Header list of 1v60.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 26-NOV-03 1V60
TITLE SOLUTION STRUCTURE OF BOLA1 PROTEIN FROM MUS MUSCULUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIKEN CDNA 1810037G04;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: BOLA1;
COMPND 5 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 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PCR2.1;
SOURCE 7 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS STATIONARY PHASE MORPHOGENE, STRUCTURAL GENOMICS, RIKEN STRUCTURAL
KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.KASAI,T.TOMIZAWA,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1V60 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1V60 1 VERSN
REVDAT 1 18-JAN-05 1V60 0
JRNL AUTH T.KASAI,T.TOMIZAWA,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF BOLA1 PROTEIN FROM MUS MUSCULUS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2.1, CYANA 1.0.7
REMARK 3 AUTHORS : DELAGLIO (NMRPIPE), GUENTERT (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE ARE BASED ON 3720 NOESY
REMARK 3 CROSS-PEAKS, 91 DIHEDRAL ANGLE RESTRAINTS AND 22 HYDROGEN BOND
REMARK 3 RESTRAINTS.
REMARK 4
REMARK 4 1V60 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-NOV-03.
REMARK 100 THE DEPOSITION ID IS D_1000006249.
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 : 100MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.5MM U-13C,15N BOLA1; 20MM
REMARK 210 SODIUM PHOSPHATE BUFFER, 100MM
REMARK 210 SODIUM CHLORIDE, 0.02% SODIUM
REMARK 210 AZIDE, 1MM D-DTT; 90% H2O, 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; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW 5.0.4, CYANA 1.0.7
REMARK 210 METHOD USED : SIMULATED ANNEALING, TORSION
REMARK 210 ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
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: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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 H GLU A 47 O VAL A 73 1.49
REMARK 500 O ARG A 87 H GLU A 91 1.56
REMARK 500 O HIS A 86 H HIS A 90 1.57
REMARK 500 O ALA A 35 H LYS A 39 1.57
REMARK 500 O ALA A 34 H ALA A 38 1.57
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 10 152.49 -43.58
REMARK 500 1 THR A 15 78.38 45.24
REMARK 500 1 ARG A 16 116.41 -170.66
REMARK 500 1 VAL A 19 114.24 62.67
REMARK 500 1 SER A 20 101.03 179.83
REMARK 500 1 ALA A 27 147.06 62.55
REMARK 500 1 ALA A 29 -172.83 55.78
REMARK 500 1 LYS A 39 -71.35 -69.02
REMARK 500 1 LEU A 44 -46.81 -150.69
REMARK 500 1 SER A 55 69.89 38.78
REMARK 500 1 HIS A 58 -173.23 -54.09
REMARK 500 1 ALA A 59 73.51 -105.49
REMARK 500 1 GLU A 65 54.62 -110.41
REMARK 500 1 PHE A 77 42.31 -89.50
REMARK 500 1 LEU A 93 59.61 -112.21
REMARK 500 1 ALA A 98 62.13 -116.39
REMARK 500 1 ALA A 103 111.91 -166.14
REMARK 500 1 ASP A 121 73.17 -154.03
REMARK 500 2 SER A 7 83.29 66.49
REMARK 500 2 SER A 8 170.10 65.55
REMARK 500 2 ARG A 21 164.98 57.62
REMARK 500 2 ALA A 29 -167.01 56.29
REMARK 500 2 LYS A 39 -71.08 -69.13
REMARK 500 2 LEU A 44 -46.41 -150.21
REMARK 500 2 GLU A 54 -64.20 -91.86
REMARK 500 2 SER A 55 79.90 39.43
REMARK 500 2 HIS A 58 136.98 -179.32
REMARK 500 2 ALA A 62 175.67 -58.54
REMARK 500 2 THR A 66 -65.14 -99.92
REMARK 500 2 PHE A 77 38.17 -89.02
REMARK 500 2 LEU A 93 61.18 -112.43
REMARK 500 2 PRO A 100 -78.14 -75.00
REMARK 500 2 ALA A 103 115.15 -174.07
REMARK 500 3 SER A 7 145.84 61.20
REMARK 500 3 SER A 11 88.40 -153.33
REMARK 500 3 MET A 13 94.66 56.32
REMARK 500 3 SER A 17 -57.32 -165.43
REMARK 500 3 CYS A 18 77.13 57.92
REMARK 500 3 SER A 20 89.14 40.12
REMARK 500 3 SER A 23 86.22 -172.93
REMARK 500 3 ALA A 24 78.04 -117.92
REMARK 500 3 SER A 26 -56.33 -136.20
REMARK 500 3 ALA A 27 -54.18 -166.46
REMARK 500 3 ALA A 28 168.36 172.95
REMARK 500 3 ALA A 29 -175.37 59.14
REMARK 500 3 LYS A 39 -71.28 -68.68
REMARK 500 3 LEU A 44 -46.76 -147.34
REMARK 500 3 GLU A 54 -61.64 -105.79
REMARK 500 3 SER A 55 86.46 38.17
REMARK 500 3 HIS A 58 152.94 -46.65
REMARK 500
REMARK 500 THIS ENTRY HAS 370 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MMK001001055 RELATED DB: TARGETDB
DBREF 1V60 A 13 128 UNP Q9D8S9 BOLA1_MOUSE 13 128
SEQADV 1V60 GLY A 6 UNP Q9D8S9 CLONING ARTIFACT
SEQADV 1V60 SER A 7 UNP Q9D8S9 CLONING ARTIFACT
SEQADV 1V60 SER A 8 UNP Q9D8S9 CLONING ARTIFACT
SEQADV 1V60 GLY A 9 UNP Q9D8S9 CLONING ARTIFACT
SEQADV 1V60 SER A 10 UNP Q9D8S9 CLONING ARTIFACT
SEQADV 1V60 SER A 11 UNP Q9D8S9 CLONING ARTIFACT
SEQADV 1V60 GLY A 12 UNP Q9D8S9 CLONING ARTIFACT
SEQRES 1 A 123 GLY SER SER GLY SER SER GLY MET ALA THR ARG SER CYS
SEQRES 2 A 123 VAL SER ARG GLY SER ALA GLY SER ALA ALA ALA GLY PRO
SEQRES 3 A 123 VAL GLU ALA ALA ILE ARG ALA LYS LEU GLU GLN ALA LEU
SEQRES 4 A 123 SER PRO GLU VAL LEU GLU LEU ARG ASN GLU SER GLY GLY
SEQRES 5 A 123 HIS ALA VAL PRO ALA GLY SER GLU THR HIS PHE ARG VAL
SEQRES 6 A 123 ALA VAL VAL SER SER ARG PHE GLU GLY MET SER PRO LEU
SEQRES 7 A 123 GLN ARG HIS ARG LEU VAL HIS GLU ALA LEU SER GLU GLU
SEQRES 8 A 123 LEU ALA GLY PRO VAL HIS ALA LEU ALA ILE GLN ALA LYS
SEQRES 9 A 123 THR PRO ALA GLN TRP ARG GLU ASN PRO GLN LEU ASP ILE
SEQRES 10 A 123 SER PRO PRO CYS LEU GLY
HELIX 1 1 GLY A 30 LEU A 44 1 15
HELIX 2 2 SER A 75 GLU A 78 5 4
HELIX 3 3 SER A 81 LEU A 93 1 13
HELIX 4 4 LEU A 93 ALA A 98 1 6
SHEET 1 A 3 VAL A 48 ASN A 53 0
SHEET 2 A 3 HIS A 67 VAL A 73 -1 O ALA A 71 N GLU A 50
SHEET 3 A 3 ALA A 103 LYS A 109 1 O GLN A 107 N VAL A 72
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