Header list of 1wvo.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSFERASE 22-DEC-04 1WVO
TITLE SOLUTION STRUCTURE OF RSGI RUH-029, AN ANTIFREEZE PROTEIN LIKE DOMAIN
TITLE 2 IN HUMAN N-ACETYLNEURAMINIC ACID PHOSPHATE SYNTHASE GENE.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SIALIC ACID SYNTHASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ANTIFREEZE PROTEIN LIKE DOMAIN;
COMPND 5 SYNONYM: N-ACETYLNEURAMINATE SYNTHASE, N-ACETYLNEURAMINIC ACID
COMPND 6 SYNTHASE, N-ACETYLNEURAMINATE-9-PHOSPHATE SYNTHASE, N-
COMPND 7 ACETYLNEURAMINIC ACID PHOSPHATE SYNTHASE;
COMPND 8 EC: 2.5.1.56, 2.5.1.57;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 6 EXPRESSION_SYSTEM_PLASMID: P040531-08;
SOURCE 7 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS ANTIFREEZE PROTEIN LIKE DOMAIN, N-ACETYLNEURAMINIC ACID PHOSPHATE
KEYWDS 2 SYNTHASE, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN
KEYWDS 3 STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 4 GENOMICS/PROTEOMICS INITIATIVE, RSGI, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR Y.ITO,T.HAMADA,F.HAYASHI,S.YOKOYAMA,H.HIROTA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 4 02-MAR-22 1WVO 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1WVO 1 VERSN
REVDAT 2 16-MAY-06 1WVO 1 JRNL
REVDAT 1 03-JAN-06 1WVO 0
JRNL AUTH T.HAMADA,Y.ITO,T.ABE,F.HAYASHI,P.GUNTERT,M.INOUE,T.KIGAWA,
JRNL AUTH 2 T.TERADA,M.SHIROUZU,M.YOSHIDA,A.TANAKA,S.SUGANO,S.YOKOYAMA,
JRNL AUTH 3 H.HIROTA
JRNL TITL SOLUTION STRUCTURE OF THE ANTIFREEZE-LIKE DOMAIN OF HUMAN
JRNL TITL 2 SIALIC ACID SYNTHASE
JRNL REF PROTEIN SCI. V. 15 1010 2006
JRNL REFN ISSN 0961-8368
JRNL PMID 16597820
JRNL DOI 10.1110/PS.051700406
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1C, CYANA 2.0.17, OPALP 1.4
REMARK 3 AUTHORS : VARIAN (VNMR), GUENTERT, P. (CYANA), KORADI, R.,
REMARK 3 BILLETER, M., GUNTERT, P. (OPALP)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WVO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-DEC-04.
REMARK 100 THE DEPOSITION ID IS D_1000024056.
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 NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.1MM ANTIFREEZE PROTEIN LIKE
REMARK 210 DOMAIN U-15N,13C; 20MM TRIS-HCL
REMARK 210 BUFFER (PH 7.0); 100MM NACL; 1MM
REMARK 210 D-DTT; 0.02% NAN3; 90% H2O, 10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 21_2, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9049, 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: THIS STRUCTURE WAS DETERMINED USING 3D NMR TECHNIQUES
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 5 41.00 -75.04
REMARK 500 1 PRO A 33 44.02 -80.47
REMARK 500 1 VAL A 45 93.73 -67.20
REMARK 500 1 ASP A 56 13.06 56.92
REMARK 500 1 LYS A 69 -65.03 -99.14
REMARK 500 1 ILE A 71 39.60 -74.93
REMARK 500 2 SER A 77 -122.90 -104.30
REMARK 500 3 VAL A 30 98.62 -59.63
REMARK 500 3 VAL A 45 91.29 -67.68
REMARK 500 4 GLU A 62 4.33 -65.66
REMARK 500 4 ASN A 66 135.55 179.73
REMARK 500 5 HIS A 67 -67.28 64.43
REMARK 500 5 LYS A 69 -4.48 154.68
REMARK 500 5 SER A 73 92.87 -62.40
REMARK 500 5 SER A 78 80.34 -154.62
REMARK 500 6 SER A 5 24.92 -140.79
REMARK 500 6 VAL A 45 98.70 -60.78
REMARK 500 7 SER A 2 -67.12 -131.41
REMARK 500 7 SER A 5 79.44 -153.97
REMARK 500 7 PRO A 33 31.65 -73.30
REMARK 500 7 HIS A 67 94.34 -63.63
REMARK 500 7 SER A 74 -170.70 -170.23
REMARK 500 8 SER A 6 -105.42 -102.83
REMARK 500 8 ASP A 56 1.20 82.87
REMARK 500 8 ASN A 66 114.94 173.18
REMARK 500 8 SER A 73 -168.36 -75.47
REMARK 500 9 SER A 5 -68.11 -161.46
REMARK 500 9 LYS A 70 109.38 -59.08
REMARK 500 9 SER A 73 -77.70 -78.60
REMARK 500 9 PRO A 76 9.65 -68.88
REMARK 500 9 SER A 78 -26.01 -169.92
REMARK 500 10 PRO A 33 28.80 -77.80
REMARK 500 10 ASP A 56 -6.18 72.47
REMARK 500 10 ILE A 59 93.73 -67.26
REMARK 500 11 SER A 5 127.91 -171.71
REMARK 500 12 SER A 2 -48.69 -148.32
REMARK 500 12 LYS A 34 106.15 -48.54
REMARK 500 12 HIS A 67 -55.72 -147.20
REMARK 500 12 LYS A 69 -57.36 -135.58
REMARK 500 12 PRO A 76 15.36 -67.73
REMARK 500 13 VAL A 30 89.99 -66.99
REMARK 500 13 SER A 78 -167.57 -79.12
REMARK 500 14 LYS A 34 95.32 -67.47
REMARK 500 14 ASP A 56 8.29 58.63
REMARK 500 15 SER A 2 -71.18 -54.09
REMARK 500 15 LYS A 70 105.98 -161.67
REMARK 500 15 SER A 73 -67.64 -123.38
REMARK 500 15 SER A 77 48.86 -73.79
REMARK 500 16 PRO A 33 36.23 -73.82
REMARK 500 16 VAL A 45 99.19 -68.05
REMARK 500
REMARK 500 THIS ENTRY HAS 63 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 TYR A 36 0.07 SIDE CHAIN
REMARK 500 10 TYR A 36 0.07 SIDE CHAIN
REMARK 500 11 TYR A 36 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSS001002155.1 RELATED DB: TARGETDB
DBREF 1WVO A 8 73 UNP Q9NR45 SIAS_HUMAN 294 359
SEQADV 1WVO GLY A 1 UNP Q9NR45 CLONING ARTIFACT
SEQADV 1WVO SER A 2 UNP Q9NR45 CLONING ARTIFACT
SEQADV 1WVO SER A 3 UNP Q9NR45 CLONING ARTIFACT
SEQADV 1WVO GLY A 4 UNP Q9NR45 CLONING ARTIFACT
SEQADV 1WVO SER A 5 UNP Q9NR45 CLONING ARTIFACT
SEQADV 1WVO SER A 6 UNP Q9NR45 CLONING ARTIFACT
SEQADV 1WVO GLY A 7 UNP Q9NR45 CLONING ARTIFACT
SEQADV 1WVO SER A 74 UNP Q9NR45 CLONING ARTIFACT
SEQADV 1WVO GLY A 75 UNP Q9NR45 CLONING ARTIFACT
SEQADV 1WVO PRO A 76 UNP Q9NR45 CLONING ARTIFACT
SEQADV 1WVO SER A 77 UNP Q9NR45 CLONING ARTIFACT
SEQADV 1WVO SER A 78 UNP Q9NR45 CLONING ARTIFACT
SEQADV 1WVO GLY A 79 UNP Q9NR45 CLONING ARTIFACT
SEQRES 1 A 79 GLY SER SER GLY SER SER GLY SER VAL VAL ALA LYS VAL
SEQRES 2 A 79 LYS ILE PRO GLU GLY THR ILE LEU THR MET ASP MET LEU
SEQRES 3 A 79 THR VAL LYS VAL GLY GLU PRO LYS GLY TYR PRO PRO GLU
SEQRES 4 A 79 ASP ILE PHE ASN LEU VAL GLY LYS LYS VAL LEU VAL THR
SEQRES 5 A 79 VAL GLU GLU ASP ASP THR ILE MET GLU GLU LEU VAL ASP
SEQRES 6 A 79 ASN HIS GLY LYS LYS ILE LYS SER SER GLY PRO SER SER
SEQRES 7 A 79 GLY
HELIX 1 1 THR A 22 ASP A 24 5 3
HELIX 2 2 ASP A 40 VAL A 45 1 6
HELIX 3 3 MET A 60 VAL A 64 5 5
SHEET 1 A 2 SER A 8 ALA A 11 0
SHEET 2 A 2 LEU A 26 LYS A 29 -1 O LYS A 29 N SER A 8
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