Header list of 2djj.pdb file
Complete list - r 9 2 Bytes
HEADER ISOMERASE 04-APR-06 2DJJ
TITLE SOLUTION STRUCTURE OF THE A' DOMAIN OF THERMOPHILIC FUNGAL PROTEIN
TITLE 2 DISULFIDE ISOMERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN DISULFIDE-ISOMERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: A' DOMAIN;
COMPND 5 SYNONYM: PDI;
COMPND 6 EC: 5.3.4.1;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMICOLA INSOLENS;
SOURCE 3 ORGANISM_TAXID: 34413;
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: PGEX6P-1
KEYWDS THIOREDOXIN FOLD, ISOMERASE
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR K.KATO,Y.YAMAGUCHI
REVDAT 3 09-MAR-22 2DJJ 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2DJJ 1 VERSN
REVDAT 1 25-APR-06 2DJJ 0
SPRSDE 25-APR-06 2DJJ 1XTX
JRNL AUTH M.NAKANO,A.MAENO,H.SASAKAWA,Y.YAMAGUCHI,J.KIKUCHI,O.ASAMI,
JRNL AUTH 2 T.KAJINO,K.KATO
JRNL TITL SOLUTION STRUCTURE OF THE A' DOMAIN OF THERMOPHILIC FUNGAL
JRNL TITL 2 PROTEIN DISULFIDE ISOMERASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE
REMARK 3 -KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE,
REMARK 3 SIMONSON,WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2DJJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-APR-06.
REMARK 100 THE DEPOSITION ID IS D_1000025488.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 6
REMARK 210 IONIC STRENGTH : 0.16
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1.0MM PROTEIN DISULFIDE
REMARK 210 ISOMERASE A' DOMAIN U-15N,13C;
REMARK 210 10MM SODIUM PHOSPHATE BUFFER,
REMARK 210 100MM KCL, 10MM DITIOTHREITOL;
REMARK 210 90% H2O, 10% D2O; 1.0MM PROTEIN
REMARK 210 DISULFIDE ISOMERASE A' DOMAIN;
REMARK 210 10MM SODIUM PHOSPHATE BUFFER,
REMARK 210 100MM KCL, 10MM DITIOTHREITOL;
REMARK 210 99% D2O; 0.3MM PROTEIN DISULFIDE
REMARK 210 ISOMERASE A' DOMAIN U-15N; 10MM
REMARK 210 SODIUM PHOSPHATE BUFFER, 100MM
REMARK 210 KCL, 10MM DITIOTHREITOL, 10MG/ML
REMARK 210 PF1 PHAGE; 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 2D NOESY; 1H-
REMARK 210 15N HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 920 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : ECA; DRX
REMARK 210 SPECTROMETER MANUFACTURER : JEOL; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DELTA 4.3.3, XWINNMR 2.6, SPARKY
REMARK 210 3.1, CYANA 2.1
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
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 PHE A 111 H ASN A 115 1.55
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 SER A 5 -75.75 -173.72
REMARK 500 1 LYS A 56 11.26 -155.22
REMARK 500 1 SER A 57 -102.66 -109.81
REMARK 500 1 PHE A 59 21.83 -152.37
REMARK 500 1 ARG A 62 -142.36 -125.78
REMARK 500 1 PRO A 96 -176.24 -44.09
REMARK 500 1 ARG A 103 52.47 -106.01
REMARK 500 1 PHE A 111 -77.62 -65.17
REMARK 500 1 ALA A 120 98.75 -62.94
REMARK 500 2 PRO A 2 175.93 -52.19
REMARK 500 2 LEU A 3 -52.61 -154.65
REMARK 500 2 LYS A 56 -43.38 -146.03
REMARK 500 2 SER A 57 -149.99 -61.09
REMARK 500 2 ARG A 62 -145.63 -85.03
REMARK 500 2 LYS A 86 119.03 -163.16
REMARK 500 2 PRO A 89 177.93 -55.03
REMARK 500 2 ALA A 90 54.38 -95.79
REMARK 500 2 PRO A 96 172.62 -39.82
REMARK 500 2 SER A 102 -40.45 -159.86
REMARK 500 2 PHE A 111 -77.47 -65.49
REMARK 500 3 GLU A 6 111.71 -178.81
REMARK 500 3 LYS A 56 -45.01 -143.13
REMARK 500 3 SER A 57 -153.10 -59.95
REMARK 500 3 ARG A 62 -147.06 -121.64
REMARK 500 3 VAL A 63 107.45 -48.86
REMARK 500 3 GLU A 78 95.69 -66.78
REMARK 500 3 PRO A 83 -168.00 -71.52
REMARK 500 3 PRO A 89 175.52 -51.74
REMARK 500 3 ALA A 90 53.04 -102.51
REMARK 500 3 ALA A 92 -81.14 -102.21
REMARK 500 3 GLN A 95 57.47 -144.31
REMARK 500 3 PRO A 96 177.05 -44.77
REMARK 500 3 ARG A 103 51.53 -106.17
REMARK 500 3 PHE A 111 -75.93 -64.03
REMARK 500 4 LEU A 3 116.29 61.93
REMARK 500 4 GLU A 6 -173.74 -170.95
REMARK 500 4 LYS A 56 -42.40 -139.80
REMARK 500 4 SER A 57 -159.89 -57.36
REMARK 500 4 ARG A 62 -143.66 -82.75
REMARK 500 4 PRO A 89 177.83 -56.38
REMARK 500 4 ALA A 90 54.11 -95.17
REMARK 500 4 PRO A 96 175.06 -39.03
REMARK 500 4 SER A 102 106.56 179.83
REMARK 500 4 ARG A 103 54.51 -69.00
REMARK 500 4 PHE A 111 -77.39 -64.74
REMARK 500 5 VAL A 11 92.48 -67.09
REMARK 500 5 GLU A 19 -53.75 -121.00
REMARK 500 5 LYS A 56 -42.49 -145.51
REMARK 500 5 SER A 57 -156.12 -57.69
REMARK 500 5 GLU A 58 23.77 -79.33
REMARK 500
REMARK 500 THIS ENTRY HAS 117 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2DJK RELATED DB: PDB
DBREF 2DJJ A 6 121 UNP P55059 PDI_HUMIN 354 469
SEQADV 2DJJ GLY A 1 UNP P55059 CLONING ARTIFACT
SEQADV 2DJJ PRO A 2 UNP P55059 CLONING ARTIFACT
SEQADV 2DJJ LEU A 3 UNP P55059 CLONING ARTIFACT
SEQADV 2DJJ GLY A 4 UNP P55059 CLONING ARTIFACT
SEQADV 2DJJ SER A 5 UNP P55059 CLONING ARTIFACT
SEQRES 1 A 121 GLY PRO LEU GLY SER GLU GLY PRO VAL THR VAL VAL VAL
SEQRES 2 A 121 ALA LYS ASN TYR ASN GLU ILE VAL LEU ASP ASP THR LYS
SEQRES 3 A 121 ASP VAL LEU ILE GLU PHE TYR ALA PRO TRP CYS GLY HIS
SEQRES 4 A 121 CYS LYS ALA LEU ALA PRO LYS TYR GLU GLU LEU GLY ALA
SEQRES 5 A 121 LEU TYR ALA LYS SER GLU PHE LYS ASP ARG VAL VAL ILE
SEQRES 6 A 121 ALA LYS VAL ASP ALA THR ALA ASN ASP VAL PRO ASP GLU
SEQRES 7 A 121 ILE GLN GLY PHE PRO THR ILE LYS LEU TYR PRO ALA GLY
SEQRES 8 A 121 ALA LYS GLY GLN PRO VAL THR TYR SER GLY SER ARG THR
SEQRES 9 A 121 VAL GLU ASP LEU ILE LYS PHE ILE ALA GLU ASN GLY LYS
SEQRES 10 A 121 TYR LYS ALA ALA
HELIX 1 1 HIS A 39 ALA A 55 1 17
HELIX 2 2 THR A 104 ASN A 115 1 12
SHEET 1 A 4 THR A 10 VAL A 11 0
SHEET 2 A 4 VAL A 64 ASP A 69 1 O LYS A 67 N THR A 10
SHEET 3 A 4 VAL A 28 TYR A 33 1 N LEU A 29 O VAL A 64
SHEET 4 A 4 THR A 84 TYR A 88 -1 O LYS A 86 N ILE A 30
CISPEP 1 PHE A 82 PRO A 83 1 -0.18
CISPEP 2 PHE A 82 PRO A 83 2 -0.02
CISPEP 3 PHE A 82 PRO A 83 3 0.29
CISPEP 4 PHE A 82 PRO A 83 4 0.12
CISPEP 5 PHE A 82 PRO A 83 5 -0.04
CISPEP 6 PHE A 82 PRO A 83 6 -0.20
CISPEP 7 PHE A 82 PRO A 83 7 0.02
CISPEP 8 PHE A 82 PRO A 83 8 0.21
CISPEP 9 PHE A 82 PRO A 83 9 0.14
CISPEP 10 PHE A 82 PRO A 83 10 0.15
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