Header list of 1bfx.pdb file
Complete list - 16 20 Bytes
HEADER ELECTRON TRANSPORT 23-MAY-98 1BFX TITLE THE SOLUTION NMR STRUCTURE OF THE B FORM OF OXIDIZED RAT MICROSOMAL TITLE 2 CYTOCHROME B5, MINIMIZED AVERAGE STRUCTURE COMPND MOL_ID: 1; COMPND 2 MOLECULE: CYTOCHROME B5; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: SOLUBLE DOMAIN; COMPND 5 ENGINEERED: YES; COMPND 6 OTHER_DETAILS: FROM RAT MICROSOMAL MEMBRANE SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 3 ORGANISM_COMMON: NORWAY RAT; SOURCE 4 ORGANISM_TAXID: 10116; SOURCE 5 ORGAN: LIVER; SOURCE 6 ORGANELLE: MICROSOME; SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 9 EXPRESSION_SYSTEM_STRAIN: NM522; SOURCE 10 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM; SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PUC 13 KEYWDS ELECTRON TRANSPORT, CYTOCHROME B5, PROTEIN RECOGNITION, ELECTRON KEYWDS 2 TRANSFER, SOLUTION STRUCTURE, PARAMAGNETIC NMR EXPDTA SOLUTION NMR AUTHOR F.ARNESANO,L.BANCI,I.BERTINI,I.C.FELLI REVDAT 3 16-FEB-22 1BFX 1 REMARK LINK REVDAT 2 24-FEB-09 1BFX 1 VERSN REVDAT 1 12-AUG-98 1BFX 0 JRNL AUTH F.ARNESANO,L.BANCI,I.BERTINI,I.C.FELLI,D.KOULOUGLIOTIS JRNL TITL SOLUTION STRUCTURE OF THE B FORM OF OXIDIZED RAT MICROSOMAL JRNL TITL 2 CYTOCHROME B5 AND BACKBONE DYNAMICS VIA 15N ROTATING-FRAME JRNL TITL 3 NMR-RELAXATION MEASUREMENTS. BIOLOGICAL IMPLICATIONS. JRNL REF EUR.J.BIOCHEM. V. 260 347 1999 JRNL REFN ISSN 0014-2956 JRNL PMID 10095768 JRNL DOI 10.1046/J.1432-1327.1999.00167.X 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: PSEUDOREM (BANCI, BERTINI, GORI REMARK 3 SAVELLINI, ROMAGNOLI, TURANO, CREMONINI, LUCHINAT, GRAY) ALSO REMARK 3 WAS USED. REMARK 4 REMARK 4 1BFX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000171707. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7 REMARK 210 IONIC STRENGTH : PHOSPHATE 1MM REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : H2O AND D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE 800 MHZ REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : DYANA, PSEUDYANA, AMBER REMARK 210 METHOD USED : TORSION ANGLE MOLECULAR DYNAMICS REMARK 210 SIMULATED ANNEALING, RESTRAINED REMARK 210 ENERGY MINIMIZATION. REMARK 210 PSEUDOCONTACT SHIFTS WERE USED REMARK 210 IN THE CALCULATION AND IN THE REMARK 210 MINIMIZATION AS FURTHER NON- REMARK 210 CLASSICAL CONSTRAINTS. REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 40 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : MINIMIZED AVERAGE 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 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 RES C SSSEQI REMARK 465 MET A -4 REMARK 465 ALA A -3 REMARK 465 GLU A -2 REMARK 465 GLN A -1 REMARK 465 SER A 0 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 GLU A 44 OE1 - CD - OE2 ANGL. DEV. = -38.4 DEGREES REMARK 500 GLU A 44 CG - CD - OE1 ANGL. DEV. = 45.8 DEGREES REMARK 500 GLU A 44 CG - CD - OE2 ANGL. DEV. = -39.1 DEGREES REMARK 500 GLU A 92 CA - CB - CG ANGL. DEV. = 13.4 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 LYS A 2 160.87 177.28 REMARK 500 VAL A 4 -118.70 -96.73 REMARK 500 LYS A 5 73.46 134.76 REMARK 500 SER A 18 -64.72 53.67 REMARK 500 HIS A 26 -61.62 61.36 REMARK 500 HIS A 27 32.38 -175.96 REMARK 500 LEU A 36 -63.48 -29.15 REMARK 500 HIS A 39 106.31 -46.47 REMARK 500 ASP A 82 -76.08 -52.17 REMARK 500 ILE A 87 68.50 24.64 REMARK 500 ALA A 88 106.30 -54.93 REMARK 500 GLU A 92 -140.60 -179.59 REMARK 500 THR A 93 64.91 -175.00 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 ASP A 1 LYS A 2 148.44 REMARK 500 ALA A 88 LYS A 89 -136.98 REMARK 500 PRO A 90 SER A 91 -138.72 REMARK 500 SER A 91 GLU A 92 -147.49 REMARK 500 THR A 93 LEU A 94 120.31 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 TYR A 6 0.11 SIDE CHAIN REMARK 500 PHE A 58 0.10 SIDE CHAIN REMARK 500 TYR A 74 0.09 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 HEM A 96 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 39 NE2 REMARK 620 2 HEM A 96 NA 89.2 REMARK 620 3 HEM A 96 NB 91.1 92.4 REMARK 620 4 HEM A 96 NC 89.7 177.4 90.0 REMARK 620 5 HEM A 96 ND 91.6 90.1 176.4 87.6 REMARK 620 6 HIS A 63 NE2 178.0 92.3 90.1 88.8 87.2 REMARK 620 N 1 2 3 4 5 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: NUL REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: NULL REMARK 800 REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 96 DBREF 1BFX A -3 94 UNP P00173 CYB5_RAT 1 98 SEQRES 1 A 99 MET ALA GLU GLN SER ASP LYS ASP VAL LYS TYR TYR THR SEQRES 2 A 99 LEU GLU GLU ILE GLN LYS HIS LYS ASP SER LYS SER THR SEQRES 3 A 99 TRP VAL ILE LEU HIS HIS LYS VAL TYR ASP LEU THR LYS SEQRES 4 A 99 PHE LEU GLU GLU HIS PRO GLY GLY GLU GLU VAL LEU ARG SEQRES 5 A 99 GLU GLN ALA GLY GLY ASP ALA THR GLU ASN PHE GLU ASP SEQRES 6 A 99 VAL GLY HIS SER THR ASP ALA ARG GLU LEU SER LYS THR SEQRES 7 A 99 TYR ILE ILE GLY GLU LEU HIS PRO ASP ASP ARG SER LYS SEQRES 8 A 99 ILE ALA LYS PRO SER GLU THR LEU HET HEM A 96 73 HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETSYN HEM HEME FORMUL 2 HEM C34 H32 FE N4 O4 HELIX 1 1 THR A 8 LYS A 14 1 7 HELIX 2 2 THR A 33 HIS A 39 5 7 HELIX 3 3 GLY A 42 ALA A 50 1 9 HELIX 4 4 ALA A 54 GLY A 62 1 9 HELIX 5 5 ASP A 66 TYR A 74 1 9 HELIX 6 6 PRO A 81 ILE A 87 1 7 SHEET 1 1 3 THR A 21 LEU A 25 0 SHEET 2 1 3 LYS A 28 LEU A 32 -1 SHEET 3 1 3 ILE A 75 GLY A 77 -1 LINK NE2 HIS A 39 FE HEM A 96 1555 1555 1.98 LINK NE2 HIS A 63 FE HEM A 96 1555 1555 1.97 CISPEP 1 GLU A 92 THR A 93 0 -8.03 SITE 1 NUL 2 HIS A 39 HIS A 63 SITE 1 AC1 11 LEU A 32 PHE A 35 HIS A 39 PRO A 40 SITE 2 AC1 11 LEU A 46 GLN A 49 ALA A 54 HIS A 63 SITE 3 AC1 11 SER A 64 ALA A 67 SER A 71 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
Complete list - 16 20 Bytes