Header list of 1wso.pdb file
Complete list - c 25 2 Bytes
HEADER NEUROPEPTIDE 08-NOV-04 1WSO
TITLE THE SOLUTION STRUCTURES OF HUMAN OREXIN-A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OREXIN-A;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HYPOCRETIN-1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 4 ORGANISM_COMMON: HUMAN;
SOURCE 5 ORGANISM_TAXID: 9606
KEYWDS HYPOCRETIN, OREXIN, GPCR, ORPHAN G-PROTEIN COUPLED RECEPTOR,
KEYWDS 2 NARCOLEPSY, NEUROPEPTIDE
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR T.IKEGAMI,T.TAKAI
REVDAT 3 25-DEC-19 1WSO 1 SOURCE REMARK SEQADV SEQRES
REVDAT 3 2 1 LINK
REVDAT 2 27-MAY-08 1WSO 1 JRNL VERSN
REVDAT 1 30-NOV-04 1WSO 0
JRNL AUTH T.TAKAI,T.TAKAYA,M.NAKANO,H.AKUTSU,A.NAKAGAWA,S.AIMOTO,
JRNL AUTH 2 K.NAGAI,T.IKEGAMI
JRNL TITL OREXIN-A IS COMPOSED OF A HIGHLY CONSERVED C-TERMINAL AND A
JRNL TITL 2 SPECIFIC, HYDROPHILIC N-TERMINAL REGION, REVEALING THE
JRNL TITL 3 STRUCTURAL BASIS OF SPECIFIC RECOGNITION BY THE OREXIN-1
JRNL TITL 4 RECEPTOR
JRNL REF J.PEPT.SCI. V. 12 443 2006
JRNL REFN ISSN 1075-2617
JRNL PMID 16429482
JRNL DOI 10.1002/PSC.747
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2.2, CYANA 1.0.6
REMARK 3 AUTHORS : DELAGLIO, F. (NMRPIPE), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE N- AND C-TERMINI ARE MODIFIED WITH
REMARK 3 PYRROLIDONE CARBOXYLIC ACID, OR PYROGLUTAMIC ACID, AND AN AMIDE
REMARK 3 GROUP, RESPECTIVELY. TWO INTRA-MOLECULAR DISULFIDE BONDS ARE
REMARK 3 FORMED BETWEEN CYS6 AND CYS12, AND BETWEEN CYS7 AND CYS14.
REMARK 4
REMARK 4 1WSO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-NOV-04.
REMARK 100 THE DEPOSITION ID IS D_1000023953.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 18MM POTASSIUM PHOSPHATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.76MM OREXIN-A; 18MM POTASSIUM
REMARK 210 PHOSPHATE BUFFER; 0.76MM OREXIN-
REMARK 210 A; 18MM POTASSIUM PHOSPHATE
REMARK 210 BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; 2D NOESY; DQF-COSY;
REMARK 210 15N-1H-HSQC; 13C-1H-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : SPARKY 3.106, CYANA 1.0.6, TALOS
REMARK 210 2003.027.13.05
REMARK 210 METHOD USED : SIMULATED ANNEALING TORSION
REMARK 210 ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURES WERE DETERMINED USING 2D HOMONUCLEAR AND
REMARK 210 15N, 13C NATURAL ABUNDANCE HETERONUCLEAR EXPERIMENTS.
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 12 175.34 179.54
REMARK 500 2 CYS A 12 175.34 179.21
REMARK 500 3 CYS A 12 175.37 179.14
REMARK 500 4 CYS A 12 175.37 179.58
REMARK 500 6 ARG A 15 -9.84 -55.87
REMARK 500 8 CYS A 12 175.07 179.21
REMARK 500 19 ARG A 15 -8.54 -55.35
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 NH2 A 34
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1R02 RELATED DB: PDB
REMARK 900 THE STRUCTURE OF OREXIN-A.
REMARK 900 RELATED ID: 1CQ0 RELATED DB: PDB
REMARK 900 THE STRUCTURE OF OREXIN-B.
DBREF 1WSO A 1 33 UNP O43612 OREX_HUMAN 35 66
SEQRES 1 A 34 PCA PRO LEU PRO ASP CYS CYS ARG GLN LYS THR CYS SER
SEQRES 2 A 34 CYS ARG LEU TYR GLU LEU LEU HIS GLY ALA GLY ASN HIS
SEQRES 3 A 34 ALA ALA GLY ILE LEU THR LEU NH2
MODRES 1WSO PCA A 1 GLN PYROGLUTAMIC ACID
HET PCA A 1 14
HET NH2 A 34 3
HETNAM PCA PYROGLUTAMIC ACID
HETNAM NH2 AMINO GROUP
FORMUL 1 PCA C5 H7 N O3
FORMUL 1 NH2 H2 N
HELIX 1 1 ASP A 5 LYS A 10 1 6
HELIX 2 2 ARG A 15 GLY A 24 1 10
HELIX 3 3 GLY A 24 LEU A 33 1 10
SSBOND 1 CYS A 6 CYS A 12 1555 1555 2.09
SSBOND 2 CYS A 7 CYS A 14 1555 1555 2.10
LINK C PCA A 1 N PRO A 2 1555 1555 1.34
LINK C LEU A 33 N NH2 A 34 1555 1555 1.33
SITE 1 AC1 5 GLY A 29 ILE A 30 LEU A 31 THR A 32
SITE 2 AC1 5 LEU A 33
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 - c 25 2 Bytes