Header list of 2daq.pdb file
Complete list - r 9 2 Bytes
HEADER PROTEIN BINDING 14-DEC-05 2DAQ
TITLE SOLUTION STRUCTURE OF SECOND PWWP DOMAIN OF WHSC1L1 PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: WHSC1L1 PROTEIN, ISOFORM LONG;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PWWP 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: WHSC1L1;
SOURCE 6 EXPRESSION_SYSTEM: CELL FREE SYNTHESIS;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: P050425-24;
SOURCE 9 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS PWWP DOMAIN, WHSC1L1 PROTEIN, STRUCTURAL GENOMICS, NPPSFA, NATIONAL
KEYWDS 2 PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN
KEYWDS 3 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.N.NIRAULA,N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2DAQ 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2DAQ 1 VERSN
REVDAT 1 14-JUN-06 2DAQ 0
JRNL AUTH T.N.NIRAULA,N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF SECOND PWWP DOMAIN OF WHSC1L1 PROTEIN
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 1.0.8
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2DAQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-DEC-05.
REMARK 100 THE DEPOSITION ID IS D_1000025192.
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 : 120
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.60MM PWWP DOMAIN; U-15N, 13C;
REMARK 210 20MM D-TRIS-HCL(PH 7.0); 100MM
REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3; 90%
REMARK 210 H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 700 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 0.932, CYANA 1.0.8
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 HE1 TRP A 25 O PHE A 54 1.43
REMARK 500 O LEU A 37 H GLY A 41 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 3 113.38 60.81
REMARK 500 1 SER A 6 82.52 178.50
REMARK 500 1 LYS A 8 137.26 62.72
REMARK 500 1 TYR A 11 162.51 -41.24
REMARK 500 1 ASN A 21 -178.99 58.36
REMARK 500 1 ASP A 45 -75.11 -126.72
REMARK 500 1 ASP A 48 121.90 -39.67
REMARK 500 1 HIS A 57 69.64 79.91
REMARK 500 1 HIS A 63 179.91 -53.06
REMARK 500 1 ASP A 74 161.22 157.11
REMARK 500 1 LYS A 75 -67.10 -167.87
REMARK 500 1 PHE A 77 -53.83 177.65
REMARK 500 1 GLU A 79 135.17 165.63
REMARK 500 1 GLN A 81 97.35 55.51
REMARK 500 1 ASN A 85 93.30 68.97
REMARK 500 1 SER A 108 94.22 -160.79
REMARK 500 1 SER A 109 152.31 62.91
REMARK 500 2 SER A 6 164.40 58.82
REMARK 500 2 TYR A 11 171.48 -50.99
REMARK 500 2 LEU A 19 -173.07 -62.13
REMARK 500 2 TYR A 22 85.47 37.23
REMARK 500 2 ASP A 48 152.50 -40.07
REMARK 500 2 HIS A 57 68.18 79.20
REMARK 500 2 HIS A 63 -174.66 -58.70
REMARK 500 2 ASP A 74 164.47 58.52
REMARK 500 2 PHE A 77 67.88 -116.56
REMARK 500 2 ALA A 78 -62.54 -171.93
REMARK 500 2 GLU A 79 93.29 43.09
REMARK 500 2 SER A 83 -59.22 -147.96
REMARK 500 2 ILE A 84 85.26 65.95
REMARK 500 2 ASN A 85 -59.28 -164.15
REMARK 500 2 SER A 105 102.52 -167.51
REMARK 500 2 SER A 108 134.27 64.34
REMARK 500 2 SER A 109 82.06 61.68
REMARK 500 3 SER A 3 161.50 60.91
REMARK 500 3 SER A 5 106.15 64.80
REMARK 500 3 SER A 6 -60.69 -132.85
REMARK 500 3 HIS A 10 -95.95 -156.99
REMARK 500 3 LEU A 19 -160.23 -128.24
REMARK 500 3 ASN A 21 -55.18 -147.30
REMARK 500 3 TYR A 22 -66.11 -122.89
REMARK 500 3 LEU A 42 -76.81 -43.82
REMARK 500 3 LYS A 43 136.54 75.76
REMARK 500 3 ASP A 48 117.03 -39.79
REMARK 500 3 HIS A 57 64.89 68.42
REMARK 500 3 HIS A 63 -175.37 -52.95
REMARK 500 3 ASP A 74 92.56 -174.30
REMARK 500 3 LYS A 75 158.98 168.46
REMARK 500 3 SER A 76 78.69 -165.43
REMARK 500 3 PHE A 77 78.81 -173.96
REMARK 500
REMARK 500 THIS ENTRY HAS 375 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK003000497.1 RELATED DB: TARGETDB
DBREF 2DAQ A 8 104 UNP Q9BZ95 NSD3_HUMAN 957 1053
SEQADV 2DAQ GLY A 1 UNP Q9BZ95 CLONING ARTIFACT
SEQADV 2DAQ SER A 2 UNP Q9BZ95 CLONING ARTIFACT
SEQADV 2DAQ SER A 3 UNP Q9BZ95 CLONING ARTIFACT
SEQADV 2DAQ GLY A 4 UNP Q9BZ95 CLONING ARTIFACT
SEQADV 2DAQ SER A 5 UNP Q9BZ95 CLONING ARTIFACT
SEQADV 2DAQ SER A 6 UNP Q9BZ95 CLONING ARTIFACT
SEQADV 2DAQ GLY A 7 UNP Q9BZ95 CLONING ARTIFACT
SEQADV 2DAQ SER A 105 UNP Q9BZ95 CLONING ARTIFACT
SEQADV 2DAQ GLY A 106 UNP Q9BZ95 CLONING ARTIFACT
SEQADV 2DAQ PRO A 107 UNP Q9BZ95 CLONING ARTIFACT
SEQADV 2DAQ SER A 108 UNP Q9BZ95 CLONING ARTIFACT
SEQADV 2DAQ SER A 109 UNP Q9BZ95 CLONING ARTIFACT
SEQADV 2DAQ GLY A 110 UNP Q9BZ95 CLONING ARTIFACT
SEQRES 1 A 110 GLY SER SER GLY SER SER GLY LYS LEU HIS TYR LYS GLN
SEQRES 2 A 110 ILE VAL TRP VAL LYS LEU GLY ASN TYR ARG TRP TRP PRO
SEQRES 3 A 110 ALA GLU ILE CYS ASN PRO ARG SER VAL PRO LEU ASN ILE
SEQRES 4 A 110 GLN GLY LEU LYS HIS ASP LEU GLY ASP PHE PRO VAL PHE
SEQRES 5 A 110 PHE PHE GLY SER HIS ASP TYR TYR TRP VAL HIS GLN GLY
SEQRES 6 A 110 ARG VAL PHE PRO TYR VAL GLU GLY ASP LYS SER PHE ALA
SEQRES 7 A 110 GLU GLY GLN THR SER ILE ASN LYS THR PHE LYS LYS ALA
SEQRES 8 A 110 LEU GLU GLU ALA ALA LYS ARG PHE GLN GLU LEU LYS ALA
SEQRES 9 A 110 SER GLY PRO SER SER GLY
HELIX 1 1 PRO A 36 GLY A 41 1 6
HELIX 2 2 LYS A 86 ALA A 104 1 19
SHEET 1 A 5 ASP A 58 VAL A 62 0
SHEET 2 A 5 PHE A 49 PHE A 53 -1 N PHE A 53 O ASP A 58
SHEET 3 A 5 TRP A 24 ILE A 29 -1 N GLU A 28 O PHE A 52
SHEET 4 A 5 GLN A 13 LYS A 18 -1 N VAL A 15 O ALA A 27
SHEET 5 A 5 PHE A 68 PRO A 69 -1 O PHE A 68 N TRP A 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 - r 9 2 Bytes