Header list of 1put.pdb file
Complete list - v 29 2 Bytes
HEADER ELECTRON TRANSPORT 09-JUL-94 1PUT TITLE AN NMR-DERIVED MODEL FOR THE SOLUTION STRUCTURE OF OXIDIZED TITLE 2 PUTIDAREDOXIN, A 2FE, 2-S FERREDOXIN FROM PSEUDOMONAS COMPND MOL_ID: 1; COMPND 2 MOLECULE: PUTIDAREDOXIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS PUTIDA; SOURCE 3 ORGANISM_TAXID: 303 KEYWDS ELECTRON TRANSPORT EXPDTA SOLUTION NMR NUMMDL 12 AUTHOR T.C.POCHAPSKY,X.M.YE,G.RATNASWAMY,T.A.LYONS REVDAT 4 29-NOV-17 1PUT 1 REMARK HELIX REVDAT 3 24-FEB-09 1PUT 1 VERSN REVDAT 2 01-APR-03 1PUT 1 JRNL REVDAT 1 30-SEP-94 1PUT 0 JRNL AUTH T.C.POCHAPSKY,X.M.YE,G.RATNASWAMY,T.A.LYONS JRNL TITL AN NMR-DERIVED MODEL FOR THE SOLUTION STRUCTURE OF OXIDIZED JRNL TITL 2 PUTIDAREDOXIN, A 2-FE, 2-S FERREDOXIN FROM PSEUDOMONAS. JRNL REF BIOCHEMISTRY V. 33 6424 1994 JRNL REFN ISSN 0006-2960 JRNL PMID 8204575 JRNL DOI 10.1021/BI00187A006 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH T.C.POCHAPSKY,G.RATNASWAMY,A.PATERA REMARK 1 TITL REDOX-DEPENDENT 1H NMR SPECTRAL FEATURES AND TERTIARY REMARK 1 TITL 2 STRUCTURAL CONSTRAINTS ON THE C-TERMINAL REGION OF REMARK 1 TITL 3 PUTIDAREDOXIN REMARK 1 REF BIOCHEMISTRY V. 33 6433 1994 REMARK 1 REFN ISSN 0006-2960 REMARK 1 REFERENCE 2 REMARK 1 AUTH G.RATNASWAMY,T.C.POCHAPSKY REMARK 1 TITL CHARACTERIZATION OF HYPERFINE-SHIFTED 1H RESONANCES IN REMARK 1 TITL 2 OXIDIZED AND REDUCED PUTIDAREDOXIN, AN FE2S2FERREDOXIN FROM REMARK 1 TITL 3 PSEUDOMONUS PUTIDA REMARK 1 REF MAGN.RESON.CHEM. V. 31 S73 1994 REMARK 1 REFN ISSN 0749-1581 REMARK 1 REFERENCE 3 REMARK 1 AUTH X.M.YE,T.C.POCHAPSKY,S.S.POCHAPSKY REMARK 1 TITL 1H NMR SEQUENTIAL ASSIGNMENTS AND IDENTIFICATION OF REMARK 1 TITL 2 SECONDARY STRUCTURAL ELEMENTS IN OXIDIZED PUTIDAREDOXIN, AN REMARK 1 TITL 3 ELECTRON-TRANSFER PROTEIN FROM PSEUDOMONAS REMARK 1 REF BIOCHEMISTRY V. 31 1961 1992 REMARK 1 REFN ISSN 0006-2960 REMARK 1 REFERENCE 4 REMARK 1 AUTH T.C.POCHAPSKY,X.M.YE REMARK 1 TITL 1H NMR IDENTIFICATION OF A BETA-SHEET STRUCTURE AND REMARK 1 TITL 2 DESCRIPTION OF FOLDING TOPOLOGY IN PUTIDAREDOXIN REMARK 1 REF BIOCHEMISTRY V. 30 3850 1991 REMARK 1 REFN ISSN 0006-2960 REMARK 1 REFERENCE 5 REMARK 1 AUTH W.R.RYPNIEWSKI,D.R.BREITER,M.M.BENNING,G.WESENBERG,B.H.OH, REMARK 1 AUTH 2 J.L.MARKLEY,I.RAYMENT,H.M.HOLDEN REMARK 1 TITL CRYSTALLIZATION AND STRUCTURE DETERMINATION TO 2.5-ANGSTROMS REMARK 1 TITL 2 RESOLUTION OF THE OXIDIZED [2FE-2S] FERREDOXIN ISOLATED FROM REMARK 1 TITL 3 ANABAENA 7120 REMARK 1 REF BIOCHEMISTRY V. 30 4126 1991 REMARK 1 REFN ISSN 0006-2960 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1PUT COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000175862. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : NULL REMARK 210 PH : NULL REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : NULL REMARK 210 SPECTROMETER MODEL : NULL REMARK 210 SPECTROMETER MANUFACTURER : NULL REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : NULL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 12 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL 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 1 ALA A 18 172.80 -46.31 REMARK 500 1 ASN A 30 -27.78 -38.80 REMARK 500 1 ILE A 35 40.66 -105.83 REMARK 500 1 VAL A 36 -151.51 -143.16 REMARK 500 1 ASP A 38 -53.95 -141.50 REMARK 500 1 CYS A 48 41.61 -86.72 REMARK 500 1 ASN A 53 -176.79 -64.61 REMARK 500 1 PRO A 61 172.14 -59.16 REMARK 500 1 ALA A 62 59.39 -110.14 REMARK 500 1 ASN A 64 -160.27 -57.11 REMARK 500 1 VAL A 74 171.95 -46.27 REMARK 500 1 ALA A 76 -152.52 -126.43 REMARK 500 1 CYS A 86 31.76 -86.83 REMARK 500 1 GLN A 87 24.24 -153.36 REMARK 500 1 PRO A 102 177.75 -52.99 REMARK 500 2 LEU A 15 -176.03 -176.12 REMARK 500 2 ALA A 18 172.15 -46.55 REMARK 500 2 VAL A 36 133.73 -170.03 REMARK 500 2 ASP A 38 -89.63 -161.73 REMARK 500 2 SER A 42 88.43 -59.71 REMARK 500 2 ALA A 43 99.68 -60.29 REMARK 500 2 SER A 44 22.06 -160.03 REMARK 500 2 CYS A 45 -157.89 -116.05 REMARK 500 2 ALA A 46 12.80 -147.81 REMARK 500 2 CYS A 48 42.66 -86.66 REMARK 500 2 PRO A 61 -166.03 -56.33 REMARK 500 2 ALA A 62 58.91 -110.39 REMARK 500 2 ALA A 63 107.46 -43.41 REMARK 500 2 ASN A 64 -160.93 -56.86 REMARK 500 2 CYS A 73 45.07 -99.99 REMARK 500 2 ALA A 76 -151.23 -124.86 REMARK 500 2 GLN A 87 42.85 -89.47 REMARK 500 2 PRO A 102 -171.21 -53.76 REMARK 500 2 ARG A 104 -157.96 -120.86 REMARK 500 2 GLN A 105 24.40 -154.97 REMARK 500 3 HIS A 8 -89.60 -41.87 REMARK 500 3 ASP A 9 74.95 -112.23 REMARK 500 3 ALA A 18 174.22 -47.15 REMARK 500 3 ASP A 38 -59.93 -162.31 REMARK 500 3 ALA A 43 -93.66 -59.78 REMARK 500 3 SER A 44 60.08 -160.40 REMARK 500 3 ALA A 46 20.49 -146.92 REMARK 500 3 CYS A 48 42.55 -87.18 REMARK 500 3 PRO A 61 173.43 -55.79 REMARK 500 3 ALA A 62 62.52 -110.72 REMARK 500 3 ALA A 63 126.52 -38.92 REMARK 500 3 ASN A 64 -174.91 -51.39 REMARK 500 3 ALA A 76 -148.94 -116.94 REMARK 500 3 ARG A 83 -162.34 -162.33 REMARK 500 3 GLN A 105 23.38 -152.20 REMARK 500 REMARK 500 THIS ENTRY HAS 193 RAMACHANDRAN OUTLIERS. 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 FES A 107 FE1 REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 45 SG REMARK 620 2 FES A 107 S1 105.1 REMARK 620 3 FES A 107 S2 105.1 105.0 REMARK 620 4 CYS A 39 SG 129.4 105.5 104.6 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 FES A 107 FE2 REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 48 SG REMARK 620 2 FES A 107 S1 105.7 REMARK 620 3 FES A 107 S2 104.0 104.9 REMARK 620 4 CYS A 86 SG 130.3 105.3 104.3 REMARK 620 N 1 2 3 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: FS2 REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: NULL REMARK 800 REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES A 107 DBREF 1PUT A 1 106 UNP P00259 PUTX_PSEPU 1 106 SEQADV 1PUT GLN A 14 UNP P00259 GLU 14 CONFLICT SEQRES 1 A 106 SER LYS VAL VAL TYR VAL SER HIS ASP GLY THR ARG ARG SEQRES 2 A 106 GLN LEU ASP VAL ALA ASP GLY VAL SER LEU MET GLN ALA SEQRES 3 A 106 ALA VAL SER ASN GLY ILE TYR ASP ILE VAL GLY ASP CYS SEQRES 4 A 106 GLY GLY SER ALA SER CYS ALA THR CYS HIS VAL TYR VAL SEQRES 5 A 106 ASN GLU ALA PHE THR ASP LYS VAL PRO ALA ALA ASN GLU SEQRES 6 A 106 ARG GLU ILE GLY MET LEU GLU CYS VAL THR ALA GLU LEU SEQRES 7 A 106 LYS PRO ASN SER ARG LEU CYS CYS GLN ILE ILE MET THR SEQRES 8 A 106 PRO GLU LEU ASP GLY ILE VAL VAL ASP VAL PRO ASP ARG SEQRES 9 A 106 GLN TRP HET FES A 107 4 HETNAM FES FE2/S2 (INORGANIC) CLUSTER FORMUL 2 FES FE2 S2 HELIX 1 D LEU A 23 GLY A 31 1 9 HELIX 2 F THR A 57 PRO A 61 1 5 HELIX 3 G GLU A 65 CYS A 73 1 9 SHEET 1 A 5 ARG A 12 VAL A 17 0 SHEET 2 A 5 SER A 1 VAL A 6 -1 N TYR A 5 O ARG A 13 SHEET 3 A 5 VAL A 98 VAL A 101 1 N VAL A 99 O VAL A 4 SHEET 4 A 5 VAL A 50 ASN A 53 -1 O TYR A 51 N ASP A 100 SHEET 5 A 5 SER A 82 ARG A 83 -1 N ARG A 83 O VAL A 50 SHEET 1 B 2 ILE A 89 MET A 90 0 SHEET 2 B 2 VAL A 21 SER A 22 -1 O VAL A 21 N MET A 90 LINK FE1 FES A 107 SG CYS A 45 1555 1555 2.20 LINK FE1 FES A 107 SG CYS A 39 1555 1555 2.20 LINK FE2 FES A 107 SG CYS A 48 1555 1555 2.20 LINK FE2 FES A 107 SG CYS A 86 1555 1555 2.19 SITE 1 FS2 4 CYS A 39 CYS A 45 CYS A 48 CYS A 86 SITE 1 AC1 11 GLY A 37 ASP A 38 CYS A 39 GLY A 40 SITE 2 AC1 11 ALA A 43 SER A 44 CYS A 45 CYS A 48 SITE 3 AC1 11 MET A 70 LEU A 84 CYS A 86 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 - v 29 2 Bytes