Header list of 1wnj.pdb file
Complete list - r 2 2 Bytes
HEADER PROTEIN BINDING 05-AUG-04 1WNJ TITLE NMR STRUCTURE OF HUMAN COACTOSIN-LIKE PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: COACTOSIN-LIKE PROTEIN; COMPND 3 CHAIN: A; COMPND 4 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: 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: PGEX-5X-1 KEYWDS BETA-ALPHA, PROTEIN BINDING EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR E.LIEPINSH,M.RAKONJAC,V.BOISSONNEAULT,P.PROVOST,B.SAMUELSSON, AUTHOR 2 O.RADMARK,G.OTTING REVDAT 4 02-MAR-22 1WNJ 1 REMARK SEQADV REVDAT 3 24-FEB-09 1WNJ 1 VERSN REVDAT 2 22-MAR-05 1WNJ 1 JRNL REVDAT 1 17-AUG-04 1WNJ 0 JRNL AUTH E.LIEPINSH,M.RAKONJAC,V.BOISSONNEAULT,P.PROVOST, JRNL AUTH 2 B.SAMUELSSON,O.RADMARK,G.OTTING JRNL TITL NMR STRUCTURE OF HUMAN COACTOSIN-LIKE PROTEIN JRNL REF J.BIOMOL.NMR V. 30 353 2004 JRNL REFN ISSN 0925-2738 JRNL PMID 15754059 JRNL DOI 10.1007/S10858-004-3449-Y REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DYANA 1.5, OPAL 2.6 REMARK 3 AUTHORS : GUENTERT (DYANA), LUGINBUEHL (OPAL) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1WNJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-AUG-04. REMARK 100 THE DEPOSITION ID IS D_1000023781. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7 REMARK 210 IONIC STRENGTH : 8MM TRIS, 50MM NACL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.16MM CLP; 0.16MM CLP; 0.25MM REMARK 210 15N-CLP REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY; REMARK 210 3D_15N-SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : DMX; INOVA REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 20 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES REMARK 210 SUBMITTED REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: 2D 15N-HB EXPERIMENT 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 HG SER A 118 OE1 GLU A 122 1.59 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 1 PHE A 115 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES REMARK 500 2 ARG A 21 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES REMARK 500 5 ARG A 66 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES REMARK 500 10 VAL A 59 CA - CB - CG2 ANGL. DEV. = 10.0 DEGREES REMARK 500 10 PHE A 115 CB - CG - CD2 ANGL. DEV. = -5.0 DEGREES REMARK 500 10 PHE A 115 CB - CG - CD1 ANGL. DEV. = 4.3 DEGREES REMARK 500 11 ARG A 60 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES REMARK 500 12 VAL A 59 CA - CB - CG2 ANGL. DEV. = 9.6 DEGREES REMARK 500 13 TYR A 17 CB - CG - CD1 ANGL. DEV. = -3.6 DEGREES REMARK 500 14 PHE A 115 CB - CG - CD2 ANGL. DEV. = -4.9 DEGREES REMARK 500 14 PHE A 115 CB - CG - CD1 ANGL. DEV. = 4.3 DEGREES REMARK 500 16 VAL A 59 CA - CB - CG2 ANGL. DEV. = 9.5 DEGREES REMARK 500 16 PHE A 115 CB - CG - CD2 ANGL. DEV. = -6.5 DEGREES REMARK 500 16 PHE A 115 CB - CG - CD1 ANGL. DEV. = 5.3 DEGREES REMARK 500 17 PHE A 115 CB - CG - CD2 ANGL. DEV. = -4.8 DEGREES REMARK 500 19 PHE A 115 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES REMARK 500 20 VAL A 59 CA - CB - CG2 ANGL. DEV. = 9.1 DEGREES 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 44.52 -144.19 REMARK 500 1 ASP A 57 -75.95 -81.26 REMARK 500 1 VAL A 108 25.90 -78.28 REMARK 500 1 ALA A 142 69.24 -156.63 REMARK 500 1 THR A 144 23.66 86.24 REMARK 500 2 ASP A 57 -76.57 -40.77 REMARK 500 2 MET A 73 2.90 -60.59 REMARK 500 2 VAL A 108 21.93 -76.09 REMARK 500 2 ALA A 112 -60.37 -105.14 REMARK 500 2 SER A 118 -9.85 -149.26 REMARK 500 2 THR A 144 56.40 86.46 REMARK 500 3 ARG A 3 81.11 -155.17 REMARK 500 3 ASP A 57 -71.36 -46.38 REMARK 500 3 MET A 73 7.17 -65.88 REMARK 500 3 VAL A 108 25.96 -64.80 REMARK 500 3 ALA A 112 -62.38 -104.65 REMARK 500 3 ALA A 142 79.41 -153.50 REMARK 500 3 GLN A 143 40.68 -70.65 REMARK 500 4 ASP A 57 -76.68 -54.12 REMARK 500 4 VAL A 108 26.62 -74.32 REMARK 500 4 SER A 118 -8.45 -140.08 REMARK 500 5 MET A 4 24.78 -67.53 REMARK 500 5 ASP A 57 -70.58 -49.77 REMARK 500 5 ALA A 112 -66.15 -93.68 REMARK 500 5 SER A 118 -0.59 -143.24 REMARK 500 5 ALA A 135 1.63 -68.60 REMARK 500 5 THR A 144 56.57 86.43 REMARK 500 6 ALA A 5 64.10 -101.51 REMARK 500 6 ASP A 57 -74.65 -47.21 REMARK 500 6 GLU A 87 -7.64 -54.50 REMARK 500 6 SER A 118 0.34 -151.27 REMARK 500 6 ALA A 138 99.83 -68.86 REMARK 500 7 ASP A 57 -76.38 -50.05 REMARK 500 7 GLU A 87 -3.88 -55.68 REMARK 500 7 VAL A 108 27.40 -67.58 REMARK 500 8 ASP A 57 -77.12 -55.34 REMARK 500 8 GLU A 87 -3.61 -55.00 REMARK 500 8 VAL A 108 27.25 -68.77 REMARK 500 8 ALA A 135 20.23 -76.03 REMARK 500 9 ILE A 2 -83.45 -114.58 REMARK 500 9 ASN A 110 52.08 -92.32 REMARK 500 10 ILE A 2 -73.06 -137.63 REMARK 500 10 ALA A 5 59.64 -66.27 REMARK 500 10 SER A 37 30.05 -98.34 REMARK 500 10 VAL A 108 26.16 -73.13 REMARK 500 10 ALA A 112 -66.03 -108.61 REMARK 500 10 ALA A 138 94.48 -53.96 REMARK 500 10 ALA A 142 78.50 -151.86 REMARK 500 11 ILE A 2 -104.69 -129.09 REMARK 500 11 ASP A 57 -74.76 -41.48 REMARK 500 REMARK 500 THIS ENTRY HAS 93 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 17 0.09 SIDE CHAIN REMARK 500 1 ARG A 120 0.07 SIDE CHAIN REMARK 500 2 TYR A 17 0.07 SIDE CHAIN REMARK 500 3 TYR A 17 0.07 SIDE CHAIN REMARK 500 3 TYR A 34 0.08 SIDE CHAIN REMARK 500 4 ARG A 21 0.09 SIDE CHAIN REMARK 500 4 ARG A 76 0.10 SIDE CHAIN REMARK 500 4 PHE A 127 0.10 SIDE CHAIN REMARK 500 5 TYR A 17 0.11 SIDE CHAIN REMARK 500 5 TYR A 34 0.07 SIDE CHAIN REMARK 500 5 PHE A 79 0.09 SIDE CHAIN REMARK 500 6 TYR A 17 0.09 SIDE CHAIN REMARK 500 6 TYR A 34 0.08 SIDE CHAIN REMARK 500 7 ARG A 120 0.09 SIDE CHAIN REMARK 500 7 PHE A 127 0.08 SIDE CHAIN REMARK 500 8 TYR A 17 0.07 SIDE CHAIN REMARK 500 8 TYR A 34 0.14 SIDE CHAIN REMARK 500 9 TYR A 17 0.07 SIDE CHAIN REMARK 500 9 TYR A 34 0.12 SIDE CHAIN REMARK 500 9 PHE A 127 0.09 SIDE CHAIN REMARK 500 10 TYR A 17 0.08 SIDE CHAIN REMARK 500 10 TYR A 34 0.09 SIDE CHAIN REMARK 500 10 ARG A 60 0.10 SIDE CHAIN REMARK 500 10 ARG A 66 0.12 SIDE CHAIN REMARK 500 11 TYR A 17 0.09 SIDE CHAIN REMARK 500 11 TYR A 34 0.09 SIDE CHAIN REMARK 500 11 PHE A 127 0.08 SIDE CHAIN REMARK 500 12 TYR A 34 0.11 SIDE CHAIN REMARK 500 12 ASP A 141 0.09 SIDE CHAIN REMARK 500 16 ARG A 60 0.11 SIDE CHAIN REMARK 500 16 ARG A 76 0.08 SIDE CHAIN REMARK 500 16 PHE A 79 0.09 SIDE CHAIN REMARK 500 17 ARG A 21 0.12 SIDE CHAIN REMARK 500 17 ARG A 60 0.09 SIDE CHAIN REMARK 500 17 PHE A 79 0.10 SIDE CHAIN REMARK 500 18 ARG A 3 0.12 SIDE CHAIN REMARK 500 18 ARG A 21 0.16 SIDE CHAIN REMARK 500 18 TYR A 34 0.10 SIDE CHAIN REMARK 500 18 ARG A 120 0.08 SIDE CHAIN REMARK 500 19 ARG A 60 0.10 SIDE CHAIN REMARK 500 19 ARG A 76 0.08 SIDE CHAIN REMARK 500 20 ARG A 3 0.10 SIDE CHAIN REMARK 500 20 TYR A 34 0.09 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 1WNJ A 4 145 UNP Q14019 COTL1_HUMAN 1 142 SEQADV 1WNJ GLY A 1 UNP Q14019 CLONING ARTIFACT SEQADV 1WNJ ILE A 2 UNP Q14019 CLONING ARTIFACT SEQADV 1WNJ ARG A 3 UNP Q14019 CLONING ARTIFACT SEQRES 1 A 145 GLY ILE ARG MET ALA THR LYS ILE ASP LYS GLU ALA CYS SEQRES 2 A 145 ARG ALA ALA TYR ASN LEU VAL ARG ASP ASP GLY SER ALA SEQRES 3 A 145 VAL ILE TRP VAL THR PHE LYS TYR ASP GLY SER THR ILE SEQRES 4 A 145 VAL PRO GLY GLU GLN GLY ALA GLU TYR GLN HIS PHE ILE SEQRES 5 A 145 GLN GLN CYS THR ASP ASP VAL ARG LEU PHE ALA PHE VAL SEQRES 6 A 145 ARG PHE THR THR GLY ASP ALA MET SER LYS ARG SER LYS SEQRES 7 A 145 PHE ALA LEU ILE THR TRP ILE GLY GLU ASN VAL SER GLY SEQRES 8 A 145 LEU GLN ARG ALA LYS THR GLY THR ASP LYS THR LEU VAL SEQRES 9 A 145 LYS GLU VAL VAL GLN ASN PHE ALA LYS GLU PHE VAL ILE SEQRES 10 A 145 SER ASP ARG LYS GLU LEU GLU GLU ASP PHE ILE LYS SER SEQRES 11 A 145 GLU LEU LYS LYS ALA GLY GLY ALA ASN TYR ASP ALA GLN SEQRES 12 A 145 THR GLU HELIX 1 1 ASP A 9 ARG A 21 1 13 HELIX 2 2 TYR A 48 CYS A 55 1 8 HELIX 3 3 SER A 90 VAL A 108 1 19 HELIX 4 4 ASP A 119 GLU A 124 1 6 HELIX 5 5 GLU A 124 ALA A 135 1 12 SHEET 1 A 6 LYS A 7 ILE A 8 0 SHEET 2 A 6 THR A 38 GLY A 45 1 O ILE A 39 N LYS A 7 SHEET 3 A 6 TRP A 29 ASP A 35 -1 N ASP A 35 O THR A 38 SHEET 4 A 6 LEU A 61 PHE A 67 -1 O PHE A 62 N PHE A 32 SHEET 5 A 6 LYS A 78 TRP A 84 -1 O TRP A 84 N LEU A 61 SHEET 6 A 6 LYS A 113 ILE A 117 1 O ILE A 117 N THR A 83 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