Header list of 1fov.pdb file
Complete list - b 23 2 Bytes
HEADER ELECTRON TRANSPORT 29-AUG-00 1FOV TITLE GLUTAREDOXIN 3 FROM ESCHERICHIA COLI IN THE FULLY OXIDIZED FORM COMPND MOL_ID: 1; COMPND 2 MOLECULE: GLUTAREDOXIN 3; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: GRX3; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_TAXID: 562; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET-3 KEYWDS ACTIVE SITE DISULFIDE, CIS PRO 53, ELECTRON TRANSPORT EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR K.NORDSTRAND,A.SANDSTROM,F.ASLUND,A.HOLMGREN,G.OTTING,K.D.BERNDT REVDAT 3 23-FEB-22 1FOV 1 REMARK SEQADV REVDAT 2 24-FEB-09 1FOV 1 VERSN REVDAT 1 26-OCT-00 1FOV 0 JRNL AUTH K.NORDSTRAND,A.SANDSTROM,F.ASLUND,A.HOLMGREN,G.OTTING, JRNL AUTH 2 K.D.BERNDT JRNL TITL NMR STRUCTURE OF OXIDIZED GLUTAREDOXIN 3 FROM ESCHERICHIA JRNL TITL 2 COLI. JRNL REF J.MOL.BIOL. V. 303 423 2000 JRNL REFN ISSN 0022-2836 JRNL PMID 11031118 JRNL DOI 10.1006/JMBI.2000.4145 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH K.NORDSTRAND,F.ASLUND,A.HOLMGREN,G.OTTING,K.D.BERNDT REMARK 1 TITL NMR STRUCTURE OF ESCHERICHIA COLI GLUTAREDOXIN 3 - REMARK 1 TITL 2 GLUTATHIONE MIXED DISULFIDE COMPLEX: IMPLICATIONS FOR THE REMARK 1 TITL 3 ENZYMATIC MECHANISM REMARK 1 REF J.MOL.BIOL. V. 286 541 1999 REMARK 1 REFN ISSN 0022-2836 REMARK 1 DOI 10.1006/JMBI.1998.2444 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PROSA 3.6, DYANA 1.5, OPAL 2.6 REMARK 3 AUTHORS : GUNTERT, BILLETER, OHLENSCHLAGER, BROWN, & REMARK 3 WUTHRICH (PROSA), GUNTERT, MUMENTHALER, & WUTHRICH REMARK 3 (DYANA), LUGINBUHL, GUNTERT, BILLETER, & WUTHRICH REMARK 3 (OPAL) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1FOV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-SEP-00. REMARK 100 THE DEPOSITION ID IS D_1000011781. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 301 REMARK 210 PH : 5.5 REMARK 210 IONIC STRENGTH : UNBUFFERED REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XEASY 1.4 REMARK 210 METHOD USED : SIMULATED ANNEALING IN TORSION REMARK 210 ANGLE SPACE FOLLOWED BY REMARK 210 CONJUGATE GRADIENT MINIMIZATION REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 18 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: 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 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 4 TYR A 69 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES REMARK 500 16 ARG A 16 NE - CZ - NH2 ANGL. DEV. = -3.2 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 ALA A 37 -47.31 -163.10 REMARK 500 1 ARG A 49 -58.09 -148.05 REMARK 500 1 THR A 50 10.87 83.16 REMARK 500 2 CYS A 11 101.11 -169.60 REMARK 500 2 ILE A 44 -70.61 -63.73 REMARK 500 2 ARG A 49 -53.13 -136.36 REMARK 500 2 ALA A 59 -0.16 68.37 REMARK 500 3 CYS A 11 93.68 -167.77 REMARK 500 3 ASP A 34 53.55 -64.81 REMARK 500 3 ARG A 49 -57.90 -130.52 REMARK 500 3 THR A 50 37.78 74.23 REMARK 500 4 THR A 10 -83.47 -133.32 REMARK 500 4 CYS A 11 75.99 33.99 REMARK 500 4 ALA A 37 -45.23 -163.26 REMARK 500 4 ALA A 59 -0.07 68.30 REMARK 500 5 CYS A 11 85.63 -167.00 REMARK 500 5 ARG A 49 -57.03 -136.54 REMARK 500 5 THR A 50 -6.34 79.30 REMARK 500 5 ALA A 59 -13.49 76.19 REMARK 500 5 ILE A 62 -74.95 -74.25 REMARK 500 6 THR A 10 -119.71 -140.90 REMARK 500 6 CYS A 11 85.68 58.52 REMARK 500 6 ASN A 36 38.45 -144.47 REMARK 500 6 ALA A 37 63.99 -66.63 REMARK 500 6 ALA A 38 -59.82 -163.87 REMARK 500 6 THR A 50 -9.91 86.10 REMARK 500 6 ALA A 59 -0.21 63.78 REMARK 500 7 THR A 10 -82.65 -138.82 REMARK 500 7 CYS A 11 88.35 45.43 REMARK 500 7 PRO A 12 43.67 -73.85 REMARK 500 7 TYR A 13 -50.23 -142.21 REMARK 500 7 ALA A 37 -28.35 -162.95 REMARK 500 7 ARG A 49 -70.64 -90.92 REMARK 500 7 THR A 50 -8.55 83.00 REMARK 500 7 ALA A 59 -10.54 68.78 REMARK 500 8 ALA A 37 -49.79 -163.01 REMARK 500 8 THR A 50 8.35 -154.76 REMARK 500 8 ILE A 62 -73.81 -76.67 REMARK 500 9 CYS A 11 95.45 -168.50 REMARK 500 9 ASP A 34 -143.36 -58.26 REMARK 500 9 ALA A 59 -7.96 67.04 REMARK 500 10 CYS A 11 81.74 96.34 REMARK 500 10 ILE A 44 -74.14 -63.98 REMARK 500 10 ARG A 49 -72.94 -116.55 REMARK 500 10 THR A 50 -4.78 86.63 REMARK 500 10 ALA A 59 -3.64 70.21 REMARK 500 10 ILE A 62 -74.45 -82.93 REMARK 500 10 LEU A 81 -97.27 -139.20 REMARK 500 11 CYS A 11 80.09 -155.93 REMARK 500 11 ALA A 37 55.44 -162.95 REMARK 500 REMARK 500 THIS ENTRY HAS 95 RAMACHANDRAN OUTLIERS. 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 3 TYR A 69 0.07 SIDE CHAIN REMARK 500 4 ARG A 46 0.10 SIDE CHAIN REMARK 500 4 TYR A 65 0.07 SIDE CHAIN REMARK 500 6 TYR A 6 0.07 SIDE CHAIN REMARK 500 6 ARG A 49 0.09 SIDE CHAIN REMARK 500 6 TYR A 65 0.07 SIDE CHAIN REMARK 500 7 TYR A 69 0.09 SIDE CHAIN REMARK 500 8 TYR A 69 0.09 SIDE CHAIN REMARK 500 9 ARG A 49 0.09 SIDE CHAIN REMARK 500 9 TYR A 69 0.07 SIDE CHAIN REMARK 500 9 ARG A 74 0.08 SIDE CHAIN REMARK 500 10 TYR A 69 0.07 SIDE CHAIN REMARK 500 11 ARG A 49 0.12 SIDE CHAIN REMARK 500 12 ARG A 46 0.12 SIDE CHAIN REMARK 500 12 TYR A 69 0.10 SIDE CHAIN REMARK 500 12 ARG A 74 0.11 SIDE CHAIN REMARK 500 14 TYR A 69 0.07 SIDE CHAIN REMARK 500 16 ARG A 16 0.11 SIDE CHAIN REMARK 500 16 ARG A 46 0.09 SIDE CHAIN REMARK 500 17 ARG A 40 0.11 SIDE CHAIN REMARK 500 17 ARG A 49 0.10 SIDE CHAIN REMARK 500 17 TYR A 69 0.11 SIDE CHAIN REMARK 500 17 ARG A 74 0.16 SIDE CHAIN REMARK 500 19 ARG A 46 0.10 SIDE CHAIN REMARK 500 19 TYR A 69 0.08 SIDE CHAIN REMARK 500 20 ARG A 40 0.08 SIDE CHAIN REMARK 500 20 TYR A 69 0.06 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3GRX RELATED DB: PDB REMARK 900 GLUTAREDOXIN 3 - GLUTATHIONE MIXED DISULFIDE COMPLEX DBREF 1FOV A 1 82 UNP P0AC62 GLRX3_ECOLI 1 82 SEQADV 1FOV TYR A 65 UNP P0AC62 CYS 65 CONFLICT SEQRES 1 A 82 ALA ASN VAL GLU ILE TYR THR LYS GLU THR CYS PRO TYR SEQRES 2 A 82 CYS HIS ARG ALA LYS ALA LEU LEU SER SER LYS GLY VAL SEQRES 3 A 82 SER PHE GLN GLU LEU PRO ILE ASP GLY ASN ALA ALA LYS SEQRES 4 A 82 ARG GLU GLU MET ILE LYS ARG SER GLY ARG THR THR VAL SEQRES 5 A 82 PRO GLN ILE PHE ILE ASP ALA GLN HIS ILE GLY GLY TYR SEQRES 6 A 82 ASP ASP LEU TYR ALA LEU ASP ALA ARG GLY GLY LEU ASP SEQRES 7 A 82 PRO LEU LEU LYS HELIX 1 1 CYS A 11 GLY A 25 1 15 HELIX 2 2 ALA A 37 GLY A 48 1 12 HELIX 3 3 GLY A 64 ARG A 74 1 11 HELIX 4 4 LEU A 77 LYS A 82 1 6 SHEET 1 A 4 GLN A 29 PRO A 32 0 SHEET 2 A 4 VAL A 3 THR A 7 1 O VAL A 3 N GLN A 29 SHEET 3 A 4 GLN A 54 ILE A 57 -1 O GLN A 54 N TYR A 6 SHEET 4 A 4 GLN A 60 GLY A 63 -1 O GLN A 60 N ILE A 57 SSBOND 1 CYS A 11 CYS A 14 1555 1555 2.02 CISPEP 1 VAL A 52 PRO A 53 1 -6.17 CISPEP 2 VAL A 52 PRO A 53 2 -10.41 CISPEP 3 VAL A 52 PRO A 53 3 -10.95 CISPEP 4 VAL A 52 PRO A 53 4 -8.29 CISPEP 5 VAL A 52 PRO A 53 5 -5.45 CISPEP 6 VAL A 52 PRO A 53 6 0.94 CISPEP 7 VAL A 52 PRO A 53 7 -4.17 CISPEP 8 VAL A 52 PRO A 53 8 -7.33 CISPEP 9 VAL A 52 PRO A 53 9 -11.18 CISPEP 10 VAL A 52 PRO A 53 10 -4.13 CISPEP 11 VAL A 52 PRO A 53 11 -11.13 CISPEP 12 VAL A 52 PRO A 53 12 -8.86 CISPEP 13 VAL A 52 PRO A 53 13 2.19 CISPEP 14 VAL A 52 PRO A 53 14 -7.51 CISPEP 15 VAL A 52 PRO A 53 15 -2.75 CISPEP 16 VAL A 52 PRO A 53 16 -11.43 CISPEP 17 VAL A 52 PRO A 53 17 -11.46 CISPEP 18 VAL A 52 PRO A 53 18 -0.67 CISPEP 19 VAL A 52 PRO A 53 19 -11.21 CISPEP 20 VAL A 52 PRO A 53 20 -9.84 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