Header list of 6cmh.pdb file
Complete list - 16 202 Bytes
HEADER CONTRACTILE PROTEIN 03-SEP-98 6CMH
TITLE SYNTHETIC LINEAR MODIFIED ENDOTHELIN-1 AGONIST
CAVEAT 6CMH THERE IS A CHIRALITY ERROR AT THE C-ALPHA CENTER OF LEU A
CAVEAT 2 6CMH 17.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (ENDOTHELIN-1);
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED FROM A
SOURCE 4 BIOLOGICAL SOURCE.
KEYWDS VASOCONSTRICTOR, ENDOTHELIN-1, CONTRACTILE PROTEIN
EXPDTA SOLUTION NMR
AUTHOR C.M.HEWAGE,L.JIANG,J.A.PARKINSON,R.RAMAGE,I.H.SADLER
REVDAT 3 16-MAR-22 6CMH 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 6CMH 1 VERSN
REVDAT 1 29-SEP-99 6CMH 0
JRNL AUTH C.M.HEWAGE,L.JIANG,J.A.PARKINSON,R.RAMAGE,I.H.SADLER
JRNL TITL SOLUTION STRUCTURE OF A NOVEL ETB RECEPTOR SELECTIVE AGONIST
JRNL TITL 2 ET1-21 [CYS(ACM)1,15, AIB3,11, LEU7] BY NUCLEAR MAGNETIC
JRNL TITL 3 RESONANCE SPECTROSCOPY AND MOLECULAR MODELLING.
JRNL REF J.PEPT.RES. V. 53 223 1999
JRNL REFN ISSN 1397-002X
JRNL PMID 10231710
JRNL DOI 10.1034/J.1399-3011.1999.00001.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TRIPOS 6.1
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6CMH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUL-99.
REMARK 100 THE DEPOSITION ID IS D_1000007007.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 3.6
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 50% H2O/ 50% CD3OH
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : SYBYL TRIPOS
REMARK 210 METHOD USED : DG, DSA, MD
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 10
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: BACK CALCULATED STRUCTURE. 2D NMR METHODS
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 LEU A 6 -94.22 -104.16
REMARK 500 LEU A 7 -82.68 34.43
REMARK 500 LEU A 17 25.19 48.67
REMARK 500 ASP A 18 65.13 61.34
REMARK 500 ILE A 20 -6.17 54.78
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ILE A 20 TRP A 21 148.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3CMH RELATED DB: PDB
DBREF 6CMH A 1 21 UNP P22388 EDN1_RAT 53 73
SEQADV 6CMH ALA A 3 UNP P22388 CYS 55 CONFLICT
SEQADV 6CMH LEU A 7 UNP P22388 MET 59 CONFLICT
SEQADV 6CMH AIB A 11 UNP P22388 CYS 63 CONFLICT
SEQRES 1 A 21 CYS SER ALA SER SER LEU LEU ASP LYS GLU AIB VAL TYR
SEQRES 2 A 21 PHE CYS HIS LEU ASP ILE ILE TRP
MODRES 6CMH AIB A 11 ALA ALPHA-AMINOISOBUTYRIC ACID
HET AIB A 11 13
HETNAM AIB ALPHA-AMINOISOBUTYRIC ACID
FORMUL 1 AIB C4 H9 N O2
HELIX 1 1 SER A 2 SER A 5 1 4
HELIX 2 2 LYS A 9 HIS A 16 5 8
LINK C GLU A 10 N AIB A 11 1555 1555 1.35
LINK C AIB A 11 N VAL A 12 1555 1555 1.35
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 - 16 202 Bytes