Header list of 1v5k.pdb file
Complete list - v 10 2 Bytes
HEADER STRUCTURAL PROTEIN, PROTEIN BINDING 25-NOV-03 1V5K TITLE SOLUTION STRUCTURE OF THE CH DOMAIN FROM MOUSE EB-1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: MICROTUBULE-ASSOCIATED PROTEIN, RP/EB FAMILY, MEMBER 1; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: CH DOMAIN; COMPND 5 SYNONYM: ADENOMATOSIS POLYPOSIS COLI BINDING PROTEIN EB1; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: 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 2900038A16; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P021216-20; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS CALPONIN HOMOLOGY (CH) DOMAIN, MICROTUBULE BINDING, ADENOMATOSIS KEYWDS 2 POLYPOSIS COLI BINDING PROTEIN, STRUCTURAL GENOMICS, RIKEN KEYWDS 3 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, STRUCTURAL PROTEIN, KEYWDS 4 PROTEIN BINDING EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR T.TOMIZAWA,T.KIGAWA,S.KOSHIBA,M.INOUE,S.YOKOYAMA,RIKEN STRUCTURAL AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 10-NOV-21 1V5K 1 REMARK SEQADV REVDAT 2 24-FEB-09 1V5K 1 VERSN REVDAT 1 25-MAY-04 1V5K 0 JRNL AUTH T.TOMIZAWA,T.KIGAWA,S.KOSHIBA,M.INOUE,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE CH DOMAIN FROM MOUSE EB-1 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 1.0.7 REMARK 3 AUTHORS : BRUKER (XWINNMR), GUENTERT, P. (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1V5K COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-NOV-03. REMARK 100 THE DEPOSITION ID IS D_1000006233. 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 : 120MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.03MM CH DOMAIN U-15N, 13C; REMARK 210 20MM SODIUM PHOSPHATE; 100MM REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3; 10% REMARK 210 D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N 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 0.863, CYANA 1.0.7 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS, REMARK 210 RESTRAINTED MOLECULAR 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: 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 GLN A 95 H GLU A 99 1.51 REMARK 500 O ALA A 15 H GLU A 19 1.54 REMARK 500 O PHE A 68 H GLN A 72 1.56 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 2 164.72 62.88 REMARK 500 1 SER A 3 -71.73 66.96 REMARK 500 1 SER A 5 114.68 179.90 REMARK 500 1 SER A 6 -62.68 -179.49 REMARK 500 1 GLN A 8 88.73 44.65 REMARK 500 1 ARG A 9 179.82 -56.92 REMARK 500 1 ARG A 10 -72.84 70.00 REMARK 500 1 TRP A 16 -71.18 -45.47 REMARK 500 1 GLU A 19 55.57 -96.83 REMARK 500 1 SER A 20 -44.60 -151.66 REMARK 500 1 GLN A 22 69.72 70.50 REMARK 500 1 LEU A 23 -156.63 -106.65 REMARK 500 1 ASN A 24 45.74 -173.24 REMARK 500 1 LEU A 31 33.10 -92.75 REMARK 500 1 LYS A 52 41.88 -90.51 REMARK 500 1 LYS A 53 -44.62 -159.35 REMARK 500 1 GLN A 57 26.42 -160.26 REMARK 500 1 HIS A 62 -37.47 -37.72 REMARK 500 1 VAL A 86 -68.59 66.61 REMARK 500 1 PHE A 94 -179.18 63.08 REMARK 500 1 GLN A 95 -64.47 67.01 REMARK 500 1 SER A 114 151.65 62.16 REMARK 500 2 SER A 2 84.42 57.40 REMARK 500 2 SER A 3 -57.23 -153.72 REMARK 500 2 SER A 6 154.05 -46.41 REMARK 500 2 ARG A 9 170.89 53.57 REMARK 500 2 ARG A 10 -69.61 71.00 REMARK 500 2 ASN A 18 -80.48 -42.60 REMARK 500 2 SER A 20 -38.99 -39.28 REMARK 500 2 LEU A 21 -131.00 -114.11 REMARK 500 2 GLN A 22 41.31 -145.68 REMARK 500 2 ASN A 24 43.94 -171.21 REMARK 500 2 LYS A 52 39.93 -89.71 REMARK 500 2 LYS A 53 -45.41 -157.98 REMARK 500 2 VAL A 54 156.51 -46.02 REMARK 500 2 GLN A 57 34.12 -155.80 REMARK 500 2 HIS A 62 -32.74 -38.06 REMARK 500 2 ASP A 87 -31.63 -38.58 REMARK 500 2 PHE A 94 -83.74 56.15 REMARK 500 2 SER A 113 -58.37 -126.01 REMARK 500 2 SER A 114 79.46 46.76 REMARK 500 3 SER A 6 -53.98 -143.59 REMARK 500 3 ARG A 9 168.57 60.35 REMARK 500 3 ARG A 10 -74.65 67.13 REMARK 500 3 GLU A 19 58.64 -96.41 REMARK 500 3 SER A 20 -44.85 -156.45 REMARK 500 3 GLN A 22 60.03 74.58 REMARK 500 3 LEU A 23 -156.41 -99.19 REMARK 500 3 ASN A 24 55.89 -176.13 REMARK 500 3 ALA A 50 60.35 -117.30 REMARK 500 REMARK 500 THIS ENTRY HAS 389 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: MMT007009322.1 RELATED DB: TARGETDB DBREF 1V5K A 8 109 GB 7106301 NP_031922 15 116 SEQADV 1V5K GLY A 1 GB 7106301 CLONING ARTIFACT SEQADV 1V5K SER A 2 GB 7106301 CLONING ARTIFACT SEQADV 1V5K SER A 3 GB 7106301 CLONING ARTIFACT SEQADV 1V5K GLY A 4 GB 7106301 CLONING ARTIFACT SEQADV 1V5K SER A 5 GB 7106301 CLONING ARTIFACT SEQADV 1V5K SER A 6 GB 7106301 CLONING ARTIFACT SEQADV 1V5K GLY A 7 GB 7106301 CLONING ARTIFACT SEQADV 1V5K GLN A 8 GB 7106301 LEU 15 ENGINEERED MUTATION SEQADV 1V5K ARG A 9 GB 7106301 SER 16 ENGINEERED MUTATION SEQADV 1V5K SER A 110 GB 7106301 CLONING ARTIFACT SEQADV 1V5K GLY A 111 GB 7106301 CLONING ARTIFACT SEQADV 1V5K PRO A 112 GB 7106301 CLONING ARTIFACT SEQADV 1V5K SER A 113 GB 7106301 CLONING ARTIFACT SEQADV 1V5K SER A 114 GB 7106301 CLONING ARTIFACT SEQADV 1V5K GLY A 115 GB 7106301 CLONING ARTIFACT SEQRES 1 A 115 GLY SER SER GLY SER SER GLY GLN ARG ARG HIS ASP MET SEQRES 2 A 115 LEU ALA TRP ILE ASN GLU SER LEU GLN LEU ASN LEU THR SEQRES 3 A 115 LYS ILE GLU GLN LEU CYS SER GLY ALA ALA TYR CYS GLN SEQRES 4 A 115 PHE MET ASP MET LEU PHE PRO GLY SER ILE ALA LEU LYS SEQRES 5 A 115 LYS VAL LYS PHE GLN ALA LYS LEU GLU HIS GLU TYR ILE SEQRES 6 A 115 GLN ASN PHE LYS ILE LEU GLN ALA GLY PHE LYS ARG MET SEQRES 7 A 115 GLY VAL ASP LYS ILE ILE PRO VAL ASP LYS LEU VAL LYS SEQRES 8 A 115 GLY LYS PHE GLN ASP ASN PHE GLU PHE VAL GLN TRP PHE SEQRES 9 A 115 LYS LYS PHE PHE ASP SER GLY PRO SER SER GLY HELIX 1 1 ARG A 10 GLN A 22 1 13 HELIX 2 2 ILE A 28 CYS A 32 5 5 HELIX 3 3 ALA A 35 PHE A 45 1 11 HELIX 4 4 LEU A 60 GLY A 79 1 20 HELIX 5 5 ASN A 97 SER A 110 1 14 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 - v 10 2 Bytes