Header list of 1n9u.pdb file
Complete list - 21 20 Bytes
HEADER SIGNALING PROTEIN 26-NOV-02 1N9U
TITLE DIFFERENCES AND SIMILARITIES IN SOLUTION STRUCTURES OF ANGIOTENSIN I &
TITLE 2 II: IMPLICATION FOR STRUCTURE-FUNCTION RELATIONSHIP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANGIOTENSIN I;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ANG I;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS MADE THROUGH SOLID PHASE SYNTHESIS
SOURCE 4 USING FMOC CHEMISTRY. THE SEQUENCE OF THE PEPTIDE IS NATURALLY FOUND
SOURCE 5 IN HOMO SAPIENS.
KEYWDS ANGIOTENSIN, RENIN-ANGIOTENSIN SYSTEM, SOLID PHASE PEPTIDE SYNTHESIS,
KEYWDS 2 NMR SOLUTION STRUCTURE, PEPTIDES, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 21
AUTHOR G.A.SPYROULIAS,P.NIKOLAKOPOULOU,A.TZAKOS,I.P.GEROTHANASSIS,V.MAGAFA,
AUTHOR 2 E.MANESSI-ZOUPA,P.CORDOPATIS
REVDAT 3 21-DEC-16 1N9U 1 TITLE VERSN
REVDAT 2 24-FEB-09 1N9U 1 VERSN
REVDAT 1 29-JUL-03 1N9U 0
JRNL AUTH G.A.SPYROULIAS,P.NIKOLAKOPOULOU,A.TZAKOS,I.P.GEROTHANASSIS,
JRNL AUTH 2 V.MAGAFA,E.MANESSI-ZOUPA,P.CORDOPATIS
JRNL TITL COMPARISON OF THE SOLUTION STRUCTURES OF ANGIOTENSIN I & II.
JRNL TITL 2 IMPLICATION FOR STRUCTURE-FUNCTION RELATIONSHIP.
JRNL REF EUR.J.BIOCHEM. V. 270 2163 2003
JRNL REFN ISSN 0014-2956
JRNL PMID 12752436
JRNL DOI 10.1046/J.1432-1033.2003.03573.X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.M.MATSOUKAS,J.HONDRELIS,M.KERAMIDA,T.MAVROMOUSTAKOS,
REMARK 1 AUTH 2 A.MAKRIYANNIS,R.YAMDAGNI,Q.WU,G.J.MOORE
REMARK 1 TITL ROLE OF THE NH2-TERMINAL DOMAIN OF ANGIOTENSIN II (ANG II)
REMARK 1 TITL 2 AND [SAR1]ANGIOTENSIN II ON CONFORMATION AND ACTIVITY. NMR
REMARK 1 TITL 3 EVIDENCE FOR AROMATIC RING CLUSTERING AND PEPTIDE BACKBONE
REMARK 1 TITL 4 FOLDING COMPARED WITH [DES-1,2,3]ANGIOTENSIN II
REMARK 1 REF J.BIOL.CHEM. V. 269 5303 1994
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AMBER 5.0
REMARK 3 AUTHORS : KOLLMAN, CASE, MERZ, CHEATHAM, SIMMERLING, DARDEN,
REMARK 3 PEARLMAN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THIS STRUCTURE IS BASED ON A 225 NOE-
REMARK 3 DERIVED DISTANCE CONSTRAINTS, 7 DIHEDRAL ANGLE RESTRAINTS, 1
REMARK 3 DISTANCE RESTRAINT FROM HYDROGEN BOND
REMARK 4
REMARK 4 1N9U COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-DEC-02.
REMARK 100 THE RCSB ID CODE IS RCSB017698.
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 : 2.5 MM; DMSO-D6
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D TOCSY; 2D NOESY
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 : XWINNMR 2.6, XEASY 1.3, DYANA 1.5
REMARK 210 METHOD USED : SIMULATED ANNEALING, TORSION
REMARK 210 ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 300
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION FOR MODELS 1-20,
REMARK 210 MEAN ENERGY MINIMIZED FOR MODEL 21
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 21
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES. MODELS 1-20 ARE THE FAMILY ENSEMBLE,
REMARK 210 WHILE MODEL 21 IS THE MINIMIZED AVERAGE STRUCTURE DERIVED FROM
REMARK 210 THAT ENSEMBLE.
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 PHE A 8 117.36 -171.75
REMARK 500 1 HIS A 9 58.75 -149.53
REMARK 500 2 PHE A 8 118.30 -171.58
REMARK 500 2 HIS A 9 56.59 -146.96
REMARK 500 3 PHE A 8 118.30 -171.58
REMARK 500 3 HIS A 9 56.59 -146.96
REMARK 500 4 PHE A 8 119.30 -171.72
REMARK 500 4 HIS A 9 64.97 -151.55
REMARK 500 5 PHE A 8 117.86 -171.89
REMARK 500 6 PHE A 8 118.93 -171.07
REMARK 500 6 HIS A 9 58.33 -148.27
REMARK 500 7 PHE A 8 119.21 -172.11
REMARK 500 7 HIS A 9 59.63 -148.35
REMARK 500 8 PHE A 8 117.84 -170.91
REMARK 500 8 HIS A 9 65.66 -151.10
REMARK 500 9 PHE A 8 118.31 -171.91
REMARK 500 10 PHE A 8 119.85 -170.43
REMARK 500 11 PHE A 8 118.80 -171.77
REMARK 500 12 PHE A 8 120.14 -171.48
REMARK 500 13 PHE A 8 118.31 -172.61
REMARK 500 14 PHE A 8 119.07 -171.25
REMARK 500 14 HIS A 9 58.30 -151.60
REMARK 500 15 PHE A 8 117.20 -171.72
REMARK 500 16 PHE A 8 117.45 -171.92
REMARK 500 16 HIS A 9 63.70 -151.34
REMARK 500 17 PHE A 8 119.55 -171.81
REMARK 500 17 HIS A 9 61.79 -153.46
REMARK 500 18 PHE A 8 119.22 -172.14
REMARK 500 18 HIS A 9 57.10 -149.75
REMARK 500 19 PHE A 8 118.47 -171.24
REMARK 500 19 HIS A 9 63.29 -150.37
REMARK 500 20 PHE A 8 115.71 -170.95
REMARK 500 20 HIS A 9 35.98 -153.52
REMARK 500 21 PHE A 8 122.61 -170.23
REMARK 500 21 HIS A 9 59.70 -153.61
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 14 ARG A 2 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1N9U A 1 10 UNP P01019 ANGT_HUMAN 34 43
SEQRES 1 A 10 ASP ARG VAL TYR ILE HIS PRO PHE HIS LEU
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 - 21 20 Bytes