Header list of 1fo5.pdb file
Complete list - b 23 2 Bytes
HEADER OXIDOREDUCTASE 24-AUG-00 1FO5
TITLE SOLUTION STRUCTURE OF REDUCED MJ0307
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THIOREDOXIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MJ0307 PROTEIN DISULFIDE OXIDOREDUCTASE;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METHANOCALDOCOCCUS JANNASCHII;
SOURCE 3 ORGANISM_TAXID: 2190;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PET21A
KEYWDS DISULFIDE OXIDOREDUCTASE, THIOREDOXIN FOLD, STRUCTURAL GENOMICS, BSGC
KEYWDS 2 STRUCTURE FUNDED BY NIH, PROTEIN STRUCTURE INITIATIVE, PSI, BERKELEY
KEYWDS 3 STRUCTURAL GENOMICS CENTER, OXIDOREDUCTASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.W.CAVE,H.S.CHO,A.M.BATCHELDER,R.KIM,H.YOKOTA,D.E.WEMMER,BERKELEY
AUTHOR 2 STRUCTURAL GENOMICS CENTER (BSGC)
REVDAT 5 23-FEB-22 1FO5 1 REMARK
REVDAT 4 24-FEB-09 1FO5 1 VERSN
REVDAT 3 25-JAN-05 1FO5 1 AUTHOR KEYWDS REMARK
REVDAT 2 24-AUG-04 1FO5 1 JRNL KEYWDS REMARK
REVDAT 1 11-APR-01 1FO5 0
JRNL AUTH J.W.CAVE,H.S.CHO,A.M.BATCHELDER,H.YOKOTA,R.KIM,D.E.WEMMER
JRNL TITL SOLUTION NUCLEAR MAGNETIC RESONANCE STRUCTURE OF A PROTEIN
JRNL TITL 2 DISULFIDE OXIDOREDUCTASE FROM METHANOCOCCUS JANNASCHII.
JRNL REF PROTEIN SCI. V. 10 384 2001
JRNL REFN ISSN 0961-8368
JRNL PMID 11266624
JRNL DOI 10.1110/PS.35101
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : UXNMR 910901, OPAL 2.6
REMARK 3 AUTHORS : BRUKER (UXNMR), LUGINBUHL ET AL. (OPAL)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 505 UPPER LIMIT DISTANCE CONSTRAINTS
REMARK 3 52 BACKBONE PHI TORSION ANGLE CONSTRAINTS
REMARK 3 30 HYDROGEN BOND CONSTRAINTS
REMARK 4
REMARK 4 1FO5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-SEP-00.
REMARK 100 THE DEPOSITION ID IS D_1000011761.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308; 298
REMARK 210 PH : 6.3; 6.3
REMARK 210 IONIC STRENGTH : 35MM SODIUM PHOSPHATE; 35MM
REMARK 210 SODIUM PHOSPHATE
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.5MM MJ0307 U-15N; 35MM SODIUM
REMARK 210 PHOSPHATE PH 6.3, 5 MM DTT, 0.02%
REMARK 210 SODIUM AZIDE; 1.5MM MJ0307 U-
REMARK 210 (15N,13C); 35MM SODIUM PHOSPHATE
REMARK 210 PH 6.3, 5 MM DTT, 0.02% SODIUM
REMARK 210 AZIDE; 1.5MM MJ0307; 35MM SODIUM
REMARK 210 PHOSPHATE PH 6.3, 5 MM DTT, 0.02%
REMARK 210 SODIUM AZIDE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HMQC-J; 2D NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 3D_13C-
REMARK 210 SEPARATED_NOESY; 4D_13C-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : AMX; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.0, FELIX 98, DYANA 1.5
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS (DYANA)
REMARK 210 RESTRAINED ENERGY MINIMIZATION
REMARK 210 (OPAL)
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 60
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:
REMARK 210 THE STRUCTURE WAS DETERMINED USING 2D HOMONUCLEAR TECHNIQUES AND
REMARK 210 TRIPLE-RESONANCE NMR 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 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 8 HG1 THR A 9 1.60
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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 ATM2 ATM3
REMARK 500 2 TYR A 38 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 3 ARG A 21 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 3 ARG A 21 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 6 ARG A 21 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 13 TYR A 38 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 14 TYR A 38 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 19 VAL A 26 CG1 - CB - CG2 ANGL. DEV. = 9.9 DEGREES
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 LYS A 2 162.62 66.06
REMARK 500 1 MET A 12 -31.13 -134.62
REMARK 500 1 CYS A 13 -79.36 -77.25
REMARK 500 1 ALA A 18 -118.46 46.88
REMARK 500 1 PRO A 31 39.02 -80.01
REMARK 500 1 ASP A 32 -49.70 -178.19
REMARK 500 1 ALA A 33 48.02 -77.70
REMARK 500 1 VAL A 41 99.86 -68.13
REMARK 500 1 GLU A 43 54.56 36.69
REMARK 500 1 GLN A 46 25.72 -78.96
REMARK 500 1 GLU A 50 -119.23 -69.29
REMARK 500 1 TYR A 51 -171.68 60.59
REMARK 500 1 ASN A 62 -42.96 45.77
REMARK 500 1 THR A 72 -173.73 -58.14
REMARK 500 1 LYS A 73 39.65 -70.41
REMARK 500 1 ARG A 83 81.43 -178.53
REMARK 500 2 PHE A 8 76.41 -105.81
REMARK 500 2 MET A 12 -57.73 -122.57
REMARK 500 2 HIS A 15 15.51 46.98
REMARK 500 2 ALA A 18 -74.84 -50.35
REMARK 500 2 GLU A 29 -57.53 -121.51
REMARK 500 2 ASP A 32 -26.88 -177.78
REMARK 500 2 MET A 42 -56.17 -140.84
REMARK 500 2 ASN A 44 58.71 35.98
REMARK 500 2 MET A 54 -19.92 55.15
REMARK 500 2 ASN A 62 -36.90 51.61
REMARK 500 2 THR A 72 -163.17 -65.33
REMARK 500 2 LYS A 73 27.82 -70.79
REMARK 500 2 GLU A 74 -53.30 -29.30
REMARK 500 2 ARG A 83 -55.70 -177.62
REMARK 500 3 SER A 1 62.48 -156.91
REMARK 500 3 CYS A 13 -71.70 -80.22
REMARK 500 3 HIS A 15 -61.37 57.82
REMARK 500 3 CYS A 16 168.69 58.73
REMARK 500 3 ALA A 18 -125.41 41.37
REMARK 500 3 GLU A 25 -71.98 -52.09
REMARK 500 3 ASP A 32 -63.00 -179.14
REMARK 500 3 VAL A 36 57.41 -152.52
REMARK 500 3 MET A 42 -62.98 -153.01
REMARK 500 3 GLU A 43 11.18 -145.19
REMARK 500 3 GLN A 46 19.26 -69.25
REMARK 500 3 ASN A 62 -50.24 47.23
REMARK 500 3 THR A 72 -173.20 -60.93
REMARK 500 3 GLU A 74 -49.57 -29.35
REMARK 500 3 ARG A 83 133.41 171.25
REMARK 500 4 SER A 1 -29.70 -143.28
REMARK 500 4 LYS A 2 50.28 36.54
REMARK 500 4 CYS A 13 -60.03 132.89
REMARK 500 4 PRO A 14 -73.04 -64.77
REMARK 500 4 CYS A 16 -49.63 -146.61
REMARK 500
REMARK 500 THIS ENTRY HAS 332 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 MET A 0 SER A 1 16 -142.87
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 3 TYR A 51 0.08 SIDE CHAIN
REMARK 500 4 TYR A 51 0.12 SIDE CHAIN
REMARK 500 5 TYR A 51 0.12 SIDE CHAIN
REMARK 500 6 ARG A 83 0.08 SIDE CHAIN
REMARK 500 7 ARG A 21 0.08 SIDE CHAIN
REMARK 500 12 ARG A 21 0.11 SIDE CHAIN
REMARK 500 12 ARG A 83 0.13 SIDE CHAIN
REMARK 500 13 ARG A 21 0.12 SIDE CHAIN
REMARK 500 16 ARG A 21 0.08 SIDE CHAIN
REMARK 500 16 ARG A 83 0.08 SIDE CHAIN
REMARK 500 17 TYR A 51 0.11 SIDE CHAIN
REMARK 500 19 TYR A 51 0.12 SIDE CHAIN
REMARK 500 20 ARG A 21 0.12 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: BSGCAIR30506 RELATED DB: TARGETDB
DBREF 1FO5 A 0 84 UNP Q57755 THIO_METJA 1 85
SEQRES 1 A 85 MET SER LYS VAL LYS ILE GLU LEU PHE THR SER PRO MET
SEQRES 2 A 85 CYS PRO HIS CYS PRO ALA ALA LYS ARG VAL VAL GLU GLU
SEQRES 3 A 85 VAL ALA ASN GLU MET PRO ASP ALA VAL GLU VAL GLU TYR
SEQRES 4 A 85 ILE ASN VAL MET GLU ASN PRO GLN LYS ALA MET GLU TYR
SEQRES 5 A 85 GLY ILE MET ALA VAL PRO THR ILE VAL ILE ASN GLY ASP
SEQRES 6 A 85 VAL GLU PHE ILE GLY ALA PRO THR LYS GLU ALA LEU VAL
SEQRES 7 A 85 GLU ALA ILE LYS LYS ARG LEU
HELIX 1 1 ALA A 18 MET A 30 1 13
HELIX 2 2 LYS A 73 LEU A 84 1 12
SHEET 1 A 4 VAL A 34 ASN A 40 0
SHEET 2 A 4 VAL A 3 THR A 9 1 O VAL A 3 N GLU A 35
SHEET 3 A 4 THR A 58 ILE A 61 -1 O THR A 58 N PHE A 8
SHEET 4 A 4 ASP A 64 GLU A 66 -1 N ASP A 64 O ILE A 61
CISPEP 1 VAL A 56 PRO A 57 1 -6.26
CISPEP 2 VAL A 56 PRO A 57 2 -8.23
CISPEP 3 VAL A 56 PRO A 57 3 -12.04
CISPEP 4 VAL A 56 PRO A 57 4 -6.82
CISPEP 5 VAL A 56 PRO A 57 5 -6.82
CISPEP 6 VAL A 56 PRO A 57 6 6.86
CISPEP 7 VAL A 56 PRO A 57 7 0.36
CISPEP 8 VAL A 56 PRO A 57 8 -20.70
CISPEP 9 VAL A 56 PRO A 57 9 1.38
CISPEP 10 VAL A 56 PRO A 57 10 -14.83
CISPEP 11 VAL A 56 PRO A 57 11 -9.62
CISPEP 12 VAL A 56 PRO A 57 12 -14.01
CISPEP 13 VAL A 56 PRO A 57 13 -10.28
CISPEP 14 VAL A 56 PRO A 57 14 -14.99
CISPEP 15 VAL A 56 PRO A 57 15 -4.34
CISPEP 16 VAL A 56 PRO A 57 16 -9.78
CISPEP 17 VAL A 56 PRO A 57 17 -20.71
CISPEP 18 VAL A 56 PRO A 57 18 -4.34
CISPEP 19 VAL A 56 PRO A 57 19 -9.10
CISPEP 20 VAL A 56 PRO A 57 20 -0.64
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 23 2 Bytes