Header list of 1du6.pdb file
Complete list - c 21 2 Bytes
HEADER GENE REGULATION 14-JAN-00 1DU6
TITLE SOLUTION STRUCTURE OF THE TRUNCATED PBX HOMEODOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HOMEOBOX PROTEIN PBX1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: HOMEODOMAIN;
COMPND 5 SYNONYM: PBX1;
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: PBX1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET16B
KEYWDS HOMEODOMAIN, GENE REGULATION
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR T.SPRULES,N.GREEN,M.FEATHERSTONE,K.GEHRING
REVDAT 4 21-DEC-22 1DU6 1 SEQADV
REVDAT 3 16-FEB-22 1DU6 1 REMARK
REVDAT 2 24-FEB-09 1DU6 1 VERSN
REVDAT 1 16-AUG-00 1DU6 0
JRNL AUTH T.SPRULES,N.GREEN,M.FEATHERSTONE,K.GEHRING
JRNL TITL CONFORMATIONAL CHANGES IN THE PBX HOMEODOMAIN AND C-TERMINAL
JRNL TITL 2 EXTENSION UPON BINDING DNA AND HOX-DERIVED YPWM PEPTIDES.
JRNL REF BIOCHEMISTRY V. 39 9943 2000
JRNL REFN ISSN 0006-2960
JRNL PMID 10933814
JRNL DOI 10.1021/BI0001067
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.0, CNS 0.5
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 1338 RESTRAINTS, 1268 NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 48 DIHEDRAL ANGLE RESTRAINTS, 22 DISTANCE
REMARK 3 RESTRAINTS FROM HYDROGEN BONDS
REMARK 4
REMARK 4 1DU6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JAN-00.
REMARK 100 THE DEPOSITION ID IS D_1000010371.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303; 303; 303; 303
REMARK 210 PH : 4.8; 4.8; 6.0; 6.0
REMARK 210 IONIC STRENGTH : NULL; NULL; NULL; NULL
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT;
REMARK 210 AMBIENT
REMARK 210 SAMPLE CONTENTS : 2.5 MM PBX U-15N; 10 MM
REMARK 210 PHOSPHATE BUFFER; 1 MM DTT; 90%
REMARK 210 H2O, 10% D2O; 1 MM PBX U-15N,13C;
REMARK 210 10 MM PHOSPHATE BUFFER; 1 MM
REMARK 210 DTT; 90% H2O, 10% D2O; 2 MM PBX;
REMARK 210 1MM DTT; 90% H2O, 10% D2O; 4 MM
REMARK 210 PBX; 20 MM PHOSPHATE BUFFER; 1
REMARK 210 MM DTT; 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; HNHA; 2D
REMARK 210 NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : GIFA 4.2, CNS 0.5, XEASY 1.3.13
REMARK 210 METHOD USED : DYNAMICAL ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
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 VAL A 47 H SER A 51 1.13
REMARK 500 O VAL A 47 N SER A 51 2.02
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 HIS A 4 166.65 59.57
REMARK 500 1 HIS A 9 153.83 61.25
REMARK 500 1 MET A 10 48.26 77.89
REMARK 500 1 ASN A 11 -168.43 52.86
REMARK 500 1 LYS A 12 -100.91 -67.42
REMARK 500 1 TYR A 23 -76.05 -48.24
REMARK 500 1 SER A 24 -36.88 -38.18
REMARK 500 1 ASN A 28 64.81 -169.46
REMARK 500 1 PRO A 29 -89.79 -78.67
REMARK 500 1 PRO A 31 105.59 -50.21
REMARK 500 1 SER A 32 171.24 -51.26
REMARK 500 1 ILE A 45 -112.90 -94.11
REMARK 500 1 ARG A 60 76.67 75.81
REMARK 500 1 TYR A 61 8.23 -62.55
REMARK 500 1 LYS A 62 -143.04 -86.90
REMARK 500 2 SER A 2 -51.60 -147.60
REMARK 500 2 HIS A 4 127.38 63.25
REMARK 500 2 ILE A 5 97.33 60.38
REMARK 500 2 GLU A 6 88.92 60.69
REMARK 500 2 ARG A 8 99.53 52.79
REMARK 500 2 HIS A 9 -79.21 -81.50
REMARK 500 2 MET A 10 146.94 83.29
REMARK 500 2 LYS A 12 -89.22 -66.07
REMARK 500 2 SER A 24 -38.41 -38.36
REMARK 500 2 ASN A 28 76.49 -176.57
REMARK 500 2 PRO A 29 -78.24 -83.49
REMARK 500 2 PRO A 31 100.51 -50.16
REMARK 500 2 SER A 32 -169.78 -74.26
REMARK 500 2 ILE A 45 -127.46 -108.40
REMARK 500 2 ILE A 59 -76.73 -57.36
REMARK 500 2 ARG A 60 62.41 -162.08
REMARK 500 2 TYR A 61 21.03 -68.17
REMARK 500 2 LYS A 63 29.50 -160.22
REMARK 500 3 SER A 2 -60.96 -94.11
REMARK 500 3 ILE A 5 30.74 -153.49
REMARK 500 3 ARG A 8 78.43 47.03
REMARK 500 3 MET A 10 47.10 -162.07
REMARK 500 3 ASN A 11 169.51 54.44
REMARK 500 3 LYS A 12 -86.68 -67.53
REMARK 500 3 SER A 24 -37.99 -38.31
REMARK 500 3 PRO A 29 48.36 -87.46
REMARK 500 3 SER A 32 -164.39 -74.30
REMARK 500 3 ILE A 45 -128.38 -105.07
REMARK 500 3 ILE A 59 -93.62 -89.69
REMARK 500 3 ARG A 60 -19.74 59.15
REMARK 500 3 TYR A 61 37.28 -94.29
REMARK 500 3 LYS A 62 88.80 -155.48
REMARK 500 4 ILE A 5 96.00 44.59
REMARK 500 4 ARG A 8 -91.28 63.98
REMARK 500 4 MET A 10 50.36 -165.58
REMARK 500
REMARK 500 THIS ENTRY HAS 398 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1DU6 A 11 64 UNP P41778 PBX1_MOUSE 241 294
SEQADV 1DU6 SER A 1 UNP P41778 EXPRESSION TAG
SEQADV 1DU6 SER A 2 UNP P41778 EXPRESSION TAG
SEQADV 1DU6 GLY A 3 UNP P41778 EXPRESSION TAG
SEQADV 1DU6 HIS A 4 UNP P41778 EXPRESSION TAG
SEQADV 1DU6 ILE A 5 UNP P41778 EXPRESSION TAG
SEQADV 1DU6 GLU A 6 UNP P41778 EXPRESSION TAG
SEQADV 1DU6 GLY A 7 UNP P41778 EXPRESSION TAG
SEQADV 1DU6 HIS A 9 UNP P41778 EXPRESSION TAG
SEQADV 1DU6 MET A 10 UNP P41778 EXPRESSION TAG
SEQRES 1 A 64 SER SER GLY HIS ILE GLU GLY ARG HIS MET ASN LYS GLN
SEQRES 2 A 64 ALA THR GLU ILE LEU ASN GLU TYR PHE TYR SER HIS LEU
SEQRES 3 A 64 SER ASN PRO TYR PRO SER GLU GLU ALA LYS GLU GLU LEU
SEQRES 4 A 64 ALA LYS LYS CYS GLY ILE THR VAL SER GLN VAL SER ASN
SEQRES 5 A 64 TRP PHE GLY ASN LYS ARG ILE ARG TYR LYS LYS ASN
HELIX 1 1 GLN A 13 HIS A 25 1 13
HELIX 2 2 SER A 32 GLY A 44 1 13
HELIX 3 3 THR A 46 ARG A 58 1 13
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 - c 21 2 Bytes