Header list of 1ib7.pdb file
Complete list - t 27 2 Bytes
HEADER ELECTRON TRANSPORT 27-MAR-01 1IB7
TITLE SOLUTION STRUCTURE OF F35Y MUTANT OF RAT FERRO CYTOCHROME B5, A
TITLE 2 CONFORMATION, ENSEMBLE OF 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME B5;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS RATTUS;
SOURCE 3 ORGANISM_COMMON: BLACK RAT;
SOURCE 4 ORGANISM_TAXID: 10117;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET3C
KEYWDS CYTOCHROME B5, ELECTRON TRANSPORT, SOLUTION STRUCTURES
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR N.SHAHZAD,B.DANGI,J.I.BLANKMAN,R.D.GUILES
REVDAT 3 27-OCT-21 1IB7 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1IB7 1 VERSN
REVDAT 1 04-APR-01 1IB7 0
JRNL AUTH N.SHAHZAD,B.DANGI,J.I.BLANKMAN,R.D.GUILES
JRNL TITL MUTAGENIC MODULATION OF THE ENTROPY CHANGE ON OXIDATION OF
JRNL TITL 2 CYTOCHROME B5: AN ANALYSIS OF THE CONTRIBUTION OF
JRNL TITL 3 CONFORMATIONAL ENTROPY
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5
REMARK 3 AUTHORS : GUENTERT, P.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE WAS CALCULATED USING 1167
REMARK 3 NOE RESTRAINTS AND 69 DIHEDRAL ANGLE RESTRAINTS; RESIDUES 1-3
REMARK 3 AND 89-94 WERE NOT INCLUDED IN THE REFINED MODEL BECAUSE OF A
REMARK 3 LACK OF RESTRAINTS IN THESE PRESUMABLY UNSTRUCTURED REGIONS OF
REMARK 3 THE PROTEIN.
REMARK 4
REMARK 4 1IB7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-MAR-01.
REMARK 100 THE DEPOSITION ID IS D_1000013120.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 313; 313; 313
REMARK 210 PH : 7.0; 7.0; 7.0
REMARK 210 IONIC STRENGTH : 1MM; 1MM; 1MM
REMARK 210 PRESSURE : NULL; NULL; NULL
REMARK 210 SAMPLE CONTENTS : 2MM F35Y CYTOCHROME B5; 1MM
REMARK 210 PHOSPHATE BUFFER; PURGED WITH
REMARK 210 NITROGEN GAS AND REDUCED BY
REMARK 210 ADDING FEW GRAINS OF SODIUM
REMARK 210 DITHIONATE AND SEALED USING OXY-
REMARK 210 ACETYLENE TORCH; 0.05 MM TSP AS
REMARK 210 INTERNAL REFERENCE; 2MM F35Y
REMARK 210 CYTOCHROME B5; 1MM PHOSPHATE
REMARK 210 BUFFER; PURGED WITH NITROGEN GAS
REMARK 210 AND REDUCED BY ADDING FEW GRAINS
REMARK 210 OF SODIUM DITHIONATE AND SEALED
REMARK 210 USING OXY-ACETYLENE TORCH; 0.05
REMARK 210 MM TSP AS INTERNAL REFERENCE;
REMARK 210 2MM F35Y CYTOCHROME B5; 1MM
REMARK 210 PHOSPHATE BUFFER; PURGED WITH
REMARK 210 NITROGEN GAS AND REDUCED BY
REMARK 210 ADDING FEW GRAINS OF SODIUM
REMARK 210 DITHIONATE AND SEALED USING OXY-
REMARK 210 ACETYLENE TORCH; 0.05 MM TSP AS
REMARK 210 INTERNAL REFERENCE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; HNHA; 3D_15N
REMARK 210 -SEPARATED_NOESY
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 : FELIX 97, XWINNMR 2.0
REMARK 210 METHOD USED : TORSION ANGEL DYNAMICS SIMULATED
REMARK 210 ANNEALING; RESTRAINED ENERGY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS, STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY, TARGET
REMARK 210 FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING 2D AND 3D EXPERIMENTS
REMARK 210 INCLUDING DISTANCE AND ANGULAR RESTRAINTS FROM HNHA
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 O TYR A 7 H HIS A 80 1.54
REMARK 500 O GLU A 56 H ASP A 60 1.56
REMARK 500 O LEU A 70 H TYR A 74 1.59
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 GLU A 11 -75.75 -61.64
REMARK 500 1 GLN A 13 -73.50 -55.00
REMARK 500 1 HIS A 15 45.88 -96.70
REMARK 500 1 HIS A 26 61.44 39.90
REMARK 500 1 LYS A 28 113.20 -169.96
REMARK 500 1 LEU A 32 39.66 -93.91
REMARK 500 1 ALA A 50 -92.11 -70.13
REMARK 500 1 HIS A 80 108.66 -38.68
REMARK 500 1 SER A 85 45.77 -90.85
REMARK 500 2 GLU A 11 -74.61 -61.61
REMARK 500 2 GLN A 13 -82.76 -61.80
REMARK 500 2 HIS A 15 48.31 -91.29
REMARK 500 2 HIS A 26 53.74 39.73
REMARK 500 2 LYS A 28 106.33 -169.95
REMARK 500 2 LEU A 32 36.29 -95.34
REMARK 500 2 ALA A 50 -90.11 -71.99
REMARK 500 2 THR A 55 -72.10 -50.43
REMARK 500 2 TYR A 74 41.61 -100.04
REMARK 500 2 HIS A 80 120.05 -38.52
REMARK 500 2 SER A 85 45.64 -109.37
REMARK 500 3 GLU A 11 -72.72 -61.71
REMARK 500 3 GLN A 13 -78.84 -59.40
REMARK 500 3 HIS A 15 43.67 -93.55
REMARK 500 3 HIS A 26 55.57 38.99
REMARK 500 3 LYS A 28 99.32 -168.91
REMARK 500 3 LEU A 32 44.95 -92.71
REMARK 500 3 GLU A 48 -36.43 -35.97
REMARK 500 3 GLN A 49 45.84 -143.24
REMARK 500 3 ALA A 50 -87.11 -65.48
REMARK 500 3 TYR A 74 37.94 -100.00
REMARK 500 3 HIS A 80 115.05 -37.84
REMARK 500 3 LYS A 86 30.76 -99.65
REMARK 500 4 GLU A 11 -73.53 -58.63
REMARK 500 4 GLN A 13 -78.97 -55.96
REMARK 500 4 HIS A 15 43.80 -94.13
REMARK 500 4 HIS A 26 60.31 38.83
REMARK 500 4 LYS A 28 107.07 -169.56
REMARK 500 4 LEU A 32 38.51 -90.81
REMARK 500 4 VAL A 45 -29.45 -39.86
REMARK 500 4 ALA A 50 -89.30 -68.50
REMARK 500 4 LYS A 86 35.36 -92.59
REMARK 500 5 GLU A 11 -75.66 -62.45
REMARK 500 5 GLN A 13 -70.42 -59.85
REMARK 500 5 HIS A 15 46.98 -89.76
REMARK 500 5 LYS A 28 106.20 -170.04
REMARK 500 5 LEU A 32 40.15 -92.54
REMARK 500 5 VAL A 45 -29.18 -39.98
REMARK 500 5 ALA A 50 -91.54 -70.74
REMARK 500 5 SER A 85 46.99 -93.18
REMARK 500 6 GLU A 11 -75.70 -60.09
REMARK 500
REMARK 500 THIS ENTRY HAS 184 RAMACHANDRAN OUTLIERS.
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 95 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 39 NE2
REMARK 620 2 HEM A 95 NA 89.4
REMARK 620 3 HEM A 95 NB 96.9 90.8
REMARK 620 4 HEM A 95 NC 89.9 179.1 89.8
REMARK 620 5 HEM A 95 ND 82.7 89.7 179.3 89.7
REMARK 620 6 HIS A 63 NE2 172.9 97.7 83.5 83.0 96.9
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 95
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1B5A RELATED DB: PDB
REMARK 900 WILD TYPE FERRO CYTOCHROME B5, SOLUTION STRUCTURE
DBREF 1IB7 A 1 94 UNP P00173 CYB5_RAT 5 98
SEQADV 1IB7 TYR A 35 UNP P00173 PHE 39 ENGINEERED MUTATION
SEQRES 1 A 94 ASP LYS ASP VAL LYS TYR TYR THR LEU GLU GLU ILE GLN
SEQRES 2 A 94 LYS HIS LYS ASP SER LYS SER THR TRP VAL ILE LEU HIS
SEQRES 3 A 94 HIS LYS VAL TYR ASP LEU THR LYS TYR LEU GLU GLU HIS
SEQRES 4 A 94 PRO GLY GLY GLU GLU VAL LEU ARG GLU GLN ALA GLY GLY
SEQRES 5 A 94 ASP ALA THR GLU ASN PHE GLU ASP VAL GLY HIS SER THR
SEQRES 6 A 94 ASP ALA ARG GLU LEU SER LYS THR TYR ILE ILE GLY GLU
SEQRES 7 A 94 LEU HIS PRO ASP ASP ARG SER LYS ILE ALA LYS PRO SER
SEQRES 8 A 94 GLU THR LEU
HET HEM A 95 73
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN HEM HEME
FORMUL 2 HEM C34 H32 FE N4 O4
HELIX 1 1 THR A 8 HIS A 15 1 8
HELIX 2 2 GLU A 43 GLU A 48 1 6
HELIX 3 3 ALA A 54 ASP A 60 1 7
HELIX 4 4 SER A 64 TYR A 74 1 11
HELIX 5 5 HIS A 80 SER A 85 1 6
SHEET 1 A 3 TYR A 6 TYR A 7 0
SHEET 2 A 3 ILE A 75 LEU A 79 1 O GLU A 78 N TYR A 7
SHEET 3 A 3 VAL A 29 TYR A 30 -1 N VAL A 29 O GLY A 77
LINK NE2 HIS A 39 FE HEM A 95 1555 1555 2.10
LINK NE2 HIS A 63 FE HEM A 95 1555 1555 1.89
SITE 1 AC1 16 TYR A 30 LEU A 32 TYR A 35 HIS A 39
SITE 2 AC1 16 VAL A 45 LEU A 46 ALA A 54 PHE A 58
SITE 3 AC1 16 VAL A 61 GLY A 62 HIS A 63 SER A 64
SITE 4 AC1 16 ASP A 66 ALA A 67 LEU A 70 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
MODEL 1
Complete list - t 27 2 Bytes