Header list of 1e10.pdb file
Complete list - r 25 2 Bytes
HEADER IRON-SULFUR PROTEIN 12-APR-00 1E10 TITLE [2FE-2S]-FERREDOXIN FROM HALOBACTERIUM SALINARUM COMPND MOL_ID: 1; COMPND 2 MOLECULE: FERREDOXIN; COMPND 3 CHAIN: A SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HALOBACTERIUM HALOBIUM; SOURCE 3 ORGANISM_TAXID: 2242 KEYWDS IRON-SULFUR PROTEIN, NMR, FERREDOXIN, HALOBACTERIUM KEYWDS 2 SALINARUM, HALOPHILIC EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR B.-L.MARG,K.SCHWEIMER,D.OESTERHELT,P.ROESCH,H.STICHT REVDAT 3 24-FEB-09 1E10 1 VERSN REVDAT 2 01-AUG-03 1E10 1 REMARK HET LINK ATOM REVDAT 2 2 HETATM REVDAT 1 09-APR-01 1E10 0 JRNL AUTH B.MARG,K.SCHWEIMER,H.STICHT,D.OESTERHELT JRNL TITL A TWO-ALPHA-HELIX EXTRA DOMAIN MEDIATES THE JRNL TITL 2 HALOPHILIC CHARACTER OF A PLANT-TYPE FERREDOXIN JRNL TITL 3 FROM HALOPHILIC ARCHAEA. JRNL REF BIOCHEMISTRY V. 44 29 2005 JRNL REFN ISSN 0006-2960 JRNL PMID 15628843 JRNL DOI 10.1021/BI0485169 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH K.SCHWEIMER,B.-L.MARG,D.OESTERHELT,P.ROESCH, REMARK 1 AUTH 2 H.STICHT REMARK 1 TITL SEQUENCE-SPECIFIC 1H, 13C AND 15N RESONANCE REMARK 1 TITL 2 ASSIGNMENTS AND SECONDARY STRUCTURE OF [2FE-2S] REMARK 1 TITL 3 FERREDOXIN FROM HALOBACTERIUM SALINARUM REMARK 1 REF J.BIOMOL.NMR V. 16 347 2000 REMARK 1 REFN ISSN 0925-2738 REMARK 1 PMID 10826887 REMARK 1 DOI 10.1023/A:1008381016258 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.851 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN REMARK 3 THE JRNL CITATION ABOVE. FOR RESIDUES 60-71, 87, AND 100-104 REMARK 3 NO NMR DISTANCE RESTRAINTS WERE OBTAINED BECAUSE OF THE REMARK 3 PROXIMITY TO THE PARAMAGNETIC IRON-SULFUR CLUSTER. THE REMARK 3 CORRESPONDING RESIDUES WERE NOT RESTRAINED DURING THE REMARK 3 STRUCTURE CALCULATION AND ARE THEREFORE ILL-DEFINED. REMARK 4 REMARK 4 1E10 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-APR-00. REMARK 100 THE PDBE ID CODE IS EBI-4842. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 288 REMARK 210 PH : 6.4 REMARK 210 IONIC STRENGTH : 500 MM REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 10% WATER/90% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 1H-1H NOESY, 1H-1H TOCSY, REMARK 210 1H-15N HSQC, 1H-13C CT-HSQC, REMARK 210 15N-EDITED NOESY(3D),13C-EDITED NOE REMARK 210 HNCO, HNCA, HNCACB, CBCA(CO)NH REMARK 210 HBHA(CO)NH, HNHA, HCCH-COSY, HCCH-T REMARK 210 SPECTROMETER FIELD STRENGTH : 600 REMARK 210 SPECTROMETER MODEL : DRX600 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRVIEW, NDEE REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 60 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT REMARK 210 VIOLATION, LOWEST ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING HETERONUCLEAR REMARK 210 MULTIDIMENSIONAL NMR USING 15N- AND 13C,15N LABELED REMARK 210 FERREDOXIN SAMPLES 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 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT 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 O ASP A 22 - H GLU A 25 1.54 REMARK 500 O PHE A 24 - HH TYR A 37 1.52 REMARK 500 O ASP A 33 - H ASP A 36 1.51 REMARK 500 H ASP A 81 - O SER A 105 1.54 REMARK 500 O ALA A 117 - H LEU A 120 1.50 REMARK 500 NZ LYS A 118 - O ACE A 129 2.20 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 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 ASP A 20 -72.24 -71.37 REMARK 500 1 PHE A 61 92.65 -48.48 REMARK 500 1 SER A 62 43.61 -85.12 REMARK 500 1 ALA A 67 -179.65 50.92 REMARK 500 1 ALA A 69 33.94 -171.04 REMARK 500 1 ASN A 70 69.97 -150.13 REMARK 500 1 CYS A 71 -120.96 -60.98 REMARK 500 1 ALA A 72 77.40 -173.28 REMARK 500 1 ASP A 83 -171.16 -57.50 REMARK 500 1 MET A 84 -179.15 -49.37 REMARK 500 1 GLN A 86 -53.11 -178.40 REMARK 500 1 ARG A 99 -169.11 -177.76 REMARK 500 1 CYS A 102 -76.67 -55.02 REMARK 500 1 ASP A 109 -71.37 -85.04 REMARK 500 1 LEU A 120 152.67 -41.76 REMARK 500 2 TRP A 16 -165.32 -109.46 REMARK 500 2 ASP A 20 -82.11 -79.07 REMARK 500 2 LEU A 23 -33.09 -39.51 REMARK 500 2 SER A 62 82.59 -169.39 REMARK 500 2 ALA A 67 94.49 52.72 REMARK 500 2 ALA A 69 -64.86 -94.86 REMARK 500 2 CYS A 71 -103.12 -104.90 REMARK 500 2 ALA A 72 61.32 -179.53 REMARK 500 2 MET A 84 91.95 -62.71 REMARK 500 2 ARG A 99 96.58 176.04 REMARK 500 2 THR A 101 77.32 43.56 REMARK 500 3 LEU A 32 170.20 -50.89 REMARK 500 3 ASP A 36 -45.29 -132.11 REMARK 500 3 SER A 62 29.70 -140.16 REMARK 500 3 CYS A 63 -167.91 -72.48 REMARK 500 3 ARG A 64 39.92 -164.15 REMARK 500 3 CYS A 68 -80.98 -155.90 REMARK 500 3 ALA A 69 25.28 46.43 REMARK 500 3 CYS A 71 -159.91 -58.29 REMARK 500 3 ALA A 72 86.15 -161.55 REMARK 500 3 GLN A 85 -155.27 -172.12 REMARK 500 3 ASP A 97 22.15 49.39 REMARK 500 3 CYS A 102 -88.63 -68.14 REMARK 500 4 TRP A 16 -169.45 -111.30 REMARK 500 4 ASP A 19 19.17 -143.75 REMARK 500 4 CYS A 63 94.79 -48.33 REMARK 500 4 ALA A 67 -165.63 64.79 REMARK 500 4 CYS A 68 77.32 -150.09 REMARK 500 4 CYS A 71 96.89 -66.53 REMARK 500 4 GLN A 85 -56.51 -163.16 REMARK 500 4 ARG A 99 130.76 -178.39 REMARK 500 5 SER A 62 -35.97 -172.80 REMARK 500 5 ALA A 69 -58.46 -122.76 REMARK 500 5 CYS A 71 89.55 175.41 REMARK 500 5 VAL A 75 109.70 -54.11 REMARK 500 5 GLU A 79 147.82 -175.02 REMARK 500 5 ASP A 97 14.68 59.13 REMARK 500 5 ARG A 99 -143.36 -111.77 REMARK 500 5 THR A 101 24.93 49.79 REMARK 500 5 ALA A 107 -73.79 -111.03 REMARK 500 6 PHE A 61 147.43 67.97 REMARK 500 6 SER A 62 122.18 -178.44 REMARK 500 6 CYS A 63 65.18 -65.59 REMARK 500 6 ALA A 69 -89.70 -84.73 REMARK 500 6 ASN A 70 156.02 179.53 REMARK 500 6 ALA A 72 87.67 176.68 REMARK 500 6 ASP A 83 162.97 -46.08 REMARK 500 6 GLN A 85 -36.49 -178.19 REMARK 500 6 ILE A 87 99.33 -46.58 REMARK 500 6 ASP A 97 16.69 58.53 REMARK 500 6 LEU A 100 107.28 -58.36 REMARK 500 6 ASP A 109 -78.48 -53.37 REMARK 500 6 ALA A 117 -27.56 -37.13 REMARK 500 7 ASP A 19 26.62 -158.04 REMARK 500 7 ASP A 21 49.44 -79.11 REMARK 500 7 ASP A 36 -53.04 -120.29 REMARK 500 7 PHE A 61 72.58 -69.09 REMARK 500 7 ARG A 64 77.70 -169.60 REMARK 500 7 ALA A 69 10.99 -143.75 REMARK 500 7 CYS A 71 -136.51 -116.20 REMARK 500 7 ALA A 72 58.58 -144.25 REMARK 500 7 GLN A 85 -153.18 -173.13 REMARK 500 7 GLN A 86 -87.38 -148.26 REMARK 500 7 ILE A 87 170.91 56.54 REMARK 500 7 LEU A 88 177.68 61.16 REMARK 500 7 ARG A 99 -165.52 -162.32 REMARK 500 7 ASN A 116 47.34 74.85 REMARK 500 7 VAL A 127 -73.23 -58.86 REMARK 500 8 LEU A 32 -177.14 -51.54 REMARK 500 8 ASP A 36 -51.43 -121.15 REMARK 500 8 CYS A 63 -175.40 -68.61 REMARK 500 8 ALA A 67 103.62 -45.32 REMARK 500 8 ALA A 69 -91.08 -61.10 REMARK 500 8 CYS A 71 -144.95 -95.81 REMARK 500 8 MET A 84 98.59 -66.43 REMARK 500 8 LEU A 88 -174.70 53.09 REMARK 500 8 ARG A 99 120.44 -175.97 REMARK 500 8 ASP A 109 -72.30 -66.69 REMARK 500 9 PHE A 61 171.96 62.84 REMARK 500 9 CYS A 63 64.36 -154.51 REMARK 500 9 ALA A 67 -179.07 -59.64 REMARK 500 9 ALA A 69 32.35 -140.17 REMARK 500 9 ASN A 70 -126.23 -120.72 REMARK 500 9 CYS A 71 173.27 57.00 REMARK 500 9 ALA A 72 117.18 -168.81 REMARK 500 9 GLN A 86 67.33 -100.50 REMARK 500 9 THR A 101 61.66 -108.44 REMARK 500 9 ASN A 116 43.42 70.51 REMARK 500 10 LEU A 32 -176.42 -50.53 REMARK 500 10 ILE A 48 -74.17 -41.85 REMARK 500 10 PHE A 61 174.81 52.45 REMARK 500 10 CYS A 68 40.06 -108.09 REMARK 500 10 ALA A 69 71.76 67.77 REMARK 500 10 ASN A 70 131.03 66.01 REMARK 500 10 CYS A 71 -138.16 -70.66 REMARK 500 10 GLN A 86 60.74 -158.14 REMARK 500 10 ILE A 87 -61.54 -121.57 REMARK 500 10 ASP A 97 17.70 55.03 REMARK 500 10 ARG A 99 -173.75 178.15 REMARK 500 10 CYS A 102 -90.42 -62.76 REMARK 500 10 ALA A 107 -65.50 -97.55 REMARK 500 10 ASP A 109 -77.90 -61.67 REMARK 500 10 ASN A 116 62.44 76.70 REMARK 500 11 ASP A 20 -71.20 -59.63 REMARK 500 11 GLU A 41 103.62 -59.61 REMARK 500 11 PHE A 61 -163.18 -107.94 REMARK 500 11 ALA A 67 98.56 177.15 REMARK 500 11 CYS A 68 -91.39 -133.17 REMARK 500 11 ALA A 69 13.23 58.18 REMARK 500 11 ASN A 70 17.90 -154.49 REMARK 500 11 CYS A 71 -139.08 42.51 REMARK 500 11 ALA A 72 72.52 -167.80 REMARK 500 11 GLN A 85 131.33 -177.75 REMARK 500 11 GLN A 86 -149.83 66.05 REMARK 500 11 ARG A 99 -155.26 171.21 REMARK 500 11 LEU A 100 -153.27 67.48 REMARK 500 11 THR A 101 -89.45 57.08 REMARK 500 11 CYS A 102 168.09 -44.00 REMARK 500 11 ASP A 109 -75.60 -47.82 REMARK 500 11 ASN A 116 39.44 72.18 REMARK 500 11 VAL A 127 153.83 -44.48 REMARK 500 12 ASP A 36 -61.33 -100.60 REMARK 500 12 ILE A 48 -70.85 -49.27 REMARK 500 12 PHE A 61 72.11 -66.85 REMARK 500 12 ALA A 67 164.80 55.03 REMARK 500 12 CYS A 68 33.50 -170.93 REMARK 500 12 ALA A 69 96.33 55.33 REMARK 500 12 ASN A 70 159.92 57.95 REMARK 500 12 CYS A 71 -78.84 -106.83 REMARK 500 12 ALA A 72 88.96 174.28 REMARK 500 12 GLN A 85 -61.73 -153.99 REMARK 500 12 CYS A 102 -72.04 -71.62 REMARK 500 12 ASP A 109 -84.34 -44.49 REMARK 500 12 ASN A 116 54.85 72.42 REMARK 500 12 VAL A 127 153.34 -47.24 REMARK 500 13 PHE A 61 79.92 47.54 REMARK 500 13 SER A 62 -178.19 -59.19 REMARK 500 13 CYS A 68 -84.48 -59.22 REMARK 500 13 ASN A 70 109.21 -172.95 REMARK 500 13 ASP A 97 28.55 48.31 REMARK 500 13 CYS A 102 -51.51 -145.72 REMARK 500 13 VAL A 127 168.83 -46.08 REMARK 500 14 PHE A 61 165.09 66.93 REMARK 500 14 CYS A 63 -168.55 -59.21 REMARK 500 14 ARG A 64 148.57 61.10 REMARK 500 14 ASN A 70 63.38 -161.50 REMARK 500 14 CYS A 71 165.21 -44.80 REMARK 500 14 GLN A 85 141.27 -174.94 REMARK 500 14 GLN A 86 -168.60 44.09 REMARK 500 14 ILE A 87 -83.61 -69.11 REMARK 500 14 LEU A 88 167.01 65.06 REMARK 500 14 ASP A 109 -70.17 -56.40 REMARK 500 14 ASN A 116 47.80 73.70 REMARK 500 15 ILE A 48 -78.09 -42.14 REMARK 500 15 CYS A 63 -147.46 33.09 REMARK 500 15 ARG A 64 52.27 -166.50 REMARK 500 15 ALA A 67 82.41 -62.59 REMARK 500 15 CYS A 71 -96.39 -75.30 REMARK 500 15 ALA A 72 36.25 -178.75 REMARK 500 15 MET A 84 92.70 -65.68 REMARK 500 15 ILE A 87 -69.56 -129.14 REMARK 500 15 ASP A 97 17.87 59.27 REMARK 500 16 PHE A 61 86.60 65.24 REMARK 500 16 ALA A 67 77.15 -112.42 REMARK 500 16 CYS A 68 -81.28 -77.22 REMARK 500 16 ASN A 70 -68.11 -94.19 REMARK 500 16 CYS A 71 172.59 67.16 REMARK 500 16 ALA A 72 70.02 -151.54 REMARK 500 16 GLN A 86 -163.09 -69.61 REMARK 500 16 ILE A 87 168.13 59.58 REMARK 500 16 LEU A 88 106.38 61.97 REMARK 500 16 ARG A 99 160.40 175.42 REMARK 500 16 ASP A 109 -83.63 -58.10 REMARK 500 16 ALA A 117 -25.87 -39.31 REMARK 500 17 ASP A 20 -73.10 -78.62 REMARK 500 17 LEU A 32 -178.38 -52.91 REMARK 500 17 ASP A 36 -50.02 -125.42 REMARK 500 17 ALA A 43 152.39 -43.22 REMARK 500 17 SER A 62 80.92 -160.74 REMARK 500 17 ARG A 64 -95.97 47.50 REMARK 500 17 ALA A 69 39.02 -90.17 REMARK 500 17 ASN A 70 94.06 -171.15 REMARK 500 17 CYS A 71 -145.18 -85.53 REMARK 500 17 VAL A 75 116.04 -38.92 REMARK 500 17 GLU A 79 149.42 -176.48 REMARK 500 17 GLN A 85 -84.11 -167.18 REMARK 500 17 ASP A 97 28.33 48.97 REMARK 500 17 ARG A 99 -150.96 -163.29 REMARK 500 17 CYS A 102 -125.58 -105.65 REMARK 500 17 ASP A 109 -82.47 -60.45 REMARK 500 17 LEU A 120 172.86 -46.38 REMARK 500 17 ARG A 126 50.55 -114.30 REMARK 500 17 VAL A 127 172.90 -46.76 REMARK 500 18 ASP A 19 38.72 -150.11 REMARK 500 18 ASP A 20 -97.20 -79.66 REMARK 500 18 ASP A 21 -105.75 -80.07 REMARK 500 18 ASP A 22 44.39 -155.37 REMARK 500 18 TYR A 47 155.06 -49.88 REMARK 500 18 SER A 62 70.33 -160.26 REMARK 500 18 CYS A 63 -74.30 -171.06 REMARK 500 18 ARG A 64 -152.83 -138.94 REMARK 500 18 CYS A 68 83.72 69.31 REMARK 500 18 ALA A 69 -169.36 -126.26 REMARK 500 18 ASN A 70 88.57 55.05 REMARK 500 18 CYS A 71 -151.15 -162.00 REMARK 500 18 ALA A 72 98.76 67.89 REMARK 500 18 MET A 84 86.56 -58.22 REMARK 500 18 GLN A 86 177.31 55.18 REMARK 500 18 ARG A 99 123.04 -176.62 REMARK 500 18 ASN A 116 51.36 70.90 REMARK 500 18 VAL A 127 164.43 -49.78 REMARK 500 19 ASP A 19 13.64 -147.53 REMARK 500 19 ASP A 36 -51.07 -122.46 REMARK 500 19 ARG A 64 -36.19 -134.06 REMARK 500 19 CYS A 71 -102.79 -67.04 REMARK 500 19 ALA A 72 24.48 -169.68 REMARK 500 19 GLU A 79 132.22 -171.38 REMARK 500 19 MET A 82 -169.01 -165.17 REMARK 500 19 MET A 84 85.58 -63.20 REMARK 500 19 GLN A 85 36.32 -167.50 REMARK 500 19 ASP A 109 -79.42 -47.81 REMARK 500 19 ALA A 117 -27.50 -38.61 REMARK 500 19 LEU A 120 99.85 -47.22 REMARK 500 20 ASP A 19 14.60 -150.19 REMARK 500 20 SER A 62 59.19 -170.94 REMARK 500 20 ALA A 69 -148.74 -105.50 REMARK 500 20 CYS A 71 76.90 -171.49 REMARK 500 20 ALA A 72 88.39 -176.37 REMARK 500 20 GLU A 79 136.26 -171.44 REMARK 500 20 MET A 84 105.27 -49.08 REMARK 500 20 GLN A 85 32.83 -177.35 REMARK 500 20 ILE A 87 -39.80 -155.42 REMARK 500 20 ASP A 109 -80.31 -51.30 REMARK 500 20 LEU A 120 152.51 -42.14 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 1 ARG A 64 0.31 SIDE CHAIN REMARK 500 1 ARG A 99 0.32 SIDE CHAIN REMARK 500 1 ARG A 126 0.25 SIDE CHAIN REMARK 500 2 ARG A 64 0.17 SIDE CHAIN REMARK 500 2 ARG A 99 0.25 SIDE CHAIN REMARK 500 2 ARG A 126 0.17 SIDE CHAIN REMARK 500 3 ARG A 64 0.22 SIDE CHAIN REMARK 500 3 ARG A 99 0.23 SIDE CHAIN REMARK 500 3 ARG A 126 0.31 SIDE CHAIN REMARK 500 4 ARG A 64 0.29 SIDE CHAIN REMARK 500 4 ARG A 99 0.18 SIDE CHAIN REMARK 500 4 ARG A 126 0.24 SIDE CHAIN REMARK 500 5 ARG A 64 0.21 SIDE CHAIN REMARK 500 5 ARG A 99 0.29 SIDE CHAIN REMARK 500 5 ARG A 126 0.22 SIDE CHAIN REMARK 500 6 ARG A 64 0.32 SIDE CHAIN REMARK 500 6 ARG A 99 0.22 SIDE CHAIN REMARK 500 6 ARG A 126 0.20 SIDE CHAIN REMARK 500 7 ARG A 64 0.29 SIDE CHAIN REMARK 500 7 ARG A 99 0.18 SIDE CHAIN REMARK 500 7 ARG A 126 0.27 SIDE CHAIN REMARK 500 8 ARG A 64 0.30 SIDE CHAIN REMARK 500 8 ARG A 99 0.20 SIDE CHAIN REMARK 500 8 ARG A 126 0.26 SIDE CHAIN REMARK 500 9 ARG A 64 0.25 SIDE CHAIN REMARK 500 9 ARG A 99 0.28 SIDE CHAIN REMARK 500 10 ARG A 64 0.27 SIDE CHAIN REMARK 500 10 ARG A 99 0.31 SIDE CHAIN REMARK 500 10 ARG A 126 0.16 SIDE CHAIN REMARK 500 11 ARG A 64 0.31 SIDE CHAIN REMARK 500 11 ARG A 99 0.32 SIDE CHAIN REMARK 500 11 ARG A 126 0.18 SIDE CHAIN REMARK 500 12 ARG A 64 0.26 SIDE CHAIN REMARK 500 12 ARG A 99 0.13 SIDE CHAIN REMARK 500 12 ARG A 126 0.22 SIDE CHAIN REMARK 500 13 ARG A 64 0.26 SIDE CHAIN REMARK 500 13 ARG A 99 0.30 SIDE CHAIN REMARK 500 13 ARG A 126 0.32 SIDE CHAIN REMARK 500 14 ARG A 64 0.16 SIDE CHAIN REMARK 500 14 ARG A 99 0.23 SIDE CHAIN REMARK 500 14 ARG A 126 0.29 SIDE CHAIN REMARK 500 15 ARG A 64 0.15 SIDE CHAIN REMARK 500 15 ARG A 99 0.20 SIDE CHAIN REMARK 500 15 ARG A 126 0.23 SIDE CHAIN REMARK 500 16 ARG A 64 0.27 SIDE CHAIN REMARK 500 16 ARG A 99 0.24 SIDE CHAIN REMARK 500 16 ARG A 126 0.24 SIDE CHAIN REMARK 500 17 ARG A 64 0.13 SIDE CHAIN REMARK 500 17 ARG A 99 0.10 SIDE CHAIN REMARK 500 17 ARG A 126 0.31 SIDE CHAIN REMARK 500 18 ARG A 64 0.27 SIDE CHAIN REMARK 500 18 ARG A 99 0.25 SIDE CHAIN REMARK 500 18 ARG A 126 0.11 SIDE CHAIN REMARK 500 19 ARG A 64 0.28 SIDE CHAIN REMARK 500 19 ARG A 99 0.09 SIDE CHAIN REMARK 500 19 ARG A 126 0.24 SIDE CHAIN REMARK 500 20 ARG A 64 0.16 SIDE CHAIN REMARK 500 20 ARG A 99 0.14 SIDE CHAIN REMARK 500 20 ARG A 126 0.26 SIDE CHAIN 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 130 FE1 REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 63 SG REMARK 620 2 CYS A 68 SG 109.9 REMARK 620 3 FES A 130 S1 109.8 109.9 REMARK 620 4 FES A 130 S2 109.9 109.9 107.4 REMARK 620 5 FES A 130 FE2 124.8 125.3 53.7 53.7 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 FES A 130 FE2 REMARK 620 N RES CSSEQI ATOM REMARK 620 1 FES A 130 FE1 REMARK 620 2 FES A 130 S1 53.7 REMARK 620 3 FES A 130 S2 53.7 107.4 REMARK 620 4 CYS A 71 SG 125.4 110.0 109.9 REMARK 620 5 CYS A 102 SG 124.8 110.0 109.7 109.8 REMARK 620 N 1 2 3 4 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACE A 129 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES A 130 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1E0Z RELATED DB: PDB REMARK 900 [2FE-2S]-FERREDOXIN FROM HALOBACTERIUM SALINARUM DBREF 1E10 A 1 128 UNP P00216 FER_HALHA 1 128 SEQRES 1 A 128 PRO THR VAL GLU TYR LEU ASN TYR GLU THR LEU ASP ASP SEQRES 2 A 128 GLN GLY TRP ASP MET ASP ASP ASP ASP LEU PHE GLU LYS SEQRES 3 A 128 ALA ALA ASP ALA GLY LEU ASP GLY GLU ASP TYR GLY THR SEQRES 4 A 128 MET GLU VAL ALA GLU GLY GLU TYR ILE LEU GLU ALA ALA SEQRES 5 A 128 GLU ALA GLN GLY TYR ASP TRP PRO PHE SER CYS ARG ALA SEQRES 6 A 128 GLY ALA CYS ALA ASN CYS ALA SER ILE VAL LYS GLU GLY SEQRES 7 A 128 GLU ILE ASP MET ASP MET GLN GLN ILE LEU SER ASP GLU SEQRES 8 A 128 GLU VAL GLU GLU LYS ASP VAL ARG LEU THR CYS ILE GLY SEQRES 9 A 128 SER PRO ALA ALA ASP GLU VAL LYS ILE VAL TYR ASN ALA SEQRES 10 A 128 LYS HIS LEU ASP TYR LEU GLN ASN ARG VAL ILE HET ACE A 129 6 HET FES A 130 4 HETNAM ACE ACETYL GROUP HETNAM FES FE2/S2 (INORGANIC) CLUSTER HETSYN ACE ACETYL GROUP HETSYN FES FE2/S2 (INORGANIC) CLUSTER FORMUL 2 ACE C2 H4 O FORMUL 3 FES FE2 S2 HELIX 1 1 TYR A 8 GLN A 14 1 7 HELIX 2 2 ASP A 22 GLY A 31 1 10 HELIX 3 3 TYR A 47 ALA A 54 1 8 HELIX 4 4 SER A 89 LYS A 96 1 8 HELIX 5 5 ASN A 116 LEU A 120 5 5 HELIX 6 6 LEU A 120 VAL A 127 1 8 SHEET 1 A 5 ASP A 36 GLU A 41 0 SHEET 2 A 5 THR A 2 ASN A 7 -1 N TYR A 5 O GLY A 38 SHEET 3 A 5 GLU A 110 TYR A 115 1 N VAL A 111 O THR A 2 SHEET 4 A 5 CYS A 71 GLU A 77 -1 N GLU A 77 O LYS A 112 SHEET 5 A 5 ASP A 97 THR A 101 -1 N ARG A 99 O SER A 73 SHEET 1 B 2 GLU A 79 ASP A 83 0 SHEET 2 B 2 ILE A 103 ALA A 107 -1 N SER A 105 O ASP A 81 LINK NZ LYS A 118 C ACE A 129 1555 1555 1.31 LINK FE2 FES A 130 SG CYS A 102 1555 1555 2.20 LINK FE1 FES A 130 SG CYS A 68 1555 1555 2.20 LINK FE2 FES A 130 SG CYS A 71 1555 1555 2.20 LINK FE1 FES A 130 SG CYS A 63 1555 1555 2.20 SITE 1 AC1 1 LYS A 118 SITE 1 AC2 5 SER A 62 CYS A 63 CYS A 68 CYS A 71 SITE 2 AC2 5 CYS A 102 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