Header list of 1uhr.pdb file
Complete list - r 2 2 Bytes
HEADER GENE REGULATION 09-JUL-03 1UHR
TITLE SOLUTION STRUCTURE OF THE SWIB DOMAIN OF MOUSE BRG1-ASSOCIATED FACTOR
TITLE 2 60A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SWI/SNF RELATED, MATRIX ASSOCIATED, ACTIN DEPENDENT
COMPND 3 REGULATOR OF CHROMATIN SUBFAMILY D MEMBER 1;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: SWIB DOMAIN;
COMPND 6 SYNONYM: BRG1-ASSOCIATED FACTOR 60A, BAF60A;
COMPND 7 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: RIKEN CDNA 0710008A09;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P020826-29;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS STRUCTURAL GENOMICS, SWI/SNF, CHROMATIN REMODELING, RIKEN STRUCTURAL
KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, GENE REGULATION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.YAMADA,K.SAITO,N.NAMEKI,M.INOUE,S.KOSHIBA,M.SHIROUZU,T.TERADA,
AUTHOR 2 T.YABUKI,M.AOKI,T.MATSUDA,E.SEKI,H.HIROTA,M.YOSHIDA,A.TANAKA,
AUTHOR 3 T.OSANAI,T.ARAKAWA,P.CARNINCI,J.KAWAI,Y.HAYASHIZAKI,T.KIGAWA,
AUTHOR 4 S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1UHR 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1UHR 1 VERSN
REVDAT 1 24-AUG-04 1UHR 0
JRNL AUTH K.YAMADA,K.SAITO,N.NAMEKI,M.INOUE,S.KOSHIBA,M.SHIROUZU,
JRNL AUTH 2 T.TERADA,T.YABUKI,M.AOKI,T.MATSUDA,E.SEKI,H.HIROTA,
JRNL AUTH 3 M.YOSHIDA,A.TANAKA,T.OSANAI,T.ARAKAWA,P.CARNINCI,J.KAWAI,
JRNL AUTH 4 Y.HAYASHIZAKI,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE SWIB DOMAIN OF MOUSE
JRNL TITL 2 BRG1-ASSOCIATED FACTOR 60A
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA 1
REMARK 3 AUTHORS : GUENTART, P.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1UHR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-JUL-03.
REMARK 100 THE DEPOSITION ID IS D_1000005841.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 20MM SODIUM PHOSPHATE BUFFER
REMARK 210 (PH6.0); 100MM NACL; 1MM D-DTT;
REMARK 210 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 : XWINNMR 2.6, NMRPIPE 20020425,
REMARK 210 NMRVIEW 5, CYANA 1, KUJIRA 0.706
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 300
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
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 ASP A 57 H GLN A 61 1.50
REMARK 500 H LYS A 13 O MET A 83 1.53
REMARK 500 O TYR A 39 H HIS A 43 1.55
REMARK 500 OD2 ASP A 47 H GLU A 50 1.57
REMARK 500 O LYS A 70 H GLU A 73 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 2 110.28 -166.25
REMARK 500 1 SER A 5 103.26 -167.07
REMARK 500 1 SER A 6 95.88 56.75
REMARK 500 1 GLN A 8 143.07 -39.95
REMARK 500 1 LYS A 44 58.09 39.66
REMARK 500 1 PRO A 87 -162.20 -74.99
REMARK 500 1 SER A 88 -40.48 -171.57
REMARK 500 1 SER A 91 98.64 65.03
REMARK 500 2 SER A 3 104.15 -174.95
REMARK 500 2 SER A 5 89.82 42.30
REMARK 500 2 SER A 6 -56.29 -177.95
REMARK 500 2 GLN A 8 86.69 39.69
REMARK 500 2 LYS A 44 60.06 38.85
REMARK 500 2 SER A 92 104.14 56.36
REMARK 500 3 SER A 5 116.49 62.64
REMARK 500 3 SER A 6 143.31 177.70
REMARK 500 3 GLN A 11 118.10 -164.28
REMARK 500 3 GLN A 27 -167.59 -129.63
REMARK 500 3 SER A 88 102.39 67.74
REMARK 500 4 SER A 2 -58.39 -171.54
REMARK 500 4 GLN A 11 110.27 -164.18
REMARK 500 4 ALA A 19 -32.35 -39.37
REMARK 500 4 LYS A 44 59.11 38.86
REMARK 500 4 GLU A 65 30.25 70.22
REMARK 500 4 PRO A 87 -162.25 -75.01
REMARK 500 4 SER A 88 81.19 50.21
REMARK 500 4 SER A 91 -59.21 -135.81
REMARK 500 4 SER A 92 94.91 53.11
REMARK 500 5 SER A 2 -58.61 -164.84
REMARK 500 5 SER A 5 98.86 51.11
REMARK 500 5 GLN A 11 109.37 -165.93
REMARK 500 5 LYS A 44 58.97 39.65
REMARK 500 5 ILE A 63 -62.49 -102.00
REMARK 500 6 LYS A 44 59.39 39.59
REMARK 500 6 SER A 91 -57.59 -168.92
REMARK 500 6 SER A 92 -64.86 -96.52
REMARK 500 7 SER A 3 125.70 61.87
REMARK 500 7 SER A 5 144.67 63.94
REMARK 500 7 GLN A 8 150.65 -44.89
REMARK 500 7 GLN A 11 111.46 -162.19
REMARK 500 7 GLU A 65 30.74 70.28
REMARK 500 7 PRO A 87 -162.20 -75.05
REMARK 500 7 SER A 88 75.10 58.53
REMARK 500 8 SER A 3 163.29 64.65
REMARK 500 8 SER A 6 112.79 -169.35
REMARK 500 8 ALA A 19 -31.59 -39.86
REMARK 500 8 LYS A 44 59.94 39.51
REMARK 500 8 ILE A 63 -64.38 -101.71
REMARK 500 8 PRO A 85 -166.58 -74.97
REMARK 500 9 SER A 3 99.48 62.37
REMARK 500
REMARK 500 THIS ENTRY HAS 134 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MMT007019221.1 RELATED DB: TARGETDB
DBREF 1UHR A 8 87 UNP Q61466 SMRD1_MOUSE 252 331
SEQADV 1UHR GLY A 1 UNP Q61466 CLONING ARTIFACT
SEQADV 1UHR SER A 2 UNP Q61466 CLONING ARTIFACT
SEQADV 1UHR SER A 3 UNP Q61466 CLONING ARTIFACT
SEQADV 1UHR GLY A 4 UNP Q61466 CLONING ARTIFACT
SEQADV 1UHR SER A 5 UNP Q61466 CLONING ARTIFACT
SEQADV 1UHR SER A 6 UNP Q61466 CLONING ARTIFACT
SEQADV 1UHR GLY A 7 UNP Q61466 CLONING ARTIFACT
SEQADV 1UHR SER A 88 UNP Q61466 CLONING ARTIFACT
SEQADV 1UHR GLY A 89 UNP Q61466 CLONING ARTIFACT
SEQADV 1UHR PRO A 90 UNP Q61466 CLONING ARTIFACT
SEQADV 1UHR SER A 91 UNP Q61466 CLONING ARTIFACT
SEQADV 1UHR SER A 92 UNP Q61466 CLONING ARTIFACT
SEQADV 1UHR GLY A 93 UNP Q61466 CLONING ARTIFACT
SEQRES 1 A 93 GLY SER SER GLY SER SER GLY GLN PRO PRO GLN PHE LYS
SEQRES 2 A 93 LEU ASP PRO ARG LEU ALA ARG LEU LEU GLY ILE HIS THR
SEQRES 3 A 93 GLN THR ARG PRO VAL ILE ILE GLN ALA LEU TRP GLN TYR
SEQRES 4 A 93 ILE LYS THR HIS LYS LEU GLN ASP PRO HIS GLU ARG GLU
SEQRES 5 A 93 PHE VAL LEU CYS ASP LYS TYR LEU GLN GLN ILE PHE GLU
SEQRES 6 A 93 SER GLN ARG MET LYS PHE SER GLU ILE PRO GLN ARG LEU
SEQRES 7 A 93 HIS ALA LEU LEU MET PRO PRO GLU PRO SER GLY PRO SER
SEQRES 8 A 93 SER GLY
HELIX 1 1 ARG A 17 LEU A 22 1 6
HELIX 2 2 ARG A 29 HIS A 43 1 15
HELIX 3 3 TYR A 59 PHE A 64 1 6
HELIX 4 4 ILE A 74 LEU A 81 1 8
SHEET 1 A 3 THR A 26 GLN A 27 0
SHEET 2 A 3 PHE A 12 LEU A 14 -1 N PHE A 12 O GLN A 27
SHEET 3 A 3 LEU A 82 MET A 83 -1 O MET A 83 N LYS A 13
SHEET 1 B 2 PHE A 53 LEU A 55 0
SHEET 2 B 2 ARG A 68 LYS A 70 -1 O MET A 69 N VAL A 54
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