Header list of 1wjw.pdb file
Complete list - r 2 2 Bytes
HEADER ISOMERASE 29-MAY-04 1WJW
TITLE SOLUTION STRUCTURE OF THE C-TERMINAL DOMAIN OF MOUSE
TITLE 2 PHOSPHOACETYLGLUCOSAMINE MUTASE (PAGM)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHOACETYLGLUCOSAMINE MUTASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN;
COMPND 5 SYNONYM: PAGM, ACETYLGLUCOSAMINE PHOSPHOMUTASE, N-ACETYLGLUCOSAMINE-
COMPND 6 PHOSPHATE MUTASE, PHOSPHOGLUCOMUTASE 3;
COMPND 7 EC: 5.4.2.3;
COMPND 8 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 2810473H05;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040113-52;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS PHOSPHOACETYLGLUCOSAMINE MUTASE(PAGM), CARBOHYDRATE METABOLISM,
KEYWDS 2 STRUCTURAL GENOMICS, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 3 INITIATIVE, RSGI, ISOMERASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.YONEYAMA,N.TOCHIO,K.SAITO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,
AUTHOR 2 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 4 02-MAR-22 1WJW 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1WJW 1 VERSN
REVDAT 2 17-JAN-06 1WJW 1 TITLE JRNL
REVDAT 1 29-NOV-04 1WJW 0
JRNL AUTH M.YONEYAMA,N.TOCHIO,K.SAITO,S.KOSHIBA,M.INOUE,T.KIGAWA,
JRNL AUTH 2 S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE C-TERMINAL DOMAIN OF MOUSE
JRNL TITL 2 PHOSPHOACETYLGLUCOSAMINE MUTASE (PAGM)
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 1.0.8
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WJW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000023656.
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 : 320MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM C-TERMINAL DOMAIN OF
REMARK 210 PHOSPHOACETYLGLUCOSAMINE
REMARK 210 MUTASE(PAGM) U-15N, 13C; 20MM
REMARK 210 PHOSPHATE BUFFER NA; 300MM NACL;
REMARK 210 1MM D-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 : 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 0.896, CYANA 1.0.8
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 GLU A 88 H LEU A 92 1.57
REMARK 500 O GLY A 42 H ALA A 46 1.57
REMARK 500 O LEU A 85 H VAL A 89 1.60
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 VAL A 11 122.18 -178.51
REMARK 500 1 LEU A 13 158.72 -44.85
REMARK 500 1 LYS A 21 74.97 -66.77
REMARK 500 1 ASP A 24 -163.08 174.44
REMARK 500 1 ARG A 26 -166.62 56.16
REMARK 500 1 VAL A 27 -66.25 72.24
REMARK 500 1 THR A 31 44.49 -157.99
REMARK 500 1 ALA A 33 152.26 61.73
REMARK 500 1 GLU A 34 53.19 -152.01
REMARK 500 1 GLN A 36 96.87 65.21
REMARK 500 1 ALA A 37 140.12 62.67
REMARK 500 1 PRO A 63 -162.57 -74.98
REMARK 500 1 SER A 64 149.56 -38.73
REMARK 500 1 ALA A 86 -70.99 -46.74
REMARK 500 1 PHE A 94 -33.75 -37.67
REMARK 500 1 ILE A 100 -149.66 -133.56
REMARK 500 1 GLU A 102 105.62 -50.79
REMARK 500 2 SER A 3 163.01 61.00
REMARK 500 2 TYR A 10 44.38 -148.75
REMARK 500 2 VAL A 11 122.11 -178.40
REMARK 500 2 LEU A 13 153.53 -43.66
REMARK 500 2 VAL A 22 -167.43 -122.96
REMARK 500 2 ASP A 24 96.15 49.25
REMARK 500 2 VAL A 27 50.22 -159.79
REMARK 500 2 THR A 31 70.91 56.15
REMARK 500 2 ALA A 33 -175.22 -64.69
REMARK 500 2 GLN A 36 -164.14 42.19
REMARK 500 2 ALA A 37 81.03 42.03
REMARK 500 2 ALA A 46 -71.60 -40.41
REMARK 500 2 ILE A 69 148.71 72.68
REMARK 500 2 LEU A 96 -85.41 -62.92
REMARK 500 2 SER A 107 -157.53 56.80
REMARK 500 2 SER A 110 -62.54 71.76
REMARK 500 3 VAL A 11 121.87 63.74
REMARK 500 3 ASP A 12 -93.68 -117.59
REMARK 500 3 LYS A 21 88.14 -65.71
REMARK 500 3 ALA A 23 -55.67 -121.35
REMARK 500 3 ASP A 24 -60.84 70.90
REMARK 500 3 ARG A 25 97.47 58.13
REMARK 500 3 ARG A 26 104.07 60.22
REMARK 500 3 ASP A 32 164.67 64.10
REMARK 500 3 ALA A 33 126.43 65.65
REMARK 500 3 GLU A 34 83.72 70.41
REMARK 500 3 ALA A 37 65.84 79.56
REMARK 500 3 THR A 39 157.19 -44.43
REMARK 500 3 ALA A 46 -72.13 -59.96
REMARK 500 3 GLU A 67 -86.07 172.87
REMARK 500 3 ASP A 68 30.85 -155.31
REMARK 500 3 ALA A 86 -74.04 -51.95
REMARK 500 3 PHE A 94 -39.88 -37.55
REMARK 500
REMARK 500 THIS ENTRY HAS 379 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MMT007009107.1 RELATED DB: TARGETDB
DBREF 1WJW A 8 106 UNP Q9CYR6 AGM1_MOUSE 442 540
SEQADV 1WJW GLY A 1 UNP Q9CYR6 CLONING ARTIFACT
SEQADV 1WJW SER A 2 UNP Q9CYR6 CLONING ARTIFACT
SEQADV 1WJW SER A 3 UNP Q9CYR6 CLONING ARTIFACT
SEQADV 1WJW GLY A 4 UNP Q9CYR6 CLONING ARTIFACT
SEQADV 1WJW SER A 5 UNP Q9CYR6 CLONING ARTIFACT
SEQADV 1WJW SER A 6 UNP Q9CYR6 CLONING ARTIFACT
SEQADV 1WJW GLY A 7 UNP Q9CYR6 CLONING ARTIFACT
SEQADV 1WJW SER A 107 UNP Q9CYR6 CLONING ARTIFACT
SEQADV 1WJW GLY A 108 UNP Q9CYR6 CLONING ARTIFACT
SEQADV 1WJW PRO A 109 UNP Q9CYR6 CLONING ARTIFACT
SEQADV 1WJW SER A 110 UNP Q9CYR6 CLONING ARTIFACT
SEQADV 1WJW SER A 111 UNP Q9CYR6 CLONING ARTIFACT
SEQADV 1WJW GLY A 112 UNP Q9CYR6 CLONING ARTIFACT
SEQRES 1 A 112 GLY SER SER GLY SER SER GLY ALA ILE TYR VAL ASP LEU
SEQRES 2 A 112 PRO ASN ARG GLN LEU LYS VAL LYS VAL ALA ASP ARG ARG
SEQRES 3 A 112 VAL ILE SER THR THR ASP ALA GLU ARG GLN ALA VAL THR
SEQRES 4 A 112 PRO PRO GLY LEU GLN GLU ALA ILE ASN ASP LEU VAL LYS
SEQRES 5 A 112 LYS TYR THR LEU ALA ARG ALA PHE VAL ARG PRO SER GLY
SEQRES 6 A 112 THR GLU ASP ILE VAL ARG VAL TYR ALA GLU ALA ASN SER
SEQRES 7 A 112 GLN GLU SER ALA ASP ARG LEU ALA TYR GLU VAL SER LEU
SEQRES 8 A 112 LEU VAL PHE GLN LEU ALA GLY GLY ILE GLY GLU ARG PRO
SEQRES 9 A 112 GLN PRO SER GLY PRO SER SER GLY
HELIX 1 1 GLY A 42 TYR A 54 1 13
HELIX 2 2 SER A 78 ALA A 97 1 20
SHEET 1 A 3 ASN A 15 VAL A 20 0
SHEET 2 A 3 VAL A 70 ALA A 76 -1 O ALA A 74 N ARG A 16
SHEET 3 A 3 ALA A 57 ARG A 62 -1 N ARG A 58 O GLU A 75
CISPEP 1 THR A 39 PRO A 40 1 -0.04
CISPEP 2 THR A 39 PRO A 40 2 -0.05
CISPEP 3 THR A 39 PRO A 40 3 -0.02
CISPEP 4 THR A 39 PRO A 40 4 -0.01
CISPEP 5 THR A 39 PRO A 40 5 -0.04
CISPEP 6 THR A 39 PRO A 40 6 0.03
CISPEP 7 THR A 39 PRO A 40 7 0.01
CISPEP 8 THR A 39 PRO A 40 8 -0.01
CISPEP 9 THR A 39 PRO A 40 9 0.00
CISPEP 10 THR A 39 PRO A 40 10 -0.04
CISPEP 11 THR A 39 PRO A 40 11 0.03
CISPEP 12 THR A 39 PRO A 40 12 -0.07
CISPEP 13 THR A 39 PRO A 40 13 0.03
CISPEP 14 THR A 39 PRO A 40 14 0.07
CISPEP 15 THR A 39 PRO A 40 15 -0.04
CISPEP 16 THR A 39 PRO A 40 16 0.06
CISPEP 17 THR A 39 PRO A 40 17 -0.04
CISPEP 18 THR A 39 PRO A 40 18 -0.05
CISPEP 19 THR A 39 PRO A 40 19 -0.03
CISPEP 20 THR A 39 PRO A 40 20 0.01
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