Header list of 1okd.pdb file
Complete list - n 17 2 Bytes
HEADER ELECTRON TRANSPORT 22-JUL-03 1OKD
TITLE NMR-STRUCTURE OF TRYPAREDOXIN 1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRYPAREDOXIN 1;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CRITHIDIA FASCICULATA;
SOURCE 3 ORGANISM_TAXID: 5656;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET22B(+)/TXN1H6
KEYWDS ELECTRON TRANSPORT, TRYPAREDOXIN, TRYPANOSOMATIDS, NMR SPECTROSCOPY
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR D.KRUMME,H.BUDDE,H.-J.HECHT,U.MENGE,O.OHLENSCHLAGER,A.ROSS,J.WISSING,
AUTHOR 2 V.WRAY,L.FLOHE
REVDAT 4 17-JAN-18 1OKD 1 SOURCE JRNL
REVDAT 3 24-FEB-09 1OKD 1 VERSN
REVDAT 2 18-DEC-03 1OKD 1 JRNL
REVDAT 1 28-AUG-03 1OKD 0
JRNL AUTH D.KRUMME,H.BUDDE,H.J.HECHT,U.MENGE,O.OHLENSCHLAGER,A.ROSS,
JRNL AUTH 2 J.WISSING,V.WRAY,L.FLOHE
JRNL TITL NMR STUDIES OF THE INTERACTION OF TRYPAREDOXIN WITH
JRNL TITL 2 REDOX-INACTIVE SUBSTRATE HOMOLOGUES.
JRNL REF BIOCHEMISTRY V. 42 14720 2003
JRNL REFN ISSN 0006-2960
JRNL PMID 14674746
JRNL DOI 10.1021/BI030112D
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS, GROSSE-
REMARK 3 KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ, RICE,
REMARK 3 SIMONSON,WARREN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1OKD COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-JUL-03.
REMARK 100 THE DEPOSITION ID IS D_1290012152.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CNS
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
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 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 1
REMARK 465 HIS A 150
REMARK 465 HIS A 151
REMARK 465 HIS A 152
REMARK 465 HIS A 153
REMARK 465 HIS A 154
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 MODELS 1-20
REMARK 470 RES CSSEQI ATOMS
REMARK 470 HIS A 149 CA C O CB CG ND1 CD2
REMARK 470 HIS A 149 CE1 NE2
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 ALA A 96 H LEU A 100 1.52
REMARK 500 O GLN A 139 H TRP A 142 1.54
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 16 -100.27 27.49
REMARK 500 1 LEU A 26 53.13 -117.94
REMARK 500 1 PRO A 42 -70.72 -74.90
REMARK 500 1 ARG A 44 87.89 -156.18
REMARK 500 1 THR A 47 -62.70 -173.29
REMARK 500 1 TRP A 70 38.09 -144.41
REMARK 500 1 LYS A 83 -71.56 -109.00
REMARK 500 1 MET A 84 122.42 -34.21
REMARK 500 1 TRP A 86 163.02 -45.13
REMARK 500 1 VAL A 106 103.44 -56.57
REMARK 500 1 ARG A 126 49.81 -88.04
REMARK 500 1 PHE A 140 -47.56 -27.93
REMARK 500 1 PRO A 141 4.45 -62.47
REMARK 500 1 TRP A 142 64.32 7.97
REMARK 500 1 LYS A 143 -162.12 -58.98
REMARK 500 1 ASP A 144 169.61 -47.24
REMARK 500 1 LEU A 147 51.48 -90.67
REMARK 500 2 GLU A 12 -52.93 -131.49
REMARK 500 2 ALA A 27 90.25 -10.64
REMARK 500 2 CYS A 40 164.22 -45.71
REMARK 500 2 PRO A 42 -79.88 -63.20
REMARK 500 2 CYS A 43 74.13 0.46
REMARK 500 2 ARG A 44 -43.80 -161.18
REMARK 500 2 THR A 47 -60.08 -173.36
REMARK 500 2 TRP A 70 37.37 -141.41
REMARK 500 2 LYS A 83 -146.24 -93.65
REMARK 500 2 MET A 84 110.35 36.44
REMARK 500 2 TRP A 86 162.89 -47.51
REMARK 500 2 VAL A 106 103.42 -54.32
REMARK 500 2 ASP A 121 141.38 -178.93
REMARK 500 2 THR A 125 41.55 -157.60
REMARK 500 2 ARG A 126 48.48 -175.37
REMARK 500 2 ASP A 134 78.10 -113.50
REMARK 500 2 PRO A 141 3.64 -61.71
REMARK 500 2 TRP A 142 65.03 5.00
REMARK 500 2 ASP A 144 -172.69 -60.11
REMARK 500 2 ALA A 145 108.24 -54.85
REMARK 500 2 PRO A 146 -167.85 -68.94
REMARK 500 2 LEU A 147 -79.87 -59.06
REMARK 500 3 PRO A 9 -169.95 -55.48
REMARK 500 3 ARG A 16 -88.04 -77.83
REMARK 500 3 LEU A 26 40.73 -97.95
REMARK 500 3 ARG A 44 98.99 -168.76
REMARK 500 3 TRP A 70 40.28 -146.89
REMARK 500 3 TYR A 80 -61.36 -108.23
REMARK 500 3 TRP A 86 167.25 -48.12
REMARK 500 3 VAL A 106 96.63 -54.44
REMARK 500 3 THR A 125 -54.85 -145.75
REMARK 500 3 ARG A 126 49.37 -80.96
REMARK 500 3 PRO A 141 3.97 -64.88
REMARK 500
REMARK 500 THIS ENTRY HAS 349 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EWX RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF NATIVE TRYPAREDOXIN I FROM CRITHIDIA
REMARK 900 FASCICULATA
REMARK 900 RELATED ID: 1EZK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF RECOMBINANT TRYPAREDOXIN I
REMARK 900 RELATED ID: 1O7U RELATED DB: PDB
REMARK 900 RADIATION DAMAGED TRYPAREDOXIN-I
REMARK 900 RELATED ID: 1O85 RELATED DB: PDB
REMARK 900 RADIATION-REDUCED TRYPAREDOXIN-I
REMARK 900 RELATED ID: 1O8W RELATED DB: PDB
REMARK 900 RADIATION-REDUCED TRYPARDOXIN-I
REMARK 900 RELATED ID: 1O8X RELATED DB: PDB
REMARK 900 MUTANT TRYPAREDOXIN-I CYS43ALA
REMARK 900 RELATED ID: 1QK8 RELATED DB: PDB
DBREF 1OKD A 1 146 UNP O96438 O96438 1 146
DBREF 1OKD A 147 154 PDB 1OKD 1OKD 147 154
SEQRES 1 A 154 MET SER GLY LEU ASP LYS TYR LEU PRO GLY ILE GLU LYS
SEQRES 2 A 154 LEU ARG ARG GLY ASP GLY GLU VAL GLU VAL LYS SER LEU
SEQRES 3 A 154 ALA GLY LYS LEU VAL PHE PHE TYR PHE SER ALA SER TRP
SEQRES 4 A 154 CYS PRO PRO CYS ARG GLY PHE THR PRO GLN LEU ILE GLU
SEQRES 5 A 154 PHE TYR ASP LYS PHE HIS GLU SER LYS ASN PHE GLU VAL
SEQRES 6 A 154 VAL PHE CYS THR TRP ASP GLU GLU GLU ASP GLY PHE ALA
SEQRES 7 A 154 GLY TYR PHE ALA LYS MET PRO TRP LEU ALA VAL PRO PHE
SEQRES 8 A 154 ALA GLN SER GLU ALA VAL GLN LYS LEU SER LYS HIS PHE
SEQRES 9 A 154 ASN VAL GLU SER ILE PRO THR LEU ILE GLY VAL ASP ALA
SEQRES 10 A 154 ASP SER GLY ASP VAL VAL THR THR ARG ALA ARG ALA THR
SEQRES 11 A 154 LEU VAL LYS ASP PRO GLU GLY GLU GLN PHE PRO TRP LYS
SEQRES 12 A 154 ASP ALA PRO LEU GLU HIS HIS HIS HIS HIS HIS
HELIX 1 1 SER A 2 LEU A 8 1 7
HELIX 2 2 LYS A 24 ALA A 27 5 4
HELIX 3 3 THR A 47 ASN A 62 1 16
HELIX 4 4 GLU A 73 ALA A 82 1 10
HELIX 5 5 PRO A 90 ALA A 92 5 3
HELIX 6 6 GLN A 93 ASN A 105 1 13
HELIX 7 7 ARG A 126 ASP A 134 1 9
SHEET 1 AA 2 LYS A 13 LEU A 14 0
SHEET 2 AA 2 VAL A 21 GLU A 22 -1 O VAL A 21 N LEU A 14
SHEET 1 AB 5 LEU A 87 ALA A 88 0
SHEET 2 AB 5 GLU A 64 THR A 69 1 O VAL A 65 N LEU A 87
SHEET 3 AB 5 LEU A 30 SER A 36 1 O LEU A 30 N GLU A 64
SHEET 4 AB 5 THR A 111 ASP A 116 -1 O THR A 111 N PHE A 35
SHEET 5 AB 5 VAL A 122 THR A 124 -1 N VAL A 123 O GLY A 114
SSBOND 1 CYS A 40 CYS A 43 1555 1555 2.03
CISPEP 1 ILE A 109 PRO A 110 1 0.13
CISPEP 2 ILE A 109 PRO A 110 2 0.07
CISPEP 3 ILE A 109 PRO A 110 3 0.07
CISPEP 4 ILE A 109 PRO A 110 4 0.22
CISPEP 5 ILE A 109 PRO A 110 5 0.09
CISPEP 6 ILE A 109 PRO A 110 6 0.10
CISPEP 7 ILE A 109 PRO A 110 7 0.19
CISPEP 8 ILE A 109 PRO A 110 8 0.21
CISPEP 9 ILE A 109 PRO A 110 9 0.13
CISPEP 10 ILE A 109 PRO A 110 10 0.15
CISPEP 11 ILE A 109 PRO A 110 11 0.19
CISPEP 12 ILE A 109 PRO A 110 12 0.10
CISPEP 13 ILE A 109 PRO A 110 13 0.28
CISPEP 14 ILE A 109 PRO A 110 14 0.12
CISPEP 15 ILE A 109 PRO A 110 15 0.21
CISPEP 16 ILE A 109 PRO A 110 16 0.14
CISPEP 17 ILE A 109 PRO A 110 17 0.13
CISPEP 18 ILE A 109 PRO A 110 18 0.20
CISPEP 19 ILE A 109 PRO A 110 19 0.10
CISPEP 20 ILE A 109 PRO A 110 20 0.16
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 - n 17 2 Bytes