Header list of 1wxp.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSPORT PROTEIN 28-JAN-05 1WXP
TITLE SOLUTION STRUCTURE OF THE DEATH DOMAIN OF NUCLEAR MATRIX PROTEIN P84
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THO COMPLEX SUBUNIT 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DEATH DOMAIN;
COMPND 5 SYNONYM: THO1, NUCLEAR MATRIX PROTEIN P84;
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 GENE: THOC1;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040301-33;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS DEATH DOMAIN, STRUCTURAL GENOMICS, NUCLEAR MATRIX, RIKEN STRUCTURAL
KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, TRANSPORT PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.N.NIRAULA,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1WXP 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1WXP 1 VERSN
REVDAT 1 28-JUL-05 1WXP 0
JRNL AUTH T.N.NIRAULA,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE DEATH DOMAIN OF NUCLEAR MATRIX
JRNL TITL 2 PROTEIN P84
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, CYANA 1.0.7
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WXP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-JAN-05.
REMARK 100 THE DEPOSITION ID IS D_1000024125.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.20MM DEATH DOMAIN U-13C, 15N;
REMARK 210 20MM D-TRIS-HCL(PH 7.0); 100MM
REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 200311221, NMRVIEW
REMARK 210 5.0.4, KUJIRA 0.913, CYANA 1.0.7
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: 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 LEU A 84 H LEU A 89 1.49
REMARK 500 O LEU A 63 H TRP A 67 1.51
REMARK 500 O GLN A 48 H ASP A 52 1.53
REMARK 500 O SER A 53 HE ARG A 59 1.53
REMARK 500 O ALA A 83 H SER A 87 1.53
REMARK 500 O ASN A 85 H GLY A 88 1.56
REMARK 500 O VAL A 65 H ASP A 69 1.58
REMARK 500 O GLN A 20 H PHE A 24 1.58
REMARK 500 O PHE A 24 H LEU A 28 1.59
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 2 161.26 177.85
REMARK 500 1 SER A 5 93.83 57.40
REMARK 500 1 ARG A 12 61.40 25.67
REMARK 500 1 ASP A 13 -44.02 -132.89
REMARK 500 1 ILE A 21 -70.87 -39.57
REMARK 500 1 ASN A 85 -71.11 -53.40
REMARK 500 1 ASN A 98 86.61 40.46
REMARK 500 1 ASN A 100 176.75 171.93
REMARK 500 1 THR A 102 -62.68 -130.51
REMARK 500 1 SER A 104 -57.48 -122.47
REMARK 500 1 SER A 105 -59.64 -165.43
REMARK 500 1 SER A 108 168.34 55.04
REMARK 500 2 SER A 2 161.75 57.99
REMARK 500 2 ASP A 9 112.94 59.07
REMARK 500 2 VAL A 10 91.55 41.53
REMARK 500 2 ASP A 13 -67.22 173.10
REMARK 500 2 LYS A 14 170.12 -59.43
REMARK 500 2 ILE A 21 -70.15 -39.58
REMARK 500 2 LEU A 89 38.99 -98.15
REMARK 500 2 ASN A 98 154.11 -37.85
REMARK 500 2 ASP A 99 178.54 59.84
REMARK 500 2 SER A 104 109.75 -40.37
REMARK 500 2 SER A 105 -60.00 -108.31
REMARK 500 2 SER A 108 170.58 55.13
REMARK 500 2 SER A 109 109.94 -59.38
REMARK 500 3 SER A 3 131.19 63.34
REMARK 500 3 SER A 5 -59.42 -172.65
REMARK 500 3 ASP A 13 -49.68 174.36
REMARK 500 3 VAL A 16 153.55 -41.65
REMARK 500 3 ILE A 21 -70.86 -41.23
REMARK 500 3 GLU A 40 48.17 71.84
REMARK 500 3 ALA A 75 90.21 -67.66
REMARK 500 3 LEU A 96 -73.33 -59.43
REMARK 500 3 THR A 97 -75.51 -34.43
REMARK 500 3 ASN A 98 72.33 60.68
REMARK 500 3 ASP A 99 165.44 57.44
REMARK 500 3 GLU A 101 160.60 178.71
REMARK 500 3 ASN A 103 98.09 175.73
REMARK 500 3 SER A 104 168.24 177.86
REMARK 500 4 SER A 2 109.35 178.39
REMARK 500 4 SER A 3 106.81 -176.66
REMARK 500 4 SER A 5 118.30 64.91
REMARK 500 4 ARG A 12 89.02 -67.00
REMARK 500 4 ASP A 13 -49.76 -146.33
REMARK 500 4 VAL A 16 159.25 -41.45
REMARK 500 4 ILE A 21 -70.86 -41.86
REMARK 500 4 GLU A 40 49.63 71.04
REMARK 500 4 HIS A 74 -43.68 -140.70
REMARK 500 4 ALA A 75 94.34 -46.36
REMARK 500 4 LEU A 96 -74.64 -57.03
REMARK 500
REMARK 500 THIS ENTRY HAS 267 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSS001000290.1 RELATED DB: TARGETDB
DBREF 1WXP A 8 104 UNP Q96FV9 THOC1_HUMAN 561 657
SEQADV 1WXP GLY A 1 UNP Q96FV9 CLONING ARTIFACT
SEQADV 1WXP SER A 2 UNP Q96FV9 CLONING ARTIFACT
SEQADV 1WXP SER A 3 UNP Q96FV9 CLONING ARTIFACT
SEQADV 1WXP GLY A 4 UNP Q96FV9 CLONING ARTIFACT
SEQADV 1WXP SER A 5 UNP Q96FV9 CLONING ARTIFACT
SEQADV 1WXP SER A 6 UNP Q96FV9 CLONING ARTIFACT
SEQADV 1WXP GLY A 7 UNP Q96FV9 CLONING ARTIFACT
SEQADV 1WXP SER A 105 UNP Q96FV9 CLONING ARTIFACT
SEQADV 1WXP GLY A 106 UNP Q96FV9 CLONING ARTIFACT
SEQADV 1WXP PRO A 107 UNP Q96FV9 CLONING ARTIFACT
SEQADV 1WXP SER A 108 UNP Q96FV9 CLONING ARTIFACT
SEQADV 1WXP SER A 109 UNP Q96FV9 CLONING ARTIFACT
SEQADV 1WXP GLY A 110 UNP Q96FV9 CLONING ARTIFACT
SEQRES 1 A 110 GLY SER SER GLY SER SER GLY PRO ASP VAL ARG ARG ASP
SEQRES 2 A 110 LYS PRO VAL THR GLY GLU GLN ILE GLU VAL PHE ALA ASN
SEQRES 3 A 110 LYS LEU GLY GLU GLN TRP LYS ILE LEU ALA PRO TYR LEU
SEQRES 4 A 110 GLU MET LYS ASP SER GLU ILE ARG GLN ILE GLU CYS ASP
SEQRES 5 A 110 SER GLU ASP MET LYS MET ARG ALA LYS GLN LEU LEU VAL
SEQRES 6 A 110 ALA TRP GLN ASP GLN GLU GLY VAL HIS ALA THR PRO GLU
SEQRES 7 A 110 ASN LEU ILE ASN ALA LEU ASN LYS SER GLY LEU SER ASP
SEQRES 8 A 110 LEU ALA GLU SER LEU THR ASN ASP ASN GLU THR ASN SER
SEQRES 9 A 110 SER GLY PRO SER SER GLY
HELIX 1 1 THR A 17 GLY A 29 1 13
HELIX 2 2 GLN A 31 ALA A 36 1 6
HELIX 3 3 LYS A 42 SER A 53 1 12
HELIX 4 4 ASP A 55 GLY A 72 1 18
HELIX 5 5 VAL A 73 ALA A 75 5 3
HELIX 6 6 THR A 76 SER A 87 1 12
HELIX 7 7 LEU A 89 ASN A 98 1 10
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