Header list of 1ujo.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL PROTEIN 08-AUG-03 1UJO TITLE SOLUTION STRUCTURE OF THE CH DOMAIN FROM MOUSE TRANGELIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: TRANSGELIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: CALPONIN HOMOLOGY (CH) DOMAIN; COMPND 5 SYNONYM: SMOOTH MUSCLE PROTEIN 22-ALPHA, SM22-ALPHA, ACTIN- COMPND 6 ASSOCIATED PROTEIN P27; 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 0610041C11; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P020520-56; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS TRANSGELIN, CH DOMAIN, ACTIN BINDING, STRUCTURAL GENOMICS, RIKEN KEYWDS 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, STRUCTURAL PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR T.TOMIZAWA,S.KOSHIBA,T.KIGAWA,S.YOKOYAMA,RIKEN STRUCTURAL AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 02-MAR-22 1UJO 1 REMARK SEQADV REVDAT 2 24-FEB-09 1UJO 1 VERSN REVDAT 1 14-SEP-04 1UJO 0 JRNL AUTH T.TOMIZAWA,S.KOSHIBA,T.KIGAWA,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE CH DOMAIN FROM MOUSE TRANGELIN 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 1UJO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-AUG-03. REMARK 100 THE DEPOSITION ID IS D_1000005900. 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 : 220MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.0MM CH DOMAIN U-15N, 13C; 20MM REMARK 210 TRIS-HCL(PH 7.0); 200MM NACL; REMARK 210 1MM D-DTT; 0.02% NAN3; 10% 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 0.820, 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: 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 THR A 98 H TYR A 102 1.54 REMARK 500 O GLY A 43 H SER A 47 1.54 REMARK 500 O ALA A 116 H LEU A 120 1.56 REMARK 500 H GLN A 97 OD2 ASP A 100 1.57 REMARK 500 O GLN A 111 H MET A 115 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 2 158.87 61.86 REMARK 500 1 GLU A 8 172.34 54.87 REMARK 500 1 GLN A 21 -71.08 -63.68 REMARK 500 1 ARG A 33 -171.55 49.17 REMARK 500 1 LEU A 34 -75.97 -41.98 REMARK 500 1 LEU A 40 42.98 -103.77 REMARK 500 1 LYS A 41 -60.08 -104.38 REMARK 500 1 LEU A 49 -70.81 -58.56 REMARK 500 1 LEU A 53 -72.90 -75.16 REMARK 500 1 TYR A 54 150.76 -35.13 REMARK 500 1 SER A 58 -72.21 -145.50 REMARK 500 1 LYS A 59 90.44 42.07 REMARK 500 1 SER A 69 -46.88 -141.11 REMARK 500 1 MET A 70 158.95 -43.28 REMARK 500 1 VAL A 90 151.49 -43.52 REMARK 500 1 ASP A 100 -30.53 -39.68 REMARK 500 1 LEU A 101 -61.15 -99.26 REMARK 500 1 LEU A 117 -72.28 -44.93 REMARK 500 1 LYS A 124 -77.24 -73.45 REMARK 500 1 ASN A 125 98.31 54.12 REMARK 500 1 ASP A 126 27.82 -153.58 REMARK 500 1 ASN A 128 -48.34 -147.88 REMARK 500 1 ARG A 130 39.98 -97.18 REMARK 500 1 ASN A 134 45.23 -88.58 REMARK 500 1 LYS A 138 -66.87 -162.18 REMARK 500 1 SER A 139 112.94 -167.44 REMARK 500 1 SER A 143 160.26 57.83 REMARK 500 2 SER A 2 -60.02 -158.35 REMARK 500 2 SER A 3 90.15 44.03 REMARK 500 2 SER A 5 168.51 60.36 REMARK 500 2 SER A 6 174.89 -49.52 REMARK 500 2 GLU A 8 149.96 59.90 REMARK 500 2 PRO A 29 -168.08 -74.93 REMARK 500 2 ARG A 31 169.61 -48.39 REMARK 500 2 LEU A 49 -73.55 -56.53 REMARK 500 2 LEU A 53 -84.73 -71.37 REMARK 500 2 TYR A 54 149.84 -35.90 REMARK 500 2 SER A 58 -71.20 -130.20 REMARK 500 2 LYS A 59 85.73 41.43 REMARK 500 2 GLU A 65 -72.43 74.91 REMARK 500 2 PRO A 68 -87.68 -75.02 REMARK 500 2 SER A 69 -47.80 167.94 REMARK 500 2 MET A 70 155.52 -43.16 REMARK 500 2 LEU A 101 -71.34 -107.12 REMARK 500 2 ARG A 112 -34.05 -38.21 REMARK 500 2 ASP A 126 44.60 159.66 REMARK 500 2 MET A 137 -76.60 -67.09 REMARK 500 2 SER A 142 112.14 58.16 REMARK 500 2 SER A 143 108.26 -167.13 REMARK 500 3 LEU A 10 -71.38 -40.32 REMARK 500 REMARK 500 THIS ENTRY HAS 419 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 650 REMARK 650 HELIX REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: MMK001000190.1 RELATED DB: TARGETDB DBREF 1UJO A 8 138 UNP P37804 TAGL_MOUSE 23 153 SEQADV 1UJO GLY A 1 UNP P37804 CLONING ARTIFACT SEQADV 1UJO SER A 2 UNP P37804 CLONING ARTIFACT SEQADV 1UJO SER A 3 UNP P37804 CLONING ARTIFACT SEQADV 1UJO GLY A 4 UNP P37804 CLONING ARTIFACT SEQADV 1UJO SER A 5 UNP P37804 CLONING ARTIFACT SEQADV 1UJO SER A 6 UNP P37804 CLONING ARTIFACT SEQADV 1UJO GLY A 7 UNP P37804 CLONING ARTIFACT SEQADV 1UJO SER A 139 UNP P37804 CLONING ARTIFACT SEQADV 1UJO GLY A 140 UNP P37804 CLONING ARTIFACT SEQADV 1UJO PRO A 141 UNP P37804 CLONING ARTIFACT SEQADV 1UJO SER A 142 UNP P37804 CLONING ARTIFACT SEQADV 1UJO SER A 143 UNP P37804 CLONING ARTIFACT SEQADV 1UJO GLY A 144 UNP P37804 CLONING ARTIFACT SEQRES 1 A 144 GLY SER SER GLY SER SER GLY GLU GLU LEU GLU GLU ARG SEQRES 2 A 144 LEU VAL GLU TRP ILE VAL VAL GLN CYS GLY PRO ASP VAL SEQRES 3 A 144 GLY ARG PRO ASP ARG GLY ARG LEU GLY PHE GLN VAL TRP SEQRES 4 A 144 LEU LYS ASN GLY VAL ILE LEU SER LYS LEU VAL ASN SER SEQRES 5 A 144 LEU TYR PRO GLU GLY SER LYS PRO VAL LYS VAL PRO GLU SEQRES 6 A 144 ASN PRO PRO SER MET VAL PHE LYS GLN MET GLU GLN VAL SEQRES 7 A 144 ALA GLN PHE LEU LYS ALA ALA GLU ASP TYR GLY VAL ILE SEQRES 8 A 144 LYS THR ASP MET PHE GLN THR VAL ASP LEU TYR GLU GLY SEQRES 9 A 144 LYS ASP MET ALA ALA VAL GLN ARG THR LEU MET ALA LEU SEQRES 10 A 144 GLY SER LEU ALA VAL THR LYS ASN ASP GLY ASN TYR ARG SEQRES 11 A 144 GLY ASP PRO ASN TRP PHE MET LYS SER GLY PRO SER SER SEQRES 12 A 144 GLY HELIX 1 1 GLU A 9 CYS A 22 1 14 HELIX 2 2 PHE A 36 LYS A 41 1 6 HELIX 3 3 VAL A 44 TYR A 54 1 11 HELIX 4 4 MET A 70 TYR A 88 1 19 HELIX 5 5 GLN A 97 GLU A 103 1 7 HELIX 6 6 MET A 107 LYS A 124 1 18 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