Header list of 1soc.pdb file
Complete list - 2 202 Bytes
HEADER OCTREOTIDE 26-NOV-96 1SOC
TITLE NMR STUDY OF THE BACKBONE CONFORMATIONAL EQUILIBRIA OF SANDOSTATIN,
TITLE 2 MINIMIZED AVERAGE BETA-SHEET STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SANDOSTATIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: OCTREOTIDE;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1
KEYWDS OCTREOTIDE, SANDOSTATIN
EXPDTA SOLUTION NMR
AUTHOR G.MELACINI,Q.ZHU,M.GOODMAN
REVDAT 3 02-MAR-22 1SOC 1 REMARK LINK
REVDAT 2 24-FEB-09 1SOC 1 VERSN
REVDAT 1 21-APR-97 1SOC 0
JRNL AUTH G.MELACINI,Q.ZHU,M.GOODMAN
JRNL TITL MULTICONFORMATIONAL NMR ANALYSIS OF SANDOSTATIN
JRNL TITL 2 (OCTREOTIDE): EQUILIBRIUM BETWEEN BETA-SHEET AND PARTIALLY
JRNL TITL 3 HELICAL STRUCTURES.
JRNL REF BIOCHEMISTRY V. 36 1233 1997
JRNL REFN ISSN 0006-2960
JRNL PMID 9063871
JRNL DOI 10.1021/BI962497O
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH E.POHL,A.HEINE,G.SHELDRICK,Z.DAUTNER,K.S.WILSON,J.KALLEN,
REMARK 1 AUTH 2 W.HUBER,P.J.PFAFFLI
REMARK 1 TITL STRUCTURE OF OCTREOTIDE, A SOMATOSTATIN ANALOGUE
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 51 48 1995
REMARK 1 REFN ISSN 0907-4449
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DISCOVER
REMARK 3 AUTHORS : BIOSYM
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: CVFF FORCE FIELD (USED BY DISCOVER)
REMARK 3 DGII ALSO WAS USED.
REMARK 4
REMARK 4 1SOC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000176448.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : ROESY; TOCSY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AMX 500
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 29
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: DMSO-D6
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 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2SOC RELATED DB: PDB
DBREF 1SOC A 1 8 PDB 1SOC 1SOC 1 8
SEQRES 1 A 8 DPN CYS PHE DTR LYS THR CYS THO
MODRES 1SOC DTR A 4 TRP D-TRYPTOPHAN
HET DPN A 1 21
HET DTR A 4 24
HET THO A 8 17
HETNAM DPN D-PHENYLALANINE
HETNAM DTR D-TRYPTOPHAN
HETNAM THO REDUCED THREONINE
FORMUL 1 DPN C9 H11 N O2
FORMUL 1 DTR C11 H12 N2 O2
FORMUL 1 THO C4 H11 N O2
SHEET 1 A 2 CYS A 2 PHE A 3 0
SHEET 2 A 2 THR A 6 CYS A 7 -1 O THR A 6 N PHE A 3
SSBOND 1 CYS A 2 CYS A 7 1555 1555 2.01
LINK C DPN A 1 N CYS A 2 1555 1555 1.35
LINK C PHE A 3 N DTR A 4 1555 1555 1.35
LINK C DTR A 4 N LYS A 5 1555 1555 1.34
LINK C CYS A 7 N THO A 8 1555 1555 1.34
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 - 2 202 Bytes