Header list of 1u3b.pdb file
Complete list - 2 20 Bytes
HEADER PROTEIN TRANSPORT 21-JUL-04 1U3B
TITLE AUTO-INHIBITION MECHANISM OF X11S/MINTS FAMILY SCAFFOLD PROTEINS
TITLE 2 REVEALED BY THE CLOSED CONFORMATION OF THE TANDEM PDZ DOMAINS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AMYLOID BETA A4 PRECURSOR PROTEIN-BINDING, FAMILY A, MEMBER
COMPND 3 1;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: PDZ12C DOMAIN;
COMPND 6 SYNONYM: X11ALPHA/MINT1, PHOSPHOTYROSINE-BINDING/-INTERACTING DOMAIN
COMPND 7 (PTB)-BEARING PROTEIN, NEURONAL MUNC18-1-INTERACTING PROTEIN 1,
COMPND 8 NEURON-SPECIFIC X11 PROTEIN, ADAPTOR PROTEIN X11ALPHA;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET32A
KEYWDS X11S/MINTS, PDZ DOMAIN, SCAFFOLD PROTEIN, PROTEIN TRAFFICKING,
KEYWDS 2 PROTEIN TRANSPORT
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR W.FENG,J.-F.LONG,L.-N.CHAN,C.HE,A.FU,J.XIA,N.Y.IP,M.ZHANG
REVDAT 4 02-MAR-22 1U3B 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1U3B 1 VERSN
REVDAT 2 13-SEP-05 1U3B 1 JRNL
REVDAT 1 26-JUL-05 1U3B 0
JRNL AUTH J.-F.LONG,W.FENG,R.WANG,L.-N.CHAN,F.C.IP,J.XIA,N.Y.IP,
JRNL AUTH 2 M.ZHANG
JRNL TITL AUTOINHIBITION OF X11/MINT SCAFFOLD PROTEINS REVEALED BY THE
JRNL TITL 2 CLOSED CONFORMATION OF THE PDZ TANDEM
JRNL REF NAT.STRUCT.MOL.BIOL. V. 12 722 2005
JRNL REFN ISSN 1545-9993
JRNL PMID 16007100
JRNL DOI 10.1038/NSMB958
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1, CNS 1.1
REMARK 3 AUTHORS : BRUNGER, A.T. (CNS), BRUNGER, A.T. (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1U3B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-JUL-04.
REMARK 100 THE DEPOSITION ID IS D_1000023191.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: FIRSTLY, SELECT 20 STRUCTURES FROM CALCULATED 200
REMARK 210 STRUCTURES WITH THE CRITERIA OF LOWEST ENERGY; SECONDLY,
REMARK 210 CALCULATE THE MINIMIZED AVERAGE STRUCTURE USING THE SELECTED 20
REMARK 210 STRUCTURES; THIRDLY, SUBMIT THIS AVERAGE STRUCTURE AS THE
REMARK 210 STRUCTURAL MODEL OF PDZ12C
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 ILE A 30 -78.87 17.12
REMARK 500 LEU A 31 -43.51 -179.79
REMARK 500 SER A 38 85.64 -68.38
REMARK 500 TRP A 40 -159.68 -61.78
REMARK 500 SER A 42 42.24 79.95
REMARK 500 PRO A 45 90.17 -53.06
REMARK 500 THR A 46 -154.58 -139.59
REMARK 500 PRO A 82 -179.07 -68.93
REMARK 500 ASN A 95 61.44 -102.78
REMARK 500 ASN A 129 -69.79 66.64
REMARK 500 ILE A 153 -84.55 -132.93
REMARK 500 ALA A 175 52.10 -109.69
REMARK 500 ARG A 190 60.93 -104.21
REMARK 500 LEU A 191 -90.57 29.24
REMARK 500 LEU A 192 -45.25 -134.74
REMARK 500 ALA A 194 80.53 69.90
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1U37 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN, PDZ1 DOMAIN, 20 STRUCTURES
REMARK 900 RELATED ID: 1U38 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEX WITH C-PEPTIDE, 20 STRUCTURES
REMARK 900 RELATED ID: 1U39 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN, PDZ2 DOMAIN, 20 STRUCTURES
DBREF 1U3B A 19 201 UNP Q02410 APBA1_HUMAN 655 837
SEQADV 1U3B GLU A 17 UNP Q02410 CLONING ARTIFACT
SEQADV 1U3B PHE A 18 UNP Q02410 CLONING ARTIFACT
SEQRES 1 A 185 GLU PHE LYS ASP VAL PHE ILE GLU LYS GLN LYS GLY GLU
SEQRES 2 A 185 ILE LEU GLY VAL VAL ILE VAL GLU SER GLY TRP GLY SER
SEQRES 3 A 185 ILE LEU PRO THR VAL ILE ILE ALA ASN MET MET HIS GLY
SEQRES 4 A 185 GLY PRO ALA GLU LYS SER GLY LYS LEU ASN ILE GLY ASP
SEQRES 5 A 185 GLN ILE MET SER ILE ASN GLY THR SER LEU VAL GLY LEU
SEQRES 6 A 185 PRO LEU SER THR CYS GLN SER ILE ILE LYS GLY LEU LYS
SEQRES 7 A 185 ASN GLN SER ARG VAL LYS LEU ASN ILE VAL ARG CYS PRO
SEQRES 8 A 185 PRO VAL THR THR VAL LEU ILE ARG ARG PRO ASP LEU ARG
SEQRES 9 A 185 TYR GLN LEU GLY PHE SER VAL GLN ASN GLY ILE ILE CYS
SEQRES 10 A 185 SER LEU MET ARG GLY GLY ILE ALA GLU ARG GLY GLY VAL
SEQRES 11 A 185 ARG VAL GLY HIS ARG ILE ILE GLU ILE ASN GLY GLN SER
SEQRES 12 A 185 VAL VAL ALA THR PRO HIS GLU LYS ILE VAL HIS ILE LEU
SEQRES 13 A 185 SER ASN ALA VAL GLY GLU ILE HIS MET LYS THR MET PRO
SEQRES 14 A 185 ALA ALA MET TYR ARG LEU LEU THR ALA GLN GLU GLN PRO
SEQRES 15 A 185 VAL TYR ILE
HELIX 1 1 GLY A 56 GLY A 62 1 7
HELIX 2 2 PRO A 82 LEU A 93 1 12
HELIX 3 3 GLY A 139 GLY A 145 1 7
HELIX 4 4 PRO A 164 ASN A 174 1 11
SHEET 1 A 5 PHE A 18 GLU A 24 0
SHEET 2 A 5 ARG A 98 VAL A 104 -1 O LEU A 101 N VAL A 21
SHEET 3 A 5 GLN A 69 ILE A 73 -1 N GLN A 69 O VAL A 104
SHEET 4 A 5 VAL A 47 MET A 52 -1 N VAL A 47 O ILE A 70
SHEET 5 A 5 VAL A 33 GLU A 37 -1 N VAL A 34 O ASN A 51
SHEET 1 B 4 PHE A 18 GLU A 24 0
SHEET 2 B 4 ARG A 98 VAL A 104 -1 O LEU A 101 N VAL A 21
SHEET 3 B 4 GLN A 69 ILE A 73 -1 N GLN A 69 O VAL A 104
SHEET 4 B 4 THR A 76 SER A 77 -1 O THR A 76 N ILE A 73
SHEET 1 C 4 THR A 110 ARG A 116 0
SHEET 2 C 4 GLY A 177 PRO A 185 -1 O ILE A 179 N ILE A 114
SHEET 3 C 4 HIS A 150 ILE A 155 -1 N ARG A 151 O MET A 184
SHEET 4 C 4 GLN A 158 SER A 159 -1 O GLN A 158 N ILE A 155
SHEET 1 D 2 PHE A 125 GLN A 128 0
SHEET 2 D 2 ILE A 131 LEU A 135 -1 O ILE A 131 N GLN A 128
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
Complete list - 2 20 Bytes