Header list of 1x5c.pdb file
Complete list - r 2 2 Bytes
HEADER ISOMERASE 15-MAY-05 1X5C
TITLE THE SOLUTION STRUCTURE OF THE SECOND THIOREDOXIN-LIKE DOMAIN OF HUMAN
TITLE 2 PROTEIN DISULFIDE-ISOMERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN DISULFIDE-ISOMERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: THIOREDOXIN LIKE DOMAIN;
COMPND 5 SYNONYM: PDI, PROLYL 4- HYDROXYLASE BETA SUBUNIT, CELLULAR THYROID
COMPND 6 HORMONE BINDING PROTEIN, P55;
COMPND 7 EC: 5.3.4.1;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: P4HB;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040628-09;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS DSI, ERBA2L, GIT, PDI, PDIA1, PO4DB, PO4HB, PROHB, THIOREDOXIN LIKE
KEYWDS 2 DOMAIN, REDOX, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON
KEYWDS 3 PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 4 GENOMICS/PROTEOMICS INITIATIVE, RSGI, ISOMERASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1X5C 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1X5C 1 VERSN
REVDAT 1 15-NOV-05 1X5C 0
JRNL AUTH N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA
JRNL TITL THE SOLUTION STRUCTURE OF THE SECOND THIOREDOXIN-LIKE DOMAIN
JRNL TITL 2 OF HUMAN 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 3.5, CYANA 2.0.17
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1X5C COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024398.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 296
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.2MM THIOREDOXIN LIKE DOMAIN U
REMARK 210 -15N,13C; 20MM D-TRIS HCL; 100MM
REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3; 10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 900 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20031121, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9044, CYANA 2.0.17
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION,STRUCTURES WITH
REMARK 210 THE LEAST RESTRAINT VIOLATIONS
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: 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 3 108.36 -161.78
REMARK 500 1 SER A 5 -48.13 -130.22
REMARK 500 1 SER A 6 159.78 -41.36
REMARK 500 1 HIS A 57 -175.39 -66.95
REMARK 500 1 ALA A 88 74.70 -63.41
REMARK 500 1 ARG A 92 37.40 -92.10
REMARK 500 1 ASN A 98 50.10 -112.69
REMARK 500 1 GLU A 111 -35.90 -38.72
REMARK 500 2 SER A 5 43.31 -96.77
REMARK 500 2 HIS A 39 -33.92 -39.28
REMARK 500 2 HIS A 57 -176.31 -66.89
REMARK 500 2 ALA A 88 40.45 -83.14
REMARK 500 2 ARG A 92 49.75 -93.79
REMARK 500 2 GLU A 111 -37.91 -38.94
REMARK 500 3 CYS A 37 109.44 -57.21
REMARK 500 3 HIS A 57 -174.81 -66.26
REMARK 500 3 ARG A 92 46.42 34.34
REMARK 500 3 GLU A 111 -38.82 -36.53
REMARK 500 3 SER A 120 -57.86 -134.47
REMARK 500 4 SER A 2 89.32 -61.56
REMARK 500 4 SER A 5 44.85 -101.69
REMARK 500 4 ALA A 21 -63.75 -92.28
REMARK 500 4 CYS A 37 103.70 -58.66
REMARK 500 4 HIS A 57 -175.02 -65.01
REMARK 500 4 SER A 89 140.64 -35.28
REMARK 500 4 ARG A 92 40.00 -85.63
REMARK 500 4 GLU A 111 -38.83 -38.01
REMARK 500 5 HIS A 57 -174.71 -66.11
REMARK 500 5 ALA A 88 47.29 -77.96
REMARK 500 5 GLU A 111 -37.94 -37.35
REMARK 500 5 SER A 119 113.43 -35.49
REMARK 500 6 SER A 6 96.53 -64.91
REMARK 500 6 HIS A 57 -174.36 -68.24
REMARK 500 6 ARG A 101 46.45 74.50
REMARK 500 6 GLU A 111 -36.58 -36.57
REMARK 500 6 PRO A 118 2.84 -69.75
REMARK 500 7 HIS A 57 -173.52 -65.84
REMARK 500 7 ARG A 92 42.35 34.30
REMARK 500 7 GLU A 111 -37.97 -38.35
REMARK 500 7 SER A 120 41.75 -95.89
REMARK 500 8 SER A 6 -38.45 -38.82
REMARK 500 8 HIS A 57 -174.74 -64.48
REMARK 500 8 ARG A 92 53.46 31.98
REMARK 500 8 GLU A 111 -36.53 -37.36
REMARK 500 8 SER A 119 -55.78 -121.91
REMARK 500 9 HIS A 39 -38.31 -39.35
REMARK 500 9 HIS A 57 -174.88 -66.00
REMARK 500 9 ASP A 91 34.61 -90.95
REMARK 500 9 ARG A 92 42.81 35.94
REMARK 500 9 ARG A 101 45.84 74.43
REMARK 500
REMARK 500 THIS ENTRY HAS 106 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSS001002456.1 RELATED DB: TARGETDB
DBREF 1X5C A 8 115 UNP P07237 PDIA1_HUMAN 368 475
SEQADV 1X5C GLY A 1 UNP P07237 CLONING ARTIFACT
SEQADV 1X5C SER A 2 UNP P07237 CLONING ARTIFACT
SEQADV 1X5C SER A 3 UNP P07237 CLONING ARTIFACT
SEQADV 1X5C GLY A 4 UNP P07237 CLONING ARTIFACT
SEQADV 1X5C SER A 5 UNP P07237 CLONING ARTIFACT
SEQADV 1X5C SER A 6 UNP P07237 CLONING ARTIFACT
SEQADV 1X5C GLY A 7 UNP P07237 CLONING ARTIFACT
SEQADV 1X5C SER A 116 UNP P07237 CLONING ARTIFACT
SEQADV 1X5C GLY A 117 UNP P07237 CLONING ARTIFACT
SEQADV 1X5C PRO A 118 UNP P07237 CLONING ARTIFACT
SEQADV 1X5C SER A 119 UNP P07237 CLONING ARTIFACT
SEQADV 1X5C SER A 120 UNP P07237 CLONING ARTIFACT
SEQADV 1X5C GLY A 121 UNP P07237 CLONING ARTIFACT
SEQRES 1 A 121 GLY SER SER GLY SER SER GLY PRO VAL LYS VAL LEU VAL
SEQRES 2 A 121 GLY LYS ASN PHE GLU ASP VAL ALA PHE ASP GLU LYS LYS
SEQRES 3 A 121 ASN VAL PHE VAL GLU PHE TYR ALA PRO TRP CYS GLY HIS
SEQRES 4 A 121 CYS LYS GLN LEU ALA PRO ILE TRP ASP LYS LEU GLY GLU
SEQRES 5 A 121 THR TYR LYS ASP HIS GLU ASN ILE VAL ILE ALA LYS MET
SEQRES 6 A 121 ASP SER THR ALA ASN GLU VAL GLU ALA VAL LYS VAL HIS
SEQRES 7 A 121 SER PHE PRO THR LEU LYS PHE PHE PRO ALA SER ALA ASP
SEQRES 8 A 121 ARG THR VAL ILE ASP TYR ASN GLY GLU ARG THR LEU ASP
SEQRES 9 A 121 GLY PHE LYS LYS PHE LEU GLU SER GLY GLY GLN SER GLY
SEQRES 10 A 121 PRO SER SER GLY
HELIX 1 1 ASN A 16 ALA A 21 1 6
HELIX 2 2 CYS A 37 GLU A 52 1 16
HELIX 3 3 THR A 53 LYS A 55 5 3
HELIX 4 4 THR A 102 GLY A 113 1 12
SHEET 1 A 5 LYS A 10 LEU A 12 0
SHEET 2 A 5 ILE A 60 ASP A 66 1 O LYS A 64 N LYS A 10
SHEET 3 A 5 ASN A 27 TYR A 33 1 N ASN A 27 O VAL A 61
SHEET 4 A 5 THR A 82 PHE A 86 -1 O THR A 82 N PHE A 32
SHEET 5 A 5 ILE A 95 ASP A 96 -1 O ILE A 95 N PHE A 85
CISPEP 1 PHE A 80 PRO A 81 1 0.03
CISPEP 2 PHE A 80 PRO A 81 2 0.03
CISPEP 3 PHE A 80 PRO A 81 3 -0.04
CISPEP 4 PHE A 80 PRO A 81 4 0.02
CISPEP 5 PHE A 80 PRO A 81 5 0.07
CISPEP 6 PHE A 80 PRO A 81 6 0.03
CISPEP 7 PHE A 80 PRO A 81 7 0.06
CISPEP 8 PHE A 80 PRO A 81 8 -0.04
CISPEP 9 PHE A 80 PRO A 81 9 0.02
CISPEP 10 PHE A 80 PRO A 81 10 0.03
CISPEP 11 PHE A 80 PRO A 81 11 0.00
CISPEP 12 PHE A 80 PRO A 81 12 0.00
CISPEP 13 PHE A 80 PRO A 81 13 0.07
CISPEP 14 PHE A 80 PRO A 81 14 0.04
CISPEP 15 PHE A 80 PRO A 81 15 -0.03
CISPEP 16 PHE A 80 PRO A 81 16 0.04
CISPEP 17 PHE A 80 PRO A 81 17 0.01
CISPEP 18 PHE A 80 PRO A 81 18 0.02
CISPEP 19 PHE A 80 PRO A 81 19 0.04
CISPEP 20 PHE A 80 PRO A 81 20 0.01
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 2 2 Bytes