Header list of 1id7.pdb file
Complete list - 23 202 Bytes
HEADER ANTIVIRAL PROTEIN 04-APR-01 1ID7
TITLE SOLUTION STRUCTURE OF SYR6
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SYR6;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: CHEMICALLY SYNTHESIZED
KEYWDS SYR6, ANTIVIRAL PROTEIN
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR A.SATO,K.KAWAGUCHI,K.KIMURA,R.TANIMURA,S.SONE
REVDAT 4 23-FEB-22 1ID7 1 REMARK
REVDAT 3 24-FEB-09 1ID7 1 VERSN
REVDAT 2 25-DEC-02 1ID7 1 REMARK
REVDAT 1 10-APR-02 1ID7 0
JRNL AUTH A.SATO,K.KAWAGUCHI,K.KIMURA,R.TANIMURA,S.SONE
JRNL TITL A PEPTIDE MIMETIC OF IFN, THE FIRST PROOF OF A SMALL
JRNL TITL 2 PEPTIDIC AGONIST FOR HETERODIMERIC CYTOKINE RECEPTOR
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : EMBOSS 5.0, EMBOSS 5.0
REMARK 3 AUTHORS : MORIKAWA, S. ET. AL. (EMBOSS), MORIKAWA, S. ET.
REMARK 3 AL. (EMBOSS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE AVERAGE STRUCTURE OF THE 11 STRUCTURES THAT ARE BASED ON 66
REMARK 3 NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS.
REMARK 4
REMARK 4 1ID7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-APR-01.
REMARK 100 THE DEPOSITION ID IS D_1000013177.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2.0MM SYR6; DEUTERATED DIMETHYL
REMARK 210 SULFOXIDE 100%
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; TOCSY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : 4D SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 750
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : AVERAGE STRUCTURE OF THE 11
REMARK 210 STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 RES C SSSEQI
REMARK 465 SER A 1
REMARK 465 LEU A 14
REMARK 465 TYR A 15
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 GLN A 3 -38.54 -136.05
REMARK 500 ALA A 4 -177.09 58.58
REMARK 500 ARG A 5 37.81 34.15
REMARK 500 TRP A 6 -150.46 -145.62
REMARK 500 GLU A 7 -35.46 -36.87
REMARK 500 ALA A 8 -82.21 -156.57
REMARK 500 ALA A 9 145.15 164.58
REMARK 500 PHE A 10 -88.31 -124.56
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ALA A 4 -13.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ID6 RELATED DB: PDB
REMARK 900 1ID6 CONTAINS THE ORIGNINAL 11 STRUCTURES WHICH WERE USED FOR
REMARK 900 CALCULATION OF THIS AVERAGE STRUCTURE.
DBREF 1ID7 A 1 15 GB 15076606 BAB62415 1 15
SEQRES 1 A 15 SER VAL GLN ALA ARG TRP GLU ALA ALA PHE ASP LEU ASP
SEQRES 2 A 15 LEU TYR
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
Complete list - 23 202 Bytes