Header list of 1yl9.pdb file
Complete list - 2 20 Bytes
HEADER NEUROPEPTIDE 19-JAN-05 1YL9
TITLE 3D SOLUTION STRUCTURE OF [TYR3]OCTREOTATE DERIVATIVES IN DMSO
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: [TYR3]OCTREOTATE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SOMATOSTATIN ANALOGUE;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: SYNTHETIC PEPTIDE WITH A TETRAMINE CHELATOR ATTACHED
SOURCE 4 AT THE N-TERMINAL
KEYWDS SOMATOSTATIN ANALOGUES, SANDOSTATIN, [TYR3]OCTREOTATE, DEMOTATE, NMR
KEYWDS 2 CONFORMATIONAL ANALYSIS, NEUROPEPTIDE
EXPDTA SOLUTION NMR
NUMMDL 21
MDLTYP MINIMIZED AVERAGE
AUTHOR G.A.SPYROULIAS,A.S.GALANIS,C.PETROU,D.VAHLIOTIS,P.SOTIRIOU,
AUTHOR 2 A.NIKOLOPOULOU,B.NOCK,T.MAINA,P.CORDOPATIS
REVDAT 3 02-MAR-22 1YL9 1 REMARK LINK
REVDAT 2 24-FEB-09 1YL9 1 VERSN
REVDAT 1 20-SEP-05 1YL9 0
JRNL AUTH G.A.SPYROULIAS,A.S.GALANIS,C.H.PETROU,D.VAHLIOTIS,
JRNL AUTH 2 P.SOTIRIOU,A.NIKOLOPOULOU,B.NOCK,T.MAINA,P.CORDOPATIS
JRNL TITL 3D SOLUTION STRUCTURE OF [TYR3]OCTREOTATE DERIVATIVES IN
JRNL TITL 2 DMSO: STRUCTURE DIFFERENTIATION OF PEPTIDE CORE DUE TO
JRNL TITL 3 CHELATE GROUP ATTACHMENT AND BIOLOGICALLY ACTIVE
JRNL TITL 4 CONFORMATION.
JRNL REF MED.CHEM. V. 1 487 2005
JRNL REFN ISSN 1573-4064
JRNL PMID 16787334
JRNL DOI 10.2174/1573406054864089
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, AMBER 5.0
REMARK 3 AUTHORS : BRUKER (XWINNMR), PEARLMAN, D.A.; CASE, D.A.;
REMARK 3 CALDWELL, J.W.; ROSS, W.S.; CHEATHAM, T.E.;
REMARK 3 FERGUSON, D.M.; SEIBEL, G.L.; SINGH, U.C.; WEINER,
REMARK 3 P.K.; KOLLMAN, P.A. (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE MODELS ARE CALCULATED USING 155 NOE
REMARK 3 -DERIVED CONSTRAINTS, FROM NOESY SPECTRA ACQUIRED USING 400 MS
REMARK 3 OF MIXING TIME
REMARK 4
REMARK 4 1YL9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-FEB-05.
REMARK 100 THE DEPOSITION ID IS D_1000031645.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2-3MM PEPTIDE; DMSO
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 400 MHZ
REMARK 210 SPECTROMETER MODEL : DPX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.3, DYANA 1.5
REMARK 210 METHOD USED : SIMULATED ANNEALING, TORSION
REMARK 210 ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 400
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
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 CYS A 3 40.28 -104.97
REMARK 500 1 LYS A 6 18.38 58.54
REMARK 500 1 CYS A 8 72.99 24.39
REMARK 500 2 CYS A 3 43.20 -108.25
REMARK 500 2 LYS A 6 18.33 59.33
REMARK 500 3 CYS A 3 43.94 -105.11
REMARK 500 3 LYS A 6 17.26 58.30
REMARK 500 3 CYS A 8 67.52 39.75
REMARK 500 4 CYS A 3 46.67 -108.04
REMARK 500 4 LYS A 6 17.96 57.62
REMARK 500 4 CYS A 8 70.48 41.38
REMARK 500 5 LYS A 6 18.40 58.16
REMARK 500 5 CYS A 8 66.41 35.72
REMARK 500 6 CYS A 3 44.91 -106.97
REMARK 500 6 LYS A 6 17.48 59.60
REMARK 500 6 CYS A 8 60.09 39.99
REMARK 500 7 CYS A 3 43.84 -109.72
REMARK 500 7 CYS A 8 69.17 23.70
REMARK 500 8 TYR A 4 67.04 -112.12
REMARK 500 8 LYS A 6 16.61 58.67
REMARK 500 8 CYS A 8 64.94 34.85
REMARK 500 9 TYR A 4 69.25 -112.41
REMARK 500 9 LYS A 6 18.12 57.79
REMARK 500 9 CYS A 8 71.99 31.99
REMARK 500 10 TYR A 4 67.61 -111.95
REMARK 500 10 LYS A 6 18.12 58.06
REMARK 500 10 CYS A 8 71.01 32.28
REMARK 500 11 DTR A 5 41.36 141.31
REMARK 500 11 LYS A 6 18.69 50.76
REMARK 500 11 CYS A 8 71.22 31.53
REMARK 500 12 DTR A 5 40.64 137.55
REMARK 500 12 LYS A 6 14.50 54.67
REMARK 500 12 CYS A 8 71.97 26.21
REMARK 500 13 DTR A 5 38.56 136.79
REMARK 500 13 LYS A 6 18.34 53.23
REMARK 500 13 CYS A 8 69.91 33.25
REMARK 500 14 CYS A 3 44.35 -96.55
REMARK 500 15 LYS A 6 18.44 58.01
REMARK 500 15 CYS A 8 67.35 26.31
REMARK 500 16 TYR A 4 58.66 -110.64
REMARK 500 16 DTR A 5 38.00 137.65
REMARK 500 16 LYS A 6 18.89 55.60
REMARK 500 16 CYS A 8 72.07 32.72
REMARK 500 17 TYR A 4 75.80 -118.02
REMARK 500 17 CYS A 8 65.47 33.85
REMARK 500 18 TYR A 4 74.29 -114.01
REMARK 500 18 LYS A 6 19.59 54.43
REMARK 500 18 CYS A 8 61.69 35.84
REMARK 500 19 CYS A 3 27.88 41.98
REMARK 500 19 CYS A 8 68.58 25.52
REMARK 500
REMARK 500 THIS ENTRY HAS 56 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CH4 A 0
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1SOC RELATED DB: PDB
REMARK 900 SANDOSTATIN (OCTREOTIDE) PEPTIDE
REMARK 900 RELATED ID: 2SOC RELATED DB: PDB
REMARK 900 SANDOSTATIN (OCTREOTIDE) PEPTIDE
REMARK 900 RELATED ID: 1YL8 RELATED DB: PDB
DBREF 1YL9 A 2 9 PDB 1YL9 1YL9 2 9
SEQRES 1 A 8 DPN CYS TYR DTR LYS THR CYS THR
MODRES 1YL9 DTR A 5 TRP D-TRYPTOPHAN
HET DPN A 2 20
HET DTR A 5 24
HET CH4 A 0 32
HETNAM DPN D-PHENYLALANINE
HETNAM DTR D-TRYPTOPHAN
HETNAM CH4 3-[(2-AMINOETHYL)AMINO]-2-{[(2-AMINOETHYL)
HETNAM 2 CH4 AMINO]METHYL}PROPANAL
FORMUL 1 DPN C9 H11 N O2
FORMUL 1 DTR C11 H12 N2 O2
FORMUL 2 CH4 C8 H20 N4 O
SSBOND 1 CYS A 3 CYS A 8 1555 1555 2.05
LINK C CH4 A 0 N DPN A 2 1555 1555 1.34
LINK C DPN A 2 N CYS A 3 1555 1555 1.33
LINK C TYR A 4 N DTR A 5 1555 1555 1.33
LINK C DTR A 5 N LYS A 6 1555 1555 1.34
SITE 1 AC1 3 DPN A 2 CYS A 3 THR A 9
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