Header list of 1qp3.pdb file
Complete list - r 25 2 Bytes
HEADER ELECTRON TRANSPORT 29-MAY-99 1QP3 TITLE SOLUTION STRUCTURE OF PHOTOSYSTEM I ACCESSORY PROTEIN E FROM THE TITLE 2 CYANOBACTERIUM NOSTOC SP. STRAIN PCC 8009 COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN (PSAE PROTEIN); COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: FULL LENGTH; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: NOSTOC SP.; SOURCE 3 ORGANISM_TAXID: 29413; SOURCE 4 STRAIN: PCC 8009; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET3D KEYWDS MAINLY BETA, ROLL, PLECKSTRIN TOPOLOGY, SH3-LIKE, ELECTRON TRANSPORT EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR K.L.MAYER,G.SHEN,D.A.BRYANT,J.T.J.LECOMTE,C.J.FALZONE REVDAT 4 13-JUL-11 1QP3 1 VERSN REVDAT 3 24-FEB-09 1QP3 1 VERSN REVDAT 2 01-APR-03 1QP3 1 JRNL REVDAT 1 20-OCT-99 1QP3 0 JRNL AUTH K.L.MAYER,G.SHEN,D.A.BRYANT,J.T.LECOMTE,C.J.FALZONE JRNL TITL THE SOLUTION STRUCTURE OF PHOTOSYSTEM I ACCESSORY PROTEIN E JRNL TITL 2 FROM THE CYANOBACTERIUM NOSTOC SP. STRAIN PCC 8009. JRNL REF BIOCHEMISTRY V. 38 13736 1999 JRNL REFN ISSN 0006-2960 JRNL PMID 10521281 JRNL DOI 10.1021/BI9910373 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.85 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1QP3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUN-99. REMARK 100 THE RCSB ID CODE IS RCSB009132. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.1 REMARK 210 IONIC STRENGTH : NO BUFFER OR ADDED SALT REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1 MM PSAE REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N-SEPARATED_ REMARK 210 NOESY; 3D_13C-SEPARATED_NOESY; J- REMARK 210 MODULATE HSQC REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : AMX2 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR 3.85, XWINNMR 2.0, FELIX REMARK 210 95 REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED REMARK 210 ANNEALING MOLECULAR DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR REMARK 210 SPECTROSCOPY. 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 HG11 VAL A 2 HG22 VAL A 24 1.32 REMARK 500 HD22 ASN A 44 HD13 ILE A 55 1.44 REMARK 500 HG13 VAL A 2 H GLN A 3 1.45 REMARK 500 HG3 ARG A 9 HG13 VAL A 68 1.47 REMARK 500 HG2 ARG A 9 HG21 VAL A 21 1.53 REMARK 500 HG22 VAL A 21 HG21 VAL A 68 1.55 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 TRP A 17 38.40 -96.30 REMARK 500 1 SER A 30 -51.91 -156.19 REMARK 500 1 ILE A 32 -164.62 -127.54 REMARK 500 1 ASN A 44 -164.34 -113.37 REMARK 500 1 SER A 46 -72.23 -87.44 REMARK 500 1 ASN A 56 27.83 -151.02 REMARK 500 1 VAL A 68 50.31 -114.88 REMARK 500 1 PRO A 75 177.78 -52.94 REMARK 500 1 LYS A 76 -178.29 52.93 REMARK 500 2 LEU A 11 41.22 -101.29 REMARK 500 2 TRP A 17 39.17 -96.04 REMARK 500 2 GLN A 29 49.05 -106.17 REMARK 500 2 VAL A 43 -164.88 -61.11 REMARK 500 2 ASN A 56 26.95 -145.99 REMARK 500 2 PRO A 75 172.69 -52.93 REMARK 500 2 LYS A 76 34.12 -97.29 REMARK 500 3 TRP A 17 37.65 -96.11 REMARK 500 3 ASP A 20 -168.37 -115.40 REMARK 500 3 SER A 30 -69.86 -133.64 REMARK 500 3 VAL A 43 -165.67 -66.87 REMARK 500 3 VAL A 68 58.29 -143.18 REMARK 500 3 LYS A 72 47.82 -167.67 REMARK 500 3 LYS A 74 62.98 -156.30 REMARK 500 4 VAL A 2 71.06 -69.96 REMARK 500 4 TRP A 17 40.01 -95.65 REMARK 500 4 VAL A 43 -164.93 -106.44 REMARK 500 4 GLU A 69 -154.78 -82.69 REMARK 500 4 LYS A 72 90.24 -167.74 REMARK 500 4 LYS A 76 47.78 -92.28 REMARK 500 5 GLN A 3 -169.28 -128.07 REMARK 500 5 LEU A 11 43.07 -100.32 REMARK 500 5 TRP A 17 34.33 -96.30 REMARK 500 5 VAL A 43 -173.27 -67.73 REMARK 500 5 VAL A 68 51.52 -141.44 REMARK 500 5 PRO A 71 -177.99 -52.83 REMARK 500 6 TRP A 17 37.63 -96.25 REMARK 500 6 VAL A 43 -166.59 -108.94 REMARK 500 6 VAL A 68 52.60 -140.93 REMARK 500 6 GLU A 69 80.48 -151.40 REMARK 500 6 LYS A 72 47.75 -166.37 REMARK 500 7 TRP A 17 37.22 -95.55 REMARK 500 7 SER A 30 -71.74 -135.11 REMARK 500 7 VAL A 43 -165.24 -64.60 REMARK 500 7 ASN A 58 -159.20 -148.69 REMARK 500 7 VAL A 68 28.77 -144.62 REMARK 500 7 PRO A 71 -175.89 -53.01 REMARK 500 7 LYS A 74 81.38 52.58 REMARK 500 8 LEU A 11 40.62 -101.51 REMARK 500 8 TRP A 17 38.30 -96.27 REMARK 500 8 SER A 26 -164.83 -167.76 REMARK 500 REMARK 500 THIS ENTRY HAS 143 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1QP2 RELATED DB: PDB REMARK 900 THIS ENTRY CONTAINS 20 NMR STRUCTURES. THE MINIMIZED REMARK 900 AVERAGE STRUCTURE CAN BE FOUND IN PROTEIN DATA BANK ENTRY REMARK 900 1QP2 DBREF 1QP3 A 1 77 UNP Q9WWP1 PSAE_NOSS8 1 70 SEQRES 1 A 70 MET VAL GLN ARG GLY SER LYS VAL ARG ILE LEU ARG PRO SEQRES 2 A 70 GLU SER TYR TRP PHE GLN ASP VAL GLY THR VAL ALA SER SEQRES 3 A 70 VAL ASP GLN SER GLY ILE LYS TYR PRO VAL ILE VAL ARG SEQRES 4 A 70 PHE GLU LYS VAL ASN TYR SER GLY ILE ASN THR ASN ASN SEQRES 5 A 70 PHE ALA GLU ASP GLU LEU VAL GLU VAL GLU ALA PRO LYS SEQRES 6 A 70 ALA LYS PRO LYS LYS HELIX 1 1 ALA A 61 ASP A 63 5 3 SHEET 1 A 5 THR A 57 PHE A 60 0 SHEET 2 A 5 VAL A 36 ARG A 39 -1 O VAL A 36 N PHE A 60 SHEET 3 A 5 VAL A 21 VAL A 27 -1 O THR A 23 N ARG A 39 SHEET 4 A 5 LYS A 7 ILE A 10 -1 N VAL A 8 O GLY A 22 SHEET 5 A 5 LEU A 65 GLU A 67 -1 O VAL A 66 N ARG A 9 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 - r 25 2 Bytes