Header list of 1wii.pdb file
Complete list - c 21 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 28-MAY-04 1WII
TITLE SOLUTION STRUCTURE OF RSGI RUH-025, A DUF701 DOMAIN FROM MOUSE CDNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL UPF0222 PROTEIN MGC4549;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DUF701;
COMPND 5 SYNONYM: HYPOTHETICAL PROTEIN RIKEN CDNA 3110032N15;
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 3110032N15;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040216-94;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS SYSTEM
KEYWDS DOMAIN OF UNKNOWN FUNCTION, ZINC FINGER, METAL-BINDING PROTEIN,
KEYWDS 2 STRUCTURAL GENOMICS, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 3 INITIATIVE, RSGI, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.ABE,H.HIROTA,H.HAYASHI,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 4 21-DEC-22 1WII 1 SEQADV
REVDAT 3 02-MAR-22 1WII 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1WII 1 VERSN
REVDAT 1 28-NOV-04 1WII 0
JRNL AUTH T.ABE,H.HIROTA,H.HAYASHI,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF RSGI RUH-025, A DUF701 DOMAIN FROM
JRNL TITL 2 MOUSE CDNA
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 1WII COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000023617.
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 : 100MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.20MM RSGI RUH-025 U-15N, 13C;
REMARK 210 20MM D-TRIS-HCL BUFFER; 100MM
REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3;
REMARK 210 0.01MM ZNCL2; 10% D20
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 : 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 0.896
REMARK 210 METHOD USED : SIMULATED ANNEALING, TORSION
REMARK 210 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: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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 SER A 3 155.78 174.46
REMARK 500 1 SER A 5 152.22 64.24
REMARK 500 1 SER A 6 -48.83 -157.42
REMARK 500 1 ARG A 8 131.36 61.48
REMARK 500 1 LYS A 9 96.21 -162.04
REMARK 500 1 LEU A 20 35.97 71.80
REMARK 500 1 THR A 22 24.17 41.05
REMARK 500 1 ASN A 30 79.05 63.00
REMARK 500 1 GLU A 32 -177.07 59.01
REMARK 500 1 LYS A 33 92.00 -34.05
REMARK 500 1 SER A 34 44.84 -153.02
REMARK 500 1 VAL A 52 -44.24 -150.45
REMARK 500 1 LEU A 54 60.01 66.37
REMARK 500 1 SER A 65 163.73 -46.25
REMARK 500 1 SER A 80 83.40 173.86
REMARK 500 2 SER A 2 -48.54 179.00
REMARK 500 2 SER A 3 140.68 -35.87
REMARK 500 2 LYS A 9 -65.61 -172.65
REMARK 500 2 LYS A 14 -59.28 -122.28
REMARK 500 2 LYS A 15 -63.02 74.18
REMARK 500 2 THR A 22 43.97 -104.25
REMARK 500 2 ASN A 30 83.00 77.75
REMARK 500 2 GLU A 32 110.25 -33.07
REMARK 500 2 LYS A 33 87.87 63.01
REMARK 500 2 SER A 34 42.29 -165.09
REMARK 500 2 VAL A 52 -50.25 -145.99
REMARK 500 2 SER A 65 157.89 -42.73
REMARK 500 2 SER A 83 36.45 71.85
REMARK 500 3 PRO A 12 -175.38 -69.79
REMARK 500 3 LYS A 15 113.51 -167.12
REMARK 500 3 MET A 16 140.10 -173.51
REMARK 500 3 LEU A 20 80.04 67.71
REMARK 500 3 THR A 22 40.64 -96.23
REMARK 500 3 ASN A 30 92.40 71.66
REMARK 500 3 GLU A 32 80.71 53.42
REMARK 500 3 LYS A 33 90.51 63.97
REMARK 500 3 SER A 34 43.00 -153.33
REMARK 500 3 VAL A 52 -52.86 -138.47
REMARK 500 3 TYR A 63 -34.54 -38.97
REMARK 500 3 SER A 65 152.65 -36.97
REMARK 500 3 GLU A 79 -28.85 -39.84
REMARK 500 3 SER A 83 81.77 -64.46
REMARK 500 3 SER A 84 36.86 -94.20
REMARK 500 4 SER A 2 140.74 -173.02
REMARK 500 4 THR A 19 142.50 60.37
REMARK 500 4 ASN A 30 91.00 72.31
REMARK 500 4 GLU A 32 97.67 62.02
REMARK 500 4 LYS A 33 93.42 41.98
REMARK 500 4 SER A 34 48.62 -153.93
REMARK 500 4 VAL A 52 -51.36 -142.04
REMARK 500
REMARK 500 THIS ENTRY HAS 264 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 26 SG
REMARK 620 2 CYS A 29 SG 111.6
REMARK 620 3 CYS A 50 SG 99.2 100.2
REMARK 620 4 CYS A 53 SG 118.6 120.4 101.4
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 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MMT007016237.1 RELATED DB: TARGETDB
DBREF 1WII A 8 79 UNP P60003 ELOF1_MOUSE 8 79
SEQADV 1WII GLY A 1 UNP P60003 CLONING ARTIFACT
SEQADV 1WII SER A 2 UNP P60003 CLONING ARTIFACT
SEQADV 1WII SER A 3 UNP P60003 CLONING ARTIFACT
SEQADV 1WII GLY A 4 UNP P60003 CLONING ARTIFACT
SEQADV 1WII SER A 5 UNP P60003 CLONING ARTIFACT
SEQADV 1WII SER A 6 UNP P60003 CLONING ARTIFACT
SEQADV 1WII GLY A 7 UNP P60003 CLONING ARTIFACT
SEQADV 1WII SER A 80 UNP P60003 CLONING ARTIFACT
SEQADV 1WII GLY A 81 UNP P60003 CLONING ARTIFACT
SEQADV 1WII PRO A 82 UNP P60003 CLONING ARTIFACT
SEQADV 1WII SER A 83 UNP P60003 CLONING ARTIFACT
SEQADV 1WII SER A 84 UNP P60003 CLONING ARTIFACT
SEQADV 1WII GLY A 85 UNP P60003 CLONING ARTIFACT
SEQRES 1 A 85 GLY SER SER GLY SER SER GLY ARG LYS PRO PRO PRO LYS
SEQRES 2 A 85 LYS LYS MET THR GLY THR LEU GLU THR GLN PHE THR CYS
SEQRES 3 A 85 PRO PHE CYS ASN HIS GLU LYS SER CYS ASP VAL LYS MET
SEQRES 4 A 85 ASP ARG ALA ARG ASN THR GLY VAL ILE SER CYS THR VAL
SEQRES 5 A 85 CYS LEU GLU GLU PHE GLN THR PRO ILE THR TYR LEU SER
SEQRES 6 A 85 GLU PRO VAL ASP VAL TYR SER ASP TRP ILE ASP ALA CYS
SEQRES 7 A 85 GLU SER GLY PRO SER SER GLY
HET ZN A 201 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 1 VAL A 68 GLY A 81 1 14
SHEET 1 A 3 CYS A 35 ASP A 40 0
SHEET 2 A 3 THR A 45 CYS A 50 -1 O VAL A 47 N LYS A 38
SHEET 3 A 3 GLU A 56 PRO A 60 -1 O PHE A 57 N ILE A 48
LINK SG CYS A 26 ZN ZN A 201 1555 1555 2.34
LINK SG CYS A 29 ZN ZN A 201 1555 1555 2.29
LINK SG CYS A 50 ZN ZN A 201 1555 1555 2.33
LINK SG CYS A 53 ZN ZN A 201 1555 1555 2.27
SITE 1 AC1 4 CYS A 26 CYS A 29 CYS A 50 CYS A 53
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 - c 21 2 Bytes