Header list of 1e0z.pdb file
Complete list - r 25 2 Bytes
HEADER ELECTRON TRANSPORT 11-APR-00 1E0Z 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 SALINARIUM; SOURCE 3 ORGANISM_TAXID: 2242 KEYWDS ELECTRON TRANSPORT, IRON-SULFUR PROTEIN, NMR, FERREDOXIN, KEYWDS 2 HALOPHILIC EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR K.SCHWEIMER,B.MARG,D.OESTERHELT,P.ROESCH,H.STICHT REVDAT 4 01-SEP-09 1E0Z 1 VERSN REVDAT 3 24-FEB-09 1E0Z 1 VERSN REVDAT 2 18-JUL-03 1E0Z 1 REMARK REVDAT 1 12-APR-01 1E0Z 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 CONFORMATION OF THE CORRESPONDING RESIDUES WAS MODELLED BASED REMARK 3 ON THE GEOMETRY OF THE CRYSTAL STRUCTURE OF THE HOMOLOGUOUS REMARK 3 FERREDOXIN FROM HALOARCULA MARISMORTUI. REMARK 4 REMARK 4 1E0Z COMPLIES WITH FORMAT V. 3.20, 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-4406. 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 NO 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 HH TYR A 5 - O GLY A 34 1.59 REMARK 500 O ASP A 22 - H GLU A 25 1.51 REMARK 500 H ASP A 81 - O SER A 105 1.49 REMARK 500 O GLU A 91 - H GLU A 95 1.59 REMARK 500 O ALA A 117 - H LEU A 120 1.53 REMARK 500 O LEU A 123 - H ARG A 126 1.54 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 19 12.44 -142.54 REMARK 500 1 LEU A 32 -172.55 -59.07 REMARK 500 1 ILE A 48 -70.01 -54.62 REMARK 500 1 SER A 62 -58.51 -144.25 REMARK 500 1 ALA A 72 151.55 -44.47 REMARK 500 1 MET A 84 74.97 -69.39 REMARK 500 1 GLN A 86 78.43 -162.10 REMARK 500 1 ASN A 116 54.68 72.84 REMARK 500 2 ASP A 19 11.17 -150.47 REMARK 500 2 ILE A 48 -71.98 -40.42 REMARK 500 2 TYR A 57 -169.94 -77.06 REMARK 500 2 SER A 62 -58.57 -140.33 REMARK 500 2 ALA A 72 151.10 -48.40 REMARK 500 2 GLU A 77 146.82 170.38 REMARK 500 2 GLN A 85 -146.88 179.70 REMARK 500 2 GLN A 86 35.05 -146.47 REMARK 500 2 ASP A 97 25.30 46.97 REMARK 500 2 ASN A 116 55.97 74.32 REMARK 500 3 SER A 62 -58.72 -136.63 REMARK 500 3 ALA A 72 155.14 -43.01 REMARK 500 3 GLU A 77 144.83 176.51 REMARK 500 3 ASP A 83 176.77 -48.98 REMARK 500 3 GLN A 85 109.05 175.60 REMARK 500 3 ALA A 107 -72.02 -111.36 REMARK 500 3 ASP A 109 -74.29 -46.44 REMARK 500 3 ASN A 116 49.91 72.11 REMARK 500 4 SER A 62 -58.51 -144.31 REMARK 500 4 ALA A 72 153.17 -42.15 REMARK 500 4 GLU A 77 166.98 175.94 REMARK 500 4 MET A 84 177.38 -47.74 REMARK 500 4 GLN A 86 -36.41 -136.00 REMARK 500 4 ASP A 109 -76.25 -62.42 REMARK 500 4 ASN A 116 55.15 73.42 REMARK 500 5 ALA A 30 -66.39 -91.10 REMARK 500 5 LEU A 32 178.91 -49.50 REMARK 500 5 ILE A 48 -70.88 -43.65 REMARK 500 5 SER A 62 -58.57 -144.10 REMARK 500 5 ALA A 72 157.06 -43.01 REMARK 500 5 MET A 84 70.51 -65.97 REMARK 500 5 GLN A 85 135.62 -178.97 REMARK 500 5 ARG A 99 -152.43 -170.04 REMARK 500 5 ASP A 109 -78.77 -61.17 REMARK 500 6 LEU A 32 -171.68 -60.04 REMARK 500 6 SER A 62 -58.53 -144.26 REMARK 500 6 GLU A 77 151.71 176.65 REMARK 500 6 GLN A 85 -178.42 -170.49 REMARK 500 6 GLN A 86 19.16 -145.44 REMARK 500 6 LEU A 88 -169.97 -124.93 REMARK 500 6 ASN A 116 56.80 73.75 REMARK 500 7 ASP A 19 20.52 -154.51 REMARK 500 7 SER A 62 -58.58 -143.35 REMARK 500 7 ALA A 72 153.55 -46.55 REMARK 500 7 GLU A 77 157.26 174.17 REMARK 500 7 MET A 84 75.77 -63.71 REMARK 500 7 GLN A 85 157.43 175.66 REMARK 500 7 GLN A 86 85.37 -150.47 REMARK 500 7 ARG A 99 -160.43 -161.34 REMARK 500 7 ASN A 116 54.25 73.24 REMARK 500 8 SER A 62 -58.68 -144.29 REMARK 500 8 ALA A 72 150.84 -43.03 REMARK 500 8 GLU A 79 101.42 -168.91 REMARK 500 8 MET A 84 63.84 -69.58 REMARK 500 8 GLN A 85 60.00 -171.49 REMARK 500 8 ASP A 109 -74.53 -46.76 REMARK 500 8 ASN A 116 53.94 74.97 REMARK 500 9 SER A 62 -58.61 -144.14 REMARK 500 9 ALA A 72 156.85 -46.98 REMARK 500 9 GLU A 77 173.64 178.89 REMARK 500 9 GLN A 85 -163.35 -163.57 REMARK 500 9 GLN A 86 30.66 -171.12 REMARK 500 9 ASP A 97 23.73 47.17 REMARK 500 9 ALA A 107 -75.64 -117.02 REMARK 500 9 ALA A 108 171.17 -50.84 REMARK 500 9 ASN A 116 53.26 72.90 REMARK 500 10 SER A 62 -58.58 -143.41 REMARK 500 10 ALA A 72 155.91 -40.49 REMARK 500 10 GLU A 77 143.05 172.76 REMARK 500 10 ASP A 109 -74.79 -70.08 REMARK 500 10 ASN A 116 58.96 75.09 REMARK 500 10 GLN A 124 -73.81 -51.08 REMARK 500 11 LEU A 32 176.21 -53.25 REMARK 500 11 ASP A 36 -52.55 -123.51 REMARK 500 11 SER A 62 -58.60 -142.66 REMARK 500 11 ALA A 72 153.90 -44.25 REMARK 500 11 GLU A 77 132.57 177.46 REMARK 500 11 ASP A 109 -76.91 -57.68 REMARK 500 11 ASN A 116 53.43 72.49 REMARK 500 12 TRP A 16 -168.22 -113.42 REMARK 500 12 ASP A 20 -70.12 -55.24 REMARK 500 12 LEU A 32 -178.06 -51.60 REMARK 500 12 SER A 62 -58.46 -144.32 REMARK 500 12 ALA A 72 158.11 -42.57 REMARK 500 12 GLU A 77 152.66 172.01 REMARK 500 12 GLN A 85 138.73 -177.49 REMARK 500 12 ASP A 109 -75.43 -73.24 REMARK 500 12 ASN A 116 58.33 74.47 REMARK 500 12 LEU A 120 159.06 -43.31 REMARK 500 13 ASP A 19 21.10 -159.90 REMARK 500 13 ASP A 21 -105.25 -80.03 REMARK 500 13 ASP A 22 47.36 -141.15 REMARK 500 13 LEU A 23 -84.75 -46.53 REMARK 500 13 SER A 62 -58.59 -144.13 REMARK 500 13 ALA A 72 156.55 -45.77 REMARK 500 13 SER A 73 -159.44 -136.46 REMARK 500 13 GLU A 77 167.29 179.77 REMARK 500 13 GLN A 85 -167.35 -171.01 REMARK 500 13 ASN A 116 55.25 74.33 REMARK 500 14 ASP A 17 -167.83 -116.10 REMARK 500 14 ASP A 19 20.41 -152.52 REMARK 500 14 ASP A 21 -105.51 -80.14 REMARK 500 14 ASP A 22 40.80 -170.45 REMARK 500 14 SER A 62 -58.57 -144.18 REMARK 500 14 ALA A 72 154.68 -44.40 REMARK 500 14 GLU A 77 -177.06 -173.21 REMARK 500 14 GLN A 85 -75.80 -156.47 REMARK 500 14 GLN A 86 98.42 64.50 REMARK 500 14 ASP A 109 -75.46 -50.96 REMARK 500 14 ASN A 116 59.13 75.95 REMARK 500 14 LEU A 120 152.20 -42.81 REMARK 500 15 ASP A 36 -51.93 -127.79 REMARK 500 15 SER A 62 -59.24 -144.39 REMARK 500 15 ALA A 72 152.93 -39.02 REMARK 500 15 GLU A 77 169.07 173.39 REMARK 500 15 LEU A 120 95.50 -53.90 REMARK 500 16 TRP A 16 -168.63 -111.96 REMARK 500 16 SER A 62 -58.71 -144.13 REMARK 500 16 ALA A 72 157.99 -48.43 REMARK 500 16 GLU A 77 162.11 173.21 REMARK 500 16 GLN A 86 89.35 -160.50 REMARK 500 16 ASP A 109 -73.27 -72.72 REMARK 500 16 ASN A 116 57.44 74.89 REMARK 500 16 LEU A 120 96.34 -40.16 REMARK 500 17 ASP A 19 -30.00 -136.61 REMARK 500 17 ASP A 33 151.89 -45.63 REMARK 500 17 ILE A 48 -71.22 -44.27 REMARK 500 17 SER A 62 -58.50 -144.30 REMARK 500 17 ALA A 72 150.87 -43.70 REMARK 500 17 GLN A 85 -158.66 -161.11 REMARK 500 17 ARG A 99 -176.75 -175.02 REMARK 500 17 ASP A 109 -79.65 -68.57 REMARK 500 17 ASN A 116 66.16 81.59 REMARK 500 18 SER A 62 -58.50 -144.22 REMARK 500 18 ALA A 72 150.82 -44.65 REMARK 500 18 GLU A 77 166.86 178.52 REMARK 500 18 ASP A 109 -93.45 -87.31 REMARK 500 18 ASN A 116 22.07 103.34 REMARK 500 19 ASP A 17 -176.02 -63.33 REMARK 500 19 SER A 62 -58.63 -144.26 REMARK 500 19 ALA A 72 154.08 -46.06 REMARK 500 19 GLU A 77 174.14 176.12 REMARK 500 19 GLN A 86 25.16 -146.46 REMARK 500 19 ASP A 97 25.73 47.15 REMARK 500 19 ALA A 108 -168.95 -100.88 REMARK 500 19 ASP A 109 -70.87 -85.92 REMARK 500 20 LEU A 32 -177.55 -68.15 REMARK 500 20 ILE A 48 -72.95 -42.97 REMARK 500 20 SER A 62 -58.56 -144.08 REMARK 500 20 ALA A 72 150.37 -41.56 REMARK 500 20 VAL A 75 109.04 -45.71 REMARK 500 20 GLU A 77 153.02 172.72 REMARK 500 20 GLU A 79 140.84 -173.74 REMARK 500 20 GLN A 85 -161.37 -161.79 REMARK 500 20 GLN A 86 25.88 -142.30 REMARK 500 20 ASP A 97 19.85 56.76 REMARK 500 20 ASP A 109 -84.53 -68.32 REMARK 500 20 ASN A 116 49.08 71.08 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 0.27 SIDE CHAIN REMARK 500 1 ARG A 99 0.32 SIDE CHAIN REMARK 500 1 ARG A 126 0.31 SIDE CHAIN REMARK 500 2 ARG A 64 0.29 SIDE CHAIN REMARK 500 2 ARG A 99 0.17 SIDE CHAIN REMARK 500 2 ARG A 126 0.25 SIDE CHAIN REMARK 500 3 ARG A 64 0.32 SIDE CHAIN REMARK 500 3 ARG A 99 0.31 SIDE CHAIN REMARK 500 3 ARG A 126 0.32 SIDE CHAIN REMARK 500 4 ARG A 99 0.31 SIDE CHAIN REMARK 500 4 ARG A 126 0.32 SIDE CHAIN REMARK 500 5 ARG A 64 0.29 SIDE CHAIN REMARK 500 5 ARG A 99 0.19 SIDE CHAIN REMARK 500 5 ARG A 126 0.32 SIDE CHAIN REMARK 500 6 ARG A 64 0.26 SIDE CHAIN REMARK 500 6 ARG A 99 0.21 SIDE CHAIN REMARK 500 6 ARG A 126 0.23 SIDE CHAIN REMARK 500 7 ARG A 64 0.32 SIDE CHAIN REMARK 500 7 ARG A 99 0.31 SIDE CHAIN REMARK 500 7 ARG A 126 0.24 SIDE CHAIN REMARK 500 8 ARG A 64 0.30 SIDE CHAIN REMARK 500 8 ARG A 99 0.17 SIDE CHAIN REMARK 500 8 ARG A 126 0.32 SIDE CHAIN REMARK 500 9 ARG A 64 0.32 SIDE CHAIN REMARK 500 9 ARG A 99 0.27 SIDE CHAIN REMARK 500 9 ARG A 126 0.19 SIDE CHAIN REMARK 500 10 ARG A 64 0.24 SIDE CHAIN REMARK 500 10 ARG A 99 0.28 SIDE CHAIN REMARK 500 10 ARG A 126 0.32 SIDE CHAIN REMARK 500 11 ARG A 64 0.32 SIDE CHAIN REMARK 500 11 ARG A 99 0.30 SIDE CHAIN REMARK 500 11 ARG A 126 0.09 SIDE CHAIN REMARK 500 12 ARG A 64 0.23 SIDE CHAIN REMARK 500 12 ARG A 99 0.17 SIDE CHAIN REMARK 500 12 ARG A 126 0.17 SIDE CHAIN REMARK 500 13 ARG A 64 0.29 SIDE CHAIN REMARK 500 13 ARG A 99 0.12 SIDE CHAIN REMARK 500 13 ARG A 126 0.27 SIDE CHAIN REMARK 500 14 ARG A 99 0.25 SIDE CHAIN REMARK 500 14 ARG A 126 0.30 SIDE CHAIN REMARK 500 15 ARG A 64 0.30 SIDE CHAIN REMARK 500 15 ARG A 99 0.23 SIDE CHAIN REMARK 500 15 ARG A 126 0.32 SIDE CHAIN REMARK 500 16 ARG A 64 0.19 SIDE CHAIN REMARK 500 16 ARG A 99 0.14 SIDE CHAIN REMARK 500 16 ARG A 126 0.28 SIDE CHAIN REMARK 500 17 ARG A 64 0.26 SIDE CHAIN REMARK 500 17 ARG A 99 0.27 SIDE CHAIN REMARK 500 17 ARG A 126 0.18 SIDE CHAIN REMARK 500 18 ARG A 64 0.32 SIDE CHAIN REMARK 500 18 ARG A 99 0.31 SIDE CHAIN REMARK 500 18 ARG A 126 0.24 SIDE CHAIN REMARK 500 19 ARG A 64 0.26 SIDE CHAIN REMARK 500 19 ARG A 99 0.21 SIDE CHAIN REMARK 500 19 ARG A 126 0.20 SIDE CHAIN REMARK 500 20 ARG A 64 0.31 SIDE CHAIN REMARK 500 20 ARG A 99 0.19 SIDE CHAIN REMARK 500 20 ARG A 126 0.31 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 FES A 130 S2 109.6 REMARK 620 3 FES A 130 FE2 123.1 53.5 REMARK 620 4 FES A 130 S1 110.3 107.1 53.7 REMARK 620 5 CYS A 68 SG 109.8 109.8 127.1 110.1 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 S2 53.7 REMARK 620 3 CYS A 71 SG 127.4 109.6 REMARK 620 4 CYS A 102 SG 122.7 109.5 109.9 REMARK 620 5 FES A 130 S1 53.6 107.2 110.6 110.0 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 FES A 130 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1E10 RELATED DB: PDB REMARK 900 [2FE-2S]-FERREDOXIN FROM HALOBACTERIUM SALINARUM DBREF 1E0Z A 1 128 UNP P00216 FER_HALSA 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 ALY HIS LEU ASP TYR LEU GLN ASN ARG VAL ILE MODRES 1E0Z ALY A 118 LYS N(6)-ACETYLLYSINE HET FES A 130 4 HET ALY A 118 25 HETNAM ALY N(6)-ACETYLLYSINE HETNAM FES FE2/S2 (INORGANIC) CLUSTER FORMUL 2 ALY C8 H16 N2 O3 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 C ALA A 117 N ALY A 118 1555 1555 1.30 LINK C ALY A 118 N HIS A 119 1555 1555 1.31 LINK FE2 FES A 130 SG CYS A 71 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 102 1555 1555 2.20 LINK FE1 FES A 130 SG CYS A 63 1555 1555 2.20 SITE 1 AC1 9 SER A 62 CYS A 63 ARG A 64 GLY A 66 SITE 2 AC1 9 ALA A 67 CYS A 68 CYS A 71 LEU A 100 SITE 3 AC1 9 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