Header list of 2a20.pdb file
Complete list - r 9 2 Bytes
HEADER METAL BINDING PROTEIN 21-JUN-05 2A20 TITLE SOLUTION STRUCTURE OF RIM2 ZINC FINGER DOMAIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: REGULATING SYNAPTIC MEMBRANE EXOCYTOSIS PROTEIN 2; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: ZINC-FINGER DOMAIN, FYVE-TYPE, RESIDUES 83-142; COMPND 5 SYNONYM: RAB3-INTERACTING MOLECULE 2, RIM 2; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 3 ORGANISM_COMMON: NORWAY RAT; SOURCE 4 ORGANISM_TAXID: 10116; SOURCE 5 GENE: RIMS2, RIM2; 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: PGEX-KT KEYWDS ZINC-FINGER DOMAIN, METAL BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR I.DULUBOVA,X.LOU,J.LU,I.HURYEVA,A.ALAM,R.SCHNEGGENBURGER,T.C.SUDHOF, AUTHOR 2 J.RIZO REVDAT 4 09-MAR-22 2A20 1 REMARK SEQADV LINK REVDAT 3 24-FEB-09 2A20 1 VERSN REVDAT 2 30-AUG-05 2A20 1 JRNL REVDAT 1 16-AUG-05 2A20 0 JRNL AUTH I.DULUBOVA,X.LOU,J.LU,I.HURYEVA,A.ALAM,R.SCHNEGGENBURGER, JRNL AUTH 2 T.C.SUDHOF,J.RIZO JRNL TITL A MUNC13/RIM/RAB3 TRIPARTITE COMPLEX: FROM PRIMING TO JRNL TITL 2 PLASTICITY? JRNL REF EMBO J. V. 24 2839 2005 JRNL REFN ISSN 0261-4189 JRNL PMID 16052212 JRNL DOI 10.1038/SJ.EMBOJ.7600753 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NMRPIPE 2.3, CNS 1.1 REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE REMARK 3 -KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE, REMARK 3 SIMONSON,WARREN (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2A20 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-AUG-05. REMARK 100 THE DEPOSITION ID IS D_1000033392. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.9 REMARK 210 IONIC STRENGTH : 150 MM NACL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1 MM U-15N,13C RIM2 ZF DOMAIN, REMARK 210 20 MM PIPES PH 6.9, 150 MM NACL, REMARK 210 1 MM TCEP, 90% H2O, 10% D2O; 1 REMARK 210 MM U-15N RIM2 ZF DOMAIN, 20 MM REMARK 210 PIPES PH 6.9, 150 MM NACL, 1 MM REMARK 210 TCEP, 90% H2O, 10% D2O; 1MM U- REMARK 210 15N RIM2 ZF DOMAIN, 20 MM PIPES REMARK 210 PH 6.9, 150 MM NACL, 1 MM TCEP, REMARK 210 100% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; 2D NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRVIEW 5.0.16, ARIA 2.0A REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 500 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 MODELS 1-20 REMARK 465 RES C SSSEQI REMARK 465 GLY A 81 REMARK 465 SER A 82 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 ASP A 102 94.76 -58.18 REMARK 500 1 TYR A 110 -77.69 -104.94 REMARK 500 1 ARG A 126 135.17 67.19 REMARK 500 1 SER A 127 97.47 -44.08 REMARK 500 1 ASN A 128 -36.46 179.82 REMARK 500 2 GLN A 85 -77.29 -154.49 REMARK 500 2 ILE A 94 -70.38 -124.45 REMARK 500 2 HIS A 96 29.55 45.39 REMARK 500 2 TYR A 110 -73.63 -111.11 REMARK 500 2 ARG A 126 -60.80 -139.99 REMARK 500 2 SER A 127 -38.17 -175.26 REMARK 500 3 ILE A 94 -70.14 -120.72 REMARK 500 3 PHE A 100 174.72 -51.57 REMARK 500 3 ALA A 101 -73.56 -48.12 REMARK 500 3 TYR A 110 -76.54 -104.46 REMARK 500 3 ARG A 126 -170.37 54.15 REMARK 500 3 ASN A 128 39.29 -176.83 REMARK 500 4 PHE A 100 174.24 -54.44 REMARK 500 4 ASP A 102 27.35 45.88 REMARK 500 4 CYS A 104 56.15 -146.66 REMARK 500 4 TYR A 110 -72.15 -111.34 REMARK 500 4 ARG A 126 -82.21 63.75 REMARK 500 4 SER A 127 -53.83 -169.74 REMARK 500 5 ILE A 94 -70.27 -123.84 REMARK 500 5 HIS A 96 25.68 48.12 REMARK 500 5 LYS A 97 -60.59 -109.58 REMARK 500 5 ASP A 102 -63.47 67.38 REMARK 500 5 TYR A 110 -72.42 -111.38 REMARK 500 5 ARG A 126 -71.43 -52.23 REMARK 500 5 SER A 127 -83.73 -49.17 REMARK 500 5 ASN A 128 33.90 -178.10 REMARK 500 6 GLN A 85 83.92 -155.28 REMARK 500 6 LYS A 86 -41.44 -176.99 REMARK 500 6 ILE A 94 -69.77 -127.06 REMARK 500 6 PHE A 100 -175.11 -61.09 REMARK 500 6 ALA A 101 -160.12 -72.70 REMARK 500 6 TYR A 110 -73.75 -107.71 REMARK 500 6 LEU A 125 48.28 -93.98 REMARK 500 6 ARG A 126 -62.62 69.27 REMARK 500 6 SER A 127 -158.16 -63.53 REMARK 500 7 HIS A 96 25.64 48.66 REMARK 500 7 ALA A 101 -72.60 -48.56 REMARK 500 7 ASP A 102 80.46 -177.91 REMARK 500 7 TYR A 110 -75.17 -106.93 REMARK 500 7 ARG A 126 40.66 -92.68 REMARK 500 7 SER A 127 28.33 -144.27 REMARK 500 7 ASN A 128 63.20 66.04 REMARK 500 8 GLN A 85 -63.12 73.19 REMARK 500 8 ILE A 94 -68.71 -126.40 REMARK 500 8 HIS A 96 28.71 48.26 REMARK 500 REMARK 500 THIS ENTRY HAS 143 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 292 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 92 SG REMARK 620 2 CYS A 95 SG 110.1 REMARK 620 3 CYS A 116 SG 115.6 99.7 REMARK 620 4 CYS A 119 SG 130.2 105.7 90.4 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 308 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 108 SG REMARK 620 2 CYS A 111 SG 125.8 REMARK 620 3 CYS A 134 SG 114.2 108.7 REMARK 620 4 CYS A 137 SG 121.3 88.0 91.5 REMARK 620 N 1 2 3 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 292 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 308 DBREF 2A20 A 83 142 UNP Q9JIS1 RIMS2_RAT 83 142 SEQADV 2A20 GLY A 81 UNP Q9JIS1 CLONING ARTIFACT SEQADV 2A20 SER A 82 UNP Q9JIS1 CLONING ARTIFACT SEQRES 1 A 62 GLY SER GLN GLU GLN LYS GLY ASP ALA PRO THR CYS GLY SEQRES 2 A 62 ILE CYS HIS LYS THR LYS PHE ALA ASP GLY CYS GLY HIS SEQRES 3 A 62 ASN CYS SER TYR CYS GLN THR LYS PHE CYS ALA ARG CYS SEQRES 4 A 62 GLY GLY ARG VAL SER LEU ARG SER ASN LYS VAL MET TRP SEQRES 5 A 62 VAL CYS ASN LEU CYS ARG LYS GLN GLN GLU HET ZN A 292 1 HET ZN A 308 1 HETNAM ZN ZINC ION FORMUL 2 ZN 2(ZN 2+) HELIX 1 1 ASN A 135 GLN A 141 1 7 SHEET 1 A 2 HIS A 106 ASN A 107 0 SHEET 2 A 2 LYS A 114 PHE A 115 -1 O PHE A 115 N HIS A 106 SHEET 1 B 2 GLY A 120 SER A 124 0 SHEET 2 B 2 VAL A 130 CYS A 134 -1 O MET A 131 N VAL A 123 LINK SG CYS A 92 ZN ZN A 292 1555 1555 1.61 LINK SG CYS A 95 ZN ZN A 292 1555 1555 2.66 LINK SG CYS A 108 ZN ZN A 308 1555 1555 1.61 LINK SG CYS A 111 ZN ZN A 308 1555 1555 2.59 LINK SG CYS A 116 ZN ZN A 292 1555 1555 2.61 LINK SG CYS A 119 ZN ZN A 292 1555 1555 2.54 LINK SG CYS A 134 ZN ZN A 308 1555 1555 2.59 LINK SG CYS A 137 ZN ZN A 308 1555 1555 2.58 SITE 1 AC1 5 CYS A 92 ILE A 94 CYS A 95 CYS A 116 SITE 2 AC1 5 CYS A 119 SITE 1 AC2 4 CYS A 108 CYS A 111 CYS A 134 CYS A 137 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 9 2 Bytes