Header list of 1vfi.pdb file
Complete list - r 2 2 Bytes
HEADER METAL BINDING PROTEIN 13-APR-04 1VFI TITLE SOLUTION STRUCTURE OF VANABIN2 (RUH-017), A VANADIUM-BINDING PROTEIN TITLE 2 FROM ASCIDIA SYDNEIENSIS SAMEA COMPND MOL_ID: 1; COMPND 2 MOLECULE: VANADIUM-BINDING PROTEIN 2; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 1-95; COMPND 5 SYNONYM: VANABIN2, RUH-017; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ASCIDIA SYDNEIENSIS SAMEA; SOURCE 3 ORGANISM_TAXID: 79730; SOURCE 4 STRAIN: SAMEA; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PMAL-C KEYWDS VANADIUM-BINDING, ASCIDIAN, RIKEN STRUCTURAL GENOMICS/PROTEOMICS KEYWDS 2 INITIATIVE, RSGI, STRUCTURAL GENOMICS, METAL BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR T.HAMADA,H.HIROTA,M.ASANUMA,F.HAYASHI,N.KOBAYASHI,T.UEKI,H.MICHIBATA, AUTHOR 2 S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 4 02-MAR-22 1VFI 1 REMARK SEQADV REVDAT 3 24-FEB-09 1VFI 1 VERSN REVDAT 2 05-APR-05 1VFI 1 JRNL REVDAT 1 22-MAR-05 1VFI 0 JRNL AUTH T.HAMADA,M.ASANUMA,T.UEKI,F.HAYASHI,N.KOBAYASHI,S.YOKOYAMA, JRNL AUTH 2 H.MICHIBATA,H.HIROTA JRNL TITL SOLUTION STRUCTURE OF VANABIN2, A VANADIUM(IV)-BINDING JRNL TITL 2 PROTEIN FROM THE VANADIUM-RICH ASCIDIAN ASCIDIA SYDNEIENSIS JRNL TITL 3 SAMEA JRNL REF J.AM.CHEM.SOC. V. 127 4216 2005 JRNL REFN ISSN 0002-7863 JRNL PMID 15783203 JRNL DOI 10.1021/JA042687J REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 2.6, CYANA 1.0.7 REMARK 3 AUTHORS : BRUKER (XWINNMR), GUENTERT, P. (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1VFI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-APR-04. REMARK 100 THE DEPOSITION ID IS D_1000006559. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.7MM VANADIUM-BINDING PROTEIN U REMARK 210 -15N, 13C; 20MM POTASSIUM REMARK 210 PHOSPHATE BUFFER (PH 6.9) REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 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 0.8995, CYANA 1.0.7 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: 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: 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 CYS A 63 H CYS A 67 1.51 REMARK 500 O LYS A 24 H ALA A 28 1.53 REMARK 500 O ALA A 58 H LYS A 62 1.54 REMARK 500 O LYS A 38 H ARG A 42 1.54 REMARK 500 O LYS A 62 H ALA A 66 1.57 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 ALA A 5 165.19 67.15 REMARK 500 1 CYS A 9 -50.68 -147.06 REMARK 500 1 CYS A 13 50.43 -160.41 REMARK 500 1 CYS A 31 50.85 -108.15 REMARK 500 1 ASP A 36 66.14 65.13 REMARK 500 1 ASP A 48 41.90 -161.30 REMARK 500 1 ALA A 70 -94.58 -75.46 REMARK 500 1 ASN A 71 -72.80 -40.21 REMARK 500 1 ALA A 73 -46.98 -177.93 REMARK 500 1 HIS A 81 70.80 -159.24 REMARK 500 2 GLU A 3 -60.27 -107.86 REMARK 500 2 PRO A 6 -162.99 -74.98 REMARK 500 2 ASP A 8 85.59 40.02 REMARK 500 2 CYS A 9 -73.63 -42.36 REMARK 500 2 LYS A 10 -106.57 39.08 REMARK 500 2 CYS A 13 56.58 -104.71 REMARK 500 2 CYS A 31 55.50 -113.68 REMARK 500 2 ALA A 35 -78.26 64.95 REMARK 500 2 ASP A 36 73.92 -116.19 REMARK 500 2 ASP A 48 47.19 -156.79 REMARK 500 2 CYS A 49 28.71 -146.50 REMARK 500 2 ALA A 70 -88.83 -65.55 REMARK 500 2 LYS A 78 52.86 -90.42 REMARK 500 2 HIS A 79 -63.16 -166.53 REMARK 500 2 LYS A 82 48.54 -155.25 REMARK 500 3 PHE A 4 167.45 56.41 REMARK 500 3 ALA A 5 152.82 67.99 REMARK 500 3 ASP A 8 70.45 46.52 REMARK 500 3 CYS A 31 48.54 -98.90 REMARK 500 3 THR A 33 -58.62 -144.42 REMARK 500 3 SER A 34 -179.41 50.86 REMARK 500 3 ASP A 48 46.22 -168.87 REMARK 500 3 CYS A 49 39.47 -141.52 REMARK 500 3 ALA A 70 -74.42 -61.71 REMARK 500 3 ALA A 73 -63.95 -167.80 REMARK 500 3 PRO A 77 -167.05 -74.97 REMARK 500 3 HIS A 79 179.33 85.79 REMARK 500 3 GLU A 80 131.13 65.63 REMARK 500 3 HIS A 81 -51.11 -128.46 REMARK 500 4 SER A 2 160.45 177.85 REMARK 500 4 PHE A 4 -61.34 68.67 REMARK 500 4 ALA A 5 154.20 64.34 REMARK 500 4 CYS A 9 -73.71 -47.04 REMARK 500 4 LYS A 10 -106.45 38.36 REMARK 500 4 CYS A 13 52.35 -104.55 REMARK 500 4 ASP A 48 34.05 -171.72 REMARK 500 4 ALA A 70 -70.06 -79.04 REMARK 500 4 ASN A 71 -70.96 -78.20 REMARK 500 4 ALA A 73 -41.45 -174.58 REMARK 500 4 PRO A 77 -164.61 -75.03 REMARK 500 REMARK 500 THIS ENTRY HAS 264 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: AR_001000080.1 RELATED DB: TARGETDB DBREF 1VFI A 5 95 UNP Q86BW2 Q86BW2_ASCSS 30 120 SEQADV 1VFI ILE A 1 UNP Q86BW2 CLONING ARTIFACT SEQADV 1VFI SER A 2 UNP Q86BW2 CLONING ARTIFACT SEQADV 1VFI GLU A 3 UNP Q86BW2 CLONING ARTIFACT SEQADV 1VFI PHE A 4 UNP Q86BW2 CLONING ARTIFACT SEQRES 1 A 95 ILE SER GLU PHE ALA PRO VAL ASP CYS LYS GLY GLN CYS SEQRES 2 A 95 THR THR PRO CYS GLU PRO LEU THR ALA CYS LYS GLU LYS SEQRES 3 A 95 CYS ALA GLU SER CYS GLU THR SER ALA ASP LYS LYS THR SEQRES 4 A 95 CYS ARG ARG ASN CYS LYS LYS ALA ASP CYS GLU PRO GLN SEQRES 5 A 95 ASP LYS VAL CYS ASP ALA CYS ARG MET LYS CYS HIS LYS SEQRES 6 A 95 ALA CYS ARG ALA ALA ASN CYS ALA SER GLU CYS PRO LYS SEQRES 7 A 95 HIS GLU HIS LYS SER ASP THR CYS ARG ALA CYS MET LYS SEQRES 8 A 95 THR ASN CYS LYS HELIX 1 1 CYS A 17 CYS A 31 1 15 HELIX 2 2 ASP A 36 CYS A 49 1 14 HELIX 3 3 CYS A 49 ASN A 71 1 23 HELIX 4 4 SER A 83 ASN A 93 1 11 SSBOND 1 CYS A 9 CYS A 63 1555 1555 2.11 SSBOND 2 CYS A 13 CYS A 59 1555 1555 2.02 SSBOND 3 CYS A 17 CYS A 56 1555 1555 2.00 SSBOND 4 CYS A 23 CYS A 49 1555 1555 1.97 SSBOND 5 CYS A 27 CYS A 44 1555 1555 2.11 SSBOND 6 CYS A 31 CYS A 40 1555 1555 1.99 SSBOND 7 CYS A 67 CYS A 94 1555 1555 2.10 SSBOND 8 CYS A 72 CYS A 89 1555 1555 2.01 SSBOND 9 CYS A 76 CYS A 86 1555 1555 2.05 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