Header list of 1l6u.pdb file
Complete list - b 5 2 Bytes
HEADER ELECTRON TRANSPORT 14-MAR-02 1L6U
TITLE NMR STRUCTURE OF OXIDIZED ADRENODOXIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADRENODOXIN 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ADRENAL FERREDOXIN, HEPATO-FERREDOXIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 ORGAN: ADRENAL GLAND;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS [2FE-2S]-CLUSTER, PRIMARY INTERACTION DOMAIN (HELIX FROM ASP72-
KEYWDS 2 ASP79), (ALPHA-BETA)-PROTEIN, 5 HELICES, 5 BETA STRANDS, ELECTRON
KEYWDS 3 TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR D.BEILKE,R.WEISS,F.LOHR,P.PRISTOVSEK,F.HANNEMANN,R.BERNHARDT,
AUTHOR 2 H.RUETERJANS
REVDAT 4 05-FEB-20 1L6U 1 REMARK ATOM
REVDAT 3 24-FEB-09 1L6U 1 VERSN
REVDAT 2 01-APR-03 1L6U 1 JRNL
REVDAT 1 26-JUN-02 1L6U 0
JRNL AUTH D.BEILKE,R.WEISS,F.LOHR,P.PRISTOVSEK,F.HANNEMANN,
JRNL AUTH 2 R.BERNHARDT,H.RUTERJANS
JRNL TITL A NEW ELECTRON TRANSPORT MECHANISM IN MITOCHONDRIAL STEROID
JRNL TITL 2 HYDROXYLASE SYSTEMS BASED ON STRUCTURAL CHANGES UPON THE
JRNL TITL 3 REDUCTION OF ADRENODOXIN.
JRNL REF BIOCHEMISTRY V. 41 7969 2002
JRNL REFN ISSN 0006-2960
JRNL PMID 12069587
JRNL DOI 10.1021/BI0160361
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.MULLER,J.J.MULLER,Y.A.MULLER,H.UHLMANN,R.BERNHARDT,
REMARK 1 AUTH 2 U.HEINEMANN
REMARK 1 TITL NEW ASPECTS OF ELECTRON TRANSFER REVEALED BY THE CRYSTAL
REMARK 1 TITL 2 STRUCTURE OF A TRUNCATED BOVINE ADRENODOXIN, ADX(4-108)
REMARK 1 REF STRUCTURE V. 6 269 1998
REMARK 1 REFN ISSN 0969-2126
REMARK 1 DOI 10.1016/S0969-2126(98)00031-8
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 1.1, DYANA 1.5
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUENTERT (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1L6U COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-MAR-02.
REMARK 100 THE DEPOSITION ID IS D_1000015698.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 7.4
REMARK 210 IONIC STRENGTH : 100 MM SALT
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 2-3MM ADRENODOXIN 15N,13C, 50 MM
REMARK 210 PHOSPHATE BUFFER, 50MM NACL, 10%
REMARK 210 D2O, 0.04% NAN3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA 1.5, NMR2ST 1.0
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY
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 1-10
REMARK 465 RES C SSSEQI
REMARK 465 ASP A 109
REMARK 465 ALA A 110
REMARK 465 VAL A 111
REMARK 465 SER A 112
REMARK 465 ASP A 113
REMARK 465 ALA A 114
REMARK 465 ARG A 115
REMARK 465 GLU A 116
REMARK 465 SER A 117
REMARK 465 ILE A 118
REMARK 465 ASP A 119
REMARK 465 MET A 120
REMARK 465 GLY A 121
REMARK 465 MET A 122
REMARK 465 ASN A 123
REMARK 465 SER A 124
REMARK 465 SER A 125
REMARK 465 LYS A 126
REMARK 465 ILE A 127
REMARK 465 GLU A 128
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 MODELS 1-10
REMARK 470 RES CSSEQI ATOMS
REMARK 470 LYS A 6 NZ
REMARK 470 HIS A 10 NE2
REMARK 470 LYS A 22 NZ
REMARK 470 LYS A 24 NZ
REMARK 470 HIS A 56 NE2
REMARK 470 HIS A 62 NE2
REMARK 470 LYS A 66 NZ
REMARK 470 LYS A 98 NZ
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 PHE A 11 H LEU A 19 1.49
REMARK 500 H ILE A 12 O VAL A 105 1.50
REMARK 500 SG CYS A 52 FE1 FES A 146 1.52
REMARK 500 O LEU A 30 H VAL A 34 1.55
REMARK 500 O VAL A 9 H THR A 21 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 SER A 2 -72.29 -166.25
REMARK 500 1 SER A 3 176.05 174.76
REMARK 500 1 GLU A 4 132.95 -179.83
REMARK 500 1 LYS A 6 127.33 -174.90
REMARK 500 1 LYS A 24 101.77 163.37
REMARK 500 1 ILE A 25 98.63 -32.66
REMARK 500 1 ASP A 27 -152.57 -61.47
REMARK 500 1 SER A 28 119.97 -160.05
REMARK 500 1 LEU A 29 153.78 -42.01
REMARK 500 1 LEU A 30 -52.20 87.70
REMARK 500 1 LEU A 38 88.23 35.17
REMARK 500 1 ASP A 41 104.71 -38.86
REMARK 500 1 PHE A 43 177.15 -47.73
REMARK 500 1 ALA A 45 -47.71 -131.74
REMARK 500 1 GLU A 47 -8.96 86.26
REMARK 500 1 LEU A 50 78.08 72.78
REMARK 500 1 ALA A 51 30.66 -175.11
REMARK 500 1 CYS A 52 -46.92 -142.54
REMARK 500 1 CYS A 55 -122.55 -103.13
REMARK 500 1 HIS A 56 124.77 61.50
REMARK 500 1 HIS A 62 -6.50 82.40
REMARK 500 1 LEU A 84 107.87 -39.88
REMARK 500 1 THR A 85 -168.35 -76.86
REMARK 500 1 ARG A 87 25.87 -146.09
REMARK 500 1 ILE A 94 -161.58 43.29
REMARK 500 1 ASP A 101 96.29 -57.48
REMARK 500 1 ASN A 102 37.76 81.50
REMARK 500 2 LYS A 6 136.82 -170.12
REMARK 500 2 ASN A 13 164.59 -45.46
REMARK 500 2 ILE A 25 104.22 -36.15
REMARK 500 2 LEU A 38 87.61 36.69
REMARK 500 2 ASP A 39 37.88 -98.64
REMARK 500 2 CYS A 46 3.04 -68.53
REMARK 500 2 GLU A 47 -0.85 79.32
REMARK 500 2 LEU A 50 90.25 68.77
REMARK 500 2 ALA A 51 -38.76 -173.36
REMARK 500 2 CYS A 55 -76.39 -41.38
REMARK 500 2 HIS A 56 -176.12 48.71
REMARK 500 2 LEU A 57 169.75 169.92
REMARK 500 2 GLU A 60 141.79 -38.13
REMARK 500 2 ARG A 87 27.79 -140.12
REMARK 500 2 ARG A 89 144.56 175.67
REMARK 500 2 CYS A 92 47.66 -141.19
REMARK 500 2 GLN A 93 -38.54 -176.65
REMARK 500 2 ASP A 101 92.60 14.43
REMARK 500 2 ASN A 102 36.27 82.00
REMARK 500 3 SER A 2 87.84 -164.12
REMARK 500 3 GLU A 4 134.65 179.73
REMARK 500 3 ASP A 5 131.59 162.11
REMARK 500 3 LYS A 24 82.30 176.51
REMARK 500
REMARK 500 THIS ENTRY HAS 225 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 FES A 146 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 46 SG
REMARK 620 2 FES A 146 S1 97.3
REMARK 620 3 FES A 146 S2 110.2 92.0
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES A 146
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4566 RELATED DB: BMRB
REMARK 900 ASSIGNMENT OF OXIDIZED BOVINE ADRENODOXIN
REMARK 900 RELATED ID: 1L6V RELATED DB: PDB
REMARK 900 STRUCTURE OF REDUCED BOVINE ADRENODOXIN
DBREF 1L6U A 1 128 UNP P00257 ADX1_BOVIN 59 186
SEQRES 1 A 128 SER SER SER GLU ASP LYS ILE THR VAL HIS PHE ILE ASN
SEQRES 2 A 128 ARG ASP GLY GLU THR LEU THR THR LYS GLY LYS ILE GLY
SEQRES 3 A 128 ASP SER LEU LEU ASP VAL VAL VAL GLN ASN ASN LEU ASP
SEQRES 4 A 128 ILE ASP GLY PHE GLY ALA CYS GLU GLY THR LEU ALA CYS
SEQRES 5 A 128 SER THR CYS HIS LEU ILE PHE GLU GLN HIS ILE PHE GLU
SEQRES 6 A 128 LYS LEU GLU ALA ILE THR ASP GLU GLU ASN ASP MET LEU
SEQRES 7 A 128 ASP LEU ALA TYR GLY LEU THR ASP ARG SER ARG LEU GLY
SEQRES 8 A 128 CYS GLN ILE CYS LEU THR LYS ALA MET ASP ASN MET THR
SEQRES 9 A 128 VAL ARG VAL PRO ASP ALA VAL SER ASP ALA ARG GLU SER
SEQRES 10 A 128 ILE ASP MET GLY MET ASN SER SER LYS ILE GLU
HET FES A 146 4
HETNAM FES FE2/S2 (INORGANIC) CLUSTER
FORMUL 2 FES FE2 S2
HELIX 1 1 LEU A 30 ASN A 36 1 7
HELIX 2 2 THR A 71 LEU A 78 1 8
HELIX 3 3 THR A 97 ASP A 101 5 5
SHEET 1 A 5 LEU A 19 THR A 21 0
SHEET 2 A 5 VAL A 9 ILE A 12 -1 N PHE A 11 O LEU A 19
SHEET 3 A 5 MET A 103 ARG A 106 1 O VAL A 105 N ILE A 12
SHEET 4 A 5 LEU A 57 PHE A 59 -1 N ILE A 58 O ARG A 106
SHEET 5 A 5 SER A 88 ARG A 89 -1 O ARG A 89 N LEU A 57
SSBOND 1 CYS A 55 CYS A 92 1555 1555 2.98
LINK SG CYS A 46 FE1 FES A 146 1555 1555 2.19
SITE 1 AC1 7 GLY A 44 CYS A 46 GLY A 48 LEU A 50
SITE 2 AC1 7 CYS A 52 CYS A 55 CYS A 92
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 5 2 Bytes