500 18 ALA A 34 50.26 71.77
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1Y03 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN AT 278 K
REMARK 900 RELATED ID: 1WFA RELATED DB: PDB
REMARK 900 TYPE 1 ANTIFREEZE PROTEIN FROM WINTER FLOUNDER (4 DEGREES C)
REMARK 900 RELATED ID: 1WFB RELATED DB: PDB
REMARK 900 TYPE 1 ANTIFREEZE PROTEIN FROM WINTER FLOUNDER (-180 DEGREES C)
DBREF 1Y04 A 3 35 UNP P04367 ANP3_MYOSC 1 33
SEQADV 1Y04 GLY A 1 UNP P04367 CLONING ARTIFACT
SEQADV 1Y04 SER A 2 UNP P04367 CLONING ARTIFACT
SEQRES 1 A 35 GLY SER MET ASN ALA PRO ALA ARG ALA ALA ALA LYS THR
SEQRES 2 A 35 ALA ALA ASP ALA LEU ALA ALA ALA LYS LYS THR ALA ALA
SEQRES 3 A 35 ASP ALA ALA ALA ALA ALA ALA ALA ALA
HELIX 1 1 ASN A 4 ALA A 11 1 8
HELIX 2 2 ALA A 11 ALA A 34 1 24
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