Header list of 1vqx.pdb file
Complete list - 2 20 Bytes
HEADER SIGNALING PROTEIN 07-JAN-05 1VQX TITLE ARRESTIN-BOUND NMR STRUCTURES OF THE PHOSPHORYLATED CARBOXY-TERMINAL TITLE 2 DOMAIN OF RHODOPSIN, REFINED COMPND MOL_ID: 1; COMPND 2 MOLECULE: RHODOPSIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: C-TERMINAL DOMAIN; 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 IS NATURALLY FOUND IN BOS TAURUS. KEYWDS HELIX-LOOP, SIGNALING PROTEIN EXPDTA SOLUTION NMR NUMMDL 15 AUTHOR O.G.KISSELEV,M.A.DOWNS,J.H.MCDOWELL,P.A.HARGRAVE REVDAT 3 02-MAR-22 1VQX 1 REMARK SEQADV LINK REVDAT 2 24-FEB-09 1VQX 1 VERSN REVDAT 1 18-JAN-05 1VQX 0 SPRSDE 18-JAN-05 1VQX 1TQK JRNL AUTH O.G.KISSELEV,M.A.DOWNS,J.H.MCDOWELL,P.A.HARGRAVE JRNL TITL CONFORMATIONAL CHANGES IN THE PHOSPHORYLATED C-TERMINAL JRNL TITL 2 DOMAIN OF RHODOPSIN DURING RHODOPSIN ARRESTIN INTERACTIONS JRNL REF J.BIOL.CHEM. V. 279 51203 2004 JRNL REFN ISSN 0021-9258 JRNL PMID 15351781 JRNL DOI 10.1074/JBC.M407341200 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : TINKER 3.9 REMARK 3 AUTHORS : PONDER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1VQX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JAN-05. REMARK 100 THE DEPOSITION ID IS D_1000002071. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 278 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : 100 MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.16 MM PURIFIED ARRESTIN, 1.77 REMARK 210 MM 7-PHOSPHO-RH(330-348) IN REMARK 210 SODIUM PHOSPHATE BUFFER, 10% D2O REMARK 210 IN A TOTAL VOLUME OF 0.6 ML REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; 2D NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : UNITY REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : VNMR 5.2, TINKER 3.9 REMARK 210 METHOD USED : NULL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: PHOSPHATES ARE MISSING IN THIS STRUCTURE BECAUSE THEY WERE REMARK 210 NOT PART OF THE CALCULATIONS. 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 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME; REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 470 MODELS 1-15 REMARK 470 RES CSSEQI ATOMS REMARK 470 SEP A 5 OG P O1P O2P O3P REMARK 470 TPO A 6 P O1P O2P O3P REMARK 470 TPO A 7 P O1P O2P O3P REMARK 470 SEP A 9 OG P O1P O2P O3P REMARK 470 TPO A 11 P O1P O2P O3P REMARK 470 TPO A 13 P O1P O2P O3P REMARK 470 SEP A 14 OG P O1P O2P O3P 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 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 SEP A 9 91.13 -69.31 REMARK 500 3 SEP A 5 -82.93 -71.27 REMARK 500 7 SEP A 9 78.19 -104.49 REMARK 500 8 SEP A 9 53.27 -93.15 REMARK 500 13 SEP A 9 68.72 -109.28 REMARK 500 14 PRO A 18 -82.10 -65.05 REMARK 500 15 TPO A 7 -83.90 -120.91 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1NZS RELATED DB: PDB REMARK 900 INITIAL SET OF NMR STRUCTURES OF PHOSPHORYLATED CARBOXY TERMINUS OF REMARK 900 BOVINE RHODOPSIN IN ARRESTIN-BOUND STATE DBREF 1VQX A 1 19 UNP P02699 OPSD_BOVIN 330 348 SEQADV 1VQX SEP A 5 UNP P02699 SER 334 MODIFIED RESIDUE SEQADV 1VQX TPO A 6 UNP P02699 THR 335 MODIFIED RESIDUE SEQADV 1VQX TPO A 7 UNP P02699 THR 336 MODIFIED RESIDUE SEQADV 1VQX SEP A 9 UNP P02699 SER 338 MODIFIED RESIDUE SEQADV 1VQX TPO A 11 UNP P02699 THR 340 MODIFIED RESIDUE SEQADV 1VQX TPO A 13 UNP P02699 THR 342 MODIFIED RESIDUE SEQADV 1VQX SEP A 14 UNP P02699 SER 343 MODIFIED RESIDUE SEQRES 1 A 19 ASP ASP GLU ALA SEP TPO TPO VAL SEP LYS TPO GLU TPO SEQRES 2 A 19 SEP GLN VAL ALA PRO ALA MODRES 1VQX SEP A 5 SER PHOSPHOSERINE MODRES 1VQX TPO A 6 THR PHOSPHOTHREONINE MODRES 1VQX TPO A 7 THR PHOSPHOTHREONINE MODRES 1VQX SEP A 9 SER PHOSPHOSERINE MODRES 1VQX TPO A 11 THR PHOSPHOTHREONINE MODRES 1VQX TPO A 13 THR PHOSPHOTHREONINE MODRES 1VQX SEP A 14 SER PHOSPHOSERINE HET SEP A 5 6 HET TPO A 6 8 HET TPO A 7 8 HET SEP A 9 6 HET TPO A 11 8 HET TPO A 13 8 HET SEP A 14 6 HETNAM SEP PHOSPHOSERINE HETNAM TPO PHOSPHOTHREONINE HETSYN SEP PHOSPHONOSERINE HETSYN TPO PHOSPHONOTHREONINE FORMUL 1 SEP 3(C3 H8 N O6 P) FORMUL 1 TPO 4(C4 H10 N O6 P) HELIX 1 1 TPO A 11 ALA A 17 1 7 LINK C ALA A 4 N SEP A 5 1555 1555 1.33 LINK C SEP A 5 N TPO A 6 1555 1555 1.33 LINK C TPO A 6 N TPO A 7 1555 1555 1.33 LINK C TPO A 7 N VAL A 8 1555 1555 1.34 LINK C VAL A 8 N SEP A 9 1555 1555 1.34 LINK C SEP A 9 N LYS A 10 1555 1555 1.33 LINK C LYS A 10 N TPO A 11 1555 1555 1.33 LINK C TPO A 11 N GLU A 12 1555 1555 1.33 LINK C GLU A 12 N TPO A 13 1555 1555 1.33 LINK C TPO A 13 N SEP A 14 1555 1555 1.33 LINK C SEP A 14 N GLN A 15 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 MODEL 1
Complete list - 2 20 Bytes