Header list of 1bc6.pdb file
Complete list - b 16 2 Bytes
HEADER ELECTRON TRANSPORT 05-MAY-98 1BC6 TITLE 7-FE FERREDOXIN FROM BACILLUS SCHLEGELII, NMR, 20 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: 7-FE FERREDOXIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SCHLEGELII; SOURCE 3 ORGANISM_TAXID: 1484; SOURCE 4 ATCC: ATCC 43741; SOURCE 5 COLLECTION: ATCC 43741; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: JM 109; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACTERIUM; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PKKFD54 KEYWDS ELECTRON TRANSPORT, IRON-SULFUR EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR S.AONO,D.BENTROP,I.BERTINI,A.DONAIRE,C.LUCHINAT,Y.NIIKURA,A.ROSATO REVDAT 5 16-FEB-22 1BC6 1 REMARK LINK REVDAT 4 24-MAR-09 1BC6 1 ATOM CONECT REVDAT 3 24-FEB-09 1BC6 1 VERSN REVDAT 2 01-SEP-99 1BC6 1 JRNL REVDAT 1 17-JUN-98 1BC6 0 JRNL AUTH S.AONO,D.BENTROP,I.BERTINI,A.DONAIRE,C.LUCHINAT,Y.NIIKURA, JRNL AUTH 2 A.ROSATO JRNL TITL SOLUTION STRUCTURE OF THE OXIDIZED FE7S8 FERREDOXIN FROM THE JRNL TITL 2 THERMOPHILIC BACTERIUM BACILLUS SCHLEGELII BY 1H NMR JRNL TITL 3 SPECTROSCOPY. JRNL REF BIOCHEMISTRY V. 37 9812 1998 JRNL REFN ISSN 0006-2960 JRNL PMID 9657695 JRNL DOI 10.1021/BI972818B REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH S.AONO,I.BERTINI,J.A.COWAN,C.LUCHINAT,A.ROSATO,M.S.VIEZZOLI REMARK 1 TITL 1H NMR STUDIES OF THE FE7S8 FERREDOXIN FROM BACILLUS REMARK 1 TITL 2 SCHLEGELII: A FURTHER ATTEMPT TO UNDERSTAND FE3S4 CLUSTERS REMARK 1 REF J.BIOL.INORG.CHEM. V. 1 523 1996 REMARK 1 REFN ISSN 0949-8257 REMARK 1 REFERENCE 2 REMARK 1 AUTH S.AONO,S.NAKAMURA,R.AONO,I.OKURA REMARK 1 TITL CLONING AND EXPRESSION OF THE GENE ENCODING THE 7FE TYPE REMARK 1 TITL 2 FERREDOXIN FROM A THERMOPHILIC HYDROGEN OXIDIZING BACTERIUM, REMARK 1 TITL 3 BACILLUS SCHLEGELII REMARK 1 REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 201 938 1994 REMARK 1 REFN ISSN 0006-291X REMARK 1 REFERENCE 3 REMARK 1 AUTH S.AONO,H.KURITA,S.UNO,I.OKURA REMARK 1 TITL PURIFICATION AND CHARACTERIZATION OF A 7FE FERREDOXIN FROM A REMARK 1 TITL 2 THERMOPHILIC HYDROGEN-OXIDIZING BACTERIUM, BACILLUS REMARK 1 TITL 3 SCHLEGELII REMARK 1 REF J.BIOCHEM.(TOKYO) V. 112 792 1992 REMARK 1 REFN ISSN 0021-924X 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: THE STRUCTURE CALCULATIONS WERE CARRIED REMARK 3 OUT WITH THE PROGRAM DYANA (BY GUNTERT,MUMENTHALER,WUTHRICH). REMARK 3 THE 20 STRUCTURES OF THE DYANA FAMILY WITH THE LOWEST TARGET REMARK 3 FUNCTION VALUES WERE REFINED BY RESTRAINED ENERGY MINIMIZATION REMARK 3 (REM) AND RESTRAINED MOLECULAR DYNAMICS IN VACUO. REFINEMENT REMARK 3 DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE. REMARK 4 REMARK 4 1BC6 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_1000171579. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 288 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; DQF-COSY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : AMX600; DRX 500 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : DYANA REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 300 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION 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: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 2 CYS A 16 CA - CB - SG ANGL. DEV. = 8.3 DEGREES REMARK 500 3 CYS A 42 CA - CB - SG ANGL. DEV. = 7.5 DEGREES REMARK 500 10 CYS A 42 CA - CB - SG ANGL. DEV. = 7.4 DEGREES REMARK 500 15 ALA A 1 CB - CA - C ANGL. DEV. = 16.1 DEGREES REMARK 500 15 TYR A 32 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES REMARK 500 18 CYS A 42 CA - CB - SG ANGL. DEV. = 7.7 DEGREES REMARK 500 20 CYS A 42 CA - CB - SG ANGL. DEV. = 9.3 DEGREES 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 THR A 5 -98.40 -130.34 REMARK 500 1 GLU A 6 -58.40 -147.54 REMARK 500 1 LYS A 12 -156.77 60.93 REMARK 500 1 ALA A 14 -168.27 60.16 REMARK 500 1 CYS A 16 -53.98 -166.90 REMARK 500 1 ASP A 30 -68.58 -103.62 REMARK 500 1 ALA A 44 -72.09 62.95 REMARK 500 1 GLU A 46 -54.20 -29.97 REMARK 500 2 GLU A 6 -62.98 -18.74 REMARK 500 2 ASP A 13 172.70 -56.10 REMARK 500 2 ALA A 14 102.11 -8.22 REMARK 500 2 CYS A 16 -50.34 58.50 REMARK 500 2 VAL A 22 65.57 -110.47 REMARK 500 2 CYS A 24 28.92 -144.28 REMARK 500 2 ASP A 30 -63.67 -102.54 REMARK 500 2 ALA A 44 -70.42 68.20 REMARK 500 3 THR A 5 -92.57 -122.80 REMARK 500 3 GLU A 6 -65.55 -157.36 REMARK 500 3 LYS A 12 -101.59 58.95 REMARK 500 3 ASP A 23 16.19 56.81 REMARK 500 3 ASP A 30 -71.64 -89.46 REMARK 500 3 ALA A 44 -61.97 72.82 REMARK 500 4 GLU A 6 -64.45 -18.74 REMARK 500 4 GLU A 18 -43.85 75.13 REMARK 500 4 ASP A 23 55.97 32.19 REMARK 500 4 CYS A 24 40.66 -103.35 REMARK 500 4 GLU A 29 -75.71 -54.15 REMARK 500 4 ALA A 44 -56.57 176.49 REMARK 500 5 THR A 5 -94.08 -124.15 REMARK 500 5 GLU A 6 -59.80 -155.48 REMARK 500 5 ILE A 9 125.26 -36.35 REMARK 500 5 ASP A 13 -74.56 -78.77 REMARK 500 5 VAL A 17 -54.68 167.52 REMARK 500 5 ASP A 23 68.76 14.02 REMARK 500 5 ILE A 25 111.38 89.86 REMARK 500 5 ASP A 30 -64.73 -103.18 REMARK 500 5 ALA A 44 -57.71 74.78 REMARK 500 5 LYS A 76 -160.00 -141.72 REMARK 500 6 GLU A 6 -67.15 -10.79 REMARK 500 6 LYS A 12 -155.11 58.84 REMARK 500 6 ALA A 14 -81.09 -79.82 REMARK 500 6 SER A 15 -50.90 74.30 REMARK 500 6 ASP A 23 -15.88 57.05 REMARK 500 7 GLU A 6 -59.87 -16.15 REMARK 500 7 ASP A 23 -33.27 70.35 REMARK 500 7 CYS A 24 49.97 -80.05 REMARK 500 7 GLN A 31 -143.31 -92.01 REMARK 500 7 CYS A 39 103.30 -57.45 REMARK 500 7 ILE A 40 20.58 -68.40 REMARK 500 7 ALA A 44 -61.80 175.92 REMARK 500 REMARK 500 THIS ENTRY HAS 160 RAMACHANDRAN OUTLIERS. 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 THR A 5 GLU A 6 1 -146.58 REMARK 500 LYS A 76 LYS A 77 1 -149.08 REMARK 500 CYS A 16 VAL A 17 4 149.76 REMARK 500 LYS A 76 LYS A 77 4 -149.10 REMARK 500 THR A 5 GLU A 6 5 -148.72 REMARK 500 LYS A 76 LYS A 77 5 148.14 REMARK 500 THR A 5 GLU A 6 8 -145.03 REMARK 500 CYS A 8 ILE A 9 8 -147.29 REMARK 500 ASP A 23 CYS A 24 11 -145.76 REMARK 500 PHE A 75 LYS A 76 12 -130.62 REMARK 500 CYS A 24 ILE A 25 13 143.43 REMARK 500 LYS A 76 LYS A 77 14 -146.13 REMARK 500 THR A 5 GLU A 6 15 -148.92 REMARK 500 LYS A 76 LYS A 77 16 -146.46 REMARK 500 THR A 5 GLU A 6 17 -148.11 REMARK 500 CYS A 24 ILE A 25 19 138.81 REMARK 500 GLY A 43 ALA A 44 19 147.81 REMARK 500 THR A 5 GLU A 6 20 -149.45 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 HIS A 56 0.09 SIDE CHAIN REMARK 500 1 ARG A 72 0.09 SIDE CHAIN REMARK 500 2 TYR A 2 0.08 SIDE CHAIN REMARK 500 2 TYR A 32 0.09 SIDE CHAIN REMARK 500 2 PHE A 74 0.10 SIDE CHAIN REMARK 500 3 TYR A 32 0.07 SIDE CHAIN REMARK 500 4 TYR A 2 0.10 SIDE CHAIN REMARK 500 4 TYR A 32 0.14 SIDE CHAIN REMARK 500 5 TYR A 2 0.10 SIDE CHAIN REMARK 500 5 TYR A 55 0.07 SIDE CHAIN REMARK 500 5 ARG A 72 0.08 SIDE CHAIN REMARK 500 5 PHE A 75 0.09 SIDE CHAIN REMARK 500 6 TYR A 2 0.11 SIDE CHAIN REMARK 500 7 TYR A 2 0.22 SIDE CHAIN REMARK 500 7 TYR A 32 0.09 SIDE CHAIN REMARK 500 7 TYR A 55 0.07 SIDE CHAIN REMARK 500 7 ARG A 72 0.08 SIDE CHAIN REMARK 500 7 PHE A 75 0.09 SIDE CHAIN REMARK 500 8 TYR A 2 0.14 SIDE CHAIN REMARK 500 8 TYR A 32 0.23 SIDE CHAIN REMARK 500 8 PHE A 74 0.10 SIDE CHAIN REMARK 500 8 PHE A 75 0.17 SIDE CHAIN REMARK 500 9 TYR A 2 0.14 SIDE CHAIN REMARK 500 9 TYR A 33 0.08 SIDE CHAIN REMARK 500 9 TYR A 55 0.08 SIDE CHAIN REMARK 500 9 PHE A 75 0.08 SIDE CHAIN REMARK 500 10 TYR A 32 0.08 SIDE CHAIN REMARK 500 10 PHE A 75 0.11 SIDE CHAIN REMARK 500 11 TYR A 2 0.10 SIDE CHAIN REMARK 500 11 PHE A 75 0.07 SIDE CHAIN REMARK 500 12 TYR A 32 0.08 SIDE CHAIN REMARK 500 12 PHE A 75 0.08 SIDE CHAIN REMARK 500 13 TYR A 2 0.14 SIDE CHAIN REMARK 500 13 PHE A 74 0.14 SIDE CHAIN REMARK 500 13 PHE A 75 0.11 SIDE CHAIN REMARK 500 14 TYR A 2 0.21 SIDE CHAIN REMARK 500 14 TYR A 33 0.10 SIDE CHAIN REMARK 500 14 TYR A 55 0.09 SIDE CHAIN REMARK 500 14 PHE A 75 0.10 SIDE CHAIN REMARK 500 15 PHE A 74 0.13 SIDE CHAIN REMARK 500 16 TYR A 33 0.08 SIDE CHAIN REMARK 500 16 ARG A 72 0.08 SIDE CHAIN REMARK 500 16 PHE A 74 0.12 SIDE CHAIN REMARK 500 18 TYR A 2 0.09 SIDE CHAIN REMARK 500 18 TYR A 55 0.08 SIDE CHAIN REMARK 500 18 ARG A 72 0.08 SIDE CHAIN REMARK 500 18 PHE A 74 0.08 SIDE CHAIN REMARK 500 19 TYR A 2 0.07 SIDE CHAIN REMARK 500 19 TYR A 32 0.08 SIDE CHAIN REMARK 500 19 ARG A 72 0.08 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 55 PLANE DEVIATIONS. 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 F3S A 78 FE1 REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 8 SG REMARK 620 2 F3S A 78 S1 118.4 REMARK 620 3 F3S A 78 S2 118.3 99.6 REMARK 620 4 F3S A 78 S3 112.8 102.7 102.6 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 F3S A 78 FE4 REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 16 SG REMARK 620 2 F3S A 78 S2 113.2 REMARK 620 3 F3S A 78 S3 111.5 110.0 REMARK 620 4 F3S A 78 S4 114.2 96.6 110.5 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 SF4 A 79 FE1 REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 20 SG REMARK 620 2 SF4 A 79 S2 117.1 REMARK 620 3 SF4 A 79 S3 116.6 102.8 REMARK 620 4 SF4 A 79 S4 111.9 103.7 103.1 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 SF4 A 79 FE2 REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 39 SG REMARK 620 2 SF4 A 79 S1 104.0 REMARK 620 3 SF4 A 79 S3 113.5 104.4 REMARK 620 4 SF4 A 79 S4 113.6 108.8 111.6 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 SF4 A 79 FE3 REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 42 SG REMARK 620 2 SF4 A 79 S1 114.0 REMARK 620 3 SF4 A 79 S2 113.0 106.0 REMARK 620 4 SF4 A 79 S4 111.3 101.4 110.4 REMARK 620 5 GLY A 43 O 71.6 65.6 79.8 165.8 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 SF4 A 79 FE4 REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 45 SG REMARK 620 2 SF4 A 79 S1 102.7 REMARK 620 3 SF4 A 79 S2 111.1 108.9 REMARK 620 4 SF4 A 79 S3 123.5 104.5 105.3 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 F3S A 78 FE3 REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 49 SG REMARK 620 2 F3S A 78 S1 116.5 REMARK 620 3 F3S A 78 S3 114.6 109.4 REMARK 620 4 F3S A 78 S4 110.9 98.8 104.9 REMARK 620 N 1 2 3 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S A 78 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 79 DBREF 1BC6 A 1 77 UNP Q45560 FER_BACSC 1 77 SEQRES 1 A 77 ALA TYR VAL ILE THR GLU PRO CYS ILE GLY THR LYS ASP SEQRES 2 A 77 ALA SER CYS VAL GLU VAL CYS PRO VAL ASP CYS ILE HIS SEQRES 3 A 77 GLU GLY GLU ASP GLN TYR TYR ILE ASP PRO ASP VAL CYS SEQRES 4 A 77 ILE ASP CYS GLY ALA CYS GLU ALA VAL CYS PRO VAL SER SEQRES 5 A 77 ALA ILE TYR HIS GLU ASP PHE VAL PRO GLU GLU TRP LYS SEQRES 6 A 77 SER TYR ILE GLN LYS ASN ARG ASP PHE PHE LYS LYS HET F3S A 78 7 HET SF4 A 79 8 HETNAM F3S FE3-S4 CLUSTER HETNAM SF4 IRON/SULFUR CLUSTER FORMUL 2 F3S FE3 S4 FORMUL 3 SF4 FE4 S4 HELIX 1 1 CYS A 45 VAL A 48 1 4 HELIX 2 2 PRO A 50 SER A 52 5 3 HELIX 3 3 GLU A 62 PHE A 75 1 14 SHEET 1 A 2 ILE A 25 GLU A 27 0 SHEET 2 A 2 TYR A 32 ILE A 34 -1 N TYR A 33 O HIS A 26 SHEET 1 B 2 TYR A 2 VAL A 3 0 SHEET 2 B 2 TYR A 55 HIS A 56 -1 O TYR A 55 N VAL A 3 LINK SG CYS A 8 FE1 F3S A 78 1555 1555 2.08 LINK SG CYS A 16 FE4 F3S A 78 1555 1555 2.16 LINK SG CYS A 20 FE1 SF4 A 79 1555 1555 2.07 LINK SG CYS A 39 FE2 SF4 A 79 1555 1555 2.09 LINK SG CYS A 42 FE3 SF4 A 79 1555 1555 2.13 LINK O GLY A 43 FE3 SF4 A 79 1555 1555 3.06 LINK SG CYS A 45 FE4 SF4 A 79 1555 1555 2.07 LINK SG CYS A 49 FE3 F3S A 78 1555 1555 2.20 SITE 1 AC1 8 CYS A 8 LYS A 12 ALA A 14 SER A 15 SITE 2 AC1 8 CYS A 16 CYS A 49 PRO A 50 ILE A 54 SITE 1 AC2 8 TYR A 2 CYS A 20 ILE A 34 CYS A 39 SITE 2 AC2 8 ILE A 40 CYS A 42 GLY A 43 CYS A 45 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 - b 16 2 Bytes