Header list of 1a2s.pdb file
Complete list - 16 20 Bytes
HEADER ELECTRON TRANSPORT 10-JAN-98 1A2S TITLE THE SOLUTION NMR STRUCTURE OF OXIDIZED CYTOCHROME C6 FROM THE GREEN TITLE 2 ALGA MONORAPHIDIUM BRAUNII, MINIMIZED AVERAGE STRUCTURE COMPND MOL_ID: 1; COMPND 2 MOLECULE: CYTOCHROME C6; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: CYTOCHROME C552; COMPND 5 OTHER_DETAILS: OXIDIZED FORM SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MONORAPHIDIUM BRAUNII; SOURCE 3 ORGANISM_TAXID: 34112 KEYWDS CYTOCHROME C6, PHOTOSYSTEM I, ELECTRON TRANSPORT, PARAMAGNETIC NMR, KEYWDS 2 SOLUTION STRUCTURE, HEME PROTEIN EXPDTA SOLUTION NMR AUTHOR L.BANCI,I.BERTINI,M.A.DE LA ROSA,D.KOULOUGLIOTIS,J.A.NAVARRO,O.WALTER REVDAT 3 16-FEB-22 1A2S 1 REMARK LINK REVDAT 2 24-FEB-09 1A2S 1 VERSN REVDAT 1 29-APR-98 1A2S 0 JRNL AUTH L.BANCI,I.BERTINI,M.A.DE LA ROSA,D.KOULOUGLIOTIS, JRNL AUTH 2 J.A.NAVARRO,O.WALTER JRNL TITL SOLUTION STRUCTURE OF OXIDIZED CYTOCHROME C6 FROM THE GREEN JRNL TITL 2 ALGA MONORAPHIDIUM BRAUNII. JRNL REF BIOCHEMISTRY V. 37 4831 1998 JRNL REFN ISSN 0006-2960 JRNL PMID 9538000 JRNL DOI 10.1021/BI972765Y REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : AMBER REMARK 3 AUTHORS : PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM, REMARK 3 FERGUSON,SEIBEL,SINGH,WEINER,KOLLMAN REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1A2S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000170320. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 300 REMARK 210 PH : 5.0 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; COSY; 1D NOE REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : DRX 500; AMX 600; AVANCE 800 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : DYANA, PSEUDYANA, AMBER REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 40 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : MINIMIZED AVERAGE STRUCTURE REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL 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: 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 ALA A 2 152.86 123.98 REMARK 500 ALA A 20 122.08 -39.39 REMARK 500 ASN A 25 -55.82 -120.08 REMARK 500 ASP A 29 -45.97 -160.50 REMARK 500 HIS A 30 94.15 -66.87 REMARK 500 THR A 31 -131.04 -87.24 REMARK 500 LEU A 32 39.34 -145.00 REMARK 500 PHE A 45 84.65 -63.66 REMARK 500 GLN A 53 -50.85 -123.88 REMARK 500 ASP A 69 165.69 47.60 REMARK 500 ASP A 71 -72.88 -78.97 REMARK 500 ASN A 87 17.24 82.97 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 ARG A 67 LEU A 68 -145.95 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEC A 90 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 19 NE2 REMARK 620 2 HEC A 90 NA 96.1 REMARK 620 3 HEC A 90 NB 90.2 91.8 REMARK 620 4 HEC A 90 NC 87.2 176.7 88.6 REMARK 620 5 HEC A 90 ND 90.6 90.9 177.1 88.6 REMARK 620 6 MET A 61 SD 167.1 78.1 101.4 98.6 78.1 REMARK 620 N 1 2 3 4 5 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: NUL REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: HEC SITE REMARK 800 REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 90 DBREF 1A2S A 1 89 UNP Q09099 CYC6_MONBR 1 89 SEQRES 1 A 89 GLU ALA ASP LEU ALA LEU GLY LYS ALA VAL PHE ASP GLY SEQRES 2 A 89 ASN CYS ALA ALA CYS HIS ALA GLY GLY GLY ASN ASN VAL SEQRES 3 A 89 ILE PRO ASP HIS THR LEU GLN LYS ALA ALA ILE GLU GLN SEQRES 4 A 89 PHE LEU ASP GLY GLY PHE ASN ILE GLU ALA ILE VAL TYR SEQRES 5 A 89 GLN ILE GLU ASN GLY LYS GLY ALA MET PRO ALA TRP ASP SEQRES 6 A 89 GLY ARG LEU ASP GLU ASP GLU ILE ALA GLY VAL ALA ALA SEQRES 7 A 89 TYR VAL TYR ASP GLN ALA ALA GLY ASN LYS TRP HET HEC A 90 75 HETNAM HEC HEME C FORMUL 2 HEC C34 H34 FE N4 O4 HELIX 1 1 LEU A 4 ASN A 14 1 11 HELIX 2 2 ALA A 16 HIS A 19 1 4 HELIX 3 3 LYS A 34 PHE A 40 1 7 HELIX 4 4 ILE A 47 ILE A 54 1 8 HELIX 5 5 GLU A 72 GLY A 86 1 15 LINK SG CYS A 15 CAB HEC A 90 1555 1555 1.82 LINK SG CYS A 18 CAC HEC A 90 1555 1555 1.83 LINK NE2 HIS A 19 FE HEC A 90 1555 1555 1.98 LINK SD MET A 61 FE HEC A 90 1555 1555 2.44 SITE 1 NUL 1 HEC A 90 SITE 1 AC1 19 ASN A 14 CYS A 15 CYS A 18 HIS A 19 SITE 2 AC1 19 ASN A 24 ILE A 27 HIS A 30 THR A 31 SITE 3 AC1 19 LEU A 32 PHE A 40 LEU A 41 ILE A 50 SITE 4 AC1 19 GLN A 53 ILE A 54 LYS A 58 GLY A 59 SITE 5 AC1 19 ALA A 60 MET A 61 TRP A 64 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
Complete list - 16 20 Bytes