Header list of 1v87.pdb file
Complete list - r 2 2 Bytes
HEADER METAL BINDING PROTEIN 29-DEC-03 1V87
TITLE SOLUTION STRUCTURE OF THE RING-H2 FINGER DOMAIN OF MOUSE DELTEX
TITLE 2 PROTEIN 2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DELTEX PROTEIN 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RING-H2 FINGER DOMAIN;
COMPND 5 SYNONYM: DELTEX-2, DELTEX2, MDTX2;
COMPND 6 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 2610524D08;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P030421-37;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS RING-H2 DOMAIN, ZINC-BINDING DOMAIN, NOTCH SIGNALING, STRUCTURAL
KEYWDS 2 GENOMICS, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI,
KEYWDS 3 METAL BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.MIYAMOTO,Y.MUTO,N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,
AUTHOR 2 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1V87 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1V87 1 VERSN
REVDAT 1 29-JUN-04 1V87 0
JRNL AUTH K.MIYAMOTO,Y.MUTO,N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,
JRNL AUTH 2 S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE RING-H2 FINGER DOMAIN OF MOUSE
JRNL TITL 2 DELTEX PROTEIN 2
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, CYANA 2.0.17
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1V87 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-JAN-04.
REMARK 100 THE DEPOSITION ID IS D_1000006328.
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 : 1.05MM RING-H2 DOMAIN U-13C,
REMARK 210 15N; 20MM D-TRIS-HCL(PH7.0);
REMARK 210 100MM NACL; 1MM D-DTT; 0.02%
REMARK 210 NAN3; 0.1MM ZNCL; 90% H2O, 10%D2O
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 0.880, 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 : 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: 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 PRO A 24 -166.28 -69.80
REMARK 500 1 GLU A 25 33.35 -98.39
REMARK 500 1 SER A 42 -36.26 -36.40
REMARK 500 1 LEU A 58 175.88 -58.32
REMARK 500 1 LYS A 60 -73.63 -95.09
REMARK 500 1 HIS A 66 101.01 -50.36
REMARK 500 1 LEU A 67 -33.09 -36.18
REMARK 500 1 ASN A 78 80.41 -69.55
REMARK 500 1 PRO A 86 7.63 -69.72
REMARK 500 1 SER A 87 -69.30 -106.85
REMARK 500 1 GLU A 94 -76.01 -32.58
REMARK 500 1 THR A 98 163.36 -41.39
REMARK 500 2 GLU A 8 150.23 -42.76
REMARK 500 2 GLU A 25 32.49 -92.25
REMARK 500 2 ALA A 38 176.00 -57.09
REMARK 500 2 SER A 42 -27.63 -38.72
REMARK 500 2 LYS A 60 -71.35 -100.52
REMARK 500 2 HIS A 66 102.44 -56.47
REMARK 500 2 LEU A 67 -27.84 -37.26
REMARK 500 2 PRO A 86 2.37 -69.78
REMARK 500 2 GLU A 94 133.61 -175.21
REMARK 500 2 THR A 98 142.03 -175.07
REMARK 500 2 LYS A 103 41.73 -89.87
REMARK 500 2 SER A 113 118.28 -172.62
REMARK 500 3 GLU A 19 139.11 -38.13
REMARK 500 3 LYS A 21 -39.35 -39.23
REMARK 500 3 PRO A 24 -165.10 -69.77
REMARK 500 3 ALA A 38 170.56 -58.39
REMARK 500 3 ASP A 46 40.23 -99.04
REMARK 500 3 LYS A 60 -59.82 -124.11
REMARK 500 3 HIS A 66 103.63 -49.35
REMARK 500 3 LEU A 67 -27.17 -38.55
REMARK 500 3 LYS A 79 68.51 -69.58
REMARK 500 3 PRO A 86 3.92 -69.72
REMARK 500 3 LYS A 89 45.52 35.88
REMARK 500 3 LYS A 95 -60.45 -124.40
REMARK 500 3 LYS A 103 118.18 -168.55
REMARK 500 3 SER A 109 42.06 -107.75
REMARK 500 3 SER A 113 -59.08 -122.21
REMARK 500 4 LYS A 21 -37.13 -37.30
REMARK 500 4 ALA A 23 130.54 -37.14
REMARK 500 4 PRO A 24 -179.07 -69.80
REMARK 500 4 GLU A 25 33.80 -88.75
REMARK 500 4 ALA A 38 -179.47 -62.70
REMARK 500 4 ASP A 46 33.28 -95.32
REMARK 500 4 LEU A 58 173.88 -51.11
REMARK 500 4 LYS A 60 -62.45 -90.24
REMARK 500 4 HIS A 66 104.44 -51.06
REMARK 500 4 LEU A 67 -26.39 -39.86
REMARK 500 4 PRO A 86 3.06 -69.70
REMARK 500
REMARK 500 THIS ENTRY HAS 257 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 28 SG
REMARK 620 2 CYS A 31 SG 93.5
REMARK 620 3 HIS A 66 ND1 91.2 111.0
REMARK 620 4 CYS A 69 SG 119.3 117.3 119.2
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 61 SG
REMARK 620 2 HIS A 63 ND1 96.0
REMARK 620 3 CYS A 85 SG 115.1 118.9
REMARK 620 4 CYS A 88 SG 87.0 119.3 113.8
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: MMT007011434.1 RELATED DB: TARGETDB
DBREF 1V87 A 8 108 UNP Q8R3P2 DTX2_MOUSE 389 489
SEQADV 1V87 GLY A 1 UNP Q8R3P2 CLONING ARTIFACT
SEQADV 1V87 SER A 2 UNP Q8R3P2 CLONING ARTIFACT
SEQADV 1V87 SER A 3 UNP Q8R3P2 CLONING ARTIFACT
SEQADV 1V87 GLY A 4 UNP Q8R3P2 CLONING ARTIFACT
SEQADV 1V87 SER A 5 UNP Q8R3P2 CLONING ARTIFACT
SEQADV 1V87 SER A 6 UNP Q8R3P2 CLONING ARTIFACT
SEQADV 1V87 GLY A 7 UNP Q8R3P2 CLONING ARTIFACT
SEQADV 1V87 SER A 109 UNP Q8R3P2 CLONING ARTIFACT
SEQADV 1V87 GLY A 110 UNP Q8R3P2 CLONING ARTIFACT
SEQADV 1V87 PRO A 111 UNP Q8R3P2 CLONING ARTIFACT
SEQADV 1V87 SER A 112 UNP Q8R3P2 CLONING ARTIFACT
SEQADV 1V87 SER A 113 UNP Q8R3P2 CLONING ARTIFACT
SEQADV 1V87 GLY A 114 UNP Q8R3P2 CLONING ARTIFACT
SEQRES 1 A 114 GLY SER SER GLY SER SER GLY GLU PRO GLU GLN VAL ILE
SEQRES 2 A 114 ARG LYS TYR THR GLU GLU LEU LYS VAL ALA PRO GLU GLU
SEQRES 3 A 114 ASP CYS ILE ILE CYS MET GLU LYS LEU ALA VAL ALA SER
SEQRES 4 A 114 GLY TYR SER ASP MET THR ASP SER LYS ALA LEU GLY PRO
SEQRES 5 A 114 MET VAL VAL GLY ARG LEU THR LYS CYS SER HIS ALA PHE
SEQRES 6 A 114 HIS LEU LEU CYS LEU LEU ALA MET TYR CYS ASN GLY ASN
SEQRES 7 A 114 LYS ASP GLY SER LEU GLN CYS PRO SER CYS LYS THR ILE
SEQRES 8 A 114 TYR GLY GLU LYS THR GLY THR GLN PRO TRP GLY LYS MET
SEQRES 9 A 114 GLU VAL PHE ARG 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 PRO A 9 TYR A 16 1 8
HELIX 2 2 LEU A 67 ASN A 76 1 10
HELIX 3 3 TYR A 41 THR A 45 1 5
SHEET 1 A 3 THR A 17 GLU A 19 0
SHEET 2 A 3 GLY A 56 LEU A 58 -1 O ARG A 57 N GLU A 18
SHEET 3 A 3 ALA A 64 PHE A 65 -1 O PHE A 65 N GLY A 56
SHEET 1 B 2 ASP A 27 CYS A 28 0
SHEET 2 B 2 GLU A 33 LYS A 34 -1 O GLU A 33 N CYS A 28
LINK SG CYS A 28 ZN ZN A 201 1555 1555 2.33
LINK SG CYS A 31 ZN ZN A 201 1555 1555 2.33
LINK SG CYS A 61 ZN ZN A 401 1555 1555 2.32
LINK ND1 HIS A 63 ZN ZN A 401 1555 1555 2.32
LINK ND1 HIS A 66 ZN ZN A 201 1555 1555 2.33
LINK SG CYS A 69 ZN ZN A 201 1555 1555 2.32
LINK SG CYS A 85 ZN ZN A 401 1555 1555 2.33
LINK SG CYS A 88 ZN ZN A 401 1555 1555 2.32
SITE 1 AC1 4 CYS A 28 CYS A 31 HIS A 66 CYS A 69
SITE 1 AC2 4 CYS A 61 HIS A 63 CYS A 85 CYS A 88
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