Header list of 1l6v.pdb file
Complete list - b 23 2 Bytes
HEADER ELECTRON TRANSPORT 14-MAR-02 1L6V TITLE STRUCTURE OF REDUCED BOVINE ADRENODOXIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: ADRENODOXIN 1; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: ADRENAL FERREDOXIN, HEPATO-FERREDOXIN; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 3 ORGANISM_COMMON: CATTLE; SOURCE 4 ORGANISM_TAXID: 9913; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS PRIMARY INTERACTION DOMAIN (HELIX 72-79), [2FE-2S]-CLUSTER, 5 KEYWDS 2 HELICES, 5 BETA STRANDS, ELECTRON TRANSPORT EXPDTA SOLUTION NMR NUMMDL 10 AUTHOR D.BEILKE,R.WEISS,F.LOHR,P.PRISTOVSEK,F.HANNEMANN,R.BERNHARDT, AUTHOR 2 H.RUETERJANS REVDAT 4 23-FEB-22 1L6V 1 REMARK LINK REVDAT 3 24-FEB-09 1L6V 1 VERSN REVDAT 2 01-APR-03 1L6V 1 JRNL REVDAT 1 26-JUN-02 1L6V 0 JRNL AUTH D.BEILKE,R.WEISS,F.LOHR,P.PRISTOVSEK,F.HANNEMANN, JRNL AUTH 2 R.BERNHARDT,H.RUTERJANS JRNL TITL A NEW ELECTRON TRANSPORT MECHANISM IN MITOCHONDRIAL STEROID JRNL TITL 2 HYDROXYLASE SYSTEMS BASED ON STRUCTURAL CHANGES UPON THE JRNL TITL 3 REDUCTION OF ADRENODOXIN. JRNL REF BIOCHEMISTRY V. 41 7969 2002 JRNL REFN ISSN 0006-2960 JRNL PMID 12069587 JRNL DOI 10.1021/BI0160361 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 1.1, DYANA 1.5 REMARK 3 AUTHORS : BRUKER (XWINNMR), GUENTERT (DYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1L6V COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-MAR-02. REMARK 100 THE DEPOSITION ID IS D_1000015699. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 300 REMARK 210 PH : 7.4 REMARK 210 IONIC STRENGTH : 100MM SALT REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 2-3MM ADRENODOXIN, 0MM REMARK 210 PHOSPHATE, 50MM NACL, DITHIONITE, REMARK 210 10% D2O, 90% H2O, 0.04% NAN3 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : DYANA 1.5, NMR2ST 1.0 REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR REMARK 210 SPECTROSCOPY 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 MODELS 1-10 REMARK 465 RES C SSSEQI REMARK 465 SER A 1 REMARK 465 SER A 2 REMARK 465 SER A 3 REMARK 465 GLU A 4 REMARK 465 VAL A 111 REMARK 465 SER A 112 REMARK 465 ASP A 113 REMARK 465 ALA A 114 REMARK 465 ARG A 115 REMARK 465 GLU A 116 REMARK 465 SER A 117 REMARK 465 ILE A 118 REMARK 465 ASP A 119 REMARK 465 MET A 120 REMARK 465 GLY A 121 REMARK 465 MET A 122 REMARK 465 ASN A 123 REMARK 465 SER A 124 REMARK 465 SER A 125 REMARK 465 LYS A 126 REMARK 465 ILE A 127 REMARK 465 GLU A 128 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME; REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 470 MODELS 1-10 REMARK 470 RES CSSEQI ATOMS REMARK 470 LYS A 6 NZ REMARK 470 HIS A 10 NE2 REMARK 470 LYS A 22 NZ REMARK 470 LYS A 24 NZ REMARK 470 HIS A 56 NE2 REMARK 470 HIS A 62 NE2 REMARK 470 LYS A 66 NZ REMARK 470 LYS A 98 NZ REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS 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 ALA A 45 O CYS A 46 0.66 REMARK 500 C CYS A 46 H GLU A 47 1.02 REMARK 500 O CYS A 46 H GLU A 47 1.09 REMARK 500 C ALA A 45 O CYS A 46 1.10 REMARK 500 C ALA A 45 H CYS A 46 1.22 REMARK 500 H ASN A 13 HA GLU A 17 1.29 REMARK 500 O GLU A 60 H ILE A 63 1.43 REMARK 500 O ALA A 81 H LEU A 84 1.44 REMARK 500 O PHE A 11 H LEU A 19 1.46 REMARK 500 H HIS A 10 O MET A 103 1.48 REMARK 500 O ILE A 7 H GLY A 23 1.49 REMARK 500 O THR A 8 H ASN A 102 1.52 REMARK 500 O HIS A 10 H VAL A 105 1.56 REMARK 500 O ALA A 45 H GLU A 47 1.56 REMARK 500 C GLY A 44 O ALA A 45 1.62 REMARK 500 O GLY A 44 O CYS A 46 1.93 REMARK 500 C GLY A 44 O CYS A 46 1.95 REMARK 500 O PHE A 11 N LEU A 19 2.12 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) 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 RES CSSEQI ATM2 DEVIATION REMARK 500 1 ALA A 45 C CYS A 46 N -0.278 REMARK 500 1 CYS A 46 C GLU A 47 N -0.314 REMARK 500 2 ALA A 45 C CYS A 46 N -0.335 REMARK 500 2 CYS A 46 C GLU A 47 N -0.315 REMARK 500 3 ALA A 45 C CYS A 46 N -0.287 REMARK 500 3 CYS A 46 C GLU A 47 N -0.315 REMARK 500 4 ALA A 45 C CYS A 46 N -0.278 REMARK 500 4 CYS A 46 C GLU A 47 N -0.314 REMARK 500 5 ALA A 45 C CYS A 46 N -0.317 REMARK 500 6 ALA A 45 C CYS A 46 N -0.258 REMARK 500 6 CYS A 46 C GLU A 47 N -0.314 REMARK 500 7 ALA A 45 C CYS A 46 N -0.300 REMARK 500 7 CYS A 46 C GLU A 47 N -0.315 REMARK 500 8 ALA A 45 C CYS A 46 N -0.308 REMARK 500 8 CYS A 46 C GLU A 47 N -0.315 REMARK 500 9 ALA A 45 C CYS A 46 N -0.304 REMARK 500 9 CYS A 46 C GLU A 47 N -0.315 REMARK 500 10 ALA A 45 C CYS A 46 N -0.316 REMARK 500 10 CYS A 46 C GLU A 47 N -0.315 REMARK 500 REMARK 500 REMARK: NULL 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 1 ALA A 45 N - CA - C ANGL. DEV. = -38.6 DEGREES REMARK 500 1 CYS A 46 C - N - CA ANGL. DEV. = 25.9 DEGREES REMARK 500 1 CYS A 46 CB - CA - C ANGL. DEV. = 19.9 DEGREES REMARK 500 1 CYS A 46 N - CA - C ANGL. DEV. = -44.6 DEGREES REMARK 500 1 CYS A 46 CA - C - N ANGL. DEV. = 13.6 DEGREES REMARK 500 1 GLU A 47 C - N - CA ANGL. DEV. = 49.9 DEGREES REMARK 500 2 ALA A 45 N - CA - C ANGL. DEV. = -44.9 DEGREES REMARK 500 2 CYS A 46 C - N - CA ANGL. DEV. = 35.2 DEGREES REMARK 500 2 CYS A 46 CB - CA - C ANGL. DEV. = 19.9 DEGREES REMARK 500 2 CYS A 46 N - CA - C ANGL. DEV. = -44.6 DEGREES REMARK 500 2 CYS A 46 CA - C - N ANGL. DEV. = 13.5 DEGREES REMARK 500 2 GLU A 47 C - N - CA ANGL. DEV. = 50.0 DEGREES REMARK 500 3 ALA A 45 N - CA - C ANGL. DEV. = -39.6 DEGREES REMARK 500 3 CYS A 46 C - N - CA ANGL. DEV. = 27.2 DEGREES REMARK 500 3 CYS A 46 CB - CA - C ANGL. DEV. = 19.9 DEGREES REMARK 500 3 CYS A 46 N - CA - C ANGL. DEV. = -44.6 DEGREES REMARK 500 3 CYS A 46 CA - C - N ANGL. DEV. = 13.6 DEGREES REMARK 500 3 GLU A 47 C - N - CA ANGL. DEV. = 50.0 DEGREES REMARK 500 4 ALA A 45 N - CA - C ANGL. DEV. = -38.6 DEGREES REMARK 500 4 CYS A 46 C - N - CA ANGL. DEV. = 25.9 DEGREES REMARK 500 4 CYS A 46 CB - CA - C ANGL. DEV. = 19.9 DEGREES REMARK 500 4 CYS A 46 N - CA - C ANGL. DEV. = -44.6 DEGREES REMARK 500 4 CYS A 46 CA - C - N ANGL. DEV. = 13.6 DEGREES REMARK 500 4 GLU A 47 C - N - CA ANGL. DEV. = 49.9 DEGREES REMARK 500 5 ALA A 45 N - CA - C ANGL. DEV. = -43.0 DEGREES REMARK 500 5 CYS A 46 C - N - CA ANGL. DEV. = 32.0 DEGREES REMARK 500 6 ALA A 45 N - CA - C ANGL. DEV. = -36.1 DEGREES REMARK 500 6 CYS A 46 C - N - CA ANGL. DEV. = 23.1 DEGREES REMARK 500 6 CYS A 46 CB - CA - C ANGL. DEV. = 19.8 DEGREES REMARK 500 6 CYS A 46 N - CA - C ANGL. DEV. = -44.6 DEGREES REMARK 500 6 CYS A 46 CA - C - N ANGL. DEV. = 13.5 DEGREES REMARK 500 6 GLU A 47 C - N - CA ANGL. DEV. = 50.0 DEGREES REMARK 500 7 ALA A 45 N - CA - C ANGL. DEV. = -41.0 DEGREES REMARK 500 7 CYS A 46 C - N - CA ANGL. DEV. = 28.9 DEGREES REMARK 500 7 CYS A 46 CB - CA - C ANGL. DEV. = 20.0 DEGREES REMARK 500 7 CYS A 46 N - CA - C ANGL. DEV. = -44.6 DEGREES REMARK 500 7 CYS A 46 CA - C - N ANGL. DEV. = 13.4 DEGREES REMARK 500 7 GLU A 47 C - N - CA ANGL. DEV. = 49.9 DEGREES REMARK 500 8 ALA A 45 N - CA - C ANGL. DEV. = -42.0 DEGREES REMARK 500 8 CYS A 46 C - N - CA ANGL. DEV. = 30.4 DEGREES REMARK 500 8 CYS A 46 CB - CA - C ANGL. DEV. = 19.9 DEGREES REMARK 500 8 CYS A 46 N - CA - C ANGL. DEV. = -44.6 DEGREES REMARK 500 8 CYS A 46 CA - C - N ANGL. DEV. = 13.5 DEGREES REMARK 500 8 GLU A 47 C - N - CA ANGL. DEV. = 49.9 DEGREES REMARK 500 9 ALA A 45 N - CA - C ANGL. DEV. = -41.5 DEGREES REMARK 500 9 CYS A 46 C - N - CA ANGL. DEV. = 29.7 DEGREES REMARK 500 9 CYS A 46 CB - CA - C ANGL. DEV. = 19.9 DEGREES REMARK 500 9 CYS A 46 N - CA - C ANGL. DEV. = -44.6 DEGREES REMARK 500 9 CYS A 46 CA - C - N ANGL. DEV. = 13.5 DEGREES REMARK 500 9 GLU A 47 C - N - CA ANGL. DEV. = 50.0 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 56 ANGLE DEVIATIONS. 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 ASN A 13 -143.83 -128.45 REMARK 500 1 ASP A 15 -74.15 -67.99 REMARK 500 1 GLU A 17 100.95 31.72 REMARK 500 1 THR A 18 32.06 160.86 REMARK 500 1 LEU A 19 -155.07 -55.39 REMARK 500 1 THR A 20 168.16 169.30 REMARK 500 1 THR A 21 137.67 -175.64 REMARK 500 1 ILE A 25 103.61 -56.78 REMARK 500 1 ASP A 27 168.86 -45.63 REMARK 500 1 ASP A 31 -164.09 -114.38 REMARK 500 1 VAL A 32 -92.58 67.56 REMARK 500 1 VAL A 33 -74.05 -41.25 REMARK 500 1 ASN A 37 24.42 83.01 REMARK 500 1 LEU A 38 153.98 -39.98 REMARK 500 1 ILE A 40 69.30 32.31 REMARK 500 1 ASP A 41 89.92 -55.62 REMARK 500 1 PHE A 43 93.96 40.17 REMARK 500 1 ALA A 45 -167.09 -65.82 REMARK 500 1 CYS A 46 172.57 -3.64 REMARK 500 1 GLU A 47 15.48 -57.37 REMARK 500 1 LEU A 50 124.46 73.88 REMARK 500 1 ALA A 51 -32.87 170.53 REMARK 500 1 THR A 54 62.53 -104.32 REMARK 500 1 CYS A 55 -68.89 -127.77 REMARK 500 1 LEU A 57 177.28 70.24 REMARK 500 1 GLU A 60 108.66 -23.15 REMARK 500 1 LYS A 66 44.68 -80.51 REMARK 500 1 ALA A 69 112.99 -176.74 REMARK 500 1 ILE A 70 125.17 -173.84 REMARK 500 1 ASP A 72 -31.56 -39.44 REMARK 500 1 ASN A 75 -72.32 -41.39 REMARK 500 1 ASP A 76 -63.82 78.11 REMARK 500 1 LEU A 78 -96.55 -47.78 REMARK 500 1 ASP A 79 -64.01 74.10 REMARK 500 1 LEU A 80 43.20 -155.22 REMARK 500 1 ALA A 81 93.92 -47.64 REMARK 500 1 TYR A 82 99.24 -32.10 REMARK 500 1 THR A 85 -88.63 -133.27 REMARK 500 1 ASP A 86 24.12 -151.92 REMARK 500 1 ARG A 87 -43.50 -133.69 REMARK 500 1 ARG A 89 108.89 -176.34 REMARK 500 1 GLN A 93 27.98 -165.66 REMARK 500 1 LEU A 96 173.47 -50.63 REMARK 500 1 ASP A 101 95.80 -62.36 REMARK 500 1 ASN A 102 44.52 84.75 REMARK 500 1 ASP A 109 98.12 70.95 REMARK 500 2 ARG A 14 39.19 -87.59 REMARK 500 2 ASP A 15 -39.92 -157.97 REMARK 500 2 THR A 18 120.38 -36.48 REMARK 500 2 THR A 20 136.18 66.91 REMARK 500 REMARK 500 THIS ENTRY HAS 397 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 ALA A 45 CYS A 46 1 -142.12 REMARK 500 CYS A 46 GLU A 47 1 133.79 REMARK 500 ALA A 45 CYS A 46 2 -141.68 REMARK 500 CYS A 46 GLU A 47 2 133.55 REMARK 500 ALA A 45 CYS A 46 3 -141.75 REMARK 500 CYS A 46 GLU A 47 3 134.07 REMARK 500 ALA A 45 CYS A 46 4 -142.12 REMARK 500 CYS A 46 GLU A 47 4 133.79 REMARK 500 ALA A 45 CYS A 46 5 -140.92 REMARK 500 ALA A 45 CYS A 46 6 -143.38 REMARK 500 CYS A 46 GLU A 47 6 134.41 REMARK 500 ALA A 45 CYS A 46 7 -141.28 REMARK 500 CYS A 46 GLU A 47 7 133.87 REMARK 500 ALA A 45 CYS A 46 8 -140.98 REMARK 500 CYS A 46 GLU A 47 8 133.81 REMARK 500 ALA A 45 CYS A 46 9 -141.22 REMARK 500 CYS A 46 GLU A 47 9 134.20 REMARK 500 ALA A 45 CYS A 46 10 -140.92 REMARK 500 CYS A 46 GLU A 47 10 134.33 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 146 FE1 REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 46 SG REMARK 620 2 FES A 146 S1 100.0 REMARK 620 3 FES A 146 S2 129.2 101.6 REMARK 620 4 CYS A 52 SG 117.1 106.4 99.8 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 FES A 146 FE2 REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 55 SG REMARK 620 2 FES A 146 S1 160.5 REMARK 620 3 FES A 146 S2 74.7 105.7 REMARK 620 4 CYS A 92 SG 89.4 89.8 164.0 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 FES A 146 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1L6U RELATED DB: PDB REMARK 900 NMR STRUCTURE OF OXIDIZED ADRENODOXIN DBREF 1L6V A 1 128 UNP P00257 ADX1_BOVIN 59 186 SEQRES 1 A 128 SER SER SER GLU ASP LYS ILE THR VAL HIS PHE ILE ASN SEQRES 2 A 128 ARG ASP GLY GLU THR LEU THR THR LYS GLY LYS ILE GLY SEQRES 3 A 128 ASP SER LEU LEU ASP VAL VAL VAL GLN ASN ASN LEU ASP SEQRES 4 A 128 ILE ASP GLY PHE GLY ALA CYS GLU GLY THR LEU ALA CYS SEQRES 5 A 128 SER THR CYS HIS LEU ILE PHE GLU GLN HIS ILE PHE GLU SEQRES 6 A 128 LYS LEU GLU ALA ILE THR ASP GLU GLU ASN ASP MET LEU SEQRES 7 A 128 ASP LEU ALA TYR GLY LEU THR ASP ARG SER ARG LEU GLY SEQRES 8 A 128 CYS GLN ILE CYS LEU THR LYS ALA MET ASP ASN MET THR SEQRES 9 A 128 VAL ARG VAL PRO ASP ALA VAL SER ASP ALA ARG GLU SER SEQRES 10 A 128 ILE ASP MET GLY MET ASN SER SER LYS ILE GLU HET FES A 146 4 HETNAM FES FE2/S2 (INORGANIC) CLUSTER FORMUL 2 FES FE2 S2 HELIX 1 1 VAL A 32 ASN A 37 1 6 HELIX 2 2 GLU A 60 GLU A 65 1 6 HELIX 3 3 THR A 71 ASP A 76 1 6 SHEET 1 A 3 THR A 21 LYS A 24 0 SHEET 2 A 3 LYS A 6 PHE A 11 -1 N ILE A 7 O GLY A 23 SHEET 3 A 3 MET A 103 VAL A 105 1 O MET A 103 N HIS A 10 LINK SG CYS A 46 FE1 FES A 146 1555 1555 2.19 LINK SG CYS A 52 FE1 FES A 146 1555 1555 2.27 LINK SG CYS A 55 FE2 FES A 146 1555 1555 2.54 LINK SG CYS A 92 FE2 FES A 146 1555 1555 2.23 SITE 1 AC1 10 GLY A 44 ALA A 45 CYS A 46 GLY A 48 SITE 2 AC1 10 LEU A 50 ALA A 51 CYS A 52 CYS A 55 SITE 3 AC1 10 LEU A 90 CYS A 92 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 23 2 Bytes