HEADER ELECTRON TRANSPORT 08-AUG-96 1YFC
TITLE SOLUTION NMR STRUCTURE OF A YEAST ISO-1-FERROCYTOCHROME C
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: YEAST ISO-1-FERROCYTOCHROME C;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 OTHER_DETAILS: REDUCED FORM
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 VARIANT: C102S;
SOURCE 6 GENE: YEAST ISO-1-CYTOCHROME C;
SOURCE 7 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 8 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 4932
KEYWDS FERROCYTOCHROME, MITOCHONDRION, ELECTRON TRANSPORT, RESPIRATORY
KEYWDS 2 CHAIN, METHYLATION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR P.BAISTROCCHI,L.BANCI,I.BERTINI,P.TURANO,K.L.BREN,H.B.GRAY
REVDAT 4 03-NOV-21 1YFC 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1YFC 1 VERSN
REVDAT 2 21-JUN-05 1YFC 1 TITLE
REVDAT 1 12-MAR-97 1YFC 0
JRNL AUTH P.BAISTROCCHI,L.BANCI,I.BERTINI,P.TURANO,K.L.BREN,H.B.GRAY
JRNL TITL THREE-DIMENSIONAL SOLUTION STRUCTURE OF SACCHAROMYCES
JRNL TITL 2 CEREVISIAE REDUCED ISO-1-CYTOCHROME C.
JRNL REF BIOCHEMISTRY V. 35 13788 1996
JRNL REFN ISSN 0006-2960
JRNL PMID 8901521
JRNL DOI 10.1021/BI961110E
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH Y.GAO,J.BOYD,R.J.WILLIAMS,G.J.PIELAK
REMARK 1 TITL ASSIGNMENT OF PROTON RESONANCES, IDENTIFICATION OF SECONDARY
REMARK 1 TITL 2 STRUCTURAL ELEMENTS, AND ANALYSIS OF BACKBONE CHEMICAL
REMARK 1 TITL 3 SHIFTS FOR THE C102T VARIANT OF YEAST ISO-1-CYTOCHROME C AND
REMARK 1 TITL 4 HORSE CYTOCHROME C
REMARK 1 REF BIOCHEMISTRY V. 29 6994 1990
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH G.V.LOUIE,G.D.BRAYER
REMARK 1 TITL HIGH-RESOLUTION REFINEMENT OF YEAST ISO-1-CYTOCHROME C AND
REMARK 1 TITL 2 COMPARISONS WITH OTHER EUKARYOTIC CYTOCHROMES C
REMARK 1 REF J.MOL.BIOL. V. 214 527 1990
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DIANA, DIANA
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1YFC COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000177388.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX-600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 500
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION <= 0.82 A2
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 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 LEU A 94 H LEU A 98 1.49
REMARK 500 O CYS A 14 H CYS A 17 1.49
REMARK 500 O GLU A 88 HD21 ASN A 92 1.50
REMARK 500 O LEU A 98 H SER A 102 1.52
REMARK 500 O ASP A 90 H LEU A 94 1.57
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 PHE A -3 -174.65 -51.56
REMARK 500 1 ALA A -1 170.05 54.51
REMARK 500 1 SER A 2 61.66 175.23
REMARK 500 1 LYS A 4 -141.55 -62.00
REMARK 500 1 LEU A 9 -77.37 -75.41
REMARK 500 1 LYS A 11 -79.10 -37.53
REMARK 500 1 THR A 12 52.46 -95.68
REMARK 500 1 ARG A 13 -45.41 -150.12
REMARK 500 1 GLU A 21 175.18 -52.69
REMARK 500 1 HIS A 26 136.63 87.31
REMARK 500 1 LYS A 27 -96.20 -123.44
REMARK 500 1 LEU A 32 -61.94 -94.88
REMARK 500 1 HIS A 33 -147.05 66.81
REMARK 500 1 ILE A 35 -144.77 -60.00
REMARK 500 1 PHE A 36 106.47 53.89
REMARK 500 1 SER A 40 -153.44 36.16
REMARK 500 1 GLN A 42 27.95 -141.50
REMARK 500 1 ALA A 51 -54.10 -121.06
REMARK 500 1 LYS A 54 46.85 -85.26
REMARK 500 1 LYS A 55 -47.14 -141.20
REMARK 500 1 VAL A 57 93.55 -63.40
REMARK 500 1 LEU A 58 109.47 -54.04
REMARK 500 1 ASP A 60 -64.78 -167.14
REMARK 500 1 GLU A 61 -77.77 -166.77
REMARK 500 1 LYS A 73 -66.33 -101.52
REMARK 500 1 MET A 80 95.04 -63.42
REMARK 500 1 GLU A 88 -32.08 -38.95
REMARK 500 1 LEU A 94 -76.64 -43.28
REMARK 500 2 GLU A -4 60.08 -169.13
REMARK 500 2 SER A 2 -95.53 55.49
REMARK 500 2 ALA A 3 -143.30 51.16
REMARK 500 2 LYS A 5 -34.14 173.01
REMARK 500 2 LEU A 9 -78.22 -77.09
REMARK 500 2 LYS A 11 -32.64 -38.49
REMARK 500 2 ARG A 13 21.21 89.61
REMARK 500 2 CYS A 14 -71.77 -156.10
REMARK 500 2 HIS A 26 137.38 84.03
REMARK 500 2 LYS A 27 -100.49 -114.54
REMARK 500 2 HIS A 33 103.64 -38.85
REMARK 500 2 ILE A 35 -158.10 -60.81
REMARK 500 2 PHE A 36 92.90 58.01
REMARK 500 2 SER A 40 -160.31 39.01
REMARK 500 2 ASN A 52 -80.08 -65.43
REMARK 500 2 ILE A 53 -32.86 -39.58
REMARK 500 2 LYS A 54 46.89 -85.12
REMARK 500 2 LYS A 55 -46.99 -139.53
REMARK 500 2 ASP A 60 -69.60 -153.65
REMARK 500 2 GLU A 61 -80.39 -167.67
REMARK 500 2 THR A 69 -55.37 72.88
REMARK 500 2 MET A 80 92.19 -58.93
REMARK 500
REMARK 500 THIS ENTRY HAS 538 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 HEC A 104 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 18 NE2
REMARK 620 2 HEC A 104 NA 88.1
REMARK 620 3 HEC A 104 NB 88.3 93.9
REMARK 620 4 HEC A 104 NC 89.6 172.3 93.3
REMARK 620 5 HEC A 104 ND 89.1 85.9 177.3 86.7
REMARK 620 6 MET A 80 SD 166.3 83.0 102.6 97.9 80.0
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 HEC A 104
DBREF 1YFC A -5 103 UNP P00044 CYC1_YEAST 1 108
SEQADV 1YFC M3L A 72 UNP P00044 LYS 77 MODIFIED RESIDUE
SEQADV 1YFC SER A 102 UNP P00044 CYS 107 ENGINEERED MUTATION
SEQRES 1 A 108 THR GLU PHE LYS ALA GLY SER ALA LYS LYS GLY ALA THR
SEQRES 2 A 108 LEU PHE LYS THR ARG CYS LEU GLN CYS HIS THR VAL GLU
SEQRES 3 A 108 LYS GLY GLY PRO HIS LYS VAL GLY PRO ASN LEU HIS GLY
SEQRES 4 A 108 ILE PHE GLY ARG HIS SER GLY GLN ALA GLU GLY TYR SER
SEQRES 5 A 108 TYR THR ASP ALA ASN ILE LYS LYS ASN VAL LEU TRP ASP
SEQRES 6 A 108 GLU ASN ASN MET SER GLU TYR LEU THR ASN PRO M3L LYS
SEQRES 7 A 108 TYR ILE PRO GLY THR LYS MET ALA PHE GLY GLY LEU LYS
SEQRES 8 A 108 LYS GLU LYS ASP ARG ASN ASP LEU ILE THR TYR LEU LYS
SEQRES 9 A 108 LYS ALA SER GLU
MODRES 1YFC M3L A 72 LYS N-TRIMETHYLLYSINE
HET M3L A 72 31
HET HEC A 104 75
HETNAM M3L N-TRIMETHYLLYSINE
HETNAM HEC HEME C
FORMUL 1 M3L C9 H21 N2 O2 1+
FORMUL 2 HEC C34 H34 FE N4 O4
HELIX 1 1 ALA A 7 LYS A 11 1 5
HELIX 2 2 ASN A 62 THR A 69 1 8
HELIX 3 3 PRO A 71 TYR A 74 5 4
HELIX 4 4 GLU A 88 ALA A 101 1 14
LINK SG CYS A 14 CAB HEC A 104 1555 1555 1.80
LINK SG CYS A 17 CAC HEC A 104 1555 1555 1.75
LINK C PRO A 71 N M3L A 72 1555 1555 1.32
LINK C M3L A 72 N LYS A 73 1555 1555 1.33
LINK NE2 HIS A 18 FE HEC A 104 1555 1555 1.99
LINK SD MET A 80 FE HEC A 104 1555 1555 2.55
SITE 1 AC1 18 ARG A 13 CYS A 14 GLN A 16 CYS A 17
SITE 2 AC1 18 HIS A 18 VAL A 28 PRO A 30 LEU A 32
SITE 3 AC1 18 TYR A 48 THR A 49 ASN A 52 MET A 64
SITE 4 AC1 18 TYR A 67 LEU A 68 LYS A 79 MET A 80
SITE 5 AC1 18 ALA A 81 PHE A 82
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
(ATOM LINES ARE NOT SHOWN.)
END