Header list of 1v4q.pdb file
Complete list - 10 20 Bytes
HEADER TOXIN 17-NOV-03 1V4Q TITLE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE ANALOGUE PEPTIDE OF OMEGA- TITLE 2 CONOTOXIN MVIIC COMPND MOL_ID: 1; COMPND 2 MOLECULE: OMEGA-CONOTOXIN MVIIC; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 OTHER_DETAILS: THIS PEPTIDE WAS CHEMICALLY SYNTHESIZED. KEYWDS OMEGA-CONOTOXIN, CYSTINE KNOT MOTIF, TRIPLE-STRANDED ANTIPARALLEL KEYWDS 2 BETA-SHEET, CALCIUM CHANNEL BLOCKER, TOXIN EXPDTA SOLUTION NMR NUMMDL 18 AUTHOR K.KOBAYASHI,T.SASAKI,K.SATO,T.KOHNO REVDAT 3 10-NOV-21 1V4Q 1 REMARK SEQADV LINK REVDAT 2 24-FEB-09 1V4Q 1 VERSN REVDAT 1 01-MAR-05 1V4Q 0 JRNL AUTH K.KOBAYASHI,T.SASAKI,K.SATO,T.KOHNO JRNL TITL THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE ANALOGUE PEPTIDE JRNL TITL 2 OF OMEGA-CONOTOXIN MVIIC JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 2.6, X-PLOR 3.1 REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF REMARK 3 562 RESTRAINTS, 536 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 18 REMARK 3 DIHEDRAL ANGLE RESTRAINTS, 8 DISTANCE RESTRAINTS FROM HYDROGEN REMARK 3 BONDS AND DISULFIDE BONDS. REMARK 4 REMARK 4 1V4Q COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-NOV-03. REMARK 100 THE DEPOSITION ID IS D_1000006203. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 288 REMARK 210 PH : 4.0 REMARK 210 IONIC STRENGTH : 0 REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 9MM OMEGA-CONOTOXIN MVIIC REMARK 210 ANALOGUE; 90% H2O, 10% D2O; 9MM REMARK 210 OMEGA-CONOTOXIN MVIIC ANALOGUE; REMARK 210 D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; 2D TOCSY; PE REMARK 210 -COSY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 2002, PIPP 4.3.2 REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED REMARK 210 ANNEALING, MOLECULAR DYNAMICS, REMARK 210 TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 18 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D REMARK 210 HOMONUCLEAR TECHNIQUES. 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 1 PRO A 7 101.08 -57.14 REMARK 500 1 LYS A 10 16.73 -69.81 REMARK 500 1 MET A 12 -156.71 -160.28 REMARK 500 2 PRO A 7 99.91 -56.37 REMARK 500 2 LYS A 10 23.09 -72.98 REMARK 500 2 MET A 12 -155.22 -148.78 REMARK 500 2 LYS A 17 68.08 -105.56 REMARK 500 3 PRO A 7 96.85 -57.71 REMARK 500 3 LYS A 10 23.79 -72.18 REMARK 500 3 MET A 12 -156.43 -157.05 REMARK 500 4 LYS A 2 -165.15 -79.75 REMARK 500 4 PRO A 7 89.17 -66.73 REMARK 500 4 LYS A 10 47.22 -76.44 REMARK 500 4 MET A 12 -138.35 -152.85 REMARK 500 4 TYR A 13 62.94 -118.47 REMARK 500 5 PRO A 7 93.69 -66.11 REMARK 500 5 LYS A 10 34.51 -74.48 REMARK 500 5 THR A 11 -60.93 -91.63 REMARK 500 5 MET A 12 -152.70 -143.26 REMARK 500 5 TYR A 13 75.14 -104.43 REMARK 500 6 PRO A 7 92.00 -68.79 REMARK 500 6 LYS A 10 22.93 -74.03 REMARK 500 6 MET A 12 -143.97 -155.97 REMARK 500 6 TYR A 13 71.59 -111.10 REMARK 500 7 PRO A 7 94.62 -58.85 REMARK 500 7 LYS A 10 25.17 -72.48 REMARK 500 7 MET A 12 -153.54 -150.71 REMARK 500 7 TYR A 13 68.63 -105.51 REMARK 500 7 LYS A 17 74.94 -151.99 REMARK 500 8 PRO A 7 91.96 -65.52 REMARK 500 8 LYS A 10 16.22 -69.41 REMARK 500 8 MET A 12 -158.98 -159.27 REMARK 500 8 LYS A 17 92.99 -160.26 REMARK 500 9 LYS A 2 -163.30 -79.22 REMARK 500 9 LYS A 4 106.17 -57.71 REMARK 500 9 LYS A 10 36.47 -75.16 REMARK 500 9 THR A 11 -64.69 -95.47 REMARK 500 9 MET A 12 -151.62 -139.00 REMARK 500 9 TYR A 13 67.20 -108.67 REMARK 500 10 LYS A 2 -162.30 -78.90 REMARK 500 10 PRO A 7 97.60 -59.93 REMARK 500 10 MET A 12 -151.60 -159.73 REMARK 500 10 TYR A 13 68.52 -109.55 REMARK 500 10 LYS A 17 78.61 -152.34 REMARK 500 11 PRO A 7 92.39 -61.86 REMARK 500 11 LYS A 10 32.44 -75.03 REMARK 500 11 MET A 12 -156.55 -145.97 REMARK 500 11 TYR A 13 66.97 -101.58 REMARK 500 12 PRO A 7 103.77 -58.38 REMARK 500 12 LYS A 10 22.86 -71.91 REMARK 500 REMARK 500 THIS ENTRY HAS 75 RAMACHANDRAN OUTLIERS. 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 27 DBREF 1V4Q A 1 26 UNP P37300 CXO7C_CONMA 3 28 SEQADV 1V4Q LYS A 17 UNP P37300 SER 19 ENGINEERED MUTATION SEQADV 1V4Q ARG A 19 UNP P37300 SER 21 ENGINEERED MUTATION SEQADV 1V4Q ARG A 25 UNP P37300 LYS 27 ENGINEERED MUTATION SEQRES 1 A 27 CYS LYS GLY LYS GLY ALA PRO CYS ARG LYS THR MET TYR SEQRES 2 A 27 ASP CYS CYS LYS GLY ARG CYS GLY ARG ARG GLY ARG CYS SEQRES 3 A 27 NH2 HET NH2 A 27 3 HETNAM NH2 AMINO GROUP FORMUL 1 NH2 H2 N SSBOND 1 CYS A 1 CYS A 16 1555 1555 2.03 SSBOND 2 CYS A 8 CYS A 20 1555 1555 2.03 SSBOND 3 CYS A 15 CYS A 26 1555 1555 2.03 LINK C CYS A 26 N NH2 A 27 1555 1555 1.33 SITE 1 AC1 2 ARG A 19 CYS A 26 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 - 10 20 Bytes