Header list of 1i87.pdb file
Complete list - b 23 2 Bytes
HEADER ELECTRON TRANSPORT 12-MAR-01 1I87
TITLE SOLUTION STRUCTURE OF THE WATER-SOLUBLE FRAGMENT OF RAT HEPATIC
TITLE 2 APOCYTOCHROME B5
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME B5;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: WATER-SOLUBLE DOMAIN (RESIDUES 1-98);
COMPND 5 SYNONYM: APOCYTOCHROME B5;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET3D
KEYWDS APO HEMOPROTEIN, ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR C.J.FALZONE,Y.WANG,B.C.VU,N.L.SCOTT,S.BHATTACHARYA,J.T.LECOMTE
REVDAT 3 23-FEB-22 1I87 1 REMARK
REVDAT 2 24-FEB-09 1I87 1 VERSN
REVDAT 1 16-MAY-01 1I87 0
JRNL AUTH C.J.FALZONE,Y.WANG,B.C.VU,N.L.SCOTT,S.BHATTACHARYA,
JRNL AUTH 2 J.T.LECOMTE
JRNL TITL STRUCTURAL AND DYNAMIC PERTURBATIONS INDUCED BY HEME BINDING
JRNL TITL 2 IN CYTOCHROME B5.
JRNL REF BIOCHEMISTRY V. 40 4879 2001
JRNL REFN ISSN 0006-2960
JRNL PMID 11294656
JRNL DOI 10.1021/BI002681G
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.J.FALZONE,M.R.MAYER,E.L.WHITEMAN,C.D.MOORE,J.T.J.LECOMTE
REMARK 1 TITL DESIGN CHALLENGES FOR HEMOPROTEINS: THE SOLUTION STRUCTURE
REMARK 1 TITL 2 OF APOCYTOCHROME B5
REMARK 1 REF BIOCHEMISTRY V. 35 6519 1996
REMARK 1 REFN ISSN 0006-2960
REMARK 1 DOI 10.1021/BI960501Q
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.5, X-PLOR 3.851
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HIS 26, 27, 39, 63, AND 80 WERE
REMARK 3 PROTONATED AT THE NE2 POSITION IN ACCORDANCE TO 15N NMR DATA.
REMARK 3 HIS 15 HAS A HIGH PK AND WAS PROTONATED AT THE ND1 AND NE2
REMARK 3 POSITIONS. ADDITIONAL DETAILS ARE PROVIDED IN THE PRIMARY
REMARK 3 CITATION.
REMARK 4
REMARK 4 1I87 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-MAR-01.
REMARK 100 THE DEPOSITION ID IS D_1000013026.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.2
REMARK 210 IONIC STRENGTH : LOW
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM APOCYTOCHROME B5, 13C,15N;
REMARK 210 1 MM APOCYTOCHROME B5, 15N; 2 MM
REMARK 210 APOCYTOCHROME B5; 2 MM
REMARK 210 APOCYTOCHROME B5
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 2D-NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 97, X-PLOR 3.851
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE AMINO ACID SEQUENCE NUMBERING FOLLOWS THE BOVINE
REMARK 210 SCHEME, WITH THE FIRST FOUR RESIDUES GIVEN NEGATIVE VALUES.
REMARK 210 THESE FOUR RESIDUES ARE DISORDERED AND NOT INCLUDED IN THE
REMARK 210 COORDINATES.
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 1-20
REMARK 465 RES C SSSEQI
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: 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: 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 LYS A 2 28.97 -151.86
REMARK 500 1 VAL A 4 101.91 53.64
REMARK 500 1 TYR A 7 -168.69 -61.74
REMARK 500 1 GLN A 13 48.69 -90.35
REMARK 500 1 LYS A 14 28.88 -150.35
REMARK 500 1 HIS A 15 48.10 -101.66
REMARK 500 1 ASP A 17 -157.97 -110.95
REMARK 500 1 SER A 18 -159.34 52.99
REMARK 500 1 LYS A 19 -155.20 -121.76
REMARK 500 1 SER A 20 98.53 53.13
REMARK 500 1 TRP A 22 76.64 -107.29
REMARK 500 1 LEU A 25 -76.20 -86.16
REMARK 500 1 HIS A 26 -53.01 -125.29
REMARK 500 1 HIS A 27 20.65 -141.31
REMARK 500 1 PRO A 40 91.66 -53.05
REMARK 500 1 GLU A 43 -87.08 55.53
REMARK 500 1 ARG A 47 75.36 52.23
REMARK 500 1 GLU A 48 40.01 -169.13
REMARK 500 1 ASP A 53 79.89 52.72
REMARK 500 1 ALA A 54 -166.87 52.66
REMARK 500 1 THR A 55 47.49 -100.31
REMARK 500 1 GLU A 56 -153.80 52.74
REMARK 500 1 PHE A 58 -158.51 -170.33
REMARK 500 1 ASP A 66 49.89 -94.49
REMARK 500 1 ARG A 68 -50.67 -135.58
REMARK 500 1 SER A 71 43.35 -94.54
REMARK 500 1 LYS A 72 -67.58 -146.11
REMARK 500 1 ARG A 84 -172.63 -56.11
REMARK 500 1 LYS A 86 75.69 -169.61
REMARK 500 1 SER A 91 -159.26 52.78
REMARK 500 1 THR A 93 -45.25 -140.63
REMARK 500 2 VAL A 4 166.28 56.79
REMARK 500 2 TYR A 7 -168.78 -61.76
REMARK 500 2 GLN A 13 49.13 -90.19
REMARK 500 2 LYS A 14 32.47 -159.95
REMARK 500 2 LYS A 16 32.67 -167.70
REMARK 500 2 ASP A 17 -40.44 -168.57
REMARK 500 2 LYS A 19 173.67 55.85
REMARK 500 2 SER A 20 179.43 53.45
REMARK 500 2 TRP A 22 75.45 -104.42
REMARK 500 2 HIS A 26 -39.69 -170.08
REMARK 500 2 HIS A 27 -44.29 -138.98
REMARK 500 2 LEU A 32 48.41 -88.33
REMARK 500 2 PRO A 40 103.25 -53.00
REMARK 500 2 GLU A 43 -86.70 56.28
REMARK 500 2 GLN A 49 -178.21 53.01
REMARK 500 2 ALA A 50 87.41 52.78
REMARK 500 2 ALA A 54 42.62 -94.72
REMARK 500 2 ASP A 60 -155.95 38.47
REMARK 500 2 VAL A 61 63.83 -117.27
REMARK 500
REMARK 500 THIS ENTRY HAS 541 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1I8C RELATED DB: PDB
REMARK 900 MINIMIZED AVERAGE STRUCTURE CALCULATED FROM THIS ENSEMBLE
DBREF 1I87 A -3 94 UNP P00173 CYB5_RAT 1 98
SEQRES 1 A 98 ALA GLU GLN SER ASP LYS ASP VAL LYS TYR TYR THR LEU
SEQRES 2 A 98 GLU GLU ILE GLN LYS HIS LYS ASP SER LYS SER THR TRP
SEQRES 3 A 98 VAL ILE LEU HIS HIS LYS VAL TYR ASP LEU THR LYS PHE
SEQRES 4 A 98 LEU GLU GLU HIS PRO GLY GLY GLU GLU VAL LEU ARG GLU
SEQRES 5 A 98 GLN ALA GLY GLY ASP ALA THR GLU ASN PHE GLU ASP VAL
SEQRES 6 A 98 GLY HIS SER THR ASP ALA ARG GLU LEU SER LYS THR TYR
SEQRES 7 A 98 ILE ILE GLY GLU LEU HIS PRO ASP ASP ARG SER LYS ILE
SEQRES 8 A 98 ALA LYS PRO SER GLU THR LEU
HELIX 1 1 THR A 8 GLN A 13 1 6
HELIX 2 2 LEU A 32 GLU A 37 1 6
SHEET 1 A 4 TYR A 6 TYR A 7 0
SHEET 2 A 4 GLY A 77 LEU A 79 1 O GLU A 78 N TYR A 7
SHEET 3 A 4 LYS A 28 ASP A 31 -1 N VAL A 29 O GLY A 77
SHEET 4 A 4 TRP A 22 ILE A 24 -1 O VAL A 23 N TYR A 30
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