Header list of 1wi0.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSFERASE 28-MAY-04 1WI0
TITLE SOLUTION STRUCTURE OF THE PB1 DOMAIN OF MOUSE MITOGEN ACTIVATED
TITLE 2 PROTEIN KINASE KINASE 5 (MAP2K5)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MITOGEN ACTIVATED PROTEIN KINASE KINASE 5;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PB1 DOMAIN;
COMPND 5 SYNONYM: MAP2K5;
COMPND 6 EC: 2.7.1.-;
COMPND 7 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 A230106F01;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P031125-28;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS PB1 DOMAIN, PROTEIN-PROTEIN INTERACTION SITE, CYTOPLASMIC SIGNALLING,
KEYWDS 2 STRUCTURAL GENOMICS, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 3 INITIATIVE, RSGI, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.YONEYAMA,F.HAYASHI,N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,
AUTHOR 2 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 4 02-MAR-22 1WI0 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1WI0 1 VERSN
REVDAT 2 17-JAN-06 1WI0 1 TITLE JRNL
REVDAT 1 28-NOV-04 1WI0 0
JRNL AUTH M.YONEYAMA,F.HAYASHI,N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,
JRNL AUTH 2 S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE PB1 DOMAIN OF MOUSE MITOGEN
JRNL TITL 2 ACTIVATED PROTEIN KINASE KINASE 5 (MAP2K5)
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 1.0.8
REMARK 3 AUTHORS : VARIAN (VNMR), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WI0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000023599.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 297
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM PB1 DOMAIN U-15N, 13C; 20MM
REMARK 210 D-TRIS-HCL; 100MM NACL; 1MM D-
REMARK 210 DTT; 0.02% NAN3; 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 : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW 5.0.4, KUJIRA 0.896,
REMARK 210 CYANA 1.0.8, NMRPIPE 20020425
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, 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: 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 TYR A 85 H VAL A 89 1.53
REMARK 500 O VAL A 47 H GLN A 50 1.55
REMARK 500 H ARG A 73 OE1 GLU A 77 1.56
REMARK 500 O ARG A 42 H ASP A 46 1.59
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 SER A 6 75.54 52.68
REMARK 500 1 PHE A 9 -50.73 -136.07
REMARK 500 1 CYS A 10 100.93 68.81
REMARK 500 1 MET A 12 127.60 -175.12
REMARK 500 1 GLN A 15 161.96 -44.65
REMARK 500 1 SER A 26 36.40 -177.84
REMARK 500 1 SER A 35 51.08 -91.14
REMARK 500 1 THR A 56 173.40 -54.37
REMARK 500 1 THR A 57 -74.24 -145.98
REMARK 500 1 THR A 58 -55.71 75.39
REMARK 500 1 ASP A 64 -152.37 -97.94
REMARK 500 1 ARG A 69 100.60 55.19
REMARK 500 1 GLN A 97 152.68 -40.62
REMARK 500 1 LEU A 102 85.54 -58.41
REMARK 500 1 ARG A 107 89.08 -55.34
REMARK 500 1 SER A 112 81.08 178.74
REMARK 500 2 SER A 2 -57.74 -151.32
REMARK 500 2 SER A 3 154.28 62.55
REMARK 500 2 SER A 6 -57.21 -129.84
REMARK 500 2 CYS A 10 142.21 -179.92
REMARK 500 2 ALA A 11 174.06 54.49
REMARK 500 2 MET A 12 -54.12 -123.86
REMARK 500 2 ASN A 14 -46.59 -133.68
REMARK 500 2 ASN A 25 70.81 40.25
REMARK 500 2 SER A 26 -42.46 -168.18
REMARK 500 2 ALA A 28 144.19 -175.36
REMARK 500 2 SER A 35 46.81 -98.62
REMARK 500 2 GLN A 38 46.71 -85.41
REMARK 500 2 THR A 56 173.44 -51.47
REMARK 500 2 ASP A 64 -154.97 -86.31
REMARK 500 2 ARG A 69 98.17 54.57
REMARK 500 2 GLN A 97 152.07 -39.29
REMARK 500 2 LEU A 102 84.81 -59.42
REMARK 500 2 SER A 111 112.11 -178.66
REMARK 500 2 SER A 112 112.19 60.57
REMARK 500 3 SER A 5 -58.42 -125.65
REMARK 500 3 GLU A 13 84.67 -178.10
REMARK 500 3 ASN A 14 88.12 50.15
REMARK 500 3 VAL A 16 -169.96 45.02
REMARK 500 3 ASN A 25 74.99 39.31
REMARK 500 3 SER A 26 -40.08 -174.46
REMARK 500 3 SER A 35 45.61 -90.59
REMARK 500 3 GLN A 38 43.33 -93.28
REMARK 500 3 ARG A 69 105.10 56.27
REMARK 500 3 GLN A 97 151.37 -39.70
REMARK 500 3 LEU A 102 83.17 -60.86
REMARK 500 3 SER A 111 128.73 63.05
REMARK 500 4 ASN A 14 -50.77 -159.68
REMARK 500 4 ASN A 25 71.99 41.63
REMARK 500 4 SER A 26 -42.37 -170.57
REMARK 500
REMARK 500 THIS ENTRY HAS 307 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MMT007017439.1 RELATED DB: TARGETDB
DBREF 1WI0 A 8 107 UNP Q9WVS7 MP2K5_MOUSE 8 107
SEQADV 1WI0 GLY A 1 UNP Q9WVS7 CLONING ARTIFACT
SEQADV 1WI0 SER A 2 UNP Q9WVS7 CLONING ARTIFACT
SEQADV 1WI0 SER A 3 UNP Q9WVS7 CLONING ARTIFACT
SEQADV 1WI0 GLY A 4 UNP Q9WVS7 CLONING ARTIFACT
SEQADV 1WI0 SER A 5 UNP Q9WVS7 CLONING ARTIFACT
SEQADV 1WI0 SER A 6 UNP Q9WVS7 CLONING ARTIFACT
SEQADV 1WI0 GLY A 7 UNP Q9WVS7 CLONING ARTIFACT
SEQADV 1WI0 SER A 108 UNP Q9WVS7 CLONING ARTIFACT
SEQADV 1WI0 GLY A 109 UNP Q9WVS7 CLONING ARTIFACT
SEQADV 1WI0 PRO A 110 UNP Q9WVS7 CLONING ARTIFACT
SEQADV 1WI0 SER A 111 UNP Q9WVS7 CLONING ARTIFACT
SEQADV 1WI0 SER A 112 UNP Q9WVS7 CLONING ARTIFACT
SEQADV 1WI0 GLY A 113 UNP Q9WVS7 CLONING ARTIFACT
SEQRES 1 A 113 GLY SER SER GLY SER SER GLY PRO PHE CYS ALA MET GLU
SEQRES 2 A 113 ASN GLN VAL LEU VAL ILE ARG ILE LYS ILE PRO ASN SER
SEQRES 3 A 113 GLY ALA VAL ASP TRP THR VAL HIS SER GLY PRO GLN LEU
SEQRES 4 A 113 LEU PHE ARG ASP VAL LEU ASP VAL ILE GLY GLN VAL LEU
SEQRES 5 A 113 PRO GLU ALA THR THR THR ALA PHE GLU TYR GLU ASP GLU
SEQRES 6 A 113 ASP GLY ASP ARG ILE THR VAL ARG SER ASP GLU GLU MET
SEQRES 7 A 113 LYS ALA MET LEU SER TYR TYR TYR SER THR VAL MET GLU
SEQRES 8 A 113 GLN GLN VAL ASN GLY GLN LEU ILE GLU PRO LEU GLN ILE
SEQRES 9 A 113 PHE PRO ARG SER GLY PRO SER SER GLY
HELIX 1 1 LEU A 40 LEU A 52 1 13
HELIX 2 2 SER A 74 GLY A 96 1 23
SHEET 1 A 5 ALA A 28 VAL A 33 0
SHEET 2 A 5 LEU A 17 LYS A 22 -1 N LEU A 17 O VAL A 33
SHEET 3 A 5 LEU A 102 PRO A 106 1 O ILE A 104 N LYS A 22
SHEET 4 A 5 PHE A 60 TYR A 62 -1 N GLU A 61 O PHE A 105
SHEET 5 A 5 ILE A 70 VAL A 72 -1 O VAL A 72 N PHE 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