Header list of 2bjx.pdb file
Complete list - v 6 2 Bytes
HEADER ELECTRON TRANSPORT 30-JAN-99 2BJX
TITLE PROTEIN DISULFIDE ISOMERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (PROTEIN DISULFIDE ISOMERASE);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: B DOMAIN;
COMPND 5 EC: 5.3.4.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 STRAIN: BL21 (DE3);
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET12A
KEYWDS ELECTRON TRANSPORT, REDOX-ACTIVE CENTER, ISOMERASE, ENDOPLASMIC
KEYWDS 2 RETICULUM
EXPDTA SOLUTION NMR
NUMMDL 24
AUTHOR J.KEMMINK,K.DIJKSTRA,M.MARIANI,R.M.SCHEEK,E.PENKA,M.NILGES,N.J.DARBY
REVDAT 6 06-NOV-19 2BJX 1 REMARK
REVDAT 5 30-OCT-19 2BJX 1 REMARK
REVDAT 4 24-FEB-09 2BJX 1 VERSN
REVDAT 3 05-MAY-00 2BJX 1 DBREF
REVDAT 2 23-DEC-99 2BJX 1 JRNL
REVDAT 1 09-FEB-99 2BJX 0
JRNL AUTH J.KEMMINK,K.DIJKSTRA,M.MARIANI,R.M.SCHEEK,E.PENKA,M.NILGES,
JRNL AUTH 2 N.J.DARBY
JRNL TITL THE STRUCTURE IN SOLUTION OF THE B DOMAIN OF PROTEIN
JRNL TITL 2 DISULFIDE ISOMERASE.
JRNL REF J.BIOMOL.NMR V. 13 357 1999
JRNL REFN ISSN 0925-2738
JRNL PMID 10383197
JRNL DOI 10.1023/A:1008341820489
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.KEMMINK,N.J.DARBY,K.DIJKSTRA,M.NILGES,T.E.CREIGHTON
REMARK 1 TITL THE FOLDING CATALYST PROTEIN DISULFIDE ISOMERASE IS
REMARK 1 TITL 2 CONSTRUCTED OF ACTIVE AND INACTIVE THIOREDOXIN MODULES
REMARK 1 REF CURR.BIOL. V. 7 239 1997
REMARK 1 REFN ISSN 0960-9822
REMARK 1 DOI 10.1016/S0960-9822(06)00119-9
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAIL CAN BE FOUND IN THE
REMARK 3 JRNL CITATION
REMARK 4
REMARK 4 2BJX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-FEB-99.
REMARK 100 THE DEPOSITION ID IS D_1000000421.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY; AMX
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : DISTANCE GEOMETRY AND SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 24
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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 H THR A 121 O PHE A 167 1.57
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 ASN A 172 -177.41 -53.56
REMARK 500 1 ASP A 193 -154.52 48.02
REMARK 500 1 ASN A 197 -153.57 -133.34
REMARK 500 1 ASN A 198 88.30 -174.57
REMARK 500 1 GLU A 200 -151.33 -130.00
REMARK 500 1 ASN A 215 -81.99 -89.06
REMARK 500 1 LEU A 217 100.03 54.59
REMARK 500 1 LEU A 219 -165.32 -61.00
REMARK 500 1 PHE A 223 -170.12 53.83
REMARK 500 1 THR A 224 22.44 -154.61
REMARK 500 1 GLN A 226 96.31 -59.54
REMARK 500 1 THR A 227 -61.33 -140.10
REMARK 500 2 ALA A 139 146.90 -173.13
REMARK 500 2 PHE A 143 79.38 -114.07
REMARK 500 2 ASP A 193 -160.58 53.54
REMARK 500 2 ASN A 197 -148.90 -134.65
REMARK 500 2 ASN A 198 81.25 -173.73
REMARK 500 2 LEU A 217 57.95 -145.53
REMARK 500 2 GLU A 222 89.27 52.90
REMARK 500 2 PHE A 223 171.37 -55.39
REMARK 500 2 GLN A 226 -55.82 -146.17
REMARK 500 3 ASP A 125 -170.03 179.40
REMARK 500 3 ALA A 139 130.45 -175.27
REMARK 500 3 ASP A 193 -159.17 48.79
REMARK 500 3 ASN A 197 -37.30 -134.47
REMARK 500 3 ASN A 198 83.29 57.73
REMARK 500 3 ASN A 215 -64.41 -91.89
REMARK 500 3 PRO A 218 -168.54 -77.39
REMARK 500 3 GLU A 222 -72.63 -136.00
REMARK 500 3 PHE A 223 -169.40 -108.50
REMARK 500 4 ALA A 139 137.79 -174.40
REMARK 500 4 PHE A 143 71.25 -103.48
REMARK 500 4 VAL A 147 -51.08 72.97
REMARK 500 4 SER A 149 -164.68 -70.34
REMARK 500 4 ASP A 163 19.20 -145.23
REMARK 500 4 LYS A 183 -157.40 -175.26
REMARK 500 4 ASP A 193 -159.13 46.22
REMARK 500 4 ASN A 198 80.69 -156.82
REMARK 500 4 GLU A 202 107.52 -55.96
REMARK 500 4 ILE A 221 85.17 52.67
REMARK 500 4 GLU A 222 104.33 -162.52
REMARK 500 4 GLU A 225 -69.99 -99.00
REMARK 500 5 ALA A 139 126.34 -175.27
REMARK 500 5 SER A 149 -159.52 -85.97
REMARK 500 5 LYS A 183 -163.34 179.13
REMARK 500 5 ASP A 193 -159.73 51.95
REMARK 500 5 ASN A 197 -151.31 -128.72
REMARK 500 5 ASN A 198 78.37 -174.37
REMARK 500 5 VAL A 203 102.26 -51.33
REMARK 500 5 VAL A 220 59.31 -150.14
REMARK 500
REMARK 500 THIS ENTRY HAS 258 RAMACHANDRAN OUTLIERS.
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 1 ARG A 196 0.27 SIDE CHAIN
REMARK 500 2 ARG A 196 0.32 SIDE CHAIN
REMARK 500 3 ARG A 196 0.20 SIDE CHAIN
REMARK 500 4 ARG A 196 0.31 SIDE CHAIN
REMARK 500 5 ARG A 196 0.28 SIDE CHAIN
REMARK 500 6 ARG A 196 0.22 SIDE CHAIN
REMARK 500 7 ARG A 196 0.29 SIDE CHAIN
REMARK 500 8 ARG A 196 0.17 SIDE CHAIN
REMARK 500 9 ARG A 196 0.30 SIDE CHAIN
REMARK 500 10 ARG A 196 0.30 SIDE CHAIN
REMARK 500 11 ARG A 196 0.32 SIDE CHAIN
REMARK 500 12 ARG A 196 0.32 SIDE CHAIN
REMARK 500 13 ARG A 196 0.27 SIDE CHAIN
REMARK 500 14 ARG A 196 0.26 SIDE CHAIN
REMARK 500 15 ARG A 196 0.18 SIDE CHAIN
REMARK 500 16 ARG A 196 0.32 SIDE CHAIN
REMARK 500 17 ARG A 196 0.23 SIDE CHAIN
REMARK 500 18 ARG A 196 0.29 SIDE CHAIN
REMARK 500 19 ARG A 196 0.23 SIDE CHAIN
REMARK 500 20 ARG A 196 0.27 SIDE CHAIN
REMARK 500 21 ARG A 196 0.24 SIDE CHAIN
REMARK 500 22 ARG A 196 0.31 SIDE CHAIN
REMARK 500 23 ARG A 196 0.20 SIDE CHAIN
REMARK 500 24 ARG A 196 0.21 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2BJX A 119 228 UNP P07237 PDIA1_HUMAN 136 245
SEQRES 1 A 110 ALA ALA THR THR LEU PRO ASP GLY ALA ALA ALA GLU SER
SEQRES 2 A 110 LEU VAL GLU SER SER GLU VAL ALA VAL ILE GLY PHE PHE
SEQRES 3 A 110 LYS ASP VAL GLU SER ASP SER ALA LYS GLN PHE LEU GLN
SEQRES 4 A 110 ALA ALA GLU ALA ILE ASP ASP ILE PRO PHE GLY ILE THR
SEQRES 5 A 110 SER ASN SER ASP VAL PHE SER LYS TYR GLN LEU ASP LYS
SEQRES 6 A 110 ASP GLY VAL VAL LEU PHE LYS LYS PHE ASP GLU GLY ARG
SEQRES 7 A 110 ASN ASN PHE GLU GLY GLU VAL THR LYS GLU ASN LEU LEU
SEQRES 8 A 110 ASP PHE ILE LYS HIS ASN GLN LEU PRO LEU VAL ILE GLU
SEQRES 9 A 110 PHE THR GLU GLN THR ALA
HELIX 1 1 GLY A 126 SER A 135 1 10
HELIX 2 2 ASP A 150 ALA A 161 1 12
HELIX 3 3 ASP A 174 TYR A 179 1 6
HELIX 4 4 LYS A 205 ASN A 215 1 11
SHEET 1 A 4 ALA A 120 THR A 122 0
SHEET 2 A 4 PRO A 166 ILE A 169 1 N PHE A 167 O THR A 121
SHEET 3 A 4 VAL A 138 PHE A 143 1 N VAL A 140 O PRO A 166
SHEET 4 A 4 GLY A 185 LYS A 190 -1 N PHE A 189 O ALA A 139
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 - v 6 2 Bytes