HEADER ELECTRON TRANSPORT 15-JAN-08 2JZS
TITLE SOLUTION STRUCTURE OF THE REDUCED FORM OF THE N-TERMINAL DOMAIN OF
TITLE 2 PILB FROM N. MENINGITIDIS.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEPTIDE METHIONINE SULFOXIDE REDUCTASE MSRA/MSRB;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: THIOREDOXIN DOMAIN;
COMPND 5 SYNONYM: THIOREDOXIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NEISSERIA MENINGITIDIS SEROGROUP A;
SOURCE 3 GENE: MSRAB, PILB;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_VECTOR: PETNTERPILB
KEYWDS REDUCED, NEISSERIA MENINGITIDIS, PILB, N-TERMINAL DOMAIN,
KEYWDS 2 THIOREDOXIN, ELECTRON TRANSPORT, MULTIFUNCTIONAL ENZYME,
KEYWDS 3 OXIDOREDUCTASE, REDOX-ACTIVE CENTER, TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.QUINTERNET,P.TSAN,F.NEIERS,C.BEAUFILS,S.BOSCHI-MULLER,M.AVERLANT-
AUTHOR 2 PETIT,G.BRANLANT,M.CUNG
REVDAT 4 16-MAR-22 2JZS 1 REMARK SEQADV
REVDAT 3 24-FEB-09 2JZS 1 VERSN
REVDAT 2 26-AUG-08 2JZS 1 JRNL
REVDAT 1 29-JUL-08 2JZS 0
JRNL AUTH M.QUINTERNET,P.TSAN,F.NEIERS,C.BEAUFILS,S.BOSCHI-MULLER,
JRNL AUTH 2 M.C.AVERLANT-PETIT,G.BRANLANT,M.T.CUNG
JRNL TITL SOLUTION STRUCTURE AND DYNAMICS OF THE REDUCED AND OXIDIZED
JRNL TITL 2 FORMS OF THE N-TERMINAL DOMAIN OF PILB FROM NEISSERIA
JRNL TITL 3 MENINGITIDIS.
JRNL REF BIOCHEMISTRY V. 47 8577 2008
JRNL REFN ISSN 0006-2960
JRNL PMID 18651754
JRNL DOI 10.1021/BI800884W
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5, DYANA 1.5
REMARK 3 AUTHORS : GUNTERT, BRAUN AND WUTHRICH (DYANA), GUNTERT,
REMARK 3 BRAUN AND WUTHRICH (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2JZS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-FEB-08.
REMARK 100 THE DEPOSITION ID IS D_1000100495.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 299
REMARK 210 PH : 7
REMARK 210 IONIC STRENGTH : 10
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM [U-100% 13C; U-100% 15N]
REMARK 210 NTERPILBRED, 50 MM DTT, 10 MM
REMARK 210 POTASSIUM CHLORIDE, 90% H2O/10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 3D 1H-15N NOESY;
REMARK 210 3D 1H-13C NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 1000
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
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: 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 ASP A 52 H SER A 56 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 LEU A 9 165.16 -46.55
REMARK 500 1 LYS A 22 -178.14 164.27
REMARK 500 1 LEU A 69 31.35 77.38
REMARK 500 1 LYS A 72 152.04 -39.85
REMARK 500 1 ASN A 85 -171.02 51.09
REMARK 500 1 PRO A 87 46.31 -75.10
REMARK 500 1 LYS A 88 11.71 -140.60
REMARK 500 1 ILE A 105 -79.09 -83.84
REMARK 500 1 ASP A 139 135.20 -170.14
REMARK 500 2 LEU A 9 150.10 -41.62
REMARK 500 2 ASP A 24 16.74 -144.06
REMARK 500 2 ASN A 85 -174.41 59.02
REMARK 500 2 PRO A 87 46.73 -75.00
REMARK 500 2 LYS A 88 11.72 -140.79
REMARK 500 2 ASP A 139 136.85 -174.80
REMARK 500 2 ALA A 142 99.40 -45.42
REMARK 500 3 LYS A 22 -176.79 169.30
REMARK 500 3 ASP A 24 40.05 39.18
REMARK 500 3 HIS A 70 37.54 70.28
REMARK 500 3 LYS A 72 135.94 -39.24
REMARK 500 3 ASN A 85 168.08 60.47
REMARK 500 3 PRO A 87 44.90 -75.06
REMARK 500 3 ASP A 143 160.32 174.91
REMARK 500 4 VAL A 2 64.13 -151.94
REMARK 500 4 LYS A 22 -172.42 163.95
REMARK 500 4 LEU A 84 121.78 -174.52
REMARK 500 5 VAL A 2 62.37 -160.99
REMARK 500 5 PRO A 3 -70.11 -74.99
REMARK 500 5 LYS A 22 -165.19 174.18
REMARK 500 5 ASP A 24 38.84 39.57
REMARK 500 5 ILE A 105 -100.63 -78.22
REMARK 500 5 SER A 106 -6.64 82.54
REMARK 500 5 GLN A 121 -62.12 -93.02
REMARK 500 6 VAL A 2 -52.19 163.56
REMARK 500 6 ASP A 24 34.80 177.07
REMARK 500 6 LYS A 72 142.70 -38.80
REMARK 500 6 ASN A 85 148.28 62.88
REMARK 500 6 PRO A 87 45.81 -74.99
REMARK 500 6 ASP A 143 128.74 64.77
REMARK 500 7 ASP A 24 28.01 -168.44
REMARK 500 7 ASP A 74 157.92 -49.20
REMARK 500 7 PRO A 87 44.73 -75.04
REMARK 500 7 SER A 106 30.90 -142.10
REMARK 500 7 ASP A 143 106.65 64.64
REMARK 500 8 LYS A 22 -173.49 168.15
REMARK 500 8 ASN A 85 -175.83 49.80
REMARK 500 8 PRO A 87 44.71 -74.92
REMARK 500 8 ASP A 143 151.28 68.28
REMARK 500 9 ASP A 24 18.18 -144.45
REMARK 500 9 SER A 57 -29.69 -39.39
REMARK 500
REMARK 500 THIS ENTRY HAS 134 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2JZR RELATED DB: PDB
REMARK 900 RELATED ID: 6709 RELATED DB: BMRB
DBREF 2JZS A 2 144 UNP Q9JWM8 MSRAB_NEIMA 34 176
SEQADV 2JZS MET A 1 UNP Q9JWM8 INITIATING METHIONINE
SEQRES 1 A 144 MET VAL PRO HIS THR LEU SER THR LEU LYS THR ALA ASP
SEQRES 2 A 144 ASN ARG PRO ALA SER VAL TYR LEU LYS LYS ASP LYS PRO
SEQRES 3 A 144 THR LEU ILE LYS PHE TRP ALA SER TRP CYS PRO LEU CYS
SEQRES 4 A 144 LEU SER GLU LEU GLY GLN THR GLU LYS TRP ALA GLN ASP
SEQRES 5 A 144 ALA LYS PHE SER SER ALA ASN LEU ILE THR VAL ALA SER
SEQRES 6 A 144 PRO GLY PHE LEU HIS GLU LYS LYS ASP GLY ASP PHE GLN
SEQRES 7 A 144 LYS TRP TYR ALA GLY LEU ASN TYR PRO LYS LEU PRO VAL
SEQRES 8 A 144 VAL THR ASP ASN GLY GLY THR ILE ALA GLN SER LEU ASN
SEQRES 9 A 144 ILE SER VAL TYR PRO SER TRP ALA LEU ILE GLY LYS ASP
SEQRES 10 A 144 GLY ASP VAL GLN ARG ILE VAL LYS GLY SER ILE ASN GLU
SEQRES 11 A 144 ALA GLN ALA LEU ALA LEU ILE ARG ASP PRO ASN ALA ASP
SEQRES 12 A 144 LEU
HELIX 1 1 VAL A 2 SER A 7 1 6
HELIX 2 2 PRO A 16 LEU A 21 5 6
HELIX 3 3 CYS A 36 ALA A 50 1 15
HELIX 4 4 ASP A 52 SER A 57 1 6
HELIX 5 5 GLY A 75 GLY A 83 1 9
HELIX 6 6 GLY A 97 LEU A 103 1 7
HELIX 7 7 ASN A 129 ASP A 139 1 11
SHEET 1 A 6 LYS A 10 THR A 11 0
SHEET 2 A 6 VAL A 91 THR A 93 -1 O THR A 93 N LYS A 10
SHEET 3 A 6 ASN A 59 ALA A 64 1 N ALA A 64 O VAL A 92
SHEET 4 A 6 THR A 27 PHE A 31 1 N LEU A 28 O ASN A 59
SHEET 5 A 6 SER A 110 ILE A 114 -1 O ALA A 112 N ILE A 29
SHEET 6 A 6 VAL A 120 LYS A 125 -1 O ARG A 122 N LEU A 113
CISPEP 1 TYR A 108 PRO A 109 1 0.06
CISPEP 2 TYR A 108 PRO A 109 2 0.03
CISPEP 3 TYR A 108 PRO A 109 3 0.01
CISPEP 4 TYR A 108 PRO A 109 4 0.00
CISPEP 5 TYR A 108 PRO A 109 5 -0.04
CISPEP 6 TYR A 108 PRO A 109 6 0.00
CISPEP 7 TYR A 108 PRO A 109 7 -0.06
CISPEP 8 TYR A 108 PRO A 109 8 0.00
CISPEP 9 TYR A 108 PRO A 109 9 0.10
CISPEP 10 TYR A 108 PRO A 109 10 0.07
CISPEP 11 TYR A 108 PRO A 109 11 -0.01
CISPEP 12 TYR A 108 PRO A 109 12 -0.12
CISPEP 13 TYR A 108 PRO A 109 13 -0.04
CISPEP 14 TYR A 108 PRO A 109 14 0.00
CISPEP 15 TYR A 108 PRO A 109 15 0.09
CISPEP 16 TYR A 108 PRO A 109 16 -0.04
CISPEP 17 TYR A 108 PRO A 109 17 -0.08
CISPEP 18 TYR A 108 PRO A 109 18 0.08
CISPEP 19 TYR A 108 PRO A 109 19 0.00
CISPEP 20 TYR A 108 PRO A 109 20 0.10
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
