Header list of 1v6b.pdb file
Complete list - r 2 2 Bytes
HEADER PROTEIN BINDING 28-NOV-03 1V6B
TITLE SOLUTION STRUCTURE OF THE THIRD PDZ DOMAIN OF MOUSE HARMONIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HARMONIN ISOFORM A1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PDZ DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: RIKEN CDNA 2010016F01;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P020401-47;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS STRUCTURAL GENOMICS, USHER SYNDROME, USH1, RIKEN STRUCTURAL
KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.YAMADA,N.NAMEKI,K.SAITO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1V6B 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1V6B 1 VERSN
REVDAT 1 28-MAY-04 1V6B 0
JRNL AUTH K.YAMADA,N.NAMEKI,K.SAITO,S.KOSHIBA,M.INOUE,T.KIGAWA,
JRNL AUTH 2 S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE THIRD PDZ DOMAIN OF MOUSE HARMONIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA 1
REMARK 3 AUTHORS : GUENTART, P.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1V6B COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-DEC-03.
REMARK 100 THE DEPOSITION ID IS D_1000006260.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 20MM SODIUM PHOSPHATE BUFFER,
REMARK 210 100MM NACL, 1MM D-DTT, 0.02%
REMARK 210 NAN3, 90% H2O, 10% 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 : XWINNMR 2.6, NMRPIPE 20020425,
REMARK 210 NMRVIEW 5, CYANA 1, KUJIRA 0.706
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET 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 O GLN A 89 H ASN A 93 1.48
REMARK 500 H LYS A 26 O ASP A 97 1.51
REMARK 500 O GLU A 83 H ALA A 87 1.51
REMARK 500 O ALA A 82 H ALA A 86 1.52
REMARK 500 O MET A 69 H VAL A 76 1.52
REMARK 500 O ILE A 24 H ILE A 99 1.54
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 ALA A 6 73.78 -172.03
REMARK 500 1 THR A 7 -44.55 -172.98
REMARK 500 1 SER A 29 -177.84 63.01
REMARK 500 1 LEU A 30 -67.08 -94.86
REMARK 500 1 ASP A 31 81.56 58.33
REMARK 500 1 VAL A 38 -150.31 35.14
REMARK 500 1 LYS A 64 152.08 -45.52
REMARK 500 1 MET A 69 -46.15 -139.65
REMARK 500 1 ASN A 72 18.07 58.21
REMARK 500 1 CYS A 106 117.78 -178.54
REMARK 500 1 LYS A 109 -51.95 -133.62
REMARK 500 1 GLU A 110 111.35 66.02
REMARK 500 1 TYR A 111 95.64 -177.81
REMARK 500 1 ASP A 113 110.81 -166.29
REMARK 500 1 GLU A 114 74.09 -165.58
REMARK 500 1 LEU A 115 120.81 179.93
REMARK 500 1 PHE A 117 74.50 50.27
REMARK 500 2 ALA A 5 -164.58 -127.61
REMARK 500 2 THR A 7 -52.97 -167.75
REMARK 500 2 ALA A 15 -128.81 62.93
REMARK 500 2 VAL A 38 -149.40 34.72
REMARK 500 2 VAL A 63 -161.17 -123.78
REMARK 500 2 MET A 69 -46.32 -131.92
REMARK 500 2 LYS A 109 -52.98 -132.05
REMARK 500 2 GLU A 110 116.18 65.45
REMARK 500 2 TYR A 111 118.08 -177.86
REMARK 500 2 ASP A 112 -52.67 -160.05
REMARK 500 2 ASP A 113 91.30 45.17
REMARK 500 2 GLU A 114 87.28 -157.23
REMARK 500 2 LEU A 115 -108.32 -118.07
REMARK 500 2 PHE A 117 -39.43 -37.69
REMARK 500 3 GLU A 3 70.82 64.78
REMARK 500 3 ILE A 14 -45.26 -131.48
REMARK 500 3 ALA A 15 108.32 -39.76
REMARK 500 3 LEU A 30 -61.11 -96.95
REMARK 500 3 ASP A 31 83.90 51.68
REMARK 500 3 VAL A 38 -148.85 34.13
REMARK 500 3 VAL A 63 -164.70 -116.31
REMARK 500 3 GLU A 67 73.84 -114.91
REMARK 500 3 MET A 69 -46.89 -145.16
REMARK 500 3 ASN A 72 27.53 43.41
REMARK 500 3 ASP A 78 42.45 -94.92
REMARK 500 3 CYS A 106 117.17 179.13
REMARK 500 3 LYS A 109 6.89 83.26
REMARK 500 3 PHE A 117 73.72 58.86
REMARK 500 4 GLU A 3 -55.45 -148.70
REMARK 500 4 ALA A 5 115.57 66.92
REMARK 500 4 ALA A 6 -46.58 -179.37
REMARK 500 4 LEU A 30 -63.30 -104.37
REMARK 500 4 ASP A 31 84.06 52.36
REMARK 500
REMARK 500 THIS ENTRY HAS 315 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MMK002000001.1 RELATED DB: TARGETDB
DBREF 1V6B A 8 118 UNP Q9ES64 USH1C_MOUSE 438 548
SEQADV 1V6B GLY A 1 UNP Q9ES64 CLONING ARTIFACT
SEQADV 1V6B SER A 2 UNP Q9ES64 CLONING ARTIFACT
SEQADV 1V6B GLU A 3 UNP Q9ES64 CLONING ARTIFACT
SEQADV 1V6B GLY A 4 UNP Q9ES64 CLONING ARTIFACT
SEQADV 1V6B ALA A 5 UNP Q9ES64 CLONING ARTIFACT
SEQADV 1V6B ALA A 6 UNP Q9ES64 CLONING ARTIFACT
SEQADV 1V6B THR A 7 UNP Q9ES64 CLONING ARTIFACT
SEQRES 1 A 118 GLY SER GLU GLY ALA ALA THR MET PHE SER PRO GLU GLN
SEQRES 2 A 118 ILE ALA GLY LYS ASP VAL ARG LEU LEU ARG ILE LYS LYS
SEQRES 3 A 118 GLU GLY SER LEU ASP LEU ALA LEU GLU GLY GLY VAL ASP
SEQRES 4 A 118 SER PRO VAL GLY LYS VAL VAL VAL SER ALA VAL TYR GLU
SEQRES 5 A 118 GLY GLY ALA ALA GLU ARG HIS GLY GLY VAL VAL LYS GLY
SEQRES 6 A 118 ASP GLU ILE MET ALA ILE ASN GLY LYS ILE VAL THR ASP
SEQRES 7 A 118 TYR THR LEU ALA GLU ALA GLU ALA ALA LEU GLN LYS ALA
SEQRES 8 A 118 TRP ASN GLN GLY GLY ASP TRP ILE ASP LEU VAL VAL ALA
SEQRES 9 A 118 VAL CYS PRO PRO LYS GLU TYR ASP ASP GLU LEU THR PHE
SEQRES 10 A 118 PHE
HELIX 1 1 SER A 10 ALA A 15 1 6
HELIX 2 2 GLY A 54 GLY A 60 1 7
HELIX 3 3 THR A 80 GLY A 95 1 16
SHEET 1 A 3 VAL A 19 LYS A 25 0
SHEET 2 A 3 TRP A 98 ALA A 104 -1 O ILE A 99 N ILE A 24
SHEET 3 A 3 GLU A 67 ILE A 71 -1 N GLU A 67 O ALA A 104
SHEET 1 B 2 ALA A 33 GLY A 36 0
SHEET 2 B 2 VAL A 45 ALA A 49 -1 O SER A 48 N ALA A 33
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