Header list of 1cq0.pdb file
Complete list - 14 201 Bytes
HEADER DE NOVO PROTEIN 04-AUG-99 1CQ0
TITLE SOLUTION STRUCTURE OF A HUMAN HYPOCRETIN-2/OREXIN-B'SOLUTION STRUCTURE
TITLE 2 OF A HUMAN HYPOCRETIN-2/OREXIN-B '
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (NEW HYPOTHALAMIC NEUROPEPTIDE/OREXIN-B28);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: HUMAN HYPOCRETIN-2;
COMPND 5 OTHER_DETAILS: SYNTHETIC PEPTIDE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 OTHER_DETAILS: SYNTHETIC
KEYWDS OBESITY, HUMAN HCRT-2/OX-B, NEUROPEPTIDE, SOLUTION STRUCTURE, DE NOVO
KEYWDS 2 PROTEIN
EXPDTA SOLUTION NMR
AUTHOR K.-H.LEE,E.J.BANG,K.-J.CHAE,D.W.LEE,W.LEE
REVDAT 4 14-MAR-18 1CQ0 1 REMARK
REVDAT 3 24-FEB-09 1CQ0 1 VERSN
REVDAT 2 01-APR-03 1CQ0 1 JRNL
REVDAT 1 10-JAN-00 1CQ0 0
JRNL AUTH J.H.LEE,E.BANG,K.J.CHAE,J.Y.KIM,D.W.LEE,W.LEE
JRNL TITL SOLUTION STRUCTURE OF A NEW HYPOTHALAMIC NEUROPEPTIDE, HUMAN
JRNL TITL 2 HYPOCRETIN-2/OREXIN-B.
JRNL REF EUR.J.BIOCHEM. V. 266 831 1999
JRNL REFN ISSN 0014-2956
JRNL PMID 10583376
JRNL DOI 10.1046/J.1432-1327.1999.00911.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XPLOR 3.85, XPLOR 3.85
REMARK 3 AUTHORS : AXEL ET AL. (XPLOR), AXEL ET AL. (XPLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1CQ0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-AUG-99.
REMARK 100 THE DEPOSITION ID IS D_1000009477.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 50 MM SODIUM PHOSPHATE
REMARK 210 PRESSURE : 1 BAR
REMARK 210 SAMPLE CONTENTS : 2MM
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D-NOESY; TOCSY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX500
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 25
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : REM AVERAGE CONFORMATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O LEU A 11 H LEU A 15 1.51
REMARK 500
REMARK 500 REMARK: NULL
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 LEU A 7 -87.94 -64.59
REMARK 500 LEU A 11 -73.44 -69.70
REMARK 500 SER A 18 30.65 -96.99
REMARK 500 ASN A 20 -67.90 -167.18
REMARK 500 THR A 27 29.11 -159.60
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 ARG A 10 0.09 SIDE CHAIN
REMARK 500 ARG A 13 0.21 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1CQ0 A 2 28 UNP O43612 OREX_HUMAN 71 97
SEQRES 1 A 28 PHE SER GLY PRO PRO GLY LEU GLN GLY ARG LEU GLN ARG
SEQRES 2 A 28 LEU LEU GLN ALA SER GLY ASN HIS ALA ALA GLY ILE LEU
SEQRES 3 A 28 THR MET
HELIX 1 1 GLY A 6 SER A 18 1 13
HELIX 2 2 HIS A 21 THR A 27 1 7
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
Complete list - 14 201 Bytes