HEADER ELECTRON TRANSPORT 07-OCT-11 2LK6
TITLE NMR DETERMINATION OF THE GLOBAL STRUCTURE OF THE CD-113 DERIVATIVE OF
TITLE 2 DESULFOREDOXIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DESULFOREDOXIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: DX;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DESULFOVIBRIO GIGAS;
SOURCE 3 ORGANISM_TAXID: 879;
SOURCE 4 GENE: DSR;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR: DSRT77-2
KEYWDS ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 18
AUTHOR B.J.GOODFELLOW,F.RUSNAK,I.MOURA,T.DOMKE,J.J.G.MOURA
REVDAT 1 25-JAN-12 2LK6 0
JRNL AUTH B.J.GOODFELLOW,F.RUSNAK,I.MOURA,T.DOMKE,J.J.MOURA
JRNL TITL NMR DETERMINATION OF THE GLOBAL STRUCTURE OF THE 113CD
JRNL TITL 2 DERIVATIVE OF DESULFOREDOXIN: INVESTIGATION OF THE HYDROGEN
JRNL TITL 3 BONDING PATTERN AT THE METAL CENTER.
JRNL REF PROTEIN SCI. V. 7 928 1998
JRNL REFN ISSN 0961-8368
JRNL PMID 9568899
JRNL DOI 10.1002/PRO.5560070410
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DIANA 2.8
REMARK 3 AUTHORS : GUNTERT, BRAUN AND WUTHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2LK6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-OCT-11.
REMARK 100 THE RCSB ID CODE IS RCSB102481.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 7
REMARK 210 IONIC STRENGTH : 0
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 10 MM POTASSIUM PHOSPHATE, 90%
REMARK 210 H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-1H TOCSY; 2D 1H-1H NOESY;
REMARK 210 2D DQF-COSY; 113CD-1H HSED
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 : XEASY 3.1, DIANA 2.8
REMARK 210 METHOD USED : DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 300
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 18
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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: 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 ASN A 2 130.57 67.18
REMARK 500 1 GLU A 3 167.34 -46.07
REMARK 500 1 LEU A 11 -65.59 -131.92
REMARK 500 1 GLU A 21 163.47 -43.31
REMARK 500 1 ASN B 2 112.90 -174.06
REMARK 500 1 GLU B 3 151.64 -42.09
REMARK 500 1 LEU B 11 -65.37 -130.59
REMARK 500 1 LEU B 26 78.73 -108.86
REMARK 500 2 ASN A 2 95.94 53.87
REMARK 500 2 GLU A 3 159.62 -40.16
REMARK 500 2 GLU A 10 30.21 -96.01
REMARK 500 2 LEU A 11 -66.12 -131.93
REMARK 500 2 GLU B 3 157.50 -47.55
REMARK 500 2 LEU B 11 -69.81 -133.82
REMARK 500 2 LEU B 26 76.36 -102.71
REMARK 500 2 MET B 33 150.60 -47.92
REMARK 500 3 LEU A 11 -65.19 -126.96
REMARK 500 3 GLU A 21 163.15 -48.32
REMARK 500 3 MET A 33 144.99 -38.41
REMARK 500 3 LEU B 11 -70.64 -108.40
REMARK 500 3 GLU B 21 165.85 -49.72
REMARK 500 3 LEU B 26 76.93 -107.37
REMARK 500 4 ASN A 2 98.99 58.44
REMARK 500 4 GLU A 3 152.84 -45.09
REMARK 500 4 LEU A 11 -68.12 -133.10
REMARK 500 4 LEU A 26 77.72 -109.92
REMARK 500 4 GLU B 3 157.41 -46.84
REMARK 500 4 GLU B 10 32.70 -97.24
REMARK 500 4 LEU B 11 -80.73 -141.79
REMARK 500 4 LEU B 26 73.12 -106.40
REMARK 500 4 MET B 33 153.30 -41.84
REMARK 500 5 ASN A 2 114.75 173.33
REMARK 500 5 GLU A 3 156.00 -38.45
REMARK 500 5 GLU A 10 30.11 -94.41
REMARK 500 5 LEU A 11 -65.02 -131.82
REMARK 500 5 LEU A 26 77.32 -116.54
REMARK 500 5 GLU B 3 149.61 59.60
REMARK 500 5 LEU B 11 -78.51 -141.62
REMARK 500 6 ASN A 2 90.79 41.14
REMARK 500 6 GLU A 3 151.84 -37.93
REMARK 500 6 GLU A 10 38.92 -88.84
REMARK 500 6 LEU A 11 -62.22 -140.76
REMARK 500 6 ASN B 2 129.86 69.41
REMARK 500 6 GLU B 10 35.82 -89.86
REMARK 500 6 LEU B 11 -78.73 -145.26
REMARK 500 7 ASN A 2 116.81 -176.14
REMARK 500 7 GLU A 3 152.71 -43.44
REMARK 500 7 GLU A 10 32.68 -99.28
REMARK 500 7 LEU A 11 -67.05 -135.46
REMARK 500 7 LEU A 26 73.03 -111.41
REMARK 500
REMARK 500 THIS ENTRY HAS 132 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 1 CD A 37 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 12 SG
REMARK 620 2 CYS A 29 SG 114.2
REMARK 620 3 CYS A 28 SG 110.6 120.0
REMARK 620 4 CYS A 9 SG 96.1 107.5 105.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 1 CD B 37 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 12 SG
REMARK 620 2 CYS B 29 SG 111.4
REMARK 620 3 CYS B 28 SG 109.4 124.0
REMARK 620 4 CYS B 9 SG 95.8 107.4 104.8
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 37
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 37
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DCD RELATED DB: PDB
REMARK 900 RELATED ID: 17997 RELATED DB: BMRB
DBREF 2LK6 A 1 36 UNP P00273 DESR_DESGI 2 37
DBREF 2LK6 B 1 36 UNP P00273 DESR_DESGI 2 37
SEQRES 1 A 36 ALA ASN GLU GLY ASP VAL TYR LYS CYS GLU LEU CYS GLY
SEQRES 2 A 36 GLN VAL VAL LYS VAL LEU GLU GLU GLY GLY GLY THR LEU
SEQRES 3 A 36 VAL CYS CYS GLY GLU ASP MET VAL LYS GLN
SEQRES 1 B 36 ALA ASN GLU GLY ASP VAL TYR LYS CYS GLU LEU CYS GLY
SEQRES 2 B 36 GLN VAL VAL LYS VAL LEU GLU GLU GLY GLY GLY THR LEU
SEQRES 3 B 36 VAL CYS CYS GLY GLU ASP MET VAL LYS GLN
HET CD A 37 1
HET CD B 37 1
HETNAM CD CADMIUM ION
FORMUL 3 CD 2(CD 2+)
SHEET 1 A 6 VAL A 34 LYS A 35 0
SHEET 2 A 6 ASP A 5 LYS A 8 -1 N LYS A 8 O VAL A 34
SHEET 3 A 6 VAL A 15 GLU A 20 -1 O VAL A 16 N TYR A 7
SHEET 4 A 6 VAL B 15 GLU B 20 -1 O LYS B 17 N LYS A 17
SHEET 5 A 6 ASP B 5 LYS B 8 -1 N TYR B 7 O VAL B 16
SHEET 6 A 6 VAL B 34 LYS B 35 -1 O VAL B 34 N LYS B 8
SHEET 1 B 2 VAL A 27 CYS A 28 0
SHEET 2 B 2 GLU A 31 ASP A 32 -1 O GLU A 31 N CYS A 28
SHEET 1 C 2 VAL B 27 CYS B 28 0
SHEET 2 C 2 GLU B 31 ASP B 32 -1 O GLU B 31 N CYS B 28
LINK SG CYS A 12 CD CD A 37 1555 1555 2.42
LINK SG CYS A 29 CD CD A 37 1555 1555 2.44
LINK SG CYS B 12 CD CD B 37 1555 1555 2.45
LINK SG CYS B 29 CD CD B 37 1555 1555 2.45
LINK SG CYS A 28 CD CD A 37 1555 1555 2.48
LINK SG CYS B 28 CD CD B 37 1555 1555 2.48
LINK SG CYS A 9 CD CD A 37 1555 1555 2.60
LINK SG CYS B 9 CD CD B 37 1555 1555 2.60
SITE 1 AC1 4 CYS A 9 CYS A 12 CYS A 28 CYS A 29
SITE 1 AC2 4 CYS B 9 CYS B 12 CYS B 28 CYS B 29
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
