Header list of 1x5r.pdb file
Complete list - r 2 2 Bytes
HEADER SIGNALING PROTEIN 16-MAY-05 1X5R
TITLE SOLUTION STRUCTURE OF THE FOURTH PDZ DOMAIN OF GLUTAMATE RECEPTOR
TITLE 2 INTERACTING PROTEIN 2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAMATE RECEPTOR INTERACTING PROTEIN 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PDZ DOMAIN;
COMPND 5 SYNONYM: GRIP2 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 PF00330S1;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040705-16;
SOURCE 8 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS
KEYWDS PDZ DOMAIN; GLUTAMATE RECEPTOR INTERACTING PROTEIN 2, GRIP2 PROTEIN,
KEYWDS 2 STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL
KEYWDS 3 AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 4 INITIATIVE, RSGI, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR X.R.QIN,F.HAYASHI,S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS
AUTHOR 2 INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1X5R 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1X5R 1 VERSN
REVDAT 1 16-NOV-05 1X5R 0
JRNL AUTH X.R.QIN,F.HAYASHI,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE FOURTH PDZ DOMAIN OF GLUTAMATE
JRNL TITL 2 RECEPTOR INTERACTING PROTEIN 2
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 1X5R 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_1000024413.
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 : 0.95MM 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 O GLU A 84 H GLN A 88 1.53
REMARK 500 O GLU A 85 H LEU A 89 1.58
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 PHE A 29 -88.07 -123.90
REMARK 500 1 THR A 40 77.81 -68.31
REMARK 500 1 GLU A 41 137.11 -178.93
REMARK 500 1 ASP A 68 170.93 -46.62
REMARK 500 1 PHE A 105 163.29 178.44
REMARK 500 1 SER A 107 100.08 -53.72
REMARK 500 2 SER A 2 -58.59 -157.83
REMARK 500 2 ILE A 11 126.99 65.63
REMARK 500 2 VAL A 12 106.03 58.85
REMARK 500 2 HIS A 13 106.49 -175.16
REMARK 500 2 THR A 14 157.60 -49.04
REMARK 500 2 THR A 40 -167.86 -67.14
REMARK 500 2 GLU A 41 127.83 67.71
REMARK 500 2 ASP A 68 166.20 -45.12
REMARK 500 2 ASP A 80 40.33 -100.91
REMARK 500 2 SER A 107 89.56 62.23
REMARK 500 2 SER A 111 147.05 63.28
REMARK 500 3 SER A 6 103.89 -40.26
REMARK 500 3 HIS A 13 -177.74 49.98
REMARK 500 3 THR A 14 177.09 -50.49
REMARK 500 3 PHE A 29 -89.53 -134.44
REMARK 500 3 ILE A 37 156.13 59.01
REMARK 500 3 PHE A 38 150.41 -43.28
REMARK 500 3 GLU A 41 137.28 166.74
REMARK 500 3 THR A 42 151.12 -42.88
REMARK 500 3 SER A 110 78.07 43.09
REMARK 500 4 SER A 5 160.85 66.00
REMARK 500 4 PHE A 29 -90.16 -103.33
REMARK 500 4 ILE A 37 -39.69 -39.48
REMARK 500 4 THR A 40 91.38 -67.26
REMARK 500 4 GLU A 41 145.13 166.12
REMARK 500 4 ASP A 68 150.68 -41.66
REMARK 500 4 SER A 107 105.20 57.91
REMARK 500 5 SER A 5 129.88 62.61
REMARK 500 5 SER A 6 131.30 -176.20
REMARK 500 5 PHE A 29 -85.72 -127.06
REMARK 500 5 THR A 40 -168.43 -70.57
REMARK 500 5 GLU A 41 108.91 67.18
REMARK 500 5 THR A 42 158.79 -39.10
REMARK 500 5 SER A 107 101.83 -58.40
REMARK 500 6 SER A 5 111.67 -176.10
REMARK 500 6 HIS A 13 -55.23 -125.47
REMARK 500 6 GLU A 41 136.36 174.48
REMARK 500 6 VAL A 49 82.20 -65.93
REMARK 500 6 ARG A 91 -70.45 -55.96
REMARK 500 6 SER A 111 84.73 53.47
REMARK 500 7 GLN A 10 82.32 48.04
REMARK 500 7 HIS A 13 119.24 78.90
REMARK 500 7 THR A 14 165.91 61.08
REMARK 500 7 PHE A 29 -90.62 -117.92
REMARK 500
REMARK 500 THIS ENTRY HAS 172 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK002101691.2 RELATED DB: TARGETDB
DBREF 1X5R A 8 106 UNP Q9C0E4 GRIP2_HUMAN 446 544
SEQADV 1X5R GLY A 1 UNP Q9C0E4 CLONING ARTIFACT
SEQADV 1X5R SER A 2 UNP Q9C0E4 CLONING ARTIFACT
SEQADV 1X5R SER A 3 UNP Q9C0E4 CLONING ARTIFACT
SEQADV 1X5R GLY A 4 UNP Q9C0E4 CLONING ARTIFACT
SEQADV 1X5R SER A 5 UNP Q9C0E4 CLONING ARTIFACT
SEQADV 1X5R SER A 6 UNP Q9C0E4 CLONING ARTIFACT
SEQADV 1X5R GLY A 7 UNP Q9C0E4 CLONING ARTIFACT
SEQADV 1X5R SER A 107 UNP Q9C0E4 CLONING ARTIFACT
SEQADV 1X5R GLY A 108 UNP Q9C0E4 CLONING ARTIFACT
SEQADV 1X5R PRO A 109 UNP Q9C0E4 CLONING ARTIFACT
SEQADV 1X5R SER A 110 UNP Q9C0E4 CLONING ARTIFACT
SEQADV 1X5R SER A 111 UNP Q9C0E4 CLONING ARTIFACT
SEQADV 1X5R GLY A 112 UNP Q9C0E4 CLONING ARTIFACT
SEQRES 1 A 112 GLY SER SER GLY SER SER GLY GLY GLY GLN ILE VAL HIS
SEQRES 2 A 112 THR GLU THR THR GLU VAL VAL LEU CYS GLY ASP PRO LEU
SEQRES 3 A 112 SER GLY PHE GLY LEU GLN LEU GLN GLY GLY ILE PHE ALA
SEQRES 4 A 112 THR GLU THR LEU SER SER PRO PRO LEU VAL CYS PHE ILE
SEQRES 5 A 112 GLU PRO ASP SER PRO ALA GLU ARG CYS GLY LEU LEU GLN
SEQRES 6 A 112 VAL GLY ASP ARG VAL LEU SER ILE ASN GLY ILE ALA THR
SEQRES 7 A 112 GLU ASP GLY THR MET GLU GLU ALA ASN GLN LEU LEU ARG
SEQRES 8 A 112 ASP ALA ALA LEU ALA HIS LYS VAL VAL LEU GLU VAL GLU
SEQRES 9 A 112 PHE ASP SER GLY PRO SER SER GLY
HELIX 1 1 SER A 56 CYS A 61 1 6
HELIX 2 2 THR A 82 LEU A 95 1 14
SHEET 1 A 2 GLU A 15 LEU A 21 0
SHEET 2 A 2 VAL A 99 PHE A 105 -1 O PHE A 105 N GLU A 15
SHEET 1 B 2 LEU A 31 GLN A 34 0
SHEET 2 B 2 LEU A 48 ILE A 52 -1 O PHE A 51 N GLN A 32
SHEET 1 C 2 SER A 72 ILE A 73 0
SHEET 2 C 2 ILE A 76 ALA A 77 -1 O ILE A 76 N ILE 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