Header list of 1x58.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 15-MAY-05 1X58
TITLE SOLUTION STRUCTURES OF THE MYB-LIKE DNA BINDING DOMAIN OF
TITLE 2 4930532D21RIK PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN 4930532D21RIK;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: MYB-LIKE DNA BINDING DOMAIN;
COMPND 5 SYNONYM: HYPOTHETICAL PROTEIN LOC320022;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: 4930532D21RIK;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040727-09;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS MUS MUSCULUS ADULT MALE TESTIS CDNA, RIKEN FULL-LENGTH ENRICHED
KEYWDS 2 LIBRARY, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN
KEYWDS 3 STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 4 GENOMICS/PROTEOMICS INITIATIVE, RSGI, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR N.NAMEKI,T.TOMIZAWA,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1X58 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1X58 1 VERSN
REVDAT 1 15-NOV-05 1X58 0
JRNL AUTH N.NAMEKI,T.TOMIZAWA,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURES OF THE MYB-LIKE DNA BINDING DOMAIN OF
JRNL TITL 2 4930532D21RIK 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, OPALP 1.2
REMARK 3 AUTHORS : BRUKER (XWINNMR), KORADI, R.,BILLETER, M.,GUNTERT,
REMARK 3 P. (OPALP)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1X58 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024394.
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 : 0.89MM MYB-LIKE DNA BINDING
REMARK 210 DOMAIN U-15N,13C; 20MM D-TRIS-
REMARK 210 HCL(PH 7.0); 100MM NACL; 1MM D-
REMARK 210 DTT; 0.02% NAN3; 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 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 0.9295, CYANA 1.0.7
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 RESTRAINED MOLECULAR 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: 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
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 2 104.73 -164.29
REMARK 500 1 SER A 5 23.00 -157.66
REMARK 500 1 LYS A 9 92.40 -51.72
REMARK 500 1 SER A 60 174.60 55.20
REMARK 500 1 SER A 61 74.97 48.28
REMARK 500 2 ARG A 8 -49.41 -157.51
REMARK 500 2 ASP A 10 -152.72 47.13
REMARK 500 2 SER A 36 -71.60 -59.92
REMARK 500 2 SER A 57 79.65 32.60
REMARK 500 2 SER A 61 178.05 55.83
REMARK 500 3 SER A 2 -147.77 -172.16
REMARK 500 3 SER A 6 156.69 59.57
REMARK 500 3 ARG A 8 -62.53 -133.22
REMARK 500 3 LYS A 9 -78.55 -137.48
REMARK 500 3 PHE A 11 94.75 54.68
REMARK 500 3 ASN A 28 21.54 -72.00
REMARK 500 3 SER A 57 -77.41 68.93
REMARK 500 3 SER A 61 85.09 65.01
REMARK 500 4 SER A 2 94.34 38.98
REMARK 500 4 SER A 3 84.22 64.29
REMARK 500 4 ARG A 8 -45.33 -132.33
REMARK 500 4 ASP A 10 104.75 65.72
REMARK 500 4 PHE A 11 88.79 67.62
REMARK 500 4 SER A 60 73.07 27.66
REMARK 500 5 ARG A 8 156.36 73.53
REMARK 500 5 LYS A 9 84.48 45.18
REMARK 500 5 ASP A 10 103.08 59.28
REMARK 500 5 PHE A 11 132.87 104.93
REMARK 500 5 SER A 57 72.47 -104.83
REMARK 500 5 SER A 61 77.88 -154.50
REMARK 500 6 SER A 3 -97.26 49.79
REMARK 500 6 SER A 5 82.11 27.62
REMARK 500 6 LYS A 9 -70.04 -138.83
REMARK 500 6 ASP A 10 -79.83 -144.18
REMARK 500 6 SER A 60 99.12 85.62
REMARK 500 6 SER A 61 19.98 58.92
REMARK 500 7 SER A 5 105.96 -58.34
REMARK 500 7 ASP A 10 -40.00 130.96
REMARK 500 7 SER A 60 18.27 -144.82
REMARK 500 8 SER A 2 -33.34 59.02
REMARK 500 8 LYS A 9 -92.75 56.76
REMARK 500 8 PHE A 11 122.07 70.64
REMARK 500 8 THR A 25 -61.73 -95.75
REMARK 500 8 ASN A 28 9.17 -69.51
REMARK 500 8 SER A 57 66.36 -111.65
REMARK 500 9 LYS A 9 -166.57 -70.65
REMARK 500 9 ASP A 10 -101.89 56.89
REMARK 500 10 SER A 2 84.72 56.01
REMARK 500 10 SER A 3 -154.98 58.14
REMARK 500 10 SER A 5 139.29 119.17
REMARK 500
REMARK 500 THIS ENTRY HAS 102 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LYS A 9 ASP A 10 2 -141.72
REMARK 500 GLY A 7 ARG A 8 3 148.96
REMARK 500 GLN A 40 LYS A 41 15 144.55
REMARK 500 MET A 26 GLY A 27 18 -146.42
REMARK 500 SER A 61 GLY A 62 19 145.58
REMARK 500 SER A 60 SER A 61 20 145.29
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 2 ARG A 43 0.09 SIDE CHAIN
REMARK 500 3 ARG A 43 0.09 SIDE CHAIN
REMARK 500 4 ARG A 44 0.13 SIDE CHAIN
REMARK 500 10 ARG A 8 0.07 SIDE CHAIN
REMARK 500 10 ARG A 43 0.08 SIDE CHAIN
REMARK 500 14 ARG A 54 0.14 SIDE CHAIN
REMARK 500 15 ARG A 44 0.07 SIDE CHAIN
REMARK 500 20 TYR A 18 0.08 SIDE CHAIN
REMARK 500 20 ARG A 44 0.10 SIDE CHAIN
REMARK 500 20 ARG A 54 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MMT008001488.1 RELATED DB: TARGETDB
DBREF 1X58 A 8 56 UNP Q8C0V1 Q8C0V1_MOUSE 712 760
SEQADV 1X58 GLY A 1 UNP Q8C0V1 CLONING ARTIFACT
SEQADV 1X58 SER A 2 UNP Q8C0V1 CLONING ARTIFACT
SEQADV 1X58 SER A 3 UNP Q8C0V1 CLONING ARTIFACT
SEQADV 1X58 GLY A 4 UNP Q8C0V1 CLONING ARTIFACT
SEQADV 1X58 SER A 5 UNP Q8C0V1 CLONING ARTIFACT
SEQADV 1X58 SER A 6 UNP Q8C0V1 CLONING ARTIFACT
SEQADV 1X58 GLY A 7 UNP Q8C0V1 CLONING ARTIFACT
SEQADV 1X58 SER A 57 UNP Q8C0V1 CLONING ARTIFACT
SEQADV 1X58 GLY A 58 UNP Q8C0V1 CLONING ARTIFACT
SEQADV 1X58 PRO A 59 UNP Q8C0V1 CLONING ARTIFACT
SEQADV 1X58 SER A 60 UNP Q8C0V1 CLONING ARTIFACT
SEQADV 1X58 SER A 61 UNP Q8C0V1 CLONING ARTIFACT
SEQADV 1X58 GLY A 62 UNP Q8C0V1 CLONING ARTIFACT
SEQRES 1 A 62 GLY SER SER GLY SER SER GLY ARG LYS ASP PHE THR LYS
SEQRES 2 A 62 GLU GLU VAL ASN TYR LEU PHE HIS GLY VAL LYS THR MET
SEQRES 3 A 62 GLY ASN HIS TRP ASN SER ILE LEU TRP SER PHE PRO PHE
SEQRES 4 A 62 GLN LYS GLY ARG ARG ALA VAL ASP LEU ALA HIS LYS TYR
SEQRES 5 A 62 HIS ARG LEU ILE SER GLY PRO SER SER GLY
HELIX 1 1 THR A 12 GLY A 27 1 16
HELIX 2 2 HIS A 29 PHE A 37 1 9
HELIX 3 3 ARG A 44 SER A 57 1 14
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