Header list of 2dax.pdb file
Complete list - r 9 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 14-DEC-05 2DAX
TITLE SOLUTION STRUCTURE OF THE RWD DOMAIN OF HUMAN PROTEIN C21ORF6
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN C21ORF6;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RWD DOMAIN;
COMPND 5 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: C21ORF6;
SOURCE 6 EXPRESSION_SYSTEM: CELL FREE SYNTHESIS;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: P050302-87;
SOURCE 9 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS RWD DOMAIN, ALPHA+BETA SANDWICH FOLD, STRUCTURAL GENOMICS, NPPSFA,
KEYWDS 2 NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES,
KEYWDS 3 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, UNKNOWN
KEYWDS 4 FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.YONEYAMA,T.KIGAWA,K.SAITO,N.TOCHIO,S.KOSHIBA,M.INOUE,S.YOKOYAMA,
AUTHOR 2 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2DAX 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2DAX 1 VERSN
REVDAT 1 14-JUN-06 2DAX 0
JRNL AUTH M.YONEYAMA,T.KIGAWA,K.SAITO,N.TOCHIO,S.KOSHIBA,M.INOUE,
JRNL AUTH 2 S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE RWD DOMAIN OF HUMAN PROTEIN
JRNL TITL 2 C21ORF6
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 2DAX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-DEC-05.
REMARK 100 THE DEPOSITION ID IS D_1000025198.
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 : 1.26MM RWD DOMAIN U-15N,13C;
REMARK 210 20MM D-TRIS-HCL(PH 7.0); 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 : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20030801, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9318, 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 LOWEST ENERGY,STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 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 6 165.30 -45.43
REMARK 500 1 ARG A 53 101.14 -38.10
REMARK 500 1 VAL A 57 97.08 -69.48
REMARK 500 1 PRO A 82 -179.49 -69.81
REMARK 500 1 TYR A 85 140.73 -31.24
REMARK 500 1 ALA A 87 -73.35 -31.91
REMARK 500 1 GLU A 91 55.37 -107.31
REMARK 500 1 VAL A 97 -29.27 -39.50
REMARK 500 1 THR A 109 -36.83 -39.39
REMARK 500 1 GLN A 116 -34.96 -34.82
REMARK 500 1 LYS A 117 -64.64 -93.54
REMARK 500 1 ASN A 127 -29.63 -36.69
REMARK 500 1 ARG A 133 -31.29 -36.48
REMARK 500 2 GLU A 27 53.90 33.72
REMARK 500 2 GLU A 29 -64.46 -91.37
REMARK 500 2 TYR A 85 140.76 -33.21
REMARK 500 2 ALA A 87 -70.78 -31.09
REMARK 500 2 LEU A 89 158.24 -42.91
REMARK 500 2 PRO A 90 -166.82 -69.85
REMARK 500 2 LYS A 117 -64.71 -95.74
REMARK 500 2 ASN A 127 -38.78 -39.33
REMARK 500 2 VAL A 140 103.48 -42.21
REMARK 500 2 ASP A 143 116.78 -166.12
REMARK 500 3 ALA A 12 -39.62 -37.65
REMARK 500 3 ASN A 28 57.35 -105.58
REMARK 500 3 MET A 50 102.16 -50.60
REMARK 500 3 GLU A 70 36.01 37.06
REMARK 500 3 PRO A 82 -170.56 -69.73
REMARK 500 3 TYR A 85 140.89 -33.88
REMARK 500 3 ALA A 87 -72.31 -30.56
REMARK 500 3 LEU A 89 158.04 -46.38
REMARK 500 3 PRO A 90 -173.02 -69.81
REMARK 500 3 LEU A 99 178.52 -58.83
REMARK 500 3 ARG A 101 -30.75 -35.95
REMARK 500 3 THR A 109 -35.58 -38.59
REMARK 500 3 GLN A 116 -19.94 -49.07
REMARK 500 3 ASN A 127 -32.34 -39.94
REMARK 500 3 GLU A 134 -67.16 -95.19
REMARK 500 4 SER A 2 152.54 -40.72
REMARK 500 4 ALA A 10 -33.48 -34.95
REMARK 500 4 PHE A 24 77.67 -107.94
REMARK 500 4 GLU A 70 27.28 38.23
REMARK 500 4 PRO A 82 -178.91 -69.75
REMARK 500 4 TYR A 85 141.34 -28.27
REMARK 500 4 ALA A 87 -72.64 -30.32
REMARK 500 4 LEU A 89 156.06 -48.04
REMARK 500 4 PRO A 90 -179.85 -69.74
REMARK 500 4 GLU A 91 66.02 -111.31
REMARK 500 4 GLN A 116 -36.43 -34.79
REMARK 500 4 LYS A 117 -65.14 -96.19
REMARK 500
REMARK 500 THIS ENTRY HAS 306 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSI002012821.1 RELATED DB: TARGETDB
DBREF 2DAX A 8 146 UNP P57060 CU006_HUMAN 34 173
SEQADV 2DAX GLY A 1 UNP P57060 CLONING ARTIFACT
SEQADV 2DAX SER A 2 UNP P57060 CLONING ARTIFACT
SEQADV 2DAX SER A 3 UNP P57060 CLONING ARTIFACT
SEQADV 2DAX GLY A 4 UNP P57060 CLONING ARTIFACT
SEQADV 2DAX SER A 5 UNP P57060 CLONING ARTIFACT
SEQADV 2DAX SER A 6 UNP P57060 CLONING ARTIFACT
SEQADV 2DAX GLY A 7 UNP P57060 CLONING ARTIFACT
SEQADV 2DAX SER A 147 UNP P57060 CLONING ARTIFACT
SEQADV 2DAX GLY A 148 UNP P57060 CLONING ARTIFACT
SEQADV 2DAX PRO A 149 UNP P57060 CLONING ARTIFACT
SEQADV 2DAX SER A 150 UNP P57060 CLONING ARTIFACT
SEQADV 2DAX SER A 151 UNP P57060 CLONING ARTIFACT
SEQADV 2DAX GLY A 152 UNP P57060 CLONING ARTIFACT
SEQRES 1 A 152 GLY SER SER GLY SER SER GLY GLU GLN ALA GLU ALA GLN
SEQRES 2 A 152 LEU ALA GLU LEU ASP LEU LEU ALA SER MET PHE PRO GLY
SEQRES 3 A 152 GLU ASN GLU LEU ILE VAL ASN ASP GLN LEU ALA VAL ALA
SEQRES 4 A 152 GLU LEU LYS ASP CYS ILE GLU LYS LYS THR MET GLU GLY
SEQRES 5 A 152 ARG SER SER LYS VAL TYR PHE THR ILE ASN MET ASN LEU
SEQRES 6 A 152 ASP VAL SER ASP GLU LYS MET ALA MET PHE SER LEU ALA
SEQRES 7 A 152 CYS ILE LEU PRO PHE LYS TYR PRO ALA VAL LEU PRO GLU
SEQRES 8 A 152 ILE THR VAL ARG SER VAL LEU LEU SER ARG SER GLN GLN
SEQRES 9 A 152 THR GLN LEU ASN THR ASP LEU THR ALA PHE LEU GLN LYS
SEQRES 10 A 152 HIS CYS HIS GLY ASP VAL CYS ILE LEU ASN ALA THR GLU
SEQRES 11 A 152 TRP VAL ARG GLU HIS ALA SER GLY TYR VAL SER ARG ASP
SEQRES 12 A 152 THR SER SER SER GLY PRO SER SER GLY
HELIX 1 1 GLY A 7 PHE A 24 1 18
HELIX 2 2 ASP A 34 LYS A 48 1 15
HELIX 3 3 SER A 100 HIS A 118 1 19
HELIX 4 4 ILE A 125 VAL A 140 1 16
SHEET 1 A 4 LEU A 30 VAL A 32 0
SHEET 2 A 4 VAL A 57 ASP A 66 -1 O THR A 60 N ILE A 31
SHEET 3 A 4 MET A 72 LEU A 81 -1 O ALA A 73 N LEU A 65
SHEET 4 A 4 THR A 93 ARG A 95 -1 O ARG A 95 N SER A 76
CISPEP 1 TYR A 85 PRO A 86 1 -0.03
CISPEP 2 TYR A 85 PRO A 86 2 -0.06
CISPEP 3 TYR A 85 PRO A 86 3 -0.03
CISPEP 4 TYR A 85 PRO A 86 4 -0.01
CISPEP 5 TYR A 85 PRO A 86 5 -0.05
CISPEP 6 TYR A 85 PRO A 86 6 -0.03
CISPEP 7 TYR A 85 PRO A 86 7 -0.13
CISPEP 8 TYR A 85 PRO A 86 8 -0.09
CISPEP 9 TYR A 85 PRO A 86 9 -0.07
CISPEP 10 TYR A 85 PRO A 86 10 -0.05
CISPEP 11 TYR A 85 PRO A 86 11 -0.06
CISPEP 12 TYR A 85 PRO A 86 12 -0.05
CISPEP 13 TYR A 85 PRO A 86 13 0.00
CISPEP 14 TYR A 85 PRO A 86 14 -0.04
CISPEP 15 TYR A 85 PRO A 86 15 -0.07
CISPEP 16 TYR A 85 PRO A 86 16 -0.05
CISPEP 17 TYR A 85 PRO A 86 17 -0.06
CISPEP 18 TYR A 85 PRO A 86 18 -0.10
CISPEP 19 TYR A 85 PRO A 86 19 -0.06
CISPEP 20 TYR A 85 PRO A 86 20 -0.12
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