HEADER OXIDOREDUCTASE 15-AUG-07 2JU5
TITLE DSBH OXIDOREDUCTASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THIOREDOXIN DISULFIDE ISOMERASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CHLAMYDOPHILA PNEUMONIAE;
SOURCE 3 ORGANISM_TAXID: 182082;
SOURCE 4 STRAIN: TW-183;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET44-DSBH
KEYWDS PROTEIN, OXIDOREDUCTASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.S.ULMER
REVDAT 7 14-JUN-23 2JU5 1 REMARK
REVDAT 6 20-OCT-21 2JU5 1 SEQADV
REVDAT 5 19-FEB-20 2JU5 1 REMARK SEQADV
REVDAT 4 13-JUL-11 2JU5 1 VERSN
REVDAT 3 24-FEB-09 2JU5 1 VERSN
REVDAT 2 22-JAN-08 2JU5 1 JRNL
REVDAT 1 27-NOV-07 2JU5 0
JRNL AUTH T.T.MAC,A.VON HACHT,K.C.HUNG,R.J.DUTTON,D.BOYD,J.C.BARDWELL,
JRNL AUTH 2 T.S.ULMER
JRNL TITL INSIGHT INTO DISULFIDE BOND CATALYSIS IN CHLAMYDIA FROM THE
JRNL TITL 2 STRUCTURE AND FUNCTION OF DSBH, A NOVEL OXIDOREDUCTASE.
JRNL REF J.BIOL.CHEM. V. 283 824 2008
JRNL REFN ISSN 0021-9258
JRNL PMID 18003611
JRNL DOI 10.1074/JBC.M707863200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR NIH
REMARK 3 AUTHORS : SCHWIETERS, C.D. ET AL.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2JU5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-AUG-07.
REMARK 100 THE DEPOSITION ID IS D_1000100293.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298.2
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 100 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.0 MM [U-99% 13C; U-99% 15N]
REMARK 210 DSBH, 95% H2O/5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D 1H-13C NOESY; 3D 1H-15N
REMARK 210 NOESY; 3D HNCO; 3D HNCACB; 3D
REMARK 210 CBCA(CO)NH
REMARK 210 SPECTROMETER FIELD STRENGTH : 700 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 : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES
REMARK 210 SUBMITTED
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 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 1-20
REMARK 465 RES C SSSEQI
REMARK 465 MET A -9
REMARK 465 ALA A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 SER A -1
REMARK 465 ALA A 0
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 HIS A 32 H ASP A 36 1.49
REMARK 500 OD1 ASP A 114 H LYS A 118 1.50
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 ARG A 14 71.90 59.06
REMARK 500 1 ALA A 17 -120.74 57.47
REMARK 500 1 THR A 105 -50.35 -120.03
REMARK 500 2 ARG A 2 51.13 -68.30
REMARK 500 2 ARG A 14 85.03 56.42
REMARK 500 3 ARG A 4 92.49 51.09
REMARK 500 3 GLN A 11 -166.65 53.04
REMARK 500 3 ALA A 17 132.24 70.84
REMARK 500 3 ASN A 20 -178.40 59.57
REMARK 500 4 GLN A 12 -81.86 56.75
REMARK 500 4 ARG A 14 98.59 -34.11
REMARK 500 5 ARG A 14 82.92 51.42
REMARK 500 6 ASN A 9 73.57 54.82
REMARK 500 6 ARG A 14 76.39 -163.15
REMARK 500 7 ARG A 14 75.51 53.09
REMARK 500 7 ALA A 17 -162.55 57.63
REMARK 500 7 ASN A 20 148.17 56.41
REMARK 500 8 ARG A 14 77.97 -169.49
REMARK 500 8 ALA A 17 99.73 42.07
REMARK 500 9 ARG A 2 -85.86 42.34
REMARK 500 9 ALA A 17 11.41 -157.80
REMARK 500 9 ASN A 20 -141.91 -154.13
REMARK 500 10 ALA A 18 17.33 -151.69
REMARK 500 11 ARG A 14 56.03 -141.62
REMARK 500 11 ALA A 19 -38.82 69.22
REMARK 500 12 GLU A 8 77.85 55.55
REMARK 500 12 ARG A 14 82.53 -158.20
REMARK 500 13 ALA A 5 -41.97 68.23
REMARK 500 13 ASN A 9 79.12 47.88
REMARK 500 13 GLN A 11 83.82 51.68
REMARK 500 14 ALA A 5 105.69 54.40
REMARK 500 14 ALA A 18 134.89 59.39
REMARK 500 14 ASN A 20 -179.32 54.13
REMARK 500 15 ALA A 19 155.44 66.89
REMARK 500 16 HIS A 86 30.32 -97.31
REMARK 500 18 ALA A 17 -69.87 -157.70
REMARK 500 18 ALA A 18 -167.41 42.46
REMARK 500 18 ALA A 19 134.89 63.51
REMARK 500 18 ASN A 20 148.72 64.13
REMARK 500 19 ARG A 14 78.02 -151.66
REMARK 500 20 ALA A 5 178.00 55.74
REMARK 500 20 ARG A 14 68.35 78.30
REMARK 500 20 ALA A 19 95.94 -165.03
REMARK 500 20 THR A 105 -50.40 -122.30
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 15431 RELATED DB: BMRB
DBREF 2JU5 A 1 144 UNP Q9Z6Y0 Q9Z6Y0_CHLPN 23 166
SEQADV 2JU5 MET A -9 UNP Q9Z6Y0 EXPRESSION TAG
SEQADV 2JU5 ALA A -8 UNP Q9Z6Y0 EXPRESSION TAG
SEQADV 2JU5 HIS A -7 UNP Q9Z6Y0 EXPRESSION TAG
SEQADV 2JU5 HIS A -6 UNP Q9Z6Y0 EXPRESSION TAG
SEQADV 2JU5 HIS A -5 UNP Q9Z6Y0 EXPRESSION TAG
SEQADV 2JU5 HIS A -4 UNP Q9Z6Y0 EXPRESSION TAG
SEQADV 2JU5 HIS A -3 UNP Q9Z6Y0 EXPRESSION TAG
SEQADV 2JU5 HIS A -2 UNP Q9Z6Y0 EXPRESSION TAG
SEQADV 2JU5 SER A -1 UNP Q9Z6Y0 EXPRESSION TAG
SEQADV 2JU5 ALA A 0 UNP Q9Z6Y0 EXPRESSION TAG
SEQADV 2JU5 GLY A 41 UNP Q9Z6Y0 CYS 63 ENGINEERED MUTATION
SEQRES 1 A 154 MET ALA HIS HIS HIS HIS HIS HIS SER ALA ALA ARG ARG
SEQRES 2 A 154 ARG ALA SER GLY GLU ASN LEU GLN GLN THR ARG PRO ILE
SEQRES 3 A 154 ALA ALA ALA ASN LEU GLN TRP GLU SER TYR ALA GLU ALA
SEQRES 4 A 154 LEU GLU HIS SER LYS GLN ASP HIS LYS PRO ILE GLY LEU
SEQRES 5 A 154 PHE PHE THR GLY SER ASP TRP CYS MET TRP CYS ILE LYS
SEQRES 6 A 154 MET GLN ASP GLN ILE LEU GLN SER SER GLU PHE LYS HIS
SEQRES 7 A 154 PHE ALA GLY VAL HIS LEU HIS MET VAL GLU VAL ASP PHE
SEQRES 8 A 154 PRO GLN LYS ASN HIS GLN PRO GLU GLU GLN ARG GLN LYS
SEQRES 9 A 154 ASN GLN GLU LEU LYS ALA GLN TYR LYS VAL THR GLY PHE
SEQRES 10 A 154 PRO GLU LEU VAL PHE ILE ASP ALA GLU GLY LYS GLN LEU
SEQRES 11 A 154 ALA ARG MET GLY PHE GLU PRO GLY GLY GLY ALA ALA TYR
SEQRES 12 A 154 VAL SER LYS VAL LYS SER ALA LEU LYS LEU ARG
HELIX 1 1 ALA A 1 SER A 6 1 6
HELIX 2 2 SER A 25 HIS A 37 1 13
HELIX 3 3 CYS A 50 ILE A 60 1 11
HELIX 4 4 SER A 63 LEU A 74 1 12
HELIX 5 5 PRO A 88 TYR A 102 1 15
HELIX 6 6 GLY A 129 LYS A 142 1 14
SHEET 1 A 5 TRP A 23 GLU A 24 0
SHEET 2 A 5 HIS A 75 ASP A 80 1 O MET A 76 N GLU A 24
SHEET 3 A 5 ILE A 40 THR A 45 1 N GLY A 41 O VAL A 77
SHEET 4 A 5 GLU A 109 ILE A 113 -1 O ILE A 113 N ILE A 40
SHEET 5 A 5 GLN A 119 MET A 123 -1 O MET A 123 N LEU A 110
SSBOND 1 CYS A 50 CYS A 53 1555 1555 2.02
CISPEP 1 PHE A 107 PRO A 108 1 -0.68
CISPEP 2 PHE A 107 PRO A 108 2 -0.04
CISPEP 3 PHE A 107 PRO A 108 3 -0.63
CISPEP 4 PHE A 107 PRO A 108 4 -0.67
CISPEP 5 PHE A 107 PRO A 108 5 0.88
CISPEP 6 PHE A 107 PRO A 108 6 0.34
CISPEP 7 PHE A 107 PRO A 108 7 0.05
CISPEP 8 PHE A 107 PRO A 108 8 -0.64
CISPEP 9 PHE A 107 PRO A 108 9 -0.35
CISPEP 10 PHE A 107 PRO A 108 10 0.17
CISPEP 11 PHE A 107 PRO A 108 11 -0.06
CISPEP 12 PHE A 107 PRO A 108 12 -0.73
CISPEP 13 PHE A 107 PRO A 108 13 -0.99
CISPEP 14 PHE A 107 PRO A 108 14 -0.37
CISPEP 15 PHE A 107 PRO A 108 15 -0.40
CISPEP 16 PHE A 107 PRO A 108 16 -0.43
CISPEP 17 PHE A 107 PRO A 108 17 -0.87
CISPEP 18 PHE A 107 PRO A 108 18 -0.75
CISPEP 19 PHE A 107 PRO A 108 19 -0.38
CISPEP 20 PHE A 107 PRO A 108 20 -0.87
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
