Header list of 1v6r.pdb file
Complete list - 2 20 Bytes
HEADER CONTRACTILE PROTEIN 03-DEC-03 1V6R
TITLE SOLUTION STRUCTURE OF ENDOTHELIN-1 WITH ITS C-TERMINAL FOLDING
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDOTHELIN-1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ET-1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE
SOURCE 4 OF THE PEPTIDE OCCURS NATURALLY IN HUMANS.
KEYWDS ENDOTHELIN, A-HELIX, C-TERMINAL FOLDING, CARDIOVASCULAR BIOACTIVE
KEYWDS 2 PEPTIDE, G-PROTEIN COUPLED-RECEPTOR LIGAND, CONTRACTILE PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.TAKASHIMA,N.MIMURA,T.OHKUBO,T.YOSHIDA,H.TAMAOKI,Y.KOBAYASHI
REVDAT 4 02-MAR-22 1V6R 1 REMARK
REVDAT 3 24-FEB-09 1V6R 1 VERSN
REVDAT 2 20-APR-04 1V6R 1 JRNL
REVDAT 1 16-MAR-04 1V6R 0
JRNL AUTH H.TAKASHIMA,N.MIMURA,T.OHKUBO,T.YOSHIDA,H.TAMAOKI,
JRNL AUTH 2 Y.KOBAYASHI
JRNL TITL DISTRIBUTED COMPUTING AND NMR CONSTRAINT-BASED
JRNL TITL 2 HIGH-RESOLUTION STRUCTURE DETERMINATION: APPLIED FOR
JRNL TITL 3 BIOACTIVE PEPTIDE ENDOTHELIN-1 TO DETERMINE C-TERMINAL
JRNL TITL 4 FOLDING
JRNL REF J.AM.CHEM.SOC. V. 126 4504 2004
JRNL REFN ISSN 0002-7863
JRNL PMID 15070353
JRNL DOI 10.1021/JA031637W
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XPLOR-NIH 2.0.6, XPLOR-NIH 2.0.6
REMARK 3 AUTHORS : SCHWIETERS, C.D. (XPLOR-NIH), SCHWIETERS, C.D.
REMARK 3 (XPLOR-NIH)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: DISTRIBUTED COMPUTING BASED STRUCTURE
REMARK 3 CALCULATION TO EXPLORE THE CONFORMATIONAL SPACE COMPREHENSIVELY.
REMARK 4
REMARK 4 1V6R COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-DEC-03.
REMARK 100 THE DEPOSITION ID IS D_1000006276.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 297.7
REMARK 210 PH : 3
REMARK 210 IONIC STRENGTH : 5% ACETIC ACID
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2.5MM ENDOTHELIN-1
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; 2D TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 3200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY, TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 OD1 ASP A 8 H LYS A 9 1.56
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 1 SER A 2 98.47 -177.35
REMARK 500 1 ASP A 8 -174.03 -52.49
REMARK 500 1 LYS A 9 -76.40 -109.20
REMARK 500 1 HIS A 16 42.44 77.27
REMARK 500 1 LEU A 17 63.08 -108.94
REMARK 500 1 ASP A 18 72.94 39.49
REMARK 500 1 ILE A 20 78.56 -115.14
REMARK 500 2 SER A 2 100.27 179.94
REMARK 500 2 ASP A 8 -175.10 -51.83
REMARK 500 2 LYS A 9 -75.88 -109.04
REMARK 500 2 HIS A 16 40.76 77.55
REMARK 500 2 LEU A 17 63.51 -108.04
REMARK 500 2 ASP A 18 74.71 38.90
REMARK 500 2 ILE A 20 78.97 -116.10
REMARK 500 3 ASP A 8 -171.19 -56.96
REMARK 500 3 LYS A 9 -75.93 -110.48
REMARK 500 3 HIS A 16 41.27 79.97
REMARK 500 3 LEU A 17 63.56 -109.57
REMARK 500 3 ASP A 18 72.89 39.79
REMARK 500 3 ILE A 20 78.54 -115.49
REMARK 500 4 SER A 2 92.35 -162.93
REMARK 500 4 ASP A 8 -152.57 -59.02
REMARK 500 4 LYS A 9 -76.59 -130.38
REMARK 500 4 HIS A 16 40.54 77.48
REMARK 500 4 LEU A 17 63.45 -107.85
REMARK 500 4 ASP A 18 75.75 39.94
REMARK 500 4 ILE A 20 78.82 -115.76
REMARK 500 5 SER A 2 93.81 -165.81
REMARK 500 5 ASP A 8 -158.93 -58.70
REMARK 500 5 LYS A 9 -76.76 -121.37
REMARK 500 5 HIS A 16 39.55 77.21
REMARK 500 5 LEU A 17 64.85 -109.29
REMARK 500 5 ASP A 18 78.07 41.98
REMARK 500 5 ILE A 19 60.78 -66.03
REMARK 500 6 SER A 2 102.25 173.19
REMARK 500 6 ASP A 8 -151.90 -59.17
REMARK 500 6 LYS A 9 -76.73 -130.90
REMARK 500 6 HIS A 16 41.05 78.58
REMARK 500 6 LEU A 17 63.76 -108.48
REMARK 500 6 ASP A 18 78.17 40.66
REMARK 500 6 ILE A 20 79.00 -116.56
REMARK 500 7 SER A 2 92.48 -162.91
REMARK 500 7 ASP A 8 -164.51 -62.81
REMARK 500 7 LYS A 9 -74.47 -116.80
REMARK 500 7 HIS A 16 40.71 77.83
REMARK 500 7 LEU A 17 63.44 -108.08
REMARK 500 7 ASP A 18 76.38 40.30
REMARK 500 7 ILE A 20 78.84 -116.09
REMARK 500 8 SER A 2 101.92 174.47
REMARK 500 8 ASP A 8 -163.35 -62.74
REMARK 500
REMARK 500 THIS ENTRY HAS 134 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1V6R A 1 21 UNP P05305 EDN1_HUMAN 53 73
SEQRES 1 A 21 CYS SER CYS SER SER LEU MET ASP LYS GLU CYS VAL TYR
SEQRES 2 A 21 PHE CYS HIS LEU ASP ILE ILE TRP
HELIX 1 1 LYS A 9 PHE A 14 1 6
SSBOND 1 CYS A 1 CYS A 15 1555 1555 2.02
SSBOND 2 CYS A 3 CYS A 11 1555 1555 2.02
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 - 2 20 Bytes