Header list of 2arf.pdb file
Complete list - t 20 2 Bytes
HEADER HYDROLASE 19-AUG-05 2ARF TITLE SOLUTION STRUCTURE OF THE WILSON ATPASE N-DOMAIN IN THE PRESENCE OF TITLE 2 ATP COMPND MOL_ID: 1; COMPND 2 MOLECULE: WILSON DISEASE ATPASE; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: N-DOMAIN; COMPND 5 SYNONYM: COPPER PUMP 2, WILSON DISEASE-ASSOCIATED PROTEIN; COMPND 6 EC: 3.6.3.4; COMPND 7 ENGINEERED: YES; COMPND 8 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: ATP7B; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PTYB12-N-ABD KEYWDS ATPASE, WILSON DISEASE, P-TYPE ATPASE, ATP7B, COPPER TRANSPORT, KEYWDS 2 NUCLEOTIDE BINDING, ATP BINDING, HYDROLASE EXPDTA SOLUTION NMR NUMMDL 10 AUTHOR O.DMITRIEV,R.TSIVKOVSKII,F.ABILDGAARD,C.T.MORGAN,J.L.MARKLEY, AUTHOR 2 S.LUTSENKO REVDAT 4 20-OCT-21 2ARF 1 REMARK SEQADV REVDAT 3 24-FEB-09 2ARF 1 VERSN REVDAT 2 25-APR-06 2ARF 1 JRNL REVDAT 1 28-FEB-06 2ARF 0 JRNL AUTH O.DMITRIEV,R.TSIVKOVSKII,F.ABILDGAARD,C.T.MORGAN, JRNL AUTH 2 J.L.MARKLEY,S.LUTSENKO JRNL TITL SOLUTION STRUCTURE OF THE N-DOMAIN OF WILSON DISEASE JRNL TITL 2 PROTEIN: DISTINCT NUCLEOTIDE-BINDING ENVIRONMENT AND EFFECTS JRNL TITL 3 OF DISEASE MUTATIONS JRNL REF PROC.NATL.ACAD.SCI.USA V. 103 5302 2006 JRNL REFN ISSN 0027-8424 JRNL PMID 16567646 JRNL DOI 10.1073/PNAS.0507416103 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 3.5, CYANA 1.0 REMARK 3 AUTHORS : BRUKER INC (XWINNMR), GUNTERT (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2ARF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-SEP-05. REMARK 100 THE DEPOSITION ID IS D_1000034225. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 300 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : 50 MM SODIUM PHOSPHATE REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.75 MM WILSON ATPASE N-DOMAIN U REMARK 210 -15N, U-13C, 50 MM SODIUM REMARK 210 PHOSPHATE, PH 6.0, 5 MM DTT, 50 REMARK 210 MM NAN3, 5 MM ATP, 95% H2O, 5% REMARK 210 D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY; 4D_13C/15N- REMARK 210 SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : DMX; AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : FELIX 2000, CYANA 1.0 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS, REMARK 210 SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET 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 HE ARG A 1155 OG SER A 1166 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 PRO A1037 -162.76 -75.07 REMARK 500 1 LEU A1045 22.50 -144.72 REMARK 500 1 ASP A1047 162.83 175.93 REMARK 500 1 SER A1067 152.01 94.56 REMARK 500 1 GLU A1068 -28.62 159.20 REMARK 500 1 PRO A1070 44.20 -74.90 REMARK 500 1 LEU A1071 -37.83 174.11 REMARK 500 1 THR A1087 146.46 -36.35 REMARK 500 1 LEU A1088 114.93 169.08 REMARK 500 1 ASP A1093 81.73 -160.90 REMARK 500 1 GLN A1095 146.70 -178.57 REMARK 500 1 CYS A1100 -68.81 -150.59 REMARK 500 1 ASN A1108 -32.75 162.92 REMARK 500 1 HIS A1115 171.96 -47.22 REMARK 500 1 ARG A1118 76.07 55.18 REMARK 500 1 SER A1125 101.34 67.70 REMARK 500 1 ASN A1128 143.97 -38.47 REMARK 500 1 SER A1132 96.93 71.14 REMARK 500 1 LYS A1137 121.64 68.66 REMARK 500 1 LEU A1159 -160.37 -123.91 REMARK 500 1 THR A1160 -169.62 -107.75 REMARK 500 1 ILE A1161 160.83 59.17 REMARK 500 1 CYS A1189 -62.96 -145.10 REMARK 500 2 MET A1035 111.80 -162.52 REMARK 500 2 LEU A1045 29.86 -141.40 REMARK 500 2 VAL A1048 31.01 -94.24 REMARK 500 2 SER A1067 -150.27 -99.02 REMARK 500 2 LEU A1071 -45.49 -130.35 REMARK 500 2 THR A1087 153.83 -40.38 REMARK 500 2 LEU A1088 -169.15 -115.81 REMARK 500 2 ASP A1093 77.76 -170.77 REMARK 500 2 PHE A1094 -167.85 -106.86 REMARK 500 2 GLN A1095 164.07 178.21 REMARK 500 2 CYS A1100 -74.51 -141.93 REMARK 500 2 ASN A1108 -57.80 141.33 REMARK 500 2 ALA A1114 -158.87 -93.48 REMARK 500 2 HIS A1115 121.09 65.29 REMARK 500 2 GLU A1117 74.89 56.84 REMARK 500 2 LEU A1120 -74.49 -43.72 REMARK 500 2 SER A1125 -63.47 78.19 REMARK 500 2 HIS A1126 -48.67 81.54 REMARK 500 2 ASN A1128 107.72 -35.55 REMARK 500 2 GLU A1129 94.03 -64.21 REMARK 500 2 ALA A1130 -177.19 56.48 REMARK 500 2 SER A1132 79.80 -111.66 REMARK 500 2 GLU A1136 -51.69 -136.57 REMARK 500 2 LYS A1137 159.11 64.57 REMARK 500 2 ALA A1139 81.01 63.97 REMARK 500 2 VAL A1140 136.69 -38.96 REMARK 500 2 THR A1160 -165.52 -69.98 REMARK 500 REMARK 500 THIS ENTRY HAS 244 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 2ARF A 1032 1196 UNP P35670 ATP7B_HUMAN 1032 1196 SEQADV 2ARF ALA A 1032 UNP P35670 ILE 1032 ENGINEERED MUTATION SEQADV 2ARF GLY A 1033 UNP P35670 THR 1033 ENGINEERED MUTATION SEQADV 2ARF MET A 1035 UNP P35670 GLY 1035 ENGINEERED MUTATION SEQRES 1 A 165 ALA GLY HIS MET VAL PRO ARG VAL MET ARG VAL LEU LEU SEQRES 2 A 165 LEU GLY ASP VAL ALA THR LEU PRO LEU ARG LYS VAL LEU SEQRES 3 A 165 ALA VAL VAL GLY THR ALA GLU ALA SER SER GLU HIS PRO SEQRES 4 A 165 LEU GLY VAL ALA VAL THR LYS TYR CYS LYS GLU GLU LEU SEQRES 5 A 165 GLY THR GLU THR LEU GLY TYR CYS THR ASP PHE GLN ALA SEQRES 6 A 165 VAL PRO GLY CYS GLY ILE GLY CYS LYS VAL SER ASN VAL SEQRES 7 A 165 GLU GLY ILE LEU ALA HIS SER GLU ARG PRO LEU SER ALA SEQRES 8 A 165 PRO ALA SER HIS LEU ASN GLU ALA GLY SER LEU PRO ALA SEQRES 9 A 165 GLU LYS ASP ALA VAL PRO GLN THR PHE SER VAL LEU ILE SEQRES 10 A 165 GLY ASN ARG GLU TRP LEU ARG ARG ASN GLY LEU THR ILE SEQRES 11 A 165 SER SER ASP VAL SER ASP ALA MET THR ASP HIS GLU MET SEQRES 12 A 165 LYS GLY GLN THR ALA ILE LEU VAL ALA ILE ASP GLY VAL SEQRES 13 A 165 LEU CYS GLY MET ILE ALA ILE ALA ASP HELIX 1 1 PRO A 1052 ALA A 1065 1 14 HELIX 2 2 LEU A 1071 GLY A 1084 1 14 HELIX 3 3 ASN A 1108 ALA A 1114 1 7 HELIX 4 4 ASN A 1150 LEU A 1159 1 10 HELIX 5 5 SER A 1162 MET A 1174 1 13 SHEET 1 A 6 VAL A1039 LEU A1044 0 SHEET 2 A 6 VAL A1187 ILE A1194 -1 O ALA A1193 N ARG A1041 SHEET 3 A 6 THR A1178 ILE A1184 -1 N THR A1178 O ILE A1194 SHEET 4 A 6 THR A1143 GLY A1149 -1 N LEU A1147 O ALA A1183 SHEET 5 A 6 GLY A1101 SER A1107 -1 N CYS A1104 O VAL A1146 SHEET 6 A 6 CYS A1091 VAL A1097 -1 N GLN A1095 O GLY A1103 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 - t 20 2 Bytes