Header list of 1j3x.pdb file
Complete list - v 10 2 Bytes
HEADER DNA BINDING PROTEIN 19-FEB-03 1J3X
TITLE SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF THE HMGB2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HIGH MOBILITY GROUP PROTEIN 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN;
COMPND 5 SYNONYM: HIGH MOBILITY GROUP B2(HMG2) A DOMAIN;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-22B
KEYWDS HMG-BOX, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR J.KURITA,H.SHIMAHARA,M.YOSHIDA,S.TATE
REVDAT 3 10-NOV-21 1J3X 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1J3X 1 VERSN
REVDAT 1 29-JUN-04 1J3X 0
JRNL AUTH J.KURITA,H.SHIMAHARA,M.YOSHIDA,S.TATE
JRNL TITL STRUCUTRAL COMPARISON OF TWO HMG-BOXES IN THE NON-HISTONE
JRNL TITL 2 PROTEIN HMG-2 WITH IN THE HMG-1
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE WAS ALSO REFINED WITH
REMARK 3 ARIA VER.1.1
REMARK 4
REMARK 4 1J3X COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-FEB-03.
REMARK 100 THE DEPOSITION ID IS D_1000005599.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 5.0
REMARK 210 IONIC STRENGTH : 50MM NA2SO4
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM N-TERMINAL DOMAIN U-15N,13C;
REMARK 210 50MM ACETATE BUFFER NA; 1MM N-
REMARK 210 TERMINAL DOMAIN U-15N; 50MM
REMARK 210 ACETATE BUFFER NA; 1MM N-
REMARK 210 TERMINAL DOMAIN NON-LABEL; 50MM
REMARK 210 ACETATE BUFFER NA
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 2D NOESY; CT_
REMARK 210 HMQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2001.157.17.50
REMARK 210 METHOD USED : SIMULATED 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: 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 O PHE A 38 H SER A 42 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 LYS A 3 -67.63 -103.19
REMARK 500 1 LYS A 12 -167.93 -104.43
REMARK 500 1 MET A 13 -159.46 -116.19
REMARK 500 1 ASP A 33 65.29 -107.38
REMARK 500 1 VAL A 36 74.81 -106.21
REMARK 500 1 ASN A 37 -176.06 -58.92
REMARK 500 1 ARG A 73 42.23 -100.61
REMARK 500 1 GLU A 74 -56.26 -126.92
REMARK 500 2 PRO A 9 -165.63 -72.58
REMARK 500 2 ARG A 10 -169.05 -79.42
REMARK 500 2 LYS A 12 -167.26 52.88
REMARK 500 2 MET A 13 -169.58 -129.36
REMARK 500 2 VAL A 36 103.34 -167.77
REMARK 500 3 ASP A 5 -59.97 -174.77
REMARK 500 3 ARG A 10 44.50 -154.23
REMARK 500 3 VAL A 36 71.51 -162.95
REMARK 500 3 ASN A 37 -168.50 -59.49
REMARK 500 3 GLU A 74 -44.84 -133.10
REMARK 500 4 ASN A 7 -158.96 -125.31
REMARK 500 4 ARG A 10 36.29 -153.10
REMARK 500 4 LYS A 29 -41.24 -168.25
REMARK 500 4 ASP A 33 58.71 -92.39
REMARK 500 4 VAL A 36 69.48 -167.52
REMARK 500 4 ASN A 37 -173.14 -60.41
REMARK 500 5 LYS A 12 -169.22 -102.88
REMARK 500 5 MET A 13 -168.47 -101.95
REMARK 500 5 ASP A 33 41.26 -107.89
REMARK 500 5 ASN A 37 177.10 -58.21
REMARK 500 6 ASP A 5 56.26 -158.18
REMARK 500 6 ASN A 7 -47.61 -138.86
REMARK 500 6 LYS A 12 -168.80 52.77
REMARK 500 6 SER A 35 172.47 56.17
REMARK 500 6 VAL A 36 79.04 -168.32
REMARK 500 6 ASN A 37 172.90 -59.86
REMARK 500 6 ARG A 73 34.99 -98.99
REMARK 500 6 GLU A 74 -43.50 -131.69
REMARK 500 7 LYS A 3 -44.35 -154.92
REMARK 500 7 PRO A 9 -166.73 -72.62
REMARK 500 7 MET A 13 -75.88 -106.96
REMARK 500 7 HIS A 27 30.20 -96.87
REMARK 500 7 LYS A 28 -51.28 -126.89
REMARK 500 7 HIS A 31 69.70 -117.43
REMARK 500 7 ASP A 33 59.10 -93.46
REMARK 500 7 VAL A 36 69.22 -156.04
REMARK 500 7 ASN A 37 -178.26 -60.18
REMARK 500 7 ARG A 73 36.60 -98.63
REMARK 500 7 GLU A 74 -45.11 -130.97
REMARK 500 8 LYS A 3 32.53 -153.56
REMARK 500 8 ARG A 10 177.27 -58.52
REMARK 500 8 LYS A 12 -179.04 53.22
REMARK 500
REMARK 500 THIS ENTRY HAS 219 RAMACHANDRAN OUTLIERS.
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 1 ARG A 10 0.29 SIDE CHAIN
REMARK 500 1 ARG A 24 0.32 SIDE CHAIN
REMARK 500 1 ARG A 48 0.31 SIDE CHAIN
REMARK 500 1 ARG A 70 0.26 SIDE CHAIN
REMARK 500 1 ARG A 73 0.29 SIDE CHAIN
REMARK 500 2 ARG A 10 0.31 SIDE CHAIN
REMARK 500 2 ARG A 24 0.29 SIDE CHAIN
REMARK 500 2 ARG A 48 0.32 SIDE CHAIN
REMARK 500 2 ARG A 70 0.28 SIDE CHAIN
REMARK 500 2 ARG A 73 0.28 SIDE CHAIN
REMARK 500 3 ARG A 10 0.28 SIDE CHAIN
REMARK 500 3 ARG A 24 0.24 SIDE CHAIN
REMARK 500 3 ARG A 48 0.29 SIDE CHAIN
REMARK 500 3 ARG A 70 0.30 SIDE CHAIN
REMARK 500 3 ARG A 73 0.27 SIDE CHAIN
REMARK 500 4 ARG A 10 0.29 SIDE CHAIN
REMARK 500 4 ARG A 24 0.32 SIDE CHAIN
REMARK 500 4 ARG A 48 0.30 SIDE CHAIN
REMARK 500 4 ARG A 70 0.30 SIDE CHAIN
REMARK 500 4 ARG A 73 0.29 SIDE CHAIN
REMARK 500 5 ARG A 10 0.27 SIDE CHAIN
REMARK 500 5 ARG A 24 0.31 SIDE CHAIN
REMARK 500 5 ARG A 48 0.32 SIDE CHAIN
REMARK 500 5 ARG A 70 0.32 SIDE CHAIN
REMARK 500 5 ARG A 73 0.30 SIDE CHAIN
REMARK 500 6 ARG A 10 0.28 SIDE CHAIN
REMARK 500 6 ARG A 24 0.32 SIDE CHAIN
REMARK 500 6 ARG A 48 0.31 SIDE CHAIN
REMARK 500 6 ARG A 70 0.26 SIDE CHAIN
REMARK 500 6 ARG A 73 0.29 SIDE CHAIN
REMARK 500 7 ARG A 10 0.28 SIDE CHAIN
REMARK 500 7 ARG A 24 0.28 SIDE CHAIN
REMARK 500 7 ARG A 48 0.30 SIDE CHAIN
REMARK 500 7 ARG A 70 0.31 SIDE CHAIN
REMARK 500 7 ARG A 73 0.32 SIDE CHAIN
REMARK 500 8 ARG A 10 0.28 SIDE CHAIN
REMARK 500 8 ARG A 24 0.28 SIDE CHAIN
REMARK 500 8 ARG A 48 0.31 SIDE CHAIN
REMARK 500 8 ARG A 70 0.23 SIDE CHAIN
REMARK 500 8 ARG A 73 0.31 SIDE CHAIN
REMARK 500 9 ARG A 10 0.26 SIDE CHAIN
REMARK 500 9 ARG A 24 0.29 SIDE CHAIN
REMARK 500 9 ARG A 48 0.26 SIDE CHAIN
REMARK 500 9 ARG A 70 0.31 SIDE CHAIN
REMARK 500 9 ARG A 73 0.30 SIDE CHAIN
REMARK 500 10 ARG A 10 0.29 SIDE CHAIN
REMARK 500 10 ARG A 24 0.32 SIDE CHAIN
REMARK 500 10 ARG A 48 0.29 SIDE CHAIN
REMARK 500 10 ARG A 70 0.30 SIDE CHAIN
REMARK 500 10 ARG A 73 0.26 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 150 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1J3X A 1 77 UNP P17741 HMG2_PIG 0 76
SEQADV 1J3X SER A 23 UNP P17741 CYS 22 ENGINEERED MUTATION
SEQRES 1 A 77 MET GLY LYS GLY ASP PRO ASN LYS PRO ARG GLY LYS MET
SEQRES 2 A 77 SER SER TYR ALA PHE PHE VAL GLN THR SER ARG GLU GLU
SEQRES 3 A 77 HIS LYS LYS LYS HIS PRO ASP SER SER VAL ASN PHE ALA
SEQRES 4 A 77 GLU PHE SER LYS LYS CYS SER GLU ARG TRP LYS THR MET
SEQRES 5 A 77 SER ALA LYS GLU LYS SER LYS PHE GLU ASP MET ALA LYS
SEQRES 6 A 77 SER ASP LYS ALA ARG TYR ASP ARG GLU MET LYS ASN
HELIX 1 1 SER A 14 GLU A 26 1 13
HELIX 2 2 HIS A 27 HIS A 31 5 5
HELIX 3 3 ASN A 37 MET A 52 1 16
HELIX 4 4 SER A 53 TYR A 71 1 19
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 - v 10 2 Bytes