Header list of 1i8x.pdb file
Complete list - 27 20 Bytes
HEADER CYTOKINE 16-MAR-01 1I8X
TITLE SEMI-AUTOMATIC STRUCTURE DETERMINATION OF THE CG1 1-30 PEPTIDE BASED
TITLE 2 ON ARIA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GRANULIN-1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINUS (RESIDUES 1-30);
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED BY SOLID PHASE
SOURCE 4 SYNTHESIS. THE SEQUENCE OF THE PEPTIDE IS NATURALLY FOUND IN
SOURCE 5 CYPRINUS CARPIO (CARP).
KEYWDS TWO BETA-HAIRPIN STACK, CYTOKINE
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR W.F.VRANKEN,S.JAMES,H.P.J.BENNETT,F.NI
REVDAT 4 27-OCT-21 1I8X 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1I8X 1 VERSN
REVDAT 2 01-APR-03 1I8X 1 JRNL
REVDAT 1 17-APR-02 1I8X 0
JRNL AUTH W.F.VRANKEN,S.JAMES,H.P.BENNETT,F.NI
JRNL TITL SOLUTION STRUCTURES OF A 30-RESIDUE AMINO-TERMINAL DOMAIN OF
JRNL TITL 2 THE CARP GRANULIN-1 PROTEIN AND ITS AMINO-TERMINALLY
JRNL TITL 3 TRUNCATED 3-30 SUBFRAGMENT: IMPLICATIONS FOR THE
JRNL TITL 4 CONFORMATIONAL STABILITY OF THE STACK OF TWO BETA-HAIRPINS.
JRNL REF PROTEINS V. 47 14 2002
JRNL REFN ISSN 0887-3585
JRNL PMID 11870861
JRNL DOI 10.1002/PROT.10077.ABS
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.1, ARIA 1.0
REMARK 3 AUTHORS : BRUKER (XWINNMR), LINGE (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 NO NOE PEAKS WERE MANUALLY ASSIGNED - CALCULATION
REMARK 3 IS BASED ON INITIAL NOE PEAK LISTS AND CHEMICAL
REMARK 3 SHIFT ASSIGNMENTS COMBINED WITH AMBIGUOUS RESTRAINTS
REMARK 3 USED IN ARIA.
REMARK 4
REMARK 4 1I8X COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-MAR-01.
REMARK 100 THE DEPOSITION ID IS D_1000013052.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 288
REMARK 210 PH : 4.5
REMARK 210 IONIC STRENGTH : 0.02
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : ACETATE BUFFER; ACETATE BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SEMI-AUTOMATED CALCULATION BASED
REMARK 210 ON A SET OF ARIA RUNS.
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
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: 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: 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 CYS A 4 -90.13 58.81
REMARK 500 1 ASP A 12 104.13 -59.52
REMARK 500 2 ALA A 7 -51.76 -124.03
REMARK 500 2 PRO A 20 -8.06 -59.31
REMARK 500 3 PRO A 20 -4.80 -58.36
REMARK 500 4 ALA A 6 15.76 58.40
REMARK 500 4 THR A 8 86.75 53.37
REMARK 500 4 ASP A 12 104.27 -59.65
REMARK 500 5 HIS A 3 -33.60 -133.90
REMARK 500 5 CYS A 4 -94.05 55.51
REMARK 500 5 ASP A 5 30.71 -94.37
REMARK 500 5 THR A 8 87.29 55.64
REMARK 500 6 HIS A 3 -64.21 -137.25
REMARK 500 6 CYS A 4 -86.40 60.93
REMARK 500 6 PRO A 20 -6.43 -59.45
REMARK 500 7 ASP A 5 18.19 59.98
REMARK 500 7 PRO A 20 -8.36 -56.62
REMARK 500 8 CYS A 4 -90.84 58.80
REMARK 500 8 ALA A 6 16.76 58.23
REMARK 500 8 ASP A 12 99.96 -55.43
REMARK 500 9 CYS A 4 -84.35 63.54
REMARK 500 9 ALA A 7 -31.46 -137.27
REMARK 500 9 ASP A 12 138.14 69.65
REMARK 500 10 CYS A 4 -87.10 60.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QGM RELATED DB: PDB
REMARK 900 1QGM IS THE SAME MOLECULE WITH A DIFFERENT STRUCTURE CALCULATION
REMARK 900 METHOD
REMARK 900 RELATED ID: 4351 RELATED DB: BMRB
REMARK 900 4351 IS NMR DATA FOR MOLECULE
DBREF 1I8X A 1 30 UNP P81013 GRN1_CYPCA 1 30
SEQADV 1I8X SER A 17 UNP P81013 CYS 17 ENGINEERED MUTATION
SEQADV 1I8X SER A 27 UNP P81013 CYS 27 ENGINEERED MUTATION
SEQRES 1 A 30 VAL ILE HIS CYS ASP ALA ALA THR ILE CYS PRO ASP GLY
SEQRES 2 A 30 THR THR CYS SER LEU SER PRO TYR GLY VAL TRP TYR CYS
SEQRES 3 A 30 SER PRO PHE SER
SHEET 1 A 2 THR A 14 LEU A 18 0
SHEET 2 A 2 TRP A 24 PRO A 28 -1 N TYR A 25 O SER A 17
SSBOND 1 CYS A 4 CYS A 16 1555 1555 2.03
SSBOND 2 CYS A 10 CYS A 26 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 - 27 20 Bytes