Header list of 2gd3.pdb file
Complete list - 20 20 Bytes
HEADER UNKNOWN FUNCTION 15-MAR-06 2GD3
TITLE NMR STRUCTURE OF S14G-HUMANIN IN 30% TFE SOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HUMANIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: S14G-HUMANIN WAS PREPARED BY FMOC-SOLID PHASE
SOURCE 4 SYNTHESIS ON O-CL-TRITYL-AMIDOMETHYL POLYSTYRENE RESIN (EVANGELOU,
SOURCE 5 A., ZIKOS, C., LIVANIOU, E., EVANGELATOS, G.P. "HIGHYIELD, SOLID-
SOURCE 6 PHASE SYNTHESIS OF HUMANIN, AN ALZHEIMER'S DISEASE ASSOCIATED, NOVEL
SOURCE 7 24-MER PEPTIDE WHICH CONTAINS A DIFFICULT SEQUENCE" J. PEPTIDE SCI.
SOURCE 8 2004, 10, 631 635). THE PEPTIDE WAS PURIFIED TO 95% WITH SEMI-
SOURCE 9 PREPARATIVE RP-HPLC AND SUITABLY CHARACTERIZED. THE SEQUENCE IS
SOURCE 10 NATURALLY FOUND IN HOMO SAPIENS (HUMAN).
KEYWDS S14G-HUMANIN; HUMANIN; ALZHEIMER'S DISEASE; NEUROPROTECTION; NMR; CD,
KEYWDS 2 UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 14
AUTHOR D.BENAKI,C.ZIKOS,A.EVANGELOU,E.LIVANIOU,M.VLASSI,E.MIKROS,M.PELECANOU
REVDAT 4 20-OCT-21 2GD3 1 REMARK SEQADV
REVDAT 3 24-FEB-09 2GD3 1 VERSN
REVDAT 2 03-OCT-06 2GD3 1 JRNL
REVDAT 1 19-SEP-06 2GD3 0
JRNL AUTH D.BENAKI,C.ZIKOS,A.EVANGELOU,E.LIVANIOU,M.VLASSI,E.MIKROS,
JRNL AUTH 2 M.PELECANOU
JRNL TITL SOLUTION STRUCTURE OF SER14GLY-HUMANIN, A POTENT RESCUE
JRNL TITL 2 FACTOR AGAINST NEURONAL CELL DEATH IN ALZHEIMER'S DISEASE.
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 349 634 2006
JRNL REFN ISSN 0006-291X
JRNL PMID 16945331
JRNL DOI 10.1016/J.BBRC.2006.08.087
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.BENAKI,C.ZIKOS,A.EVANGELOU,E.LIVANIOU,M.VLASSI,E.MIKROS,
REMARK 1 AUTH 2 M.PELECANOU
REMARK 1 TITL SOLUTION STRUCTURE OF HUMANIN, A PEPTIDE AGAINST ALZHEIMER'S
REMARK 1 TITL 2 DISEASE-RELATED NEUROTOXICITY.
REMARK 1 REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 329 152 2005
REMARK 1 REFN ISSN 0006-291X
REMARK 1 PMID 15721287
REMARK 1 DOI 10.1016/J.BBRC.2005.01.100
REMARK 1 REFERENCE 2
REMARK 1 AUTH Y.HASHIMOTO,T.NIIKURA,H.TAJIMA,T.YASUKAWA,H.SUDO,Y.ITO,
REMARK 1 AUTH 2 Y.KITA,M.KAWASUMI,K.KOUYAMA,M.DOYU,G.SOBUE,T.KOIDE,S.TSUJI,
REMARK 1 AUTH 3 J.LANG,K.KUROKAWA,I.NISHIMOTO
REMARK 1 TITL A RESCUE FACTOR ABOLISHING NEURONAL CELL DEATH BY A WIDE
REMARK 1 TITL 2 SPECTRUM OF FAMILIAL ALZHEIMER'S DISEASE GENES AND ABETA.
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 98 6336 2001
REMARK 1 REFN ISSN 0027-8424
REMARK 1 PMID 11371646
REMARK 1 DOI 10.1073/PNAS.101133498
REMARK 1 REFERENCE 3
REMARK 1 AUTH Y.HASHIMOTO,Y.ITO,T.NIIKURA,Z.SHAO,M.HATA,F.OYAMA,
REMARK 1 AUTH 2 I.NISHIMOTO
REMARK 1 TITL MECHANISMS OF NEUROPROTECTION BY A NOVEL RESCUE FACTOR
REMARK 1 TITL 2 HUMANIN FROM SWEDISH MUTANT AMYLOID PRECURSOR PROTEIN
REMARK 1 REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 283 460 2001
REMARK 1 REFN ISSN 0006-291X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CNS 1.1
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER, A.T. (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STARTING FROM AN EXTENDED STRUCTURE A
REMARK 3 TOTAL OF 300 STRUCTURES WERE GENERATED FROM 133 NOE-DERIVED
REMARK 3 DISTANCE RESTRAINTS AND 2 DISTANCE RESTRAINTS BASED ON
REMARK 3 TEMPERATURE COEFFICIENT DATA USING THE SIMULATED ANNEALING AND
REMARK 3 ENERGY MINIMIZATION PROTOCOL IN THE PROGRAM CNS, VERSION 1.1
REMARK 4
REMARK 4 2GD3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-MAR-06.
REMARK 100 THE DEPOSITION ID IS D_1000036971.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 280
REMARK 210 PH : 2.7; 2.7
REMARK 210 IONIC STRENGTH : 60 MICROM NAN3; 60 MICROM NAN3
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.3 MM S14G-HUMANIN; 60 MICROM
REMARK 210 NAN3 TO PREVENT MICROBIAL GROWTH;
REMARK 210 H2O/TFE-D3 7:3; PH 2.6
REMARK 210 (UNCORRECTED FOR THE PRESENCE OF
REMARK 210 TFE); AT 298 AND 280 K
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.6, SPARKY 3, CNS 1.1
REMARK 210 METHOD USED : SIMULATED ANNEALING TORSION
REMARK 210 ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 300
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 14
REMARK 210 CONFORMERS, SELECTION CRITERIA : 14 CONVERGENT CONFORMERS ARE
REMARK 210 PRESENTED HAVING THE LOWEST
REMARK 210 ENERGY AND THE BEST STRUCTURAL
REMARK 210 QUALITY IN RAMACHADRAN PLOT
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: 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 PRO A 3 -166.98 -70.62
REMARK 500 1 GLU A 15 -67.63 -132.94
REMARK 500 1 ILE A 16 31.23 -99.13
REMARK 500 2 ALA A 2 90.17 -175.80
REMARK 500 2 PRO A 3 -168.08 -70.96
REMARK 500 2 LEU A 18 83.23 -150.72
REMARK 500 3 LYS A 21 -47.10 -135.26
REMARK 500 3 ARG A 23 36.03 -99.47
REMARK 500 4 ASP A 17 42.13 -96.63
REMARK 500 5 ASP A 17 38.79 -142.49
REMARK 500 5 LEU A 18 77.87 -119.11
REMARK 500 5 ARG A 22 88.91 -60.40
REMARK 500 6 THR A 13 49.31 -90.39
REMARK 500 6 LYS A 21 -167.10 -123.80
REMARK 500 7 PRO A 3 -167.91 -70.76
REMARK 500 7 ARG A 4 -80.02 -119.07
REMARK 500 7 ILE A 16 45.19 -92.91
REMARK 500 7 VAL A 20 31.00 -98.13
REMARK 500 7 ARG A 23 -46.11 -130.59
REMARK 500 8 ALA A 2 108.27 -175.29
REMARK 500 8 PRO A 3 -164.09 -65.15
REMARK 500 8 ARG A 4 -71.51 -59.80
REMARK 500 8 GLU A 15 -46.23 -130.36
REMARK 500 8 VAL A 20 31.48 -98.63
REMARK 500 9 ILE A 16 44.17 -95.11
REMARK 500 9 LEU A 18 77.99 -150.41
REMARK 500 9 VAL A 20 82.79 -157.26
REMARK 500 10 ASP A 17 43.84 -95.47
REMARK 500 10 LEU A 18 77.98 -109.12
REMARK 500 10 LYS A 21 91.32 -67.15
REMARK 500 11 ALA A 2 79.66 -151.86
REMARK 500 11 PRO A 3 -164.06 -66.09
REMARK 500 11 ARG A 4 -74.36 -59.93
REMARK 500 11 THR A 13 -72.10 -60.95
REMARK 500 11 ARG A 22 31.42 -150.76
REMARK 500 12 PRO A 3 -166.12 -69.78
REMARK 500 12 PRO A 19 83.94 -68.51
REMARK 500 13 PRO A 3 -168.24 -71.29
REMARK 500 13 ARG A 4 -67.07 -127.92
REMARK 500 14 PRO A 3 -167.70 -71.08
REMARK 500 14 LEU A 18 82.51 -160.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1Y32 RELATED DB: PDB
REMARK 900 THE SOLUTION STRUCTURE IN 30% TFE OF THE PARENT PEPTIDE, HUMANIN,
REMARK 900 WHICH HAS A SER IN THE PLACE OF GLY14
DBREF 2GD3 A 1 24 UNP Q8IVG9 HUNIN_HUMAN 1 24
SEQADV 2GD3 GLY A 14 UNP Q8IVG9 SER 14 ENGINEERED MUTATION
SEQRES 1 A 24 MET ALA PRO ARG GLY PHE SER CYS LEU LEU LEU LEU THR
SEQRES 2 A 24 GLY GLU ILE ASP LEU PRO VAL LYS ARG ARG ALA
HELIX 1 1 PRO A 3 GLY A 14 1 12
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 - 20 20 Bytes