Header list of 1x61.pdb file
Complete list - r 2 2 Bytes
HEADER CELL ADHESION 17-MAY-05 1X61
TITLE SOLUTION STRUCTURE OF THE FIRST LIM DOMAIN OF THYROID RECEPTOR
TITLE 2 INTERACTING PROTEIN 6 (TRIP6)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THYROID RECEPTOR INTERACTING PROTEIN 6;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: LIM DOMAIN;
COMPND 5 SYNONYM: TRIP6, OPA-INTERACTING PROTEIN 1, ZYXIN RELATED PROTEIN 1,
COMPND 6 ZRP-1;
COMPND 7 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: TRIP6, OIP1;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040830-09;
SOURCE 8 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS
KEYWDS LIM DOMAIN, THYROID RECEPTOR INTERACTING PROTEIN 6 (TRIP6), OPA-
KEYWDS 2 INTERACTING PROTEIN 1, ZYXIN RELATED PROTEIN 1 (ZRP-1), STRUCTURAL
KEYWDS 3 GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND
KEYWDS 4 FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 5 INITIATIVE, RSGI, CELL ADHESION
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 1X61 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1X61 1 VERSN
REVDAT 1 17-NOV-05 1X61 0
JRNL AUTH X.R.QIN,T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE FIRST LIM DOMAIN OF THYROID
JRNL TITL 2 RECEPTOR INTERACTING PROTEIN 6 (TRIP6)
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 2.0.17
REMARK 3 AUTHORS : VARIAN (VNMR), GUNTERT,P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1X61 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024423.
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 : 0.96MM 13C,15N-LABELED PROTEIN;
REMARK 210 20MM D-TRIS-HCL(PH7.0); 100MM
REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3,
REMARK 210 0.01MM ZNCL2
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 2.0.17
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: 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 VAL A 31 -32.70 -39.48
REMARK 500 1 PHE A 34 102.77 -54.56
REMARK 500 1 THR A 38 -67.27 -97.97
REMARK 500 1 TYR A 61 -37.71 -39.51
REMARK 500 2 VAL A 31 -32.64 -39.13
REMARK 500 2 PHE A 34 105.37 -54.84
REMARK 500 2 TYR A 61 -39.39 -38.93
REMARK 500 2 PRO A 69 2.84 -69.81
REMARK 500 3 PHE A 34 102.03 -58.61
REMARK 500 3 THR A 38 -61.94 -97.94
REMARK 500 4 PHE A 34 103.78 -59.50
REMARK 500 4 THR A 38 -69.23 -97.95
REMARK 500 5 SER A 2 170.24 -53.19
REMARK 500 5 ASP A 18 105.22 -52.06
REMARK 500 5 THR A 38 -69.16 -97.98
REMARK 500 6 VAL A 31 -32.13 -36.76
REMARK 500 6 PHE A 34 105.75 -56.05
REMARK 500 7 THR A 38 -69.14 -98.02
REMARK 500 8 PHE A 34 102.12 -58.94
REMARK 500 8 THR A 38 -63.87 -97.64
REMARK 500 9 VAL A 31 -38.78 -33.93
REMARK 500 9 PHE A 34 107.31 -53.66
REMARK 500 9 THR A 38 -68.90 -97.99
REMARK 500 10 PHE A 34 108.32 -56.68
REMARK 500 10 THR A 38 -68.01 -97.72
REMARK 500 10 ARG A 44 -39.86 -37.95
REMARK 500 10 PRO A 69 1.53 -69.71
REMARK 500 11 ASP A 18 -36.10 -36.43
REMARK 500 11 VAL A 31 -33.30 -38.51
REMARK 500 11 PHE A 34 104.40 -56.74
REMARK 500 11 THR A 38 -69.61 -97.77
REMARK 500 12 VAL A 31 -34.62 -38.18
REMARK 500 12 PHE A 34 102.88 -52.73
REMARK 500 12 THR A 38 -70.41 -97.81
REMARK 500 13 THR A 38 -68.99 -97.95
REMARK 500 13 PRO A 69 5.76 -69.78
REMARK 500 14 THR A 38 -69.48 -97.90
REMARK 500 14 PRO A 69 7.74 -69.72
REMARK 500 15 ASP A 18 102.81 -52.12
REMARK 500 15 VAL A 31 -31.69 -36.58
REMARK 500 15 THR A 38 -68.87 -97.91
REMARK 500 15 PRO A 69 10.84 -69.72
REMARK 500 16 VAL A 31 -36.57 -37.69
REMARK 500 16 PHE A 34 106.46 -59.21
REMARK 500 16 THR A 38 -69.09 -97.99
REMARK 500 16 GLU A 66 -38.54 -35.55
REMARK 500 16 PRO A 69 6.75 -69.76
REMARK 500 17 ASP A 18 102.24 -52.74
REMARK 500 17 VAL A 31 -29.64 -38.59
REMARK 500 17 PHE A 34 105.30 -59.25
REMARK 500
REMARK 500 THIS ENTRY HAS 62 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 8 SG
REMARK 620 2 CYS A 11 SG 89.4
REMARK 620 3 HIS A 30 ND1 97.0 97.4
REMARK 620 4 CYS A 33 SG 115.9 115.8 132.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 36 SG
REMARK 620 2 CYS A 39 SG 110.1
REMARK 620 3 CYS A 57 SG 115.7 96.7
REMARK 620 4 CYS A 60 SG 113.0 111.5 108.8
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSI002005302.1 RELATED DB: TARGETDB
DBREF 1X61 A 8 66 UNP Q15654 TRIP6_HUMAN 279 337
SEQADV 1X61 GLY A 1 UNP Q15654 CLONING ARTIFACT
SEQADV 1X61 SER A 2 UNP Q15654 CLONING ARTIFACT
SEQADV 1X61 SER A 3 UNP Q15654 CLONING ARTIFACT
SEQADV 1X61 GLY A 4 UNP Q15654 CLONING ARTIFACT
SEQADV 1X61 SER A 5 UNP Q15654 CLONING ARTIFACT
SEQADV 1X61 SER A 6 UNP Q15654 CLONING ARTIFACT
SEQADV 1X61 GLY A 7 UNP Q15654 CLONING ARTIFACT
SEQADV 1X61 SER A 67 UNP Q15654 CLONING ARTIFACT
SEQADV 1X61 GLY A 68 UNP Q15654 CLONING ARTIFACT
SEQADV 1X61 PRO A 69 UNP Q15654 CLONING ARTIFACT
SEQADV 1X61 SER A 70 UNP Q15654 CLONING ARTIFACT
SEQADV 1X61 SER A 71 UNP Q15654 CLONING ARTIFACT
SEQADV 1X61 GLY A 72 UNP Q15654 CLONING ARTIFACT
SEQRES 1 A 72 GLY SER SER GLY SER SER GLY CYS GLY GLY CYS GLY GLU
SEQRES 2 A 72 ASP VAL VAL GLY ASP GLY ALA GLY VAL VAL ALA LEU ASP
SEQRES 3 A 72 ARG VAL PHE HIS VAL GLY CYS PHE VAL CYS SER THR CYS
SEQRES 4 A 72 ARG ALA GLN LEU ARG GLY GLN HIS PHE TYR ALA VAL GLU
SEQRES 5 A 72 ARG ARG ALA TYR CYS GLU GLY CYS TYR VAL ALA THR LEU
SEQRES 6 A 72 GLU SER GLY PRO SER SER GLY
HET ZN A 201 1
HET ZN A 401 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 2(ZN 2+)
HELIX 1 1 GLU A 58 SER A 67 1 10
SHEET 1 A 2 VAL A 22 VAL A 23 0
SHEET 2 A 2 VAL A 28 PHE A 29 -1 O PHE A 29 N VAL A 22
SHEET 1 B 2 PHE A 48 ALA A 50 0
SHEET 2 B 2 ALA A 55 CYS A 57 -1 O TYR A 56 N TYR A 49
LINK SG CYS A 8 ZN ZN A 201 1555 1555 2.33
LINK SG CYS A 11 ZN ZN A 201 1555 1555 2.36
LINK ND1 HIS A 30 ZN ZN A 201 1555 1555 2.04
LINK SG CYS A 33 ZN ZN A 201 1555 1555 2.33
LINK SG CYS A 36 ZN ZN A 401 1555 1555 2.33
LINK SG CYS A 39 ZN ZN A 401 1555 1555 2.34
LINK SG CYS A 57 ZN ZN A 401 1555 1555 2.34
LINK SG CYS A 60 ZN ZN A 401 1555 1555 2.33
SITE 1 AC1 4 CYS A 8 CYS A 11 HIS A 30 CYS A 33
SITE 1 AC2 4 CYS A 36 CYS A 39 CYS A 57 CYS A 60
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