Header list of 1k99.pdb file
Complete list - c 21 2 Bytes
HEADER DNA BINDING PROTEIN 28-OCT-01 1K99
TITLE SOLUTION STRUCTURE OF THE FIRST HMG BOX IN HUMAN UPSTREAM BINDING
TITLE 2 FACTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UPSTREAM BINDING FACTOR 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: HMG BOX 1;
COMPND 5 SYNONYM: NUCLEOLAR TRANSCRIPTION FACTOR 1, HUBF;
COMPND 6 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: HUBF(103-192);
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-22B
KEYWDS ALPHA-HELIX, L-SHAPE, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR Y.XU,W.YANG,J.WU,Y.SHI
REVDAT 6 21-DEC-22 1K99 1 SEQADV
REVDAT 5 23-FEB-22 1K99 1 REMARK SEQADV
REVDAT 4 24-FEB-09 1K99 1 VERSN
REVDAT 3 04-DEC-02 1K99 1 REMARK
REVDAT 2 15-MAY-02 1K99 1 JRNL
REVDAT 1 14-NOV-01 1K99 0
JRNL AUTH Y.XU,W.YANG,J.WU,Y.SHI
JRNL TITL SOLUTION STRUCTURE OF THE FIRST HMG BOX DOMAIN IN HUMAN
JRNL TITL 2 UPSTREAM BINDING FACTOR.
JRNL REF BIOCHEMISTRY V. 41 5415 2002
JRNL REFN ISSN 0006-2960
JRNL PMID 11969401
JRNL DOI 10.1021/BI015977A
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER, A.T.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1K99 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-OCT-01.
REMARK 100 THE DEPOSITION ID IS D_1000014719.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300; 305; 290
REMARK 210 PH : 5.5; 5.5; 5.5
REMARK 210 IONIC STRENGTH : 10MM; 10MM; 10MM
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 3MM HUBF HMG BOX1 U-15N; 10MM
REMARK 210 NAPO4 BUFFER PH5.5; 90% H2O, 10%
REMARK 210 D2O; 3MM HUBF HMG BOX1 U-15N,13C;
REMARK 210 10MM NAPO4 BUFFER PH5.5; 90%
REMARK 210 H2O, 10%D2O; 3MM HUBF HMG BOX1 U-
REMARK 210 15N; 10MM NAPO4 BUFFER PH5.5;
REMARK 210 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 1.3, NMRPIPE, PIPP
REMARK 210 METHOD USED : SIMULATED ANNEALING; TORSION
REMARK 210 ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 60
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS, STRUCTURES
REMARK 210 WITH THE LOWEST 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 LEU A 92
REMARK 465 GLU A 93
REMARK 465 HIS A 94
REMARK 465 HIS A 95
REMARK 465 HIS A 96
REMARK 465 HIS A 97
REMARK 465 HIS A 98
REMARK 465 HIS A 99
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 LYS A 2 141.15 -170.07
REMARK 500 1 LEU A 4 139.48 -172.33
REMARK 500 1 LYS A 5 -158.25 -122.39
REMARK 500 1 ASP A 9 93.08 59.81
REMARK 500 1 PHE A 10 78.70 59.52
REMARK 500 1 PRO A 14 173.95 -49.27
REMARK 500 1 HIS A 33 59.64 -115.32
REMARK 500 1 MET A 36 -150.36 -126.52
REMARK 500 1 SER A 37 -57.85 -139.05
REMARK 500 1 ASN A 38 -24.13 169.79
REMARK 500 1 PRO A 53 24.47 -73.49
REMARK 500 1 GLU A 54 8.50 58.93
REMARK 500 1 ASP A 81 92.08 -54.90
REMARK 500 1 PRO A 83 109.65 -59.70
REMARK 500 1 ASP A 84 87.82 -151.78
REMARK 500 1 ILE A 86 94.19 28.66
REMARK 500 1 ASN A 88 87.07 -177.09
REMARK 500 1 ALA A 89 51.93 -107.51
REMARK 500 2 LEU A 4 -172.86 -176.70
REMARK 500 2 PRO A 8 -170.38 -54.22
REMARK 500 2 PHE A 10 110.27 60.66
REMARK 500 2 LYS A 13 -61.87 -178.22
REMARK 500 2 PRO A 14 174.57 -56.05
REMARK 500 2 HIS A 33 52.07 -119.49
REMARK 500 2 MET A 36 -156.04 -127.20
REMARK 500 2 SER A 37 -57.46 -127.02
REMARK 500 2 ASN A 38 -24.54 167.83
REMARK 500 2 PRO A 53 25.28 -70.56
REMARK 500 2 GLU A 54 7.95 59.42
REMARK 500 2 HIS A 82 -54.63 -179.07
REMARK 500 2 ASP A 84 -79.51 -119.77
REMARK 500 2 LEU A 85 141.13 66.76
REMARK 500 2 ALA A 89 48.47 -87.15
REMARK 500 2 LYS A 90 -83.68 60.48
REMARK 500 3 LEU A 4 109.72 64.89
REMARK 500 3 LYS A 6 -171.06 55.85
REMARK 500 3 HIS A 7 172.86 57.04
REMARK 500 3 PRO A 8 64.45 -66.51
REMARK 500 3 ASP A 9 -47.00 -159.09
REMARK 500 3 PRO A 11 102.09 -53.16
REMARK 500 3 LYS A 13 -60.47 -177.84
REMARK 500 3 PRO A 14 173.52 -51.42
REMARK 500 3 HIS A 33 61.09 -114.46
REMARK 500 3 PRO A 53 22.28 -72.26
REMARK 500 3 GLU A 54 12.05 56.66
REMARK 500 3 GLU A 80 -81.46 -51.24
REMARK 500 3 ASP A 81 -168.49 50.43
REMARK 500 3 ASP A 84 34.69 -168.52
REMARK 500 3 GLN A 87 149.36 171.62
REMARK 500 3 ASN A 88 -51.41 76.20
REMARK 500
REMARK 500 THIS ENTRY HAS 357 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1K99 A 2 91 UNP P17480 UBF1_HUMAN 103 192
SEQADV 1K99 MET A 1 UNP P17480 INITIATING METHIONINE
SEQADV 1K99 LEU A 92 UNP P17480 EXPRESSION TAG
SEQADV 1K99 GLU A 93 UNP P17480 EXPRESSION TAG
SEQADV 1K99 HIS A 94 UNP P17480 EXPRESSION TAG
SEQADV 1K99 HIS A 95 UNP P17480 EXPRESSION TAG
SEQADV 1K99 HIS A 96 UNP P17480 EXPRESSION TAG
SEQADV 1K99 HIS A 97 UNP P17480 EXPRESSION TAG
SEQADV 1K99 HIS A 98 UNP P17480 EXPRESSION TAG
SEQADV 1K99 HIS A 99 UNP P17480 EXPRESSION TAG
SEQRES 1 A 99 MET LYS LYS LEU LYS LYS HIS PRO ASP PHE PRO LYS LYS
SEQRES 2 A 99 PRO LEU THR PRO TYR PHE ARG PHE PHE MET GLU LYS ARG
SEQRES 3 A 99 ALA LYS TYR ALA LYS LEU HIS PRO GLU MET SER ASN LEU
SEQRES 4 A 99 ASP LEU THR LYS ILE LEU SER LYS LYS TYR LYS GLU LEU
SEQRES 5 A 99 PRO GLU LYS LYS LYS MET LYS TYR ILE GLN ASP PHE GLN
SEQRES 6 A 99 ARG GLU LYS GLN GLU PHE GLU ARG ASN LEU ALA ARG PHE
SEQRES 7 A 99 ARG GLU ASP HIS PRO ASP LEU ILE GLN ASN ALA LYS LYS
SEQRES 8 A 99 LEU GLU HIS HIS HIS HIS HIS HIS
HELIX 1 1 THR A 16 LYS A 31 1 16
HELIX 2 2 ASN A 38 LEU A 52 1 15
HELIX 3 3 LYS A 56 ALA A 76 1 21
HELIX 4 4 ARG A 77 ASP A 81 5 5
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