Header list of 1ueq.pdb file
Complete list - r 2 2 Bytes
HEADER SIGNALING PROTEIN 20-MAY-03 1UEQ
TITLE SOLUTION STRUCTURE OF THE FIRST PDZ DOMAIN OF HUMAN ATROPHIN-1
TITLE 2 INTERACTING PROTEIN 1 (KIAA0705 PROTEIN)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MEMBRANE ASSOCIATED GUANYLATE KINASE INVERTED-2 (MAGI-2);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PDZ DOMAIN;
COMPND 5 SYNONYM: KIAA0705 PROTEIN;
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: KAZUSA CDNA HG03359;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P021030-27;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS ATROPHIN-1 INTERACTING PROTEIN 1, PDZ DOMAIN, STRUCTURAL GENOMICS,
KEYWDS 2 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, SIGNALING
KEYWDS 3 PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR C.ZHAO,T.KIGAWA,N.TOCHIO,S.KOSHIBA,M.INOUE,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1UEQ 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1UEQ 1 VERSN
REVDAT 1 20-NOV-03 1UEQ 0
JRNL AUTH C.ZHAO,T.KIGAWA,N.TOCHIO,S.KOSHIBA,M.INOUE,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE FIRST PDZ DOMAIN OF HUMAN
JRNL TITL 2 ATROPHIN-1 INTERACTING PROTEIN 1 (KIAA0705 PROTEIN)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, OPALP
REMARK 3 AUTHORS : BRUKER (XWINNMR), R.KORADI,M.BILLETER,P.GUNTERT
REMARK 3 (OPALP)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1UEQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-MAY-03.
REMARK 100 THE DEPOSITION ID IS D_1000005741.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298.0
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 100MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.4MM PDZ DOMAIN U-15N, 13C;
REMARK 210 20MM TRIS-HCL (PH7.0), 100MM
REMARK 210 NACL, 1MM D-DTT, 0.02% NAN3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
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 20020425, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.811, CYANA 1.0.7
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 : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS, STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY, TARGET
REMARK 210 FUNCTION
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 HG1 THR A 23 OD2 ASP A 60 1.56
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 3 ARG A 11 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 17 ARG A 11 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
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 SER A 6 -172.41 -179.53
REMARK 500 1 PHE A 9 -178.68 53.86
REMARK 500 1 THR A 10 -121.35 -88.36
REMARK 500 1 ARG A 11 -83.32 150.19
REMARK 500 1 ALA A 13 -17.67 59.03
REMARK 500 1 ASN A 29 -158.94 46.56
REMARK 500 1 MET A 30 -76.32 23.19
REMARK 500 1 ASP A 40 -42.77 95.59
REMARK 500 1 ASP A 43 76.35 -175.56
REMARK 500 1 ASP A 54 -2.59 67.76
REMARK 500 1 ASN A 73 -73.47 59.63
REMARK 500 1 GLU A 74 40.51 -157.51
REMARK 500 1 ALA A 116 97.98 141.18
REMARK 500 2 SER A 2 -163.68 -74.63
REMARK 500 2 SER A 6 -123.50 -84.69
REMARK 500 2 LEU A 8 -77.72 -117.44
REMARK 500 2 THR A 10 -112.35 -78.77
REMARK 500 2 ARG A 11 -57.90 147.13
REMARK 500 2 ASP A 12 20.78 -142.76
REMARK 500 2 ALA A 13 -17.35 61.49
REMARK 500 2 ASN A 29 -92.54 49.62
REMARK 500 2 ASP A 40 -65.43 -159.33
REMARK 500 2 PRO A 42 45.22 -83.38
REMARK 500 2 ASP A 43 34.47 -157.21
REMARK 500 2 PRO A 53 46.09 -80.83
REMARK 500 2 ASP A 54 43.65 -160.54
REMARK 500 2 VAL A 70 -61.98 -106.40
REMARK 500 2 ASN A 73 -82.96 47.77
REMARK 500 2 GLU A 74 13.70 -143.45
REMARK 500 2 ASP A 114 92.68 35.29
REMARK 500 2 ALA A 116 -62.92 159.49
REMARK 500 2 ASN A 117 162.52 69.24
REMARK 500 2 SER A 121 81.62 -65.09
REMARK 500 3 SER A 5 112.50 65.90
REMARK 500 3 PHE A 9 165.12 52.71
REMARK 500 3 THR A 10 -99.36 -82.32
REMARK 500 3 ARG A 11 -32.14 117.83
REMARK 500 3 ALA A 13 -20.30 64.30
REMARK 500 3 LEU A 16 -159.66 -70.88
REMARK 500 3 LYS A 17 -84.18 -64.04
REMARK 500 3 ASN A 29 -79.87 60.40
REMARK 500 3 ASP A 40 -41.11 -179.79
REMARK 500 3 ASN A 73 -61.67 69.88
REMARK 500 3 GLU A 74 5.70 -157.71
REMARK 500 3 ALA A 116 87.97 174.50
REMARK 500 3 ASN A 117 -179.49 58.88
REMARK 500 3 SER A 122 -178.48 -68.54
REMARK 500 4 LEU A 8 -80.14 -112.97
REMARK 500 4 THR A 10 -120.39 -88.40
REMARK 500 4 ARG A 11 -47.64 146.77
REMARK 500
REMARK 500 THIS ENTRY HAS 292 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY A 38 GLY A 39 2 142.33
REMARK 500 SER A 6 GLY A 7 10 -148.90
REMARK 500 THR A 10 ARG A 11 11 147.57
REMARK 500 MET A 30 GLY A 31 12 -148.92
REMARK 500 SER A 122 GLY A 123 12 146.80
REMARK 500 ARG A 104 GLY A 105 14 149.43
REMARK 500 SER A 122 GLY A 123 16 142.29
REMARK 500 MET A 30 GLY A 31 17 -148.45
REMARK 500 PRO A 42 ASP A 43 18 146.17
REMARK 500 SER A 122 GLY A 123 20 119.98
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 104 0.09 SIDE CHAIN
REMARK 500 2 TYR A 106 0.10 SIDE CHAIN
REMARK 500 4 PHE A 45 0.08 SIDE CHAIN
REMARK 500 4 TYR A 106 0.09 SIDE CHAIN
REMARK 500 5 TYR A 106 0.07 SIDE CHAIN
REMARK 500 10 ARG A 104 0.08 SIDE CHAIN
REMARK 500 11 ARG A 11 0.09 SIDE CHAIN
REMARK 500 12 TYR A 71 0.07 SIDE CHAIN
REMARK 500 12 ARG A 104 0.12 SIDE CHAIN
REMARK 500 17 TYR A 106 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK002000688.2 RELATED DB: TARGETDB
DBREF 1UEQ A 8 118 UNP Q86UL8 AIP1_HUMAN 454 564
SEQADV 1UEQ GLY A 1 UNP Q86UL8 CLONING ARTIFACT
SEQADV 1UEQ SER A 2 UNP Q86UL8 CLONING ARTIFACT
SEQADV 1UEQ SER A 3 UNP Q86UL8 CLONING ARTIFACT
SEQADV 1UEQ GLY A 4 UNP Q86UL8 CLONING ARTIFACT
SEQADV 1UEQ SER A 5 UNP Q86UL8 CLONING ARTIFACT
SEQADV 1UEQ SER A 6 UNP Q86UL8 CLONING ARTIFACT
SEQADV 1UEQ GLY A 7 UNP Q86UL8 CLONING ARTIFACT
SEQADV 1UEQ GLY A 119 UNP Q86UL8 CLONING ARTIFACT
SEQADV 1UEQ PRO A 120 UNP Q86UL8 CLONING ARTIFACT
SEQADV 1UEQ SER A 121 UNP Q86UL8 CLONING ARTIFACT
SEQADV 1UEQ SER A 122 UNP Q86UL8 CLONING ARTIFACT
SEQADV 1UEQ GLY A 123 UNP Q86UL8 CLONING ARTIFACT
SEQRES 1 A 123 GLY SER SER GLY SER SER GLY LEU PHE THR ARG ASP ALA
SEQRES 2 A 123 SER GLN LEU LYS GLY THR PHE LEU SER THR THR LEU LYS
SEQRES 3 A 123 LYS SER ASN MET GLY PHE GLY PHE THR ILE ILE GLY GLY
SEQRES 4 A 123 ASP GLU PRO ASP GLU PHE LEU GLN VAL LYS SER VAL ILE
SEQRES 5 A 123 PRO ASP GLY PRO ALA ALA GLN ASP GLY LYS MET GLU THR
SEQRES 6 A 123 GLY ASP VAL ILE VAL TYR ILE ASN GLU VAL CYS VAL LEU
SEQRES 7 A 123 GLY HIS THR HIS ALA ASP VAL VAL LYS LEU PHE GLN SER
SEQRES 8 A 123 VAL PRO ILE GLY GLN SER VAL ASN LEU VAL LEU CYS ARG
SEQRES 9 A 123 GLY TYR PRO LEU PRO PHE ASP PRO GLU ASP PRO ALA ASN
SEQRES 10 A 123 SER GLY PRO SER SER GLY
HELIX 1 1 PRO A 56 GLN A 59 1 4
HELIX 2 2 HIS A 82 GLN A 90 1 9
SHEET 1 A 6 GLY A 18 LYS A 26 0
SHEET 2 A 6 PHE A 34 ILE A 37 0
SHEET 3 A 6 GLN A 47 VAL A 51 -1 O SER A 50 N THR A 35
SHEET 4 A 6 VAL A 68 ILE A 72 -1 N TYR A 71 O VAL A 101
SHEET 5 A 6 VAL A 75 CYS A 76 -1 O VAL A 75 N ILE A 72
SHEET 6 A 6 SER A 97 ARG A 104 -1 O LEU A 102 N LEU A 21
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 2 2 Bytes