Header list of 1x5q.pdb file
Complete list - r 2 2 Bytes
HEADER CELL ADHESION, CELL CYCLE 16-MAY-05 1X5Q
TITLE SOLUTION STRUCTURE OF THE FIRST PDZ DOMAIN OF SCRIBBLE HOMOLOG PROTEIN
TITLE 2 (HSCRIB)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LAP4 PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PDZ DOMAIN;
COMPND 5 SYNONYM: SCRIBBLE HOMOLOG PROTEIN, HSCRIB;
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: SCRIB, CRIB1, KIAA0147, LAP4, SCRB1, VARTUL;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040628-05;
SOURCE 8 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS
KEYWDS PDZ DOMAIN, LAP4 PROTEIN, SCRIBBLE HOMOLOG PROTEIN, HSCRIB,
KEYWDS 2 STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL
KEYWDS 3 AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 4 INITIATIVE, RSGI, CELL ADHESION, CELL CYCLE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR X.R.QIN,T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1X5Q 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1X5Q 1 VERSN
REVDAT 1 16-NOV-05 1X5Q 0
JRNL AUTH X.R.QIN,T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE FIRST PDZ DOMAIN OF SCRIBBLE
JRNL TITL 2 HOMOLOG PROTEIN (HSCRIB)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1C, CYANA 1.0.7
REMARK 3 AUTHORS : VARIAN (VNMR), GUNTERT,P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1X5Q COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024412.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.20MM 13C, 15N-LABELED PROTEIN;
REMARK 210 20MM D-TRIS-HCL; 100MM NACL; 1MM
REMARK 210 D-DTT; 0.02% NAN3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 900 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20031121, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9296, CYANA 1.0.7
REMARK 210 METHOD USED : TORSION ANGLE 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: SPECTROMETER_ID 1 FOR 3D_15N_SEPARATED_NOESY;
REMARK 210 SPECTROMETER_ID 2 FOR 3D_13C_SEPARATED_NOESY
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 H ILE A 21 O VAL A 97 1.50
REMARK 500 H GLU A 15 O ARG A 103 1.51
REMARK 500 O SER A 31 H SER A 51 1.53
REMARK 500 H LEU A 71 O ARG A 100 1.54
REMARK 500 O ILE A 21 H VAL A 97 1.56
REMARK 500 O HIS A 84 H GLU A 88 1.57
REMARK 500 H ASN A 74 O GLN A 98 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 SER A 5 -58.33 -127.90
REMARK 500 1 GLU A 8 88.13 49.33
REMARK 500 1 GLU A 13 138.52 -176.91
REMARK 500 1 GLU A 14 147.71 -38.17
REMARK 500 1 GLU A 56 72.64 -105.09
REMARK 500 1 ALA A 93 135.77 -174.58
REMARK 500 1 THR A 95 -78.11 -38.20
REMARK 500 1 SER A 105 103.30 -49.82
REMARK 500 1 SER A 109 -79.42 62.82
REMARK 500 2 ALA A 10 171.12 -58.38
REMARK 500 2 GLU A 13 138.95 -176.62
REMARK 500 2 GLU A 14 155.11 -38.58
REMARK 500 2 GLN A 24 73.22 -112.20
REMARK 500 2 THR A 25 46.15 36.22
REMARK 500 2 ALA A 33 112.28 -160.15
REMARK 500 2 LYS A 42 -80.53 -104.83
REMARK 500 2 GLU A 56 42.14 -107.34
REMARK 500 2 GLN A 79 -84.05 -38.77
REMARK 500 2 THR A 95 -78.64 -41.19
REMARK 500 2 SER A 108 91.55 47.99
REMARK 500 2 SER A 109 157.97 66.27
REMARK 500 3 SER A 3 108.07 -176.67
REMARK 500 3 GLU A 13 130.22 -170.32
REMARK 500 3 GLU A 14 146.93 -38.77
REMARK 500 3 GLN A 24 116.00 171.19
REMARK 500 3 THR A 25 44.01 38.85
REMARK 500 3 LEU A 28 -179.68 73.49
REMARK 500 3 SER A 38 165.62 177.01
REMARK 500 3 LYS A 42 -84.40 -103.50
REMARK 500 3 GLU A 46 46.93 -91.05
REMARK 500 3 SER A 54 109.57 -53.40
REMARK 500 3 GLU A 56 42.29 -98.32
REMARK 500 3 THR A 95 -81.72 -39.91
REMARK 500 4 GLU A 14 145.49 -37.17
REMARK 500 4 GLN A 24 -55.13 -134.09
REMARK 500 4 LEU A 28 174.71 53.00
REMARK 500 4 LYS A 36 -107.19 -73.31
REMARK 500 4 LYS A 42 -71.88 -108.03
REMARK 500 4 SER A 54 107.36 -49.65
REMARK 500 4 GLU A 56 37.79 -96.62
REMARK 500 4 THR A 95 -81.69 -38.35
REMARK 500 5 SER A 6 159.78 -41.63
REMARK 500 5 GLU A 8 108.09 -163.80
REMARK 500 5 GLU A 13 134.92 -176.98
REMARK 500 5 GLN A 24 -59.00 -171.04
REMARK 500 5 LEU A 28 177.89 59.83
REMARK 500 5 ALA A 33 118.26 -166.35
REMARK 500 5 SER A 54 107.41 -49.82
REMARK 500 5 GLU A 56 50.25 -94.17
REMARK 500 5 LEU A 78 35.66 -92.50
REMARK 500
REMARK 500 THIS ENTRY HAS 218 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK002300144.1 RELATED DB: TARGETDB
DBREF 1X5Q A 8 104 UNP Q14160 LAP4_HUMAN 718 814
SEQADV 1X5Q GLY A 1 UNP Q14160 CLONING ARTIFACT
SEQADV 1X5Q SER A 2 UNP Q14160 CLONING ARTIFACT
SEQADV 1X5Q SER A 3 UNP Q14160 CLONING ARTIFACT
SEQADV 1X5Q GLY A 4 UNP Q14160 CLONING ARTIFACT
SEQADV 1X5Q SER A 5 UNP Q14160 CLONING ARTIFACT
SEQADV 1X5Q SER A 6 UNP Q14160 CLONING ARTIFACT
SEQADV 1X5Q GLY A 7 UNP Q14160 CLONING ARTIFACT
SEQADV 1X5Q SER A 105 UNP Q14160 CLONING ARTIFACT
SEQADV 1X5Q GLY A 106 UNP Q14160 CLONING ARTIFACT
SEQADV 1X5Q PRO A 107 UNP Q14160 CLONING ARTIFACT
SEQADV 1X5Q SER A 108 UNP Q14160 CLONING ARTIFACT
SEQADV 1X5Q SER A 109 UNP Q14160 CLONING ARTIFACT
SEQADV 1X5Q GLY A 110 UNP Q14160 CLONING ARTIFACT
SEQRES 1 A 110 GLY SER SER GLY SER SER GLY GLU PRO ALA ARG ILE GLU
SEQRES 2 A 110 GLU GLU GLU LEU THR LEU THR ILE LEU ARG GLN THR GLY
SEQRES 3 A 110 GLY LEU GLY ILE SER ILE ALA GLY GLY LYS GLY SER THR
SEQRES 4 A 110 PRO TYR LYS GLY ASP ASP GLU GLY ILE PHE ILE SER ARG
SEQRES 5 A 110 VAL SER GLU GLU GLY PRO ALA ALA ARG ALA GLY VAL ARG
SEQRES 6 A 110 VAL GLY ASP LYS LEU LEU GLU VAL ASN GLY VAL ALA LEU
SEQRES 7 A 110 GLN GLY ALA GLU HIS HIS GLU ALA VAL GLU ALA LEU ARG
SEQRES 8 A 110 GLY ALA GLY THR ALA VAL GLN MET ARG VAL TRP ARG GLU
SEQRES 9 A 110 SER GLY PRO SER SER GLY
HELIX 1 1 GLY A 57 GLY A 63 1 7
HELIX 2 2 GLU A 82 GLY A 92 1 11
SHEET 1 A 5 GLU A 15 LEU A 22 0
SHEET 2 A 5 ALA A 96 ARG A 103 -1 O VAL A 97 N ILE A 21
SHEET 3 A 5 LYS A 69 VAL A 73 -1 N LEU A 71 O ARG A 100
SHEET 4 A 5 ILE A 48 VAL A 53 -1 N ILE A 48 O LEU A 70
SHEET 5 A 5 ILE A 30 GLY A 34 -1 N SER A 31 O SER A 51
SHEET 1 B 4 GLU A 15 LEU A 22 0
SHEET 2 B 4 ALA A 96 ARG A 103 -1 O VAL A 97 N ILE A 21
SHEET 3 B 4 LYS A 69 VAL A 73 -1 N LEU A 71 O ARG A 100
SHEET 4 B 4 VAL A 76 ALA A 77 -1 O VAL A 76 N VAL A 73
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