Header list of 2d88.pdb file
Complete list - r 9 2 Bytes
HEADER SIGNALING PROTEIN, PROTEIN BINDING 02-DEC-05 2D88
TITLE SOLUTION STRUCTURE OF THE CH DOMAIN FROM HUMAN MICAL-3 PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN MICAL-3;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CH DOMAIN;
COMPND 5 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: MICAL3;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P050627-23;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS ALL ALPHA, CALPONIN HOMOLOGY DOMAIN, STRUCTURAL GENOMICS, NPPSFA,
KEYWDS 2 NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES,
KEYWDS 3 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, SIGNALING
KEYWDS 4 PROTEIN, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.TOMIZAWA,T.KIGAWA,S.KOSHIBA,M.INOUE,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2D88 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2D88 1 VERSN
REVDAT 1 02-JUN-06 2D88 0
JRNL AUTH T.TOMIZAWA,T.KIGAWA,S.KOSHIBA,M.INOUE,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE CH DOMAIN FROM HUMAN MICAL-3
JRNL TITL 2 PROTEIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, CYANA 2.0.17
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2D88 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-DEC-05.
REMARK 100 THE DEPOSITION ID IS D_1000025109.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 296
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.12MM CH DOMAIN U-15N, 13C;
REMARK 210 20MM D-TRIS-HCL(PH 7.0); 100MM
REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3; 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
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20030801, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.932, CYANA 2.0.17
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 RESTRAINTED MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION, STRUCTURES WITH
REMARK 210 THE LOWEST ENERGY, STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 VIOLATIONS
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: 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 3 128.86 -35.73
REMARK 500 1 TYR A 25 -179.64 -61.09
REMARK 500 1 ASN A 29 53.09 34.90
REMARK 500 1 VAL A 30 113.68 -38.16
REMARK 500 1 THR A 34 -74.87 -134.45
REMARK 500 1 LYS A 38 -39.74 -39.97
REMARK 500 1 ALA A 76 -71.13 -45.03
REMARK 500 1 GLU A 79 -62.44 -99.39
REMARK 500 1 GLU A 96 136.66 -170.55
REMARK 500 1 PRO A 97 -174.72 -69.71
REMARK 500 1 LEU A 100 -72.04 -50.77
REMARK 500 1 SER A 119 96.83 -52.84
REMARK 500 1 SER A 120 105.67 -49.67
REMARK 500 2 TYR A 25 -176.28 -62.77
REMARK 500 2 THR A 34 -55.86 -134.73
REMARK 500 2 LYS A 38 -39.85 -35.81
REMARK 500 2 ASN A 68 -31.28 -35.65
REMARK 500 2 LEU A 71 -71.03 -51.21
REMARK 500 2 ASP A 74 -60.85 -92.18
REMARK 500 2 GLU A 79 -68.94 -104.20
REMARK 500 3 ARG A 10 159.54 -48.59
REMARK 500 3 VAL A 28 70.71 -118.96
REMARK 500 3 THR A 34 -74.91 -120.59
REMARK 500 3 SER A 36 -29.62 -39.86
REMARK 500 3 VAL A 65 -66.52 -99.38
REMARK 500 3 LYS A 67 -71.04 -68.46
REMARK 500 3 ASN A 68 -32.19 -39.56
REMARK 500 3 ALA A 76 -70.76 -45.94
REMARK 500 3 GLU A 79 -64.79 -109.72
REMARK 500 3 ILE A 82 97.33 -62.72
REMARK 500 3 GLU A 96 126.46 -170.39
REMARK 500 3 LEU A 100 -72.66 -51.65
REMARK 500 4 SER A 2 42.32 39.94
REMARK 500 4 ALA A 9 42.33 -106.31
REMARK 500 4 SER A 11 115.33 -39.47
REMARK 500 4 THR A 34 -69.74 -134.44
REMARK 500 4 VAL A 65 -66.74 -102.25
REMARK 500 4 ASN A 68 -36.51 -35.78
REMARK 500 4 ALA A 76 -73.35 -45.78
REMARK 500 4 GLU A 79 -65.12 -104.22
REMARK 500 4 GLU A 96 130.01 -172.16
REMARK 500 4 SER A 116 104.12 -35.24
REMARK 500 5 VAL A 8 157.49 -46.38
REMARK 500 5 ARG A 10 144.11 -34.56
REMARK 500 5 VAL A 28 -74.06 -91.26
REMARK 500 5 ASN A 29 54.90 37.34
REMARK 500 5 VAL A 30 125.01 -35.51
REMARK 500 5 THR A 34 -74.35 -133.77
REMARK 500 5 LEU A 60 162.08 -49.45
REMARK 500 5 ASN A 68 -37.09 -35.58
REMARK 500
REMARK 500 THIS ENTRY HAS 209 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK002101337.1 RELATED DB: TARGETDB
DBREF 2D88 A 8 115 UNP Q7RTP6 MICA3_HUMAN 518 625
SEQADV 2D88 GLY A 1 UNP Q7RTP6 CLONING ARTIFACT
SEQADV 2D88 SER A 2 UNP Q7RTP6 CLONING ARTIFACT
SEQADV 2D88 SER A 3 UNP Q7RTP6 CLONING ARTIFACT
SEQADV 2D88 GLY A 4 UNP Q7RTP6 CLONING ARTIFACT
SEQADV 2D88 SER A 5 UNP Q7RTP6 CLONING ARTIFACT
SEQADV 2D88 SER A 6 UNP Q7RTP6 CLONING ARTIFACT
SEQADV 2D88 GLY A 7 UNP Q7RTP6 CLONING ARTIFACT
SEQADV 2D88 SER A 116 UNP Q7RTP6 CLONING ARTIFACT
SEQADV 2D88 GLY A 117 UNP Q7RTP6 CLONING ARTIFACT
SEQADV 2D88 PRO A 118 UNP Q7RTP6 CLONING ARTIFACT
SEQADV 2D88 SER A 119 UNP Q7RTP6 CLONING ARTIFACT
SEQADV 2D88 SER A 120 UNP Q7RTP6 CLONING ARTIFACT
SEQADV 2D88 GLY A 121 UNP Q7RTP6 CLONING ARTIFACT
SEQRES 1 A 121 GLY SER SER GLY SER SER GLY VAL ALA ARG SER SER LYS
SEQRES 2 A 121 LEU LEU GLY TRP CYS GLN ARG GLN THR ASP GLY TYR ALA
SEQRES 3 A 121 GLY VAL ASN VAL THR ASP LEU THR MET SER TRP LYS SER
SEQRES 4 A 121 GLY LEU ALA LEU CYS ALA ILE ILE HIS ARG TYR ARG PRO
SEQRES 5 A 121 ASP LEU ILE ASP PHE ASP SER LEU ASP GLU GLN ASN VAL
SEQRES 6 A 121 GLU LYS ASN ASN GLN LEU ALA PHE ASP ILE ALA GLU LYS
SEQRES 7 A 121 GLU LEU GLY ILE SER PRO ILE MET THR GLY LYS GLU MET
SEQRES 8 A 121 ALA SER VAL GLY GLU PRO ASP LYS LEU SER MET VAL MET
SEQRES 9 A 121 TYR LEU THR GLN PHE TYR GLU MET PHE LYS ASP SER GLY
SEQRES 10 A 121 PRO SER SER GLY
HELIX 1 1 SER A 12 THR A 22 1 11
HELIX 2 2 THR A 34 SER A 39 1 6
HELIX 3 3 GLY A 40 ARG A 51 1 12
HELIX 4 4 ASN A 64 LEU A 80 1 17
HELIX 5 5 THR A 87 VAL A 94 1 8
HELIX 6 6 ASP A 98 LYS A 114 1 17
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 9 2 Bytes