Header list of 1ieo.pdb file
Complete list - 23 20 Bytes
HEADER TOXIN 10-APR-01 1IEO TITLE SOLUTION STRUCTURE OF MRIB-NH2 COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN MRIB-NH2; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 OTHER_DETAILS: THIS PEPTIDE WAS CHEMICALLY SYNTESIZED. THIS SEQUENCE SOURCE 4 OCCURS IN CONUS MARMOREUS (MOLLUSC-HUNTING CONE SNAIL). HOWEVER, THE SOURCE 5 C-TERMINUS HAS BEEN AMIDATED WHEREAS IT EXISTS AS A FREE-ACID IN THE SOURCE 6 NATIVE FORM. KEYWDS CONOTOXIN, NEURONAL NORADRENALINE TRANSPORTER, TOXIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR I.A.SHARPE,J.GEHRMANN,M.L.LOUGHNAN,L.THOMAS,D.A.ADAMS,A.ATKINS, AUTHOR 2 E.PALANT,D.J.CRAIK,D.J.ADAMS,P.F.ALEWOOD,R.J.LEWIS REVDAT 3 23-FEB-22 1IEO 1 REMARK LINK REVDAT 2 24-FEB-09 1IEO 1 VERSN REVDAT 1 03-APR-02 1IEO 0 JRNL AUTH I.A.SHARPE,J.GEHRMANN,M.L.LOUGHNAN,L.THOMAS,D.A.ADAMS, JRNL AUTH 2 A.ATKINS,E.PALANT,D.J.CRAIK,D.J.ADAMS,P.F.ALEWOOD,R.J.LEWIS JRNL TITL TWO NEW CLASSES OF CONOPEPTIDES INHIBIT THE JRNL TITL 2 ALPHA1-ADRENOCEPTOR AND NORADRENALINE TRANSPORTER. JRNL REF NAT.NEUROSCI. V. 4 902 2001 JRNL REFN ISSN 1097-6256 JRNL PMID 11528421 JRNL DOI 10.1038/NN0901-902 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 2.6, X-PLOR 3.851 REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 THE STRUCTURES ARE CALCULATED FROM A TOTAL OF 82 DISTANCE REMARK 3 RESTRAINTS DERIVED FROM 14 INTRA-RESIDUE, REMARK 3 42 SEQUENTIAL, 3 MEDIUM AND 23 LONG RANGE NOES, AND 4 DIHEDRAL REMARK 3 RESTRAINTS. REMARK 4 REMARK 4 1IEO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-APR-01. REMARK 100 THE DEPOSITION ID IS D_1000013214. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 285 REMARK 210 PH : 3.5 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 2 MM MRIB-NH2 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; E-COSY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 750 MHZ REMARK 210 SPECTROMETER MODEL : ARX; AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : FELIX 230, X-PLOR 3.851 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : THE SUBMITTED CONFORMER MODELS REMARK 210 ARE THE 20 STRUCTURES WITH THE REMARK 210 LOWEST ENERGY. REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 8 REMARK 210 REMARK 210 REMARK: REMARK 210 THE SAMPLE WAS A PURIFIED SINGLE PEPTIDE COMPONENT BUT ON REMARK 210 DISSOLUTION DISPLAYED EVIDENCE OF REMARK 210 MULTIPLE CONFORMATIONS (MANIFEST BY PEAKS "BROTHERING" IN THE N- REMARK 210 TERMINAL REGION). THE STRUCTURES REMARK 210 SHOWN ARE FOR THE MAJOR SOLUTION CONFORMER. 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: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 3 CYS A 4 CA - CB - SG ANGL. DEV. = 6.6 DEGREES REMARK 500 4 CYS A 4 CA - CB - SG ANGL. DEV. = 9.7 DEGREES REMARK 500 7 CYS A 4 CA - CB - SG ANGL. DEV. = 7.6 DEGREES REMARK 500 10 CYS A 10 CA - CB - SG ANGL. DEV. = 7.5 DEGREES REMARK 500 11 CYS A 4 CA - CB - SG ANGL. DEV. = 9.4 DEGREES REMARK 500 13 CYS A 4 CA - CB - SG ANGL. DEV. = 9.9 DEGREES REMARK 500 14 CYS A 4 CA - CB - SG ANGL. DEV. = 7.5 DEGREES 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 CYS A 4 43.68 -109.33 REMARK 500 1 TYR A 7 -69.62 -159.39 REMARK 500 1 LYS A 8 -47.42 -167.10 REMARK 500 1 HIS A 11 -128.77 -152.79 REMARK 500 2 CYS A 4 44.92 -152.34 REMARK 500 2 TYR A 7 -56.41 -169.04 REMARK 500 2 HIS A 11 -146.76 -153.59 REMARK 500 2 HYP A 12 55.13 -99.76 REMARK 500 3 TYR A 7 -12.21 65.17 REMARK 500 3 LYS A 8 62.65 -160.60 REMARK 500 3 LEU A 9 -160.58 54.59 REMARK 500 3 HIS A 11 -139.62 -149.11 REMARK 500 3 HYP A 12 58.47 -119.04 REMARK 500 4 CYS A 4 28.27 -160.01 REMARK 500 4 LYS A 8 -60.87 -163.20 REMARK 500 4 HIS A 11 -149.52 81.88 REMARK 500 5 CYS A 4 81.18 -154.33 REMARK 500 5 TYR A 7 -78.89 63.02 REMARK 500 5 LYS A 8 -39.60 -147.40 REMARK 500 5 HIS A 11 -155.13 -147.87 REMARK 500 6 LYS A 8 60.54 -153.23 REMARK 500 6 LEU A 9 -168.29 57.86 REMARK 500 6 HIS A 11 -134.61 -148.40 REMARK 500 6 HYP A 12 42.83 -101.85 REMARK 500 7 CYS A 4 49.28 -155.18 REMARK 500 7 LYS A 8 -14.95 76.63 REMARK 500 7 HIS A 11 -150.62 -152.73 REMARK 500 8 CYS A 4 57.68 -153.97 REMARK 500 8 TYR A 7 -73.65 -164.52 REMARK 500 8 LYS A 8 -47.23 -161.63 REMARK 500 8 HIS A 11 -153.96 -142.69 REMARK 500 9 CYS A 4 55.41 -114.48 REMARK 500 9 TYR A 7 -79.15 61.68 REMARK 500 9 LYS A 8 -35.33 -148.02 REMARK 500 9 HIS A 11 -138.01 -146.75 REMARK 500 10 CYS A 4 58.77 -149.54 REMARK 500 10 TYR A 7 -24.84 -159.65 REMARK 500 10 LYS A 8 -66.80 -142.53 REMARK 500 10 HIS A 11 -157.60 -150.68 REMARK 500 11 CYS A 4 40.13 -160.08 REMARK 500 11 TYR A 7 -78.51 65.06 REMARK 500 11 LYS A 8 10.37 -163.87 REMARK 500 11 HIS A 11 -145.80 78.44 REMARK 500 12 TYR A 7 -40.26 -163.70 REMARK 500 12 HIS A 11 -139.00 -152.65 REMARK 500 13 CYS A 4 38.72 -158.20 REMARK 500 13 TYR A 7 -26.90 -157.59 REMARK 500 13 HIS A 11 -155.95 79.46 REMARK 500 14 CYS A 4 43.38 -156.22 REMARK 500 14 LYS A 8 -4.29 67.37 REMARK 500 REMARK 500 THIS ENTRY HAS 76 RAMACHANDRAN OUTLIERS. 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 HIS A 11 HYP A 12 1 146.34 REMARK 500 HIS A 11 HYP A 12 16 149.23 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 14 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1IEN RELATED DB: PDB REMARK 900 1IEN SEQUENCE (SYNTHETIC) OF CONUS TULIPA (FISH-HUNTING CONE SNAIL) DBREF 1IEO A 1 13 UNP P58810 CXL4_CONMR 1 13 SEQRES 1 A 14 VAL GLY VAL CYS CYS GLY TYR LYS LEU CYS HIS HYP CYS SEQRES 2 A 14 NH2 MODRES 1IEO HYP A 12 PRO 4-HYDROXYPROLINE HET HYP A 12 15 HET NH2 A 14 3 HETNAM HYP 4-HYDROXYPROLINE HETNAM NH2 AMINO GROUP HETSYN HYP HYDROXYPROLINE FORMUL 1 HYP C5 H9 N O3 FORMUL 1 NH2 H2 N SSBOND 1 CYS A 4 CYS A 13 1555 1555 2.01 SSBOND 2 CYS A 5 CYS A 10 1555 1555 2.02 LINK C HIS A 11 N HYP A 12 1555 1555 1.31 LINK C HYP A 12 N CYS A 13 1555 1555 1.31 LINK C CYS A 13 N NH2 A 14 1555 1555 1.31 SITE 1 AC1 2 HYP A 12 CYS A 13 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 - 23 20 Bytes