Header list of 2auv.pdb file
Complete list - r 9 2 Bytes
HEADER OXIDOREDUCTASE 29-AUG-05 2AUV
TITLE SOLUTION STRUCTURE OF HNDAC : A THIOREDOXIN-LIKE [2FE-2S] FERREDOXIN
TITLE 2 INVOLVED IN THE NADP-REDUCING HYDROGENASE COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POTENTIAL NAD-REDUCING HYDROGENASE SUBUNIT;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SUBUNIT A C-TERMINAL DOMAIN;
COMPND 5 EC: 1.12.1.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DESULFOVIBRIO FRUCTOSOVORANS;
SOURCE 3 ORGANISM_TAXID: 878;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-HNDAC
KEYWDS THIOREDOXIN, THIORDOXIN-LIKE, OXIDOREDUCTASE
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR M.NOUAILLER,X.MORELLI,O.BORNET,B.CHETRIT,Z.DERMOUN,F.GUERLESQUIN
REVDAT 3 09-MAR-22 2AUV 1 REMARK LINK
REVDAT 2 24-FEB-09 2AUV 1 VERSN
REVDAT 1 27-JUN-06 2AUV 0
JRNL AUTH M.NOUAILLER,X.MORELLI,O.BORNET,B.CHETRIT,Z.DERMOUN,
JRNL AUTH 2 F.GUERLESQUIN
JRNL TITL SOLUTION STRUCTURE OF HNDAC: A THIOREDOXIN-LIKE DOMAIN
JRNL TITL 2 INVOLVED IN THE NADP-REDUCING HYDROGENASE COMPLEX
JRNL REF PROTEIN SCI. V. 15 1369 2006
JRNL REFN ISSN 0961-8368
JRNL PMID 16731971
JRNL DOI 10.1110/PS.051916606
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.0, ARIA 1.2
REMARK 3 AUTHORS : BRUKER (XWINNMR), JP LINGE, SI O'DONOGHUE AND M
REMARK 3 NILGES (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2AUV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 31-AUG-05.
REMARK 100 THE DEPOSITION ID IS D_1000034340.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 10MM SODIUM PHOSPHATE BUFFER,
REMARK 210 100MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM OXIDIZED HNDAC, 10MM SODIUM
REMARK 210 PHOSPHATE BUFFER (PH 6.0), 100MM
REMARK 210 NACL; 1MM OXIDIZED HNDAC; 1MM
REMARK 210 OXIDIZED HNDAC U-15N, 10MM
REMARK 210 SODIUM PHOSPHATE BUFFER (PH 6.0),
REMARK 210 100MM NACL; 0.15MM OXIDIZED
REMARK 210 HNDAC U-15N,13C, 10MM SODIUM
REMARK 210 PHOSPHATE BUFFER (PH 6.0), 100MM
REMARK 210 NACL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY;
REMARK 210 3D_15N-SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_TOCSY; HNCA-J
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 3.0, FELIX 2002, CNS
REMARK 210 1.1, ARIA 1.2
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES AND 2D/3D HETERONUCLEAR TECHNIQUES
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 HA2 GLY A 5 HB2 SER A 47 1.16
REMARK 500 OD2 ASP A 39 H PHE A 46 1.58
REMARK 500 O LEU A 33 H ILE A 35 1.58
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 3 TYR A 70 CE1 TYR A 70 CZ -0.086
REMARK 500 5 TYR A 7 CE1 TYR A 7 CZ -0.089
REMARK 500 5 TYR A 7 CZ TYR A 7 CE2 0.132
REMARK 500 10 TYR A 7 CZ TYR A 7 CE2 0.102
REMARK 500 12 TYR A 7 CE1 TYR A 7 CZ -0.104
REMARK 500 12 TYR A 7 CZ TYR A 7 CE2 0.107
REMARK 500 14 TYR A 70 CE1 TYR A 70 CZ 0.102
REMARK 500 14 TYR A 70 CZ TYR A 70 CE2 -0.103
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 PRO A 8 94.35 -52.72
REMARK 500 1 LYS A 34 -18.81 61.04
REMARK 500 1 ILE A 35 -164.50 51.71
REMARK 500 1 ASP A 36 -55.64 -155.51
REMARK 500 1 ILE A 37 9.98 -167.53
REMARK 500 1 VAL A 40 -68.33 18.83
REMARK 500 1 PRO A 42 89.56 -33.06
REMARK 500 1 ASP A 43 -65.10 -144.36
REMARK 500 1 CYS A 57 -33.32 -133.19
REMARK 500 1 GLU A 67 25.88 -79.53
REMARK 500 1 VAL A 69 99.53 46.26
REMARK 500 1 TYR A 70 -153.21 -117.03
REMARK 500 1 VAL A 73 -90.31 -126.41
REMARK 500 1 THR A 74 -66.60 -137.77
REMARK 500 2 PRO A 8 92.81 -61.48
REMARK 500 2 LYS A 34 -19.52 65.77
REMARK 500 2 ILE A 35 -170.17 54.36
REMARK 500 2 ASP A 36 -49.56 -157.38
REMARK 500 2 ILE A 37 5.87 -164.92
REMARK 500 2 VAL A 40 -71.73 54.99
REMARK 500 2 THR A 41 -57.72 -151.18
REMARK 500 2 ARG A 45 -64.69 -94.70
REMARK 500 2 CYS A 57 -32.65 -135.70
REMARK 500 2 GLU A 67 37.96 -78.83
REMARK 500 2 VAL A 69 113.72 47.54
REMARK 500 2 VAL A 73 -165.05 64.33
REMARK 500 2 THR A 74 -46.67 -138.58
REMARK 500 3 LYS A 4 -74.38 -50.37
REMARK 500 3 PRO A 8 96.55 -53.34
REMARK 500 3 LYS A 34 -21.86 70.16
REMARK 500 3 ILE A 35 -176.47 56.56
REMARK 500 3 ASP A 36 -44.11 -158.68
REMARK 500 3 ILE A 37 -0.94 -168.30
REMARK 500 3 ASP A 39 135.54 -171.54
REMARK 500 3 VAL A 40 -65.57 39.06
REMARK 500 3 THR A 41 -60.11 -150.82
REMARK 500 3 ASP A 43 -1.75 83.38
REMARK 500 3 CYS A 57 -32.49 -135.12
REMARK 500 3 GLU A 67 34.48 -79.06
REMARK 500 3 VAL A 69 108.10 36.54
REMARK 500 3 VAL A 73 -168.56 63.31
REMARK 500 3 THR A 74 -46.36 -135.74
REMARK 500 4 PRO A 8 96.78 -50.69
REMARK 500 4 LYS A 34 -27.34 68.09
REMARK 500 4 ILE A 35 -173.89 55.55
REMARK 500 4 ASP A 36 -53.55 -155.14
REMARK 500 4 ILE A 37 19.42 -174.43
REMARK 500 4 ASP A 39 119.82 -165.27
REMARK 500 4 VAL A 40 -65.40 56.11
REMARK 500 4 THR A 41 -59.79 -164.19
REMARK 500
REMARK 500 THIS ENTRY HAS 235 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 THR A 41 PRO A 42 1 -149.01
REMARK 500 THR A 50 LEU A 51 1 -149.84
REMARK 500 THR A 50 LEU A 51 3 -147.97
REMARK 500 THR A 50 LEU A 51 4 -147.84
REMARK 500 ILE A 62 VAL A 63 6 147.56
REMARK 500 THR A 50 LEU A 51 8 -148.02
REMARK 500 THR A 50 LEU A 51 10 -148.17
REMARK 500 THR A 50 LEU A 51 11 -149.25
REMARK 500 ASN A 72 VAL A 73 11 -148.58
REMARK 500 ILE A 62 VAL A 63 14 148.39
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 5 TYR A 7 0.08 SIDE CHAIN
REMARK 500 6 TYR A 7 0.08 SIDE CHAIN
REMARK 500 10 TYR A 7 0.07 SIDE CHAIN
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 86 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 17 SG
REMARK 620 2 FES A 86 S1 111.4
REMARK 620 3 FES A 86 S2 145.1 94.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES A 86 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 57 SG
REMARK 620 2 FES A 86 S1 128.0
REMARK 620 3 FES A 86 S2 113.3 69.2
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 86
DBREF 2AUV A 1 85 UNP Q46505 Q46505_DESFR 87 171
SEQRES 1 A 85 MET VAL PRO LYS GLY LYS TYR PRO ILE SER VAL CYS MET
SEQRES 2 A 85 GLY THR ALA CYS PHE VAL LYS GLY ALA ASP LYS VAL VAL
SEQRES 3 A 85 HIS ALA PHE LYS GLU GLN LEU LYS ILE ASP ILE GLY ASP
SEQRES 4 A 85 VAL THR PRO ASP GLY ARG PHE SER ILE ASP THR LEU ARG
SEQRES 5 A 85 CYS VAL GLY GLY CYS ALA LEU ALA PRO ILE VAL MET VAL
SEQRES 6 A 85 GLY GLU LYS VAL TYR GLY ASN VAL THR PRO GLY GLN VAL
SEQRES 7 A 85 LYS LYS ILE LEU ALA GLU TYR
HET FES A 86 4
HETNAM FES FE2/S2 (INORGANIC) CLUSTER
FORMUL 2 FES FE2 S2
HELIX 1 1 GLY A 14 VAL A 19 1 6
HELIX 2 2 GLY A 21 LYS A 34 1 14
HELIX 3 3 GLU A 67 VAL A 69 5 3
HELIX 4 4 GLY A 76 TYR A 85 1 10
SHEET 1 A 2 ILE A 9 SER A 10 0
SHEET 2 A 2 MET A 64 VAL A 65 -1 O MET A 64 N SER A 10
LINK SG CYS A 17 FE1 FES A 86 1555 1555 2.23
LINK SG CYS A 57 FE2 FES A 86 1555 1555 2.25
SITE 1 AC1 6 CYS A 12 CYS A 17 CYS A 53 VAL A 54
SITE 2 AC1 6 GLY A 55 CYS A 57
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 - r 9 2 Bytes